|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-595 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 631.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 12 ERPKHLIRTLLKSLREYKKDTILAPTFVIVESVLEILIPTVMASMIDQGVAGGSMPAIWKFGLILLGCAVVSLFAGFMSG 91
Cdd:COG1132 3 KSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 92 RYAAIASAGFAKNLRHDLFEKVQSFSFTNIDHFSTGSIITRITTDVTNIQYAFQMCIRVAVRAPLMVVVAWLFSFRISPS 171
Cdd:COG1132 83 YLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 172 ISMIFLIIIPILGVTLTGLALSVNPVFEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEH 251
Cdd:COG1132 163 LALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAAR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 252 VLAFNWPILNTCIYGAMLIISWMGTKQIVGSHnnaavgLTTGDLTALVTYAMQILMSLNMVSMIIVMVVISRADAERICQ 331
Cdd:COG1132 243 LSALFFPLMELLGNLGLALVLLVGGLLVLSGS------LTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 332 VLNEVSTVRDNADPI-MDVPDGSITFNDVSFRYDvgSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSS 410
Cdd:COG1132 317 LLDEPPEIPDPPGAVpLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 411 GSLEVGGRDVREYDLETLRDAVAMVLQKNVLFAGTIADNIRWGNPNATDEDVRRVCKLAQADGFIREFPKGYDTYIEEGG 490
Cdd:COG1132 395 GRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 491 SNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIAQRVASVQESDEIIVMDGGRILD 570
Cdd:COG1132 475 VNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVE 554
|
570 580
....*....|....*....|....*
gi 705456738 571 RGTHDQLLQTCDEYRSIYQSQTKSQ 595
Cdd:COG1132 555 QGTHEELLARGGLYARLYRLQFGEE 579
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
10-592 |
1.49e-128 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 393.82 E-value: 1.49e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 10 EEERPKHLIRTLLKSLREYKKD--TILAPTFVIveSVLEILIPTVMASMIDQGVAGGSMPAIWKFGLILLGCAVVSLFAG 87
Cdd:COG2274 136 KRGEKPFGLRWFLRLLRRYRRLllQVLLASLLI--NLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLR 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 88 FMSGRYAAIASAGFAKNLRHDLFEKVQSFSFTNIDHFSTGSIITRITtDVTNIQyafQMCIRVAVRAPL---MVVVAWLF 164
Cdd:COG2274 214 LLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIR---EFLTGSLLTALLdllFVLIFLIV 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 165 SFRISPSISMIFLIIIPILGVtltgLALSVNPVF----EKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSE 240
Cdd:COG2274 290 LFFYSPPLALVVLLLIPLYVL----LGLLFQPRLrrlsREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 241 RIYEYFCKAEHVLAF--NWP-ILNTCIYGAMLiisWMGTKQIVGSHnnaavgLTTGDLTALVTYAMQILMSLNMVSMIIV 317
Cdd:COG2274 366 KYLNARFKLRRLSNLlsTLSgLLQQLATVALL---WLGAYLVIDGQ------LTLGQLIAFNILSGRFLAPVAQLIGLLQ 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 318 MVVISRADAERICQVLNEVSTVRDNADPI-MDVPDGSITFNDVSFRYDvGSERPVLDDINLTIASGSTIGIVGGTGSAKS 396
Cdd:COG2274 437 RFQDAKIALERLDDILDLPPEREEGRSKLsLPRLKGDIELENVSFRYP-GDSPPVLDNISLTIKPGERVAIVGRSGSGKS 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 397 SLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVAMVLQKNVLFAGTIADNIRWGNPNATDEDVRRVCKLAQADGFIR 476
Cdd:COG2274 516 TLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIE 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 477 EFPKGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIAQRVASVQE 556
Cdd:COG2274 596 ALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRL 675
|
570 580 590
....*....|....*....|....*....|....*.
gi 705456738 557 SDEIIVMDGGRILDRGTHDQLLQTCDEYRSIYQSQT 592
Cdd:COG2274 676 ADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
32-329 |
3.27e-120 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 357.86 E-value: 3.27e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 32 TILAPTFVIVESVLEILIPTVMASMIDQGVAGGSMPAIWKFGLILLGCAVVSLFAGFMSGRYAAIASAGFAKNLRHDLFE 111
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 112 KVQSFSFTNIDHFSTGSIITRITTDVTNIQYAFQMCIRVAVRAPLMVVVAWLFSFRISPSISMIFLIIIPILGVTLTGLA 191
Cdd:cd18548 81 KIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 192 LSVNPVFEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEHVLAFNWPILNTCIYGAMLII 271
Cdd:cd18548 161 KKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 705456738 272 SWMGTKQIVGShnnaavGLTTGDLTALVTYAMQILMSLNMVSMIIVMVVISRADAERI 329
Cdd:cd18548 241 LWFGGHLINAG------SLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKRI 292
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
19-591 |
9.65e-117 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 358.65 E-value: 9.65e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 19 RTLLKSLREYKKDTILAPTFVIVESVLEILIPTVMASMIDQGVAGGSMPAIWKFGLILLGCAVVSLFAGFMSGRYAAIAS 98
Cdd:TIGR02203 3 RRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSWVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 99 AGFAKNLRHDLFEKVQSFSFTNIDHFSTGSIITRITTDVTNIQYAFQMCIRVAVRAPLMVVVAWLFSFRISPSISMIFLI 178
Cdd:TIGR02203 83 NKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 179 IIPILGVTLTGLALSVNPVFEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEHVLAFNWP 258
Cdd:TIGR02203 163 MLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 259 ILNTCIYGAMLIISWmgtkqiVGSHNNAAVGLTTGDLTALVTYAMQILMSLNMVSMIIVMVVISRADAERICQVLNEVST 338
Cdd:TIGR02203 243 ITQLIASLALAVVLF------IALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 339 VRDNADPIMDVpDGSITFNDVSFRYDvGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGR 418
Cdd:TIGR02203 317 KDTGTRAIERA-RGDVEFRNVTFRYP-GRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGH 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 419 DVREYDLETLRDAVAMVLQKNVLFAGTIADNIRWGNP-NATDEDVRRVCKLAQADGFIREFPKGYDTYIEEGGSNVSGGQ 497
Cdd:TIGR02203 395 DLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQ 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 498 RQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIAQRVASVQESDEIIVMDGGRILDRGTHDQL 577
Cdd:TIGR02203 475 RQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNEL 554
|
570
....*....|....
gi 705456738 578 LQTCDEYRSIYQSQ 591
Cdd:TIGR02203 555 LARNGLYAQLHNMQ 568
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
104-589 |
9.06e-101 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 317.48 E-value: 9.06e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 104 NLRHDLFEKVQSFSFTNIDHFSTGSIITRITTDVTNIQYAFqmcIRV---AVRAPLMVVVAWLFSFRISPSISMIFLIII 180
Cdd:COG4987 89 DLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLY---LRVllpLLVALLVILAAVAFLAFFSPALALVLALGL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 181 PILGVTLTGLALSVN-PVFEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEHVLAFNWPI 259
Cdd:COG4987 166 LLAGLLLPLLAARLGrRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQAL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 260 LNTCIYGAMLIISWMGTKQIVGshnnaavGLTTGDLTALVTYAmqILMSLNMVSMIIVMVV---ISRADAERICQVLNEV 336
Cdd:COG4987 246 LQLAAGLAVVAVLWLAAPLVAA-------GALSGPLLALLVLA--ALALFEALAPLPAAAQhlgRVRAAARRLNELLDAP 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 337 STVRDNADPIMDVPDGSITFNDVSFRYDvGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVG 416
Cdd:COG4987 317 PAVTEPAEPAPAPGGPSLELEDVSFRYP-GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLG 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 417 GRDVREYDLETLRDAVAMVLQKNVLFAGTIADNIRWGNPNATDEDVRRVCKLAQADGFIREFPKGYDTYIEEGGSNVSGG 496
Cdd:COG4987 396 GVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGG 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 497 QRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIAQRVASVQESDEIIVMDGGRILDRGTHDQ 576
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEE 555
|
490
....*....|...
gi 705456738 577 LLQTCDEYRSIYQ 589
Cdd:COG4987 556 LLAQNGRYRQLYQ 568
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
14-580 |
1.51e-100 |
|
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: 316.70 E-value: 1.51e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 14 PKHLIRTLLKSLREYKKDTILAPTFVIVESVLEILIPTVMASMIDQGVAGG-SMPAIWKFGLILLGCAVVSLFAGFMSGR 92
Cdd:COG4988 1 QKPLDKRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGaPLSALLPLLGLLLAVLLLRALLAWLRER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 93 YAAIASAGFAKNLRHDLFEKVQSFSFTNIDHFSTGSIITRITTDVTNIQ-----YAFQMCirVAVRAPLMVVVawlFSFR 167
Cdd:COG4988 81 AAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDgyfarYLPQLF--LAALVPLLILV---AVFP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 168 ISPSISMIFLI---IIPILGVtLTGLALSVnpVFEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSEriyE 244
Cdd:COG4988 156 LDWLSGLILLVtapLIPLFMI-LVGKGAAK--ASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASE---D 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 245 YFCKAEHVL--AFnwpiLNTCI-----YGAMLIISWMGTKQIVGSHnnaaVGLTTGdLTALVTyAMQILMSLNMVS---- 313
Cdd:COG4988 230 FRKRTMKVLrvAF----LSSAVleffaSLSIALVAVYIGFRLLGGS----LTLFAA-LFVLLL-APEFFLPLRDLGsfyh 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 314 --MIivmvviSRADAERICQVLN-EVSTVRDNADPIMDVPDGSITFNDVSFRYDvgSERPVLDDINLTIASGSTIGIVGG 390
Cdd:COG4988 300 arAN------GIAAAEKIFALLDaPEPAAPAGTAPLPAAGPPSIELEDVSFSYP--GGRPALDGLSLTIPPGERVALVGP 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 391 TGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVAMVLQKNVLFAGTIADNIRWGNPNATDEDVRRVCKLAQ 470
Cdd:COG4988 372 SGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAG 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 471 ADGFIREFPKGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIAQR 550
Cdd:COG4988 452 LDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHR 531
|
570 580 590
....*....|....*....|....*....|
gi 705456738 551 VASVQESDEIIVMDGGRILDRGTHDQLLQT 580
Cdd:COG4988 532 LALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
222-603 |
9.01e-99 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 313.30 E-value: 9.01e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 222 VKSYDREEHESRKFGRVSERIYEYFCKAEHVLAFnwpiLNT----CIYGAMLIISWMGTKQIVGSHnnaavgLTTGDLTA 297
Cdd:COG5265 231 VKYFGNEAREARRYDEALARYERAAVKSQTSLAL----LNFgqalIIALGLTAMMLMAAQGVVAGT------MTVGDFVL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 298 LVTYAMQILMSLNMVSMIIVMVVISRADAERICQVLNEVSTVRDNAD-PIMDVPDGSITFNDVSFRYDvgSERPVLDDIN 376
Cdd:COG5265 301 VNAYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPEVADAPDaPPLVVGGGEVRFENVSFGYD--PERPILKGVS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 377 LTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVAMVLQKNVLFAGTIADNIRWGNPN 456
Cdd:COG5265 379 FEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPD 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 457 ATDEDVRRVCKLAQADGFIREFPKGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFK 536
Cdd:COG5265 459 ASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALR 538
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 705456738 537 TEIPDTTKIIIAQRVASVQESDEIIVMDGGRILDRGTHDQLLQTCDEYRSIYQSQTKSQGEGSDDDE 603
Cdd:COG5265 539 EVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEAEEALAA 605
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
10-587 |
1.19e-94 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 305.49 E-value: 1.19e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 10 EEERPKHLIRTLLKSLREYKKDTILAPTFVIVESVLEILIPTVMASMIDQGVAGGSMPA----IWKFGLILLGCavvSLF 85
Cdd:TIGR00958 141 GQSETADLLFRLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPAlasaIFFMCLLSIAS---SVS 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 86 AGFMSGRYAaIASAGFAKNLRHDLFEKV--QSFSFtnIDHFSTGSIITRITTDVTNIQYAFQMCIRVAVRAPLMVVVAWL 163
Cdd:TIGR00958 218 AGLRGGSFN-YTMARINLRIREDLFRSLlrQDLGF--FDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLG 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 164 FSFRISPSISMIFLIIIPILGVTLTGLALSVNPVFEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIY 243
Cdd:TIGR00958 295 FMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 244 EYFCKAEHVLAFNWPILNTCIYGAMLIISWMGTKQIVGSHnnaavgLTTGDLTALVTYAMQILMSLNMVSMIIVMVVISR 323
Cdd:TIGR00958 375 QLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGK------VSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAV 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 324 ADAERICQVLNEVSTVRDNADPIMDVPDGSITFNDVSFRYDVGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIP 403
Cdd:TIGR00958 449 GASEKVFEYLDRKPNIPLTGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQ 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 404 RLYDVSSGSLEVGGRDVREYDLETLRDAVAMVLQKNVLFAGTIADNIRWGNPNATDEDVRRVCKLAQADGFIREFPKGYD 483
Cdd:TIGR00958 529 NLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYD 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 484 TYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKTEipDTTKIIIAQRVASVQESDEIIVM 563
Cdd:TIGR00958 609 TEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRA--SRTVLLIAHRLSTVERADQILVL 686
|
570 580
....*....|....*....|....
gi 705456738 564 DGGRILDRGTHDQLLQTCDEYRSI 587
Cdd:TIGR00958 687 KKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
354-588 |
2.38e-93 |
|
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: 286.43 E-value: 2.38e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDvGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVA 433
Cdd:cd03251 1 VEFKNVTFRYP-GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 MVLQKNVLFAGTIADNIRWGNPNATDEDVRRVCKLAQADGFIREFPKGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKI 513
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 705456738 514 LILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIAQRVASVQESDEIIVMDGGRILDRGTHDQLLQTCDEYRSIY 588
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
354-591 |
7.18e-91 |
|
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: 280.19 E-value: 7.18e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDVGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVA 433
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 MVLQKNVLFAGTIADNIRWGNPNATDEDVRRVCKLAQADGFIREFPKGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKI 513
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 705456738 514 LILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIAQRVASVQESDEIIVMDGGRILDRGTHDQLLQTCDEYRSIYQSQ 591
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
354-591 |
2.21e-90 |
|
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: 278.73 E-value: 2.21e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDvgSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVA 433
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 MVLQKNVLFAGTIADNIRWGNPNATDEDVRRVCKLAQADGFIREFPKGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKI 513
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 705456738 514 LILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIAQRVASVQESDEIIVMDGGRILDRGTHDQLLQTCDEYRSIYQSQ 591
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
352-579 |
1.50e-88 |
|
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: 273.72 E-value: 1.50e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 352 GSITFNDVSFRYDvgSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDA 431
Cdd:cd03254 1 GEIEFENVNFSYD--EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 432 VAMVLQKNVLFAGTIADNIRWGNPNATDEDVRRVCKLAQADGFIREFPKGYDTYIEEGGSNVSGGQRQRLCIARALLKKP 511
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 705456738 512 KILILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIAQRVASVQESDEIIVMDGGRILDRGTHDQLLQ 579
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
175-579 |
1.81e-77 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 256.81 E-value: 1.81e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 175 IFLIIIPILGVTLTGLAL--------SVNPVFEKVF-HTYDHLNNIVdenlqgirVVKSYDREEHESRKFGRVseriyey 245
Cdd:PRK13657 160 LVLVVLGIVYTLITTLVMrktkdgqaAVEEHYHDLFaHVSDAIGNVS--------VVQSYNRIEAETQALRDI------- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 246 fckAEHVLAFNWPILN------------TCIygAMLIISwmgtkqIVGSHNNAAVGLTTGDLTALVTYAMQILMSLNMVS 313
Cdd:PRK13657 225 ---ADNLLAAQMPVLSwwalasvlnraaSTI--TMLAIL------VLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVV 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 314 MIIVMVVISRADAERICQVLNEVSTVRDNADPImDVPD--GSITFNDVSFRYDvgSERPVLDDINLTIASGSTIGIVGGT 391
Cdd:PRK13657 294 AFINQVFMAAPKLEEFFEVEDAVPDVRDPPGAI-DLGRvkGAVEFDDVSFSYD--NSRQGVEDVSFEAKPGQTVAIVGPT 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 392 GSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVAMVLQKNVLFAGTIADNIRWGNPNATDEDVRRVCKLAQA 471
Cdd:PRK13657 371 GAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQA 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 472 DGFIREFPKGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIAQRV 551
Cdd:PRK13657 451 HDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRL 530
|
410 420
....*....|....*....|....*...
gi 705456738 552 ASVQESDEIIVMDGGRILDRGTHDQLLQ 579
Cdd:PRK13657 531 STVRNADRILVFDNGRVVESGSFDELVA 558
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
19-591 |
3.71e-77 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 255.71 E-value: 3.71e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 19 RTLLKSLREYKKDTILAPTFVIVESVLEILIPTVMASMIDQGVAGGSMPAIWKFGLILLGCAVVSLFAGFMSGRYAAIAS 98
Cdd:PRK11176 14 RRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGFGKADRSVLKWMPLVVIGLMILRGITSFISSYCISWVS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 99 AGFAKNLRHDLFEKVQSFSFTNIDHFSTGSIITRITTDVTNIQYAFQMCIRVAVRAPLMVVVAWLFSFRISPSISMIFLI 178
Cdd:PRK11176 94 GKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 179 IIPILGVTLTGLALSVNPVFEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEHVLAFNWP 258
Cdd:PRK11176 174 IAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASSISDP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 259 ILntciygamliiswmgtkQIVGSHNNAAV-----------GLTTGDLTaLVTYAMQILM----SLNMVSmiivmvvisr 323
Cdd:PRK11176 254 II-----------------QLIASLALAFVlyaasfpsvmdTLTAGTIT-VVFSSMIALMrplkSLTNVN---------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 324 ADAER---ICQVLNEV---STVRDNADPIMDVPDGSITFNDVSFRYDvGSERPVLDDINLTIASGSTIGIVGGTGSAKSS 397
Cdd:PRK11176 306 AQFQRgmaACQTLFAIldlEQEKDEGKRVIERAKGDIEFRNVTFTYP-GKEVPALRNINFKIPAGKTVALVGRSGSGKST 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 398 LVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVAMVLQKNVLFAGTIADNIRWG-NPNATDEDVRRVCKLAQADGFIR 476
Cdd:PRK11176 385 IANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYArTEQYSREQIEEAARMAYAMDFIN 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 477 EFPKGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIAQRVASVQE 556
Cdd:PRK11176 465 KMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEK 544
|
570 580 590
....*....|....*....|....*....|....*
gi 705456738 557 SDEIIVMDGGRILDRGTHDQLLQTCDEYRSIYQSQ 591
Cdd:PRK11176 545 ADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
37-603 |
7.91e-75 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 249.24 E-value: 7.91e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 37 TFVIVESVLEILIPTVMASMIDqGVAGGSMPA---IWKFGLILLGCAVVSLFagfmsgRYAAI-----ASAGFAKNLRHD 108
Cdd:PRK10789 2 ALLIIIAMLQLIPPKVVGIIVD-GVTEQHMTTgqiLMWIGTMVLIAVVVYLL------RYVWRvllfgASYQLAVELRED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 109 LFEKV--QSFSFTnIDHfSTGSIITRITTDVTNIQYAFQMCIRVAVRAPLM-VVVAWLFSFRISPSISMIFLIIIPILGV 185
Cdd:PRK10789 75 FYRQLsrQHPEFY-LRH-RTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMgCAVLIVMSTQISWQLTLLALLPMPVMAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 186 TLTGLALSVNPVFEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEHVLAFNWPILNTCIY 265
Cdd:PRK10789 153 MIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 266 GAMLII----SWMgtkQIVGShnnaavgLTTGDLTALVTYAMqiLMSLNMVSMIIVMVVISRADA--ERICQVLNEVSTV 339
Cdd:PRK10789 233 MANLLAigggSWM---VVNGS-------LTLGQLTSFVMYLG--LMIWPMLALAWMFNIVERGSAaySRIRAMLAEAPVV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 340 RDNADPIMDVPdGSITFNDVSFRYDvGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRD 419
Cdd:PRK10789 301 KDGSEPVPEGR-GELDVNIRQFTYP-QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 420 VREYDLETLRDAVAMVLQKNVLFAGTIADNIRWGNPNATDEDVRRVCKLAQADGFIREFPKGYDTYIEEGGSNVSGGQRQ 499
Cdd:PRK10789 379 LTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQ 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 500 RLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIAQRVASVQESDEIIVMDGGRILDRGTHDQLLQ 579
Cdd:PRK10789 459 RISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQ 538
|
570 580
....*....|....*....|....
gi 705456738 580 TCDEYRSIYQSQtksQGEGSDDDE 603
Cdd:PRK10789 539 QSGWYRDMYRYQ---QLEAALDDA 559
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
354-591 |
3.52e-72 |
|
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: 231.61 E-value: 3.52e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDvGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVA 433
Cdd:cd03252 1 ITFEHVRFRYK-PDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 MVLQKNVLFAGTIADNIRWGNPNATDEDVRRVCKLAQADGFIREFPKGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKI 513
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 705456738 514 LILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIAQRVASVQESDEIIVMDGGRILDRGTHDQLLQTCDEYRSIYQSQ 591
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
44-592 |
1.33e-71 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 243.88 E-value: 1.33e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 44 VLEILIPTVMASMIDQGVAGGSMPAIWKFGLILLGCAVVSLFAGFMSGRYAAIASAGFAKNLRHDLFEKVQSFSFTNIDH 123
Cdd:TIGR01846 153 LFALVTPLLFQVVIDKVLVHRGLSTLSVLALAMLAVAIFEPALGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFES 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 124 FSTGSIITRITtDVTNIQYAFQMCIRVAVRAPLMVVVAWLFSFRISPSISMIFLIIIPILGVTLTGLALSVNPVFEKVFH 203
Cdd:TIGR01846 233 RRVGDTVARVR-ELEQIRNFLTGSALTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 204 TYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEHVLAFNWPILNTCIYGAMLIISWMGTKQIVGSH 283
Cdd:TIGR01846 312 RSAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGA 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 284 nnaavgLTTGDLTALVTYAMQIlmslnmVSMIIVMVVI------SRADAERICQVLNEVSTVRDNADPIMDVPDGSITFN 357
Cdd:TIGR01846 392 ------LSPGQLVAFNMLAGRV------TQPVLRLAQLwqdfqqTGIALERLGDILNSPTEPRSAGLAALPELRGAITFE 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 358 DVSFRYDVGSErPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVAMVLQ 437
Cdd:TIGR01846 460 NIRFRYAPDSP-EVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQ 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 438 KNVLFAGTIADNIRWGNPNATDEDVRRVCKLAQADGFIREFPKGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKILILD 517
Cdd:TIGR01846 539 ENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFD 618
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 705456738 518 DSTSAVDTKTDRLIRGAFKTEIPDTTKIIIAQRVASVQESDEIIVMDGGRILDRGTHDQLLQTCDEYRSIYQSQT 592
Cdd:TIGR01846 619 EATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQS 693
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
352-573 |
1.38e-70 |
|
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: 226.99 E-value: 1.38e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 352 GSITFNDVSFRYDVGSErPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDA 431
Cdd:cd03244 1 GDIEFKNVSLRYRPNLP-PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 432 VAMVLQKNVLFAGTIADNIrwgNPN--ATDEDVRRVCKLAQADGFIREFPKGYDTYIEEGGSNVSGGQRQRLCIARALLK 509
Cdd:cd03244 80 ISIIPQDPVLFSGTIRSNL---DPFgeYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 705456738 510 KPKILILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIAQRVASVQESDEIIVMDGGRILDRGT 573
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
354-567 |
1.02e-69 |
|
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: 222.64 E-value: 1.02e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDvGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVA 433
Cdd:cd03228 1 IEFKNVSFSYP-GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 MVLQKNVLFAGTIADNIrwgnpnatdedvrrvcklaqadgfirefpkgydtyieeggsnVSGGQRQRLCIARALLKKPKI 513
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 705456738 514 LILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIAQRVASVQESDEIIVMDGGR 567
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
352-568 |
2.01e-64 |
|
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: 210.91 E-value: 2.01e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 352 GSITFNDVSFRYDvGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDA 431
Cdd:cd03245 1 GRIEFRNVSFSYP-NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 432 VAMVLQKNVLFAGTIADNIRWGNPNATDEDVRRVCKLAQADGFIREFPKGYDTYIEEGGSNVSGGQRQRLCIARALLKKP 511
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 705456738 512 KILILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIAQRVASVQESDEIIVMDGGRI 568
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
267-585 |
3.61e-62 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 218.27 E-value: 3.61e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 267 AMLIISWMGTKQIVGShnnaavgLTTGDLTALVTYAMQILMSLNMVSMIIVMVVISRADAERICQVLN---EVSTVRDNA 343
Cdd:TIGR03796 391 SALILVVGGLRVMEGQ-------LTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEGDLNRLDDVLRnpvDPLLEEPEG 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 344 DPIMDVPD----GSITFNDVSFRYDVgSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRD 419
Cdd:TIGR03796 464 SAATSEPPrrlsGYVELRNITFGYSP-LEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIP 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 420 VREYDLETLRDAVAMVLQKNVLFAGTIADNIRWGNPNATDEDVRRVCKLAQADGFIREFPKGYDTYIEEGGSNVSGGQRQ 499
Cdd:TIGR03796 543 REEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQ 622
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 500 RLCIARALLKKPKILILDDSTSAVDTKTDRLI------RGAfkteipdtTKIIIAQRVASVQESDEIIVMDGGRILDRGT 573
Cdd:TIGR03796 623 RLEIARALVRNPSILILDEATSALDPETEKIIddnlrrRGC--------TCIIVAHRLSTIRDCDEIIVLERGKVVQRGT 694
|
330
....*....|..
gi 705456738 574 HDQLLQTCDEYR 585
Cdd:TIGR03796 695 HEELWAVGGAYA 706
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
293-591 |
3.84e-61 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 212.76 E-value: 3.84e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 293 GDLTALVTYA----MQILMSLNMVSMIIVMVVISradAERICQVLNEVSTVRDNADPIMDVPDGSITFNDVSFRYDvGSE 368
Cdd:PRK11160 277 GALIALFVFAalaaFEALMPVAGAFQHLGQVIAS---ARRINEITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYP-DQP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 369 RPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVAMVLQKNVLFAGTIAD 448
Cdd:PRK11160 353 QPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRD 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 449 NIRWGNPNATDEDVRRVC------KLAQADgfirefpKGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDSTSA 522
Cdd:PRK11160 433 NLLLAAPNASDEALIEVLqqvgleKLLEDD-------KGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEG 505
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 705456738 523 VDTKTDRLIRGAFKTEIPDTTKIIIAQRVASVQESDEIIVMDGGRILDRGTHDQLLQTCDEYRSIYQSQ 591
Cdd:PRK11160 506 LDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQRL 574
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
33-329 |
5.94e-61 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 204.20 E-value: 5.94e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 33 ILAPTFVIVESVLEILIPTVMASMIDQGVAGGSMPAIWKFGLILLGCAVVSLFAGFMSGRYAAIASAGFAKNLRHDLFEK 112
Cdd:cd18542 2 LLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 113 VQSFSFTNIDHFSTGSIITRITTDVTNIQYAFQMCIRVAVRAPLMVVVAWLFSFRISPSISMIFLIIIPILGVTLTGLAL 192
Cdd:cd18542 82 LQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 193 SVNPVFEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEHVLAFNWPILNTCIYGAMLIIS 272
Cdd:cd18542 162 KVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVL 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 705456738 273 WMGTKQIVGSHnnaavgLTTGDLTALVTYAMQILMSLNMVSMIIVMvvISRADA--ERI 329
Cdd:cd18542 242 WVGGYLVINGE------ITLGELVAFISYLWMLIWPVRQLGRLIND--MSRASAsaERI 292
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
351-568 |
1.96e-60 |
|
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: 200.39 E-value: 1.96e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 351 DGSITFNDVSFRYDVGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRD 430
Cdd:cd03248 9 KGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 431 AVAMVLQKNVLFAGTIADNIRWGNPNATDEDVRRVCKLAQADGFIREFPKGYDTYIEEGGSNVSGGQRQRLCIARALLKK 510
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 705456738 511 PKILILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIAQRVASVQESDEIIVMDGGRI 568
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
107-588 |
8.54e-60 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 211.91 E-value: 8.54e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 107 HDLFEKVQSFSFTNidhfSTGSIITRITtDVTNIQYAFQMCIRVAVRAPLMVVVAWLFSFRISPSISMIFLIIIPILGVT 186
Cdd:TIGR01193 237 KHLFELPMSFFSTR----RTGEIVSRFT-DASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYAVI 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 187 LTGLALSVNPVFEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRK----FGRVSERIYEYfCKAEHVLAFNWPILNT 262
Cdd:TIGR01193 312 IILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKidseFGDYLNKSFKY-QKADQGQQAIKAVTKL 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 263 CIygaMLIISWMGTkQIVGSHNnaavgLTTGDLtalVTYAMQILMSLNMVSMIIVMVviSRADAERICQV-LNEVSTV-- 339
Cdd:TIGR01193 391 IL---NVVILWTGA-YLVMRGK-----LTLGQL---ITFNALLSYFLTPLENIINLQ--PKLQAARVANNrLNEVYLVds 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 340 ---RDNADPIMDVPDGSITFNDVSFRYDVGSerPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVG 416
Cdd:TIGR01193 457 efiNKKKRTELNNLNGDIVINDVSYSYGYGS--NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLN 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 417 GRDVREYDLETLRDAVAMVLQKNVLFAGTIADNIRWGN-PNATDEDVRRVCKLAQADGFIREFPKGYDTYIEEGGSNVSG 495
Cdd:TIGR01193 535 GFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAkENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISG 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 496 GQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFkTEIPDTTKIIIAQRVASVQESDEIIVMDGGRILDRGTHD 575
Cdd:TIGR01193 615 GQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNL-LNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHD 693
|
490
....*....|...
gi 705456738 576 QLLQTCDEYRSIY 588
Cdd:TIGR01193 694 ELLDRNGFYASLI 706
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
18-591 |
1.44e-58 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 206.11 E-value: 1.44e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 18 IRTLLKSLREYKKDTILAPTFVIVESVLEILIPTVMASMIDQGVAGGSMPAIWKFGLIL------LGCAVVSLFAGFMSG 91
Cdd:PRK10790 11 LKRLLAYGSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDNMVAKGNLPLGLVAGLAAayvglqLLAAGLHYAQSLLFN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 92 RyaaiASAGFAKNLRHDLFEKVQSFSFTNIDHFSTGSIITRITTDVTNIQYAFQMCIRVAVRAPLMVVVAWLFSFRISPS 171
Cdd:PRK10790 91 R----AAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 172 ISMIFLIIIP-ILGVTLTGLALSVnPVFEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAE 250
Cdd:PRK10790 167 MALVAIMIFPaVLVVMVIYQRYST-PIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 251 HVLAFNW-PILNtcIYGAMLIIswmGTKQIVGSHNNAAVGLttGDLTALVTYAMQI---LMSLNMVSMIIVMVVISradA 326
Cdd:PRK10790 246 RLDGFLLrPLLS--LFSALILC---GLLMLFGFSASGTIEV--GVLYAFISYLGRLnepLIELTTQQSMLQQAVVA---G 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 327 ERICQVLNevSTVRDNADPIMDVPDGSITFNDVSFRYDvgSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLY 406
Cdd:PRK10790 316 ERVFELMD--GPRQQYGNDDRPLQSGRIDIDNVSFAYR--DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 407 DVSSGSLEVGGRDVREYDLETLRDAVAMVLQKNVLFAGTIADNIRWGNpNATDEDVRRVCKLAQADGFIREFPKGYDTYI 486
Cdd:PRK10790 392 PLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 487 EEGGSNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIAQRVASVQESDEIIVMDGG 566
Cdd:PRK10790 471 GEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRG 550
|
570 580
....*....|....*....|....*
gi 705456738 567 RILDRGTHDQLLQTCDEYRSIYQSQ 591
Cdd:PRK10790 551 QAVEQGTHQQLLAAQGRYWQMYQLQ 575
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
156-579 |
4.45e-57 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 202.04 E-value: 4.45e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 156 LMVVVAWLFSFRISPSISMIFLIIIPIL------GVTLTGLAlSVNPVFEKVF-HTYDHLNNIvdenlqgiRVVKSYDRE 228
Cdd:TIGR01192 144 LFLLIPTAFAMDWRLSIVLMVLGILYILiaklvmQRTKNGQA-AVEHHYHNVFkHVSDSISNV--------SVVHSYNRI 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 229 EHESRKFGRVSERIyeyfckaehvLAFNWPILN----------TCIYGAMLIISWMGTKQIVGSHnnaavgLTTGDLTAL 298
Cdd:TIGR01192 215 EAETSALKQFTNNL----------LSAQYPVLDwwalasglnrMASTISMMCILVIGTVLVIKGE------LSVGEVIAF 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 299 VTYAMQILMSLNMVSMIIVMVVISRADAERICQVLNEVSTVRDNAD-PIMDVPDGSITFNDVSFRYDVGSERpvLDDINL 377
Cdd:TIGR01192 279 IGFANLLIGRLDQMSGFITQIFEARAKLEDFFDLEDSVFQREEPADaPELPNVKGAVEFRHITFEFANSSQG--VFDVSF 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 378 TIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVAMVLQKNVLFAGTIADNIRWGNPNA 457
Cdd:TIGR01192 357 EAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGA 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 458 TDEDVRRVCKLAQADGFIREFPKGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKT 537
Cdd:TIGR01192 437 TDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDA 516
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 705456738 538 EIPDTTKIIIAQRVASVQESDEIIVMDGGRILDRGTHDQLLQ 579
Cdd:TIGR01192 517 LRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQ 558
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
12-580 |
6.98e-55 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 197.87 E-value: 6.98e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 12 ERPKHLIRTLLKSLREYKKD--TILAPTfvIVESVLEILIPTVMASMIDQGVAGGSMPAIWKFGLILLGCAVVS----LF 85
Cdd:TIGR03797 118 DKALGLRDLLRFALRGARRDllAILAMG--LLGTLLGMLVPIATGILIGTAIPDADRSLLVQIALALLAAAVGAaafqLA 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 86 AGFMSGRYAAIASAGFAKNLRHDLFEKVQSFsFTNidhFSTGSIITRITTdVTNIqyaFQMCIRVAVRAPLMVVVAwLFS 165
Cdd:TIGR03797 196 QSLAVLRLETRMDASLQAAVWDRLLRLPVSF-FRQ---YSTGDLASRAMG-ISQI---RRILSGSTLTTLLSGIFA-LLN 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 166 ----FRISPSISMIFLIIIPILGVTLTGLALSVNPVFEKVFHTYDHLNNIVDENLQGI---RVVKSYDREEHE-SRKFGR 237
Cdd:TIGR03797 267 lglmFYYSWKLALVAVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGIsklRVAGAENRAFARwAKLFSR 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 238 vSERIYEYFCKAEHVLA-FN--WPILntciygAMLIISWMGTKQIvgshnnAAVGLTTGDLTALVTYAMQILMSLNMVSM 314
Cdd:TIGR03797 347 -QRKLELSAQRIENLLTvFNavLPVL------TSAALFAAAISLL------GGAGLSLGSFLAFNTAFGSFSGAVTQLSN 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 315 IIVMVVISRADAERICQVLNEVSTVRDN-ADPimDVPDGSITFNDVSFRYDVGSeRPVLDDINLTIASGSTIGIVGGTGS 393
Cdd:TIGR03797 414 TLISILAVIPLWERAKPILEALPEVDEAkTDP--GKLSGAIEVDRVTFRYRPDG-PLILDDVSLQIEPGEFVAIVGPSGS 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 394 AKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVAMVLQKNVLFAGTIADNIRWGNPnATDEDVRRVCKLAQADG 473
Cdd:TIGR03797 491 GKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAP-LTLDEAWEAARMAGLAE 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 474 FIREFPKGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKTEipDTTKIIIAQRVAS 553
Cdd:TIGR03797 570 DIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL--KVTRIVIAHRLST 647
|
570 580
....*....|....*....|....*..
gi 705456738 554 VQESDEIIVMDGGRILDRGTHDQLLQT 580
Cdd:TIGR03797 648 IRNADRIYVLDAGRVVQQGTYDELMAR 674
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
44-563 |
2.95e-54 |
|
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: 192.89 E-value: 2.95e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 44 VLEILIPTVMASMIDQGVAGGSMPA-IWKFGLILLGCAVVSLFAGFMSGRYAAIASAGFAKNLRHDLFEKVQSFSFTNID 122
Cdd:TIGR02857 17 LLIIAQAWLLARVVDGLISAGEPLAeLLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 123 HFSTGSIITRITTDVTNI-----QYAFQMCIrvAVRAPLMVVVAWLFSFRISPSISMIFLIIIPILGVtLTG-LALSVNp 196
Cdd:TIGR02857 97 GRPSGELATLALEGVEALdgyfaRYLPQLVL--AVIVPLAILAAVFPQDWISGLILLLTAPLIPIFMI-LIGwAAQAAA- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 197 vfEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSEriyEYFCKAEHVL--AFnwpiLNTCIYGAMLIISWM 274
Cdd:TIGR02857 173 --RKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSE---EYRERTMRVLriAF----LSSAVLELFATLSVA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 275 GTKQIVGshnnaaVGLTTGDLT---ALVTY--AMQILMSLNMVSMIIVMVVISRADAERICQVLNEVSTVRDNADPIMDV 349
Cdd:TIGR02857 244 LVAVYIG------FRLLAGDLDlatGLFVLllAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAPRPLAGKAPVTAA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 350 PDGSITFNDVSFRYdvGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLR 429
Cdd:TIGR02857 318 PASSLEFSGVSVAY--PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWR 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 430 DAVAMVLQKNVLFAGTIADNIRWGNPNATDEDVRRVCKLAQADGFIREFPKGYDTYIEEGGSNVSGGQRQRLCIARALLK 509
Cdd:TIGR02857 396 DQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLR 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 705456738 510 KPKILILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIAQRVASVQESDEIIVM 563
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
33-329 |
4.85e-53 |
|
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: 183.14 E-value: 4.85e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 33 ILAPTFVIVESVLEILIPTVMASMIDQGVAGGSMPAIWKFGLILLGCAVVSLFAGFMSGRYAAIASAGFAKNLRHDLFEK 112
Cdd:cd07346 2 LLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 113 VQSFSFTNIDHFSTGSIITRITTDVTNIQYAFQMCIRVAVRAPLMVVVAWLFSFRISPSISMIFLIIIPILGVTLTGLAL 192
Cdd:cd07346 82 LQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 193 SVNPVFEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEHVLAFNWPILNTCIYGAMLIIS 272
Cdd:cd07346 162 RIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVL 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 705456738 273 WMGTKQIVGSHnnaavgLTTGDLTALVTYAMQILMSLNMVSMIIVMVVISRADAERI 329
Cdd:cd07346 242 LYGGYLVLQGS------LTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
80-596 |
1.48e-51 |
|
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: 191.70 E-value: 1.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 80 AVVSLFAGFMSGRYAAIASAG---FAKNLRHDLFEKVQSFSFTNIDHFSTGSIITRITTDVTNIQYAFQMCIRVAVRAPL 156
Cdd:TIGR00957 1012 GALGILQGFAVFGYSMAVSIGgiqASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLF 1091
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 157 MVVVAWLFSFRISPsismIFLIIIPILGVTLTGL---------------ALSVNPVfekvfhtYDHLNnivdENLQGIRV 221
Cdd:TIGR00957 1092 NVIGALIVILLATP----IAAVIIPPLGLLYFFVqrfyvassrqlkrleSVSRSPV-------YSHFN----ETLLGVSV 1156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 222 VKSYDREE---HESRKFGRVSERIYEYFCKAEHVLAFNWPILNTCI--YGAMLiiswmgtkQIVGSH--NNAAVGLTtgd 294
Cdd:TIGR00957 1157 IRAFEEQErfiHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIvlFAALF--------AVISRHslSAGLVGLS--- 1225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 295 ltalVTYAMQILMSLN-MVSMIIVM----VVISRadaericqvLNEVS--------TVRDNADPIMDVPDGSITFNDVSF 361
Cdd:TIGR00957 1226 ----VSYSLQVTFYLNwLVRMSSEMetniVAVER---------LKEYSetekeapwQIQETAPPSGWPPRGRVEFRNYCL 1292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 362 RYDVGSERpVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVAMVLQKNVL 441
Cdd:TIGR00957 1293 RYREDLDL-VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVL 1371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 442 FAGTIADNIrwgNP--NATDEDVRRVCKLAQADGFIREFPKGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDS 519
Cdd:TIGR00957 1372 FSGSLRMNL---DPfsQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEA 1448
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 705456738 520 TSAVDTKTDRLIRGAFKTEIPDTTKIIIAQRVASVQESDEIIVMDGGRILDRGTHDQLLQTcdeyRSIYQSQTKSQG 596
Cdd:TIGR00957 1449 TAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQ----RGIFYSMAKDAG 1521
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
351-573 |
1.55e-50 |
|
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: 173.37 E-value: 1.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 351 DGSITFNDVSFRYDVGSErPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRD 430
Cdd:cd03369 4 HGEIEVENLSVRYAPDLP-PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 431 AVAMVLQKNVLFAGTIADNIRWGNpNATDEDVRRVCKlaqadgfirefpkgydtyIEEGGSNVSGGQRQRLCIARALLKK 510
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLDPFD-EYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 705456738 511 PKILILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIAQRVASVQESDEIIVMDGGRILDRGT 573
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-593 |
1.60e-50 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 188.70 E-value: 1.60e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 18 IRTLLKSLREYKKDTILAPTFVIVESVLEILIPTVMASMIDQGVAGGSMPAIW-KFGLILLGCAVVSLFAGFMSGRYAAI 96
Cdd:PTZ00265 813 LRIVYREIFSYKKDVTIIALSILVAGGLYPVFALLYAKYVSTLFDFANLEANSnKYSLYILVIAIAMFISETLKNYYNNV 892
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 97 ASAGFAKNLRHDLFEKV--QSFSFTNIDHFSTGSIITRITTDVtniqyafqMCIRVAVRAPLMVVVAWLFSFRISPSISM 174
Cdd:PTZ00265 893 IGEKVEKTMKRRLFENIlyQEISFFDQDKHAPGLLSAHINRDV--------HLLKTGLVNNIVIFTHFIVLFLVSMVMSF 964
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 175 IFliiIPILGVTLTGLALsvnpVFEKVFHTYDHL--NNIVDE---NLQGIRVVKSYDREEHESRKFgRVSERIY------ 243
Cdd:PTZ00265 965 YF---CPIVAAVLTGTYF----IFMRVFAIRARLtaNKDVEKkeiNQPGTVFAYNSDDEIFKDPSF-LIQEAFYnmntvi 1036
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 244 -----EYFCK-AEHVLAFN------WPILNTCIYG----AMLIIS----WMG-------TKQIVGSHNNAAVGLTTGdlt 296
Cdd:PTZ00265 1037 iygleDYFCNlIEKAIDYSnkgqkrKTLVNSMLWGfsqsAQLFINsfayWFGsflirrgTILVDDFMKSLFTFLFTG--- 1113
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 297 alvTYAMQiLMSLNMVSMIivmvviSRADAERICQVLNEVST--VRDNADPIM---DVPDGSITFNDVSFRYDVGSERPV 371
Cdd:PTZ00265 1114 ---SYAGK-LMSLKGDSEN------AKLSFEKYYPLIIRKSNidVRDNGGIRIknkNDIKGKIEIMDVNFRYISRPNVPI 1183
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 372 LDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDV------------------------------------------- 408
Cdd:PTZ00265 1184 YKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltke 1263
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 409 -----------SSGSLEVGGRDVREYDLETLRDAVAMVLQKNVLFAGTIADNIRWGNPNATDEDVRRVCKLAQADGFIRE 477
Cdd:PTZ00265 1264 ggsgedstvfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIES 1343
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 478 FPKGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRgafKTEI-----PDTTKIIIAQRVA 552
Cdd:PTZ00265 1344 LPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIE---KTIVdikdkADKTIITIAHRIA 1420
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 705456738 553 SVQESDEIIVMD-----GGRILDRGTHDQLLQTCDeyrSIYQSQTK 593
Cdd:PTZ00265 1421 SIKRSDKIVVFNnpdrtGSFVQAHGTHEELLSVQD---GVYKKYVK 1463
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
370-579 |
1.30e-47 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 175.80 E-value: 1.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 370 PVLDDINLTIASGSTIGIVGGTGSAKSSLVQLI----PrlYdvsSGSLEVGGRDVREYDLETLRDAVAMVLQKNVLFAGT 445
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALlgflP--Y---QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 446 IADNIRWGNPNATDEDVRRVCKLAQADGFIREFPKGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDSTSAVDT 525
Cdd:PRK11174 439 LRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 705456738 526 KTDRLIRGAFKTEIPDTTKIIIAQRVASVQESDEIIVMDGGRILDRGTHDQLLQ 579
Cdd:PRK11174 519 HSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQ 572
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
322-579 |
4.20e-46 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 170.99 E-value: 4.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 322 SRADAERICQVLNEVSTvrdnADPIMDVPD--GSITFNDVSFRYDvGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLV 399
Cdd:TIGR01842 287 ARQAYKRLNELLANYPS----RDPAMPLPEpeGHLSVENVTIVPP-GGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLA 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 400 QLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVAMVLQKNVLFAGTIADNI-RWGNpNATDEDVRRVCKLAQADGFIREF 478
Cdd:TIGR01842 362 RLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIaRFGE-NADPEKIIEAAKLAGVHELILRL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 479 PKGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKT-EIPDTTKIIIAQRVASVQES 557
Cdd:TIGR01842 441 PDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKAlKARGITVVVITHRPSLLGCV 520
|
250 260
....*....|....*....|..
gi 705456738 558 DEIIVMDGGRILDRGTHDQLLQ 579
Cdd:TIGR01842 521 DKILVLQDGRIARFGERDEVLA 542
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
350-579 |
7.17e-46 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 170.31 E-value: 7.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 350 PDGSITFNDVSFRYDvGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLR 429
Cdd:COG4618 327 PKGRLSVENLTVVPP-GSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELG 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 430 DAVAMVLQKNVLFAGTIADNI-RWGNPNatDEDVRRVCKLAQADGFIREFPKGYDTYIEEGGSNVSGGQRQRLCIARALL 508
Cdd:COG4618 406 RHIGYLPQDVELFDGTIAENIaRFGDAD--PEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALY 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 705456738 509 KKPKILILDDSTSAVDTKTD----RLIRGAfKTEipDTTKIIIAQRVASVQESDEIIVMDGGRILDRGTHDQLLQ 579
Cdd:COG4618 484 GDPRLVVLDEPNSNLDDEGEaalaAAIRAL-KAR--GATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
94-550 |
6.91e-45 |
|
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: 167.15 E-value: 6.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 94 AAIASAGfakNLRHDLFEKVQSFSFTNIDHFSTGSIITRITTDVTNIQyafQMCIRV---AVRAPLMVVVAWLFSFRISP 170
Cdd:TIGR02868 80 AALRSLG---ALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQ---DLYVRVivpAGVALVVGAAAVAAIAVLSV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 171 SISMIFLIIIPILGVTLTGLALSVNPVFEK-VFHTYDHLNNIVDENLQGI----------RVVKSYDREEHESRKFGRVS 239
Cdd:TIGR02868 154 PAALILAAGLLLAGFVAPLVSLRAARAAEQaLARLRGELAAQLTDALDGAaelvasgalpAALAQVEEADRELTRAERRA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 240 ERiyeyfckAEHVLAfnwpILNTCIYGAMLIIS-WMGTKQiVGSHNNAAVGLTTGDLTAL-VTYAMQILmslnmvSMIIV 317
Cdd:TIGR02868 234 AA-------ATALGA----ALTLLAAGLAVLGAlWAGGPA-VADGRLAPVTLAVLVLLPLaAFEAFAAL------PAAAQ 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 318 MVVISRADAERICQVLNEVSTVRDNADPI-MDVPDG--SITFNDVSFRYDVGSerPVLDDINLTIASGSTIGIVGGTGSA 394
Cdd:TIGR02868 296 QLTRVRAAAERIVEVLDAAGPVAEGSAPAaGAVGLGkpTLELRDLSAGYPGAP--PVLDGVSLDLPPGERVAILGPSGSG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 395 KSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVAMVLQKNVLFAGTIADNIRWGNPNATDEDVRRVCKLAQADGF 474
Cdd:TIGR02868 374 KSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADW 453
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 705456738 475 IREFPKGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKT-DRLIRGAFKTEiPDTTKIIIAQR 550
Cdd:TIGR02868 454 LRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETaDELLEDLLAAL-SGRTVVLITHH 529
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-578 |
2.38e-44 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 170.16 E-value: 2.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 32 TILAPTFVIVEsVLEILIPTVMASMIDQGVAGGSMPAIWKFGLILLGCAVVSLFagfMSGRYAAIASAGFAKNLRHD--- 108
Cdd:PLN03232 915 MILLVCYLTTE-VLRVSSSTWLSIWTDQSTPKSYSPGFYIVVYALLGFGQVAVT---FTNSFWLISSSLHAAKRLHDaml 990
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 109 --LFEKVQSFSFTNidhfSTGSIITRITTDVTNIQYafqmciRVAVRAPLMVVVAW--LFSFRISPSISMIFL-IIIPIL 183
Cdd:PLN03232 991 nsILRAPMLFFHTN----PTGRVINRFSKDIGDIDR------NVANLMNMFMNQLWqlLSTFALIGTVSTISLwAIMPLL 1060
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 184 GvtltgLALSVNPVFEKVFHTYDHLNNIV--------DENLQG---IRVVKSYDREEHESRKFGRVSERiyeyFCKAEhV 252
Cdd:PLN03232 1061 I-----LFYAAYLYYQSTSREVRRLDSVTrspiyaqfGEALNGlssIRAYKAYDRMAKINGKSMDNNIR----FTLAN-T 1130
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 253 LAFNWPILNTCIYGAMLIisWMGTKQIV---GSHNNAAVGLTTGDLtaLVTYAMQILMSLNMVSMIIVMVVISRADAERI 329
Cdd:PLN03232 1131 SSNRWLTIRLETLGGVMI--WLTATFAVlrnGNAENQAGFASTMGL--LLSYTLNITTLLSGVLRQASKAENSLNSVERV 1206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 330 CQVLN---EVSTVRDNADPIMDVP-DGSITFNDVSFRYDVGSErPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRL 405
Cdd:PLN03232 1207 GNYIDlpsEATAIIENNRPVSGWPsRGSIKFEDVHLRYRPGLP-PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRI 1285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 406 YDVSSGSLEVGGRDVREYDLETLRDAVAMVLQKNVLFAGTIADNIrwgNPNA--TDEDVRRVCKLAQADGFIREFPKGYD 483
Cdd:PLN03232 1286 VELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI---DPFSehNDADLWEALERAHIKDVIDRNPFGLD 1362
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 484 TYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIAQRVASVQESDEIIVM 563
Cdd:PLN03232 1363 AEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVL 1442
|
570
....*....|....*
gi 705456738 564 DGGRILDRGTHDQLL 578
Cdd:PLN03232 1443 SSGQVLEYDSPQELL 1457
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
358-568 |
4.85e-43 |
|
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: 151.99 E-value: 4.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 358 DVSFRYDvGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVAMVLQ 437
Cdd:cd03246 5 NVSFRYP-GAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 438 KNVLFAGTIADNIrwgnpnatdedvrrvcklaqadgfirefpkgydtyieeggsnVSGGQRQRLCIARALLKKPKILILD 517
Cdd:cd03246 84 DDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 705456738 518 DSTSAVDTKTDRLIRGAFK-TEIPDTTKIIIAQRVASVQESDEIIVMDGGRI 568
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAaLKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
282-579 |
2.15e-42 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 164.53 E-value: 2.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 282 SHNNAAVGLTTGdltALVTYAMQILMSLNMVSMIIVMVVISRADAERI---CQVLNEVSTVRDNADPIMDVPD-GSITFN 357
Cdd:PLN03130 1165 AENQAAFASTMG---LLLSYALNITSLLTAVLRLASLAENSLNAVERVgtyIDLPSEAPLVIENNRPPPGWPSsGSIKFE 1241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 358 DVSFRYdvgseR----PVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVA 433
Cdd:PLN03130 1242 DVVLRY-----RpelpPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLG 1316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 MVLQKNVLFAGTIADNIRWGNPNaTDEDVRRVCKLAQADGFIREFPKGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKI 513
Cdd:PLN03130 1317 IIPQAPVLFSGTVRFNLDPFNEH-NDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKI 1395
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 705456738 514 LILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIAQRVASVQESDEIIVMDGGRILDRGTHDQLLQ 579
Cdd:PLN03130 1396 LVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLS 1461
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
352-578 |
2.18e-42 |
|
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: 153.14 E-value: 2.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 352 GSITFNDVSFRYDvGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDA 431
Cdd:cd03288 18 GEIKIHDLCVRYE-NNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 432 VAMVLQKNVLFAGTIADNIrwgNP--NATDEDVRRVCKLAQADGFIREFPKGYDTYIEEGGSNVSGGQRQRLCIARALLK 509
Cdd:cd03288 97 LSIILQDPILFSGSIRFNL---DPecKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVR 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 705456738 510 KPKILILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIAQRVASVQESDEIIVMDGGRILDRGTHDQLL 578
Cdd:cd03288 174 KSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLL 242
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
33-329 |
6.03e-42 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 153.05 E-value: 6.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 33 ILAPTFVIVESVLEILIPTVMASMID----QGVAGGSMPAIWKFGLILLGCAVVSLFAGFMSGRYAAIASAGFAKNLRHD 108
Cdd:cd18563 2 ILGFLLMLLGTALGLVPPYLTKILIDdvliQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 109 LFEKVQSFSFTNIDHFSTGSIITRITTDVTNIQYAFQMCIRVAVRAPLMVVVAWLFSFRISPSISMIFLIIIPILGVTLT 188
Cdd:cd18563 82 LYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 189 GLALSVNPVFEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEHVLAFNWPILNTCIYGAM 268
Cdd:cd18563 162 FFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLGT 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 705456738 269 LIISWMGTKQIVGSHnnaavgLTTGDLTALVTYAMQILMSLNMVSMIIVMVVISRADAERI 329
Cdd:cd18563 242 LIVWYFGGRQVLSGT------MTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
33-329 |
2.26e-41 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 151.42 E-value: 2.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 33 ILAPTFVIVESVLEILIPTVMASMIDQGVAGGSMPAIWKFGLILLGCAVVSLFAGFMSGRYAAIASAGFAKNLRHDLFEK 112
Cdd:cd18552 2 ALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 113 VQSFSFTNIDHFSTGSIITRITTDVTNIQYAFQMCIRVAVRAPLMVV--VAWLFSfrISPSISMIFLIIIPILGVTLTGL 190
Cdd:cd18552 82 LLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIglLGVLFY--LDWKLTLIALVVLPLAALPIRRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 191 ALSVNPVFEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEHVLAFNWPILNTCIYGAMLI 270
Cdd:cd18552 160 GKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIAL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 705456738 271 ISWMGTKQIVGShnnaavGLTTGDLTALVTYAMQILMSLNMVSMIIVMVVISRADAERI 329
Cdd:cd18552 240 VLWYGGYQVISG------ELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
354-567 |
1.52e-40 |
|
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: 146.46 E-value: 1.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDVGSER--PVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRdvreydletlrda 431
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 432 VAMVLQKNVLFAGTIADNIRWGNPnaTDED----VRRVCKLaQADgfIREFPKGYDTYIEEGGSNVSGGQRQRLCIARAL 507
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKP--FDEEryekVIKACAL-EPD--LEILPDGDLTEIGEKGINLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 705456738 508 LKKPKILILDDSTSAVDTKT-----DRLIRGAFKTeipDTTKIIIAQRVASVQESDEIIVMDGGR 567
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVgrhifENCILGLLLN---NKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
210-602 |
1.57e-40 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 158.65 E-value: 1.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 210 NIVDENLQGIRVVKSYDREEHESRKFGrVSERIY-EYFCKAEHVLAFNWPILNTCIYGAMLIISWMGTKQIVGSHNNAAv 288
Cdd:PTZ00265 237 SIIEEALVGIRTVVSYCGEKTILKKFN-LSEKLYsKYILKANFMESLHIGMINGFILASYAFGFWYGTRIIISDLSNQQ- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 289 glTTGDL--TALVTYAMQILMSLNMVSMI---IVMVVISRADAERICQVLNEVSTVRDNADPiMDVPD-GSITFNDVSFR 362
Cdd:PTZ00265 315 --PNNDFhgGSVISILLGVLISMFMLTIIlpnITEYMKSLEATNSLYEIINRKPLVENNDDG-KKLKDiKKIQFKNVRFH 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 363 YDVGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVG-GRDVREYDLETLRDAVAMVLQKNVL 441
Cdd:PTZ00265 392 YDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKWWRSKIGVVSQDPLL 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 442 FAGTIADNIRW------------------GNPNATDEDVRRVCKLAQADG------------------------------ 473
Cdd:PTZ00265 472 FSNSIKNNIKYslyslkdlealsnyynedGNDSQENKNKRNSCRAKCAGDlndmsnttdsneliemrknyqtikdsevvd 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 474 ---------FIREFPKGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKTEIPDTTK 544
Cdd:PTZ00265 552 vskkvlihdFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENR 631
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 545 --IIIAQRVASVQESDEIIVMDGGRILDRGTHDQLLQTCDEYRSIYQSQTKSQGEGSDDD 602
Cdd:PTZ00265 632 itIIIAHRLSTIRYANTIFVLSNRERGSTVDVDIIGEDPTKDNKENNNKNNKDDNNNNNN 691
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
354-578 |
8.07e-39 |
|
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: 142.47 E-value: 8.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDvgSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVA 433
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 MVLQ--KNVLFAGTIADNIRWG------NPNATDEDVRRVCKLAQADGFIREFPkgydtyieeggSNVSGGQRQRLCIAR 505
Cdd:COG1122 79 LVFQnpDDQLFAPTVEEDVAFGpenlglPREEIRERVEEALELVGLEHLADRPP-----------HELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 705456738 506 ALLKKPKILILDDSTSAVDTKTDRLIRGAFKtEIPD--TTKIIIAQRVASVQE-SDEIIVMDGGRILDRGTHDQLL 578
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLK-RLNKegKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVF 222
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
33-329 |
1.51e-38 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 143.70 E-value: 1.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 33 ILAPTFVIVESVLEILIPTVMASMIDQ------GVAGGSMPAIWKFGLILLGCAVVSLFAGFMSGRYAAIASAGFAKNLR 106
Cdd:cd18547 2 ILVIILAIISTLLSVLGPYLLGKAIDLiieglgGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 107 HDLFEKVQSFSFTNIDHFSTGSIITRITTDVTNIQYAFQMCIRVAVRAPLMVVVAWLFSFRISPSISMIFLIIIPILGVT 186
Cdd:cd18547 82 KDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 187 LTGLALSVNPVFEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEHVLAFNWPILN----- 261
Cdd:cd18547 162 TKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNfinnl 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 705456738 262 ----TCIYGAMLIISwmGTkqivgshnnaavgLTTGDLTALVTYAMQILMSLNMVSMIIVMVVISRADAERI 329
Cdd:cd18547 242 gyvlVAVVGGLLVIN--GA-------------LTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
260-596 |
3.83e-38 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 151.47 E-value: 3.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 260 LNTCIYGAMLIISWMGTKQIVGSHNNAAVGL-------TTGDLTALVTyaMQILMSLNMVSMIIVMVVISRADAERICQV 332
Cdd:PTZ00243 1191 LSNIVVTVIALIGVIGTMLRATSQEIGLVSLsltmamqTTATLNWLVR--QVATVEADMNSVERLLYYTDEVPHEDMPEL 1268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 333 LNEVST---------------VRDNADPIMDVPD----GSITFNDVSFRYDVGseRP-VLDDINLTIASGSTIGIVGGTG 392
Cdd:PTZ00243 1269 DEEVDAlerrtgmaadvtgtvVIEPASPTSAAPHpvqaGSLVFEGVQMRYREG--LPlVLRGVSFRIAPREKVGIVGRTG 1346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 393 SAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVAMVLQKNVLFAGTIADNIrwgNP--NATDEDVRRVCKLAQ 470
Cdd:PTZ00243 1347 SGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV---DPflEASSAEVWAALELVG 1423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 471 ADGFIREFPKGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKILIL-DDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIAQ 549
Cdd:PTZ00243 1424 LRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAH 1503
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 705456738 550 RVASVQESDEIIVMDGGRILDRGTHDQLLQTCDeyrSIYQSQTKSQG 596
Cdd:PTZ00243 1504 RLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQ---SIFHSMVEALG 1547
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
33-329 |
1.02e-37 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 141.39 E-value: 1.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 33 ILAPTFVIVESVLEILIPTVMASMIDQGVAGG-SMPAIWKFGLILLGCAVVSLFAGFMSGRYAAIASAGFAKNLRHDLFE 111
Cdd:cd18541 2 LLGILFLILVDLLQLLIPRIIGRAIDALTAGTlTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 112 KVQSFSFTNIDHFSTGSIITRITTDVTNIQYAFQMCIRVAVRAPLMVVVAWLFSFRISPSISMIFLIIIPILGVTLTGLA 191
Cdd:cd18541 82 HLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 192 LSVNPVFEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEHVLAFNWPILNTCIYGAMLII 271
Cdd:cd18541 162 KKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIV 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 705456738 272 SWMGTKQIV-GShnnaavgLTTGDLTALVTYAMQILMSLNMVSMIIVMVVISRADAERI 329
Cdd:cd18541 242 LWYGGRLVIrGT-------ITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
33-329 |
2.07e-36 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 137.60 E-value: 2.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 33 ILAPTFVIVESVLEILIPTVMASMIDQGVAGGSMPAIWKFGLILLGCAVVSLFAGFMSGRYAAIASAGFAKNLRHDLFEK 112
Cdd:cd18545 3 LLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 113 VQSFSFTNIDHFSTGSIITRITTDVTNIQYAFQMCIRVAVRAPLMVVVAWLFSFRISPSISMIFLIIIPILGVTLTGLAL 192
Cdd:cd18545 83 LQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 193 SVNPVFEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEHVLAFNWPILNTCIYGAMLIIS 272
Cdd:cd18545 163 RARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALVY 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 705456738 273 WMGTKQIVGSHnnaavgLTTGDLTALVTYAMQILMSLNMVSMIIVMVVISRADAERI 329
Cdd:cd18545 243 WYGGKLVLGGA------ITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
354-568 |
4.59e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 134.17 E-value: 4.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDvgsERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVA 433
Cdd:COG4619 1 LELEGLSFRVG---GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 MVLQKNVLFAGTIADNI----RWGNPNATDEDVRRVckLAQADgfireFPKGY-DTYIEEggsnVSGGQRQRLCIARALL 508
Cdd:COG4619 78 YVPQEPALWGGTVRDNLpfpfQLRERKFDRERALEL--LERLG-----LPPDIlDKPVER----LSGGERQRLALIRALL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 705456738 509 KKPKILILDDSTSAVDTKTDRLIRGAFKTEI--PDTTKIII------AQRVAsvqesDEIIVMDGGRI 568
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVshdpeqIERVA-----DRVLTLEAGRL 209
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
32-329 |
1.70e-35 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 135.30 E-value: 1.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 32 TILAPTFVIVESVLEILIPTVMASMIDQGVAGGSMPAIWKFGLILLGCAVVSLFAGFMSGRYAAIASAGFAKNLRHDLFE 111
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 112 KVQSFSFTNIDHFSTGSIITRITTDVTNIQYAFQMCIRVAVRApLMVVVAWLFSFRISPSISMIFLIIIPILGVTLTGLA 191
Cdd:cd18543 81 HLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPFLLGNL-LTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 192 LSVNPVFEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEHVLAFNWPILNTCIYGAMLII 271
Cdd:cd18543 160 RRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 705456738 272 SWMGTKQIVGSHnnaavgLTTGDLTALVTYAMQILMSLNMVSMIIVMVVISRADAERI 329
Cdd:cd18543 240 LALGGWLVANGS------LTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
354-577 |
1.92e-35 |
|
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: 133.07 E-value: 1.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDvgsERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDV-----SSGSLEVGGRDVRE--YDLE 426
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDldVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 427 TLRDAVAMVLQKNVLFAGTIADNIRWG-------NPNATDEDVRRVCKLAQADGfirefpKGYDtyiEEGGSNVSGGQRQ 499
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAALWD------EVKD---RLHALGLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 500 RLCIARALLKKPKILILDDSTSAVD----TKTDRLIRgafktEIPDTTKIII-------AQRVAsvqesDEIIVMDGGRI 568
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDpistAKIEELIA-----ELKKEYTIVIvthnmqqAARVA-----DRTAFLLNGRL 218
|
....*....
gi 705456738 569 LDRGTHDQL 577
Cdd:cd03260 219 VEFGPTEQI 227
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
38-329 |
3.57e-35 |
|
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: 134.23 E-value: 3.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 38 FVIVESVLEILIPTVMASMIDQGVAGGSMPAIWKFGLILLGCAVVSLFAGFMsgRYAAIASAG--FAKNLRHDLFEKV-- 113
Cdd:cd18557 4 FLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFV--RYYLFNIAGerIVARLRRDLFSSLlr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 114 QSFSFtnIDHFSTGSIITRITTDVTNIQYAFQMCIRVAVRAPLMVVVAWLFSFRISPSISMIFLIIIPILGVTLTGLALS 193
Cdd:cd18557 82 QEIAF--FDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 194 VNPVFEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEHVLAFNWPILNTCIYGAMLIISW 273
Cdd:cd18557 160 IRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLW 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 705456738 274 MGTKQIVGSHnnaavgLTTGDLTALVTYAMQILMSLNMVSMIIVMVVISRADAERI 329
Cdd:cd18557 240 YGGYLVLSGQ------LTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
354-572 |
3.63e-35 |
|
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: 130.51 E-value: 3.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDvGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDlETLRDAVA 433
Cdd:cd03247 1 LSINNVSFSYP-EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 MVLQKNVLFAGTIADNIrwgnpnatdedvrrvcklaqadgfirefpkgydtyieegGSNVSGGQRQRLCIARALLKKPKI 513
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 705456738 514 LILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIAQRVASVQESDEIIVMDGGRILDRG 572
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
8-602 |
5.46e-35 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 141.65 E-value: 5.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 8 TIEEERPKH-LIRTLLKSLreyKKDTILAPTFVIVESVLEILIPTVMASMIDQGVAGGsmPA----IWKFgLILLGCavv 82
Cdd:PLN03232 281 TEESRRPKPwLLRALNNSL---GGRFWLGGIFKIGHDLSQFVGPVILSHLLQSMQEGD--PAwvgyVYAF-LIFFGV--- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 83 sLFAGFMSGRY-AAIASAGFakNLRHDL----FEKVQSFSFTNIDHFSTGSIITRITTDVTNIQyafQMCIRV--AVRAP 155
Cdd:PLN03232 352 -TFGVLCESQYfQNVGRVGF--RLRSTLvaaiFHKSLRLTHEARKNFASGKVTNMITTDANALQ---QIAEQLhgLWSAP 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 156 LMVVVAWLFSFR----ISPSISMIFLIIIPILGVTLTglalSVNPVFEKVFHTYDHLNNIVDENLQGIRVVKSYDREEH- 230
Cdd:PLN03232 426 FRIIVSMVLLYQqlgvASLFGSLILFLLIPLQTLIVR----KMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSf 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 231 ESRKFGRVSERIyEYFCKAEHVLAFNWPILNTcIYGAMLIISWmGTKQIVGSHNNAAVGLTTGDLTALVTYamqilmSLN 310
Cdd:PLN03232 502 ESRIQGIRNEEL-SWFRKAQLLSAFNSFILNS-IPVVVTLVSF-GVFVLLGGDLTPARAFTSLSLFAVLRS------PLN 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 311 MVSMIIVMVVISRADAERICQV-LNEVSTVRDNadPIMDVPDGSITFNDVSFRYDVGSERPVLDDINLTIASGSTIGIVG 389
Cdd:PLN03232 573 MLPNLLSQVVNANVSLQRIEELlLSEERILAQN--PPLQPGAPAISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVG 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 390 GTGSAKSSLVqliprlydvssgSLEVGGRDVREYDLETLRDAVAMVLQKNVLFAGTIADNIRWGNPNATDEDVRRVCKLA 469
Cdd:PLN03232 651 GTGEGKTSLI------------SAMLGELSHAETSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTA 718
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 470 -QADgfIREFPkGYD-TYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTDR-LIRGAFKTEIPDTTKII 546
Cdd:PLN03232 719 lQHD--LDLLP-GRDlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHqVFDSCMKDELKGKTRVL 795
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 705456738 547 IAQRVASVQESDEIIVMDGGRILDRGTHDQLLQTCDEYRSIYQSQTK---SQGEGSDDD 602
Cdd:PLN03232 796 VTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGKmdaTQEVNTNDE 854
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
354-572 |
1.11e-34 |
|
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: 131.09 E-value: 1.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDVG-SERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRD-- 430
Cdd:cd03257 2 LEVKNLSVSFPTGgGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 431 -AVAMVLQK-----NVLFagTIADNIR-----WGNPNATDEDVRRVCKLA----QADGFIREFPkgydtyieeggSNVSG 495
Cdd:cd03257 82 kEIQMVFQDpmsslNPRM--TIGEQIAeplriHGKLSKKEARKEAVLLLLvgvgLPEEVLNRYP-----------HELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 496 GQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFK--TEIPDTTKIIIAQRVASVQE-SDEIIVMDGGRILDRG 572
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKklQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
309-579 |
1.39e-34 |
|
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: 137.34 E-value: 1.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 309 LNMVSMIIVM---VVISRADAERI---CQVLNEVSTVRDNADPIMDVPDGS---ITFNDVSFRYDVGS--ERPVLDDINL 377
Cdd:COG1123 207 AEIADRVVVMddgRIVEDGPPEEIlaaPQALAAVPRLGAARGRAAPAAAAAeplLEVRNLSKRYPVRGkgGVRAVDDVSL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 378 TIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREY---DLETLRDAVAMVLQkNV---LFAG-TIADNI 450
Cdd:COG1123 287 TLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrSLRELRRRVQMVFQ-DPyssLNPRmTVGDII 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 451 -------RWGNPNATDEDVRRVCKL-----AQADGFIREFpkgydtyieeggsnvSGGQRQRLCIARALLKKPKILILDD 518
Cdd:COG1123 366 aeplrlhGLLSRAERRERVAELLERvglppDLADRYPHEL---------------SGGQRQRVAIARALALEPKLLILDE 430
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 705456738 519 STSAVDTKTDRLIRGAFKT--EIPDTTKIIIAQRVASVQE-SDEIIVMDGGRILDRGTHDQLLQ 579
Cdd:COG1123 431 PTSALDVSVQAQILNLLRDlqRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
372-521 |
3.39e-34 |
|
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: 126.99 E-value: 3.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 372 LDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVAMVLQKNVLFAG-TIADNI 450
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 705456738 451 RWGnpnATDEDVRRVCKLAQADGFIREFPKGY--DTYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDSTS 521
Cdd:pfam00005 81 RLG---LLLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
38-329 |
3.62e-34 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 131.50 E-value: 3.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 38 FVIVESVLEILIPTVMASMIDQ-GVAGGSMPAIWKFGLILLGCAVVSLFAGFMSGRYAAIASAGFAKNLRHDLFEKVQSF 116
Cdd:cd18778 7 CALLSTLLGLVPPWLIRELVDLvTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLYDKLQRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 117 SFTNIDHFSTGSIITRITTDVTNIQYAFQMCIRVAVRAPLMVVVAWLFSFRISPSISMIFLIIIPILGVTLTGLALSVNP 196
Cdd:cd18778 87 SLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 197 VFEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEHVLAFNWPILNTCIYGAMLIISWMGT 276
Cdd:cd18778 167 RYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVLVLGFGG 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 705456738 277 KQIVGSHnnaavgLTTGDLTALVTYAMQILMSLNMVSMIIVMVVISRADAERI 329
Cdd:cd18778 247 RLVLAGE------LTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
354-579 |
1.25e-33 |
|
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: 134.65 E-value: 1.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDvGSERPVLDDINLTIASGSTIGIVGGTGSAKS----SLVQLIPRLYDVSsGSLEVGGRDVREYDLETLR 429
Cdd:COG1123 5 LEVRDLSVRYP-GGDVPAVDGVSLTIAPGETVALVGESGSGKStlalALMGLLPHGGRIS-GEVLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 430 DAVAMVLQ--KNVLFAGTIADNIRWG--NPNATDEDVR-RVCKLAQADGFirefPKGYDTYIEEggsnVSGGQRQRLCIA 504
Cdd:COG1123 83 RRIGMVFQdpMTQLNPVTVGDQIAEAleNLGLSRAEARaRVLELLEAVGL----ERRLDRYPHQ----LSGGQRQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 705456738 505 RALLKKPKILILDDSTSAVDTKTDRLIRGAFK--TEIPDTTKIIIAQRVASVQE-SDEIIVMDGGRILDRGTHDQLLQ 579
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
356-567 |
2.68e-33 |
|
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: 126.43 E-value: 2.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 356 FNDVSFRYDvGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVAMV 435
Cdd:cd03225 2 LKNLSFSYP-DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 436 LQ--KNVLFAGTIADNIRWGNPN---ATDEDVRRVCKLAQADGfIREFPKgYDTYieeggsNVSGGQRQRLCIARALLKK 510
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVAFGLENlglPEEEIEERVEEALELVG-LEGLRD-RSPF------TLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 511 PKILILDDSTSAVDTKTDRLIRGAFKtEIPD--TTKIIIAQRVASVQE-SDEIIVMDGGR 567
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLK-KLKAegKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
354-579 |
4.92e-33 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 126.72 E-value: 4.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDvgsERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREyDLETLRDAVA 433
Cdd:COG1131 1 IEVRGLTKRYG---DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 MVLQKNVLFAG-TIADNIRW-----GNPNAT-DEDVRRVCKLAQADGFIREFPKGYdtyieeggsnvSGGQRQRLCIARA 506
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRFfarlyGLPRKEaRERIDELLELFGLTDAADRKVGTL-----------SGGMKQRLGLALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 507 LLKKPKILILDDSTSAVDTKTDRLIRGAFKtEIPDTTKIII--------AQRVAsvqesDEIIVMDGGRILDRGTHDQLL 578
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLR-ELAAEGKTVLlsthyleeAERLC-----DRVAIIDKGRIVADGTPDELK 219
|
.
gi 705456738 579 Q 579
Cdd:COG1131 220 A 220
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
33-329 |
7.19e-33 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 127.89 E-value: 7.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 33 ILAPTFVIVESVLEILIPTVMASMIDQGVAGGS--MPAIWKFGLILLGCAVVSLFAGFMSGRYAAIASAGFAKNLRHDLF 110
Cdd:cd18544 2 ILALLLLLLATALELLGPLLIKRAIDDYIVPGQgdLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 111 EKVQSFSFTNIDHFSTGSIITRITTDVTNIQYAFQMCIRVAVRAPLMVVVAWLFSFRISPSISMIFLIIIPILGVTLTGL 190
Cdd:cd18544 82 SHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 191 ALSVNPVFEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEHVLAFNWPILNTCIYGAMLI 270
Cdd:cd18544 162 RKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALAL 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 705456738 271 ISWMGTKQIVGShnnaavGLTTGDLTALVTYAMQILMSLNMVSMIIVMVVISRADAERI 329
Cdd:cd18544 242 VLWYGGGQVLSG------AVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
354-580 |
1.21e-32 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 125.69 E-value: 1.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDVGSER-PVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAV 432
Cdd:COG1124 2 LEVRNLSVSYGQGGRRvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 433 AMVLQ---------KNVlfAGTIADNIRwgnPNATDEDVRRVCKLAQADGFIREFpkgYDTYIEEggsnVSGGQRQRLCI 503
Cdd:COG1124 82 QMVFQdpyaslhprHTV--DRILAEPLR---IHGLPDREERIAELLEQVGLPPSF---LDRYPHQ----LSGGQRQRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 504 ARALLKKPKILILDDSTSAVDTKTDRLIRGAFKT--EIPDTTKIIIAQRVASVQE-SDEIIVMDGGRILDRGTHDQLLQT 580
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILNLLKDlrEERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLAG 229
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
38-309 |
2.01e-32 |
|
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: 126.44 E-value: 2.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 38 FVIVESVLEILIPTVMASMIDQGVAGGSMPAIWKFGLILLGCAVVSLFAGFMSGRYAAIASAGFAKNLRHDLFEKVQSFS 117
Cdd:cd18576 4 LLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 118 FTNIDHFSTGSIITRITTDVTNIQYAFQMCIRVAVRAPLMVVVAWLFSFRISPSISMIFLIIIPILGVTLTGLALSVNPV 197
Cdd:cd18576 84 LSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 198 FEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEHVLAFNWPILNTCIYGAMLIISWMGTK 277
Cdd:cd18576 164 SKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGR 243
|
250 260 270
....*....|....*....|....*....|..
gi 705456738 278 QIVGSHnnaavgLTTGDLTALVTYAMQILMSL 309
Cdd:cd18576 244 LVLAGE------LTAGDLVAFLLYTLFIAGSI 269
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
33-309 |
6.95e-32 |
|
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: 124.68 E-value: 6.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 33 ILAPTFVIVESVLEILIPTVMASMIDQGVAGGSMPAIW--KFGLILLGCAVVSLFAGFMSGRYAAIASAGFAKNLRHDLF 110
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQAlnVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 111 EKVQSFSFTNIDHFSTGSIITRITTDVTNIQYAFQMCIRVAVRAPLMVVVAWLFSFRISPSISMIFLIIIPILGVTLTGL 190
Cdd:pfam00664 82 KKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 191 ALSVNPVFEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEHVLAFNWPILNTCIYGAMLI 270
Cdd:pfam00664 162 AKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYAL 241
|
250 260 270
....*....|....*....|....*....|....*....
gi 705456738 271 ISWMGTKQIVGSHnnaavgLTTGDLTALVTYAMQILMSL 309
Cdd:pfam00664 242 ALWFGAYLVISGE------LSVGDLVAFLSLFAQLFGPL 274
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
354-579 |
8.90e-32 |
|
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: 123.43 E-value: 8.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDvgsERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLEtLRDAVA 433
Cdd:COG4555 2 IEVENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 MVLQKNVLFAG-TIADNIR---WGNPNATDEDVRRVCKLAQADGFiREFpkgYDTYIEEggsnVSGGQRQRLCIARALLK 509
Cdd:COG4555 78 VLPDERGLYDRlTVRENIRyfaELYGLFDEELKKRIEELIELLGL-EEF---LDRRVGE----LSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 705456738 510 KPKILILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIAQRVASVQE--SDEIIVMDGGRILDRGTHDQLLQ 579
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEalCDRVVILHKGKVVAQGSLDELRE 221
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
124-577 |
1.29e-31 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 131.40 E-value: 1.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 124 FSTGSIITRITTDVTNIQyafQMC--IRVAVRAPLMVVVAWLFSFR----ISPSISMIFLIIIPILGVTLTGL-ALSvnp 196
Cdd:PLN03130 395 FTSGKITNLMTTDAEALQ---QICqqLHTLWSAPFRIIIAMVLLYQqlgvASLIGSLMLVLMFPIQTFIISKMqKLT--- 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 197 vfEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEHVLAFNWPILNTcIYGAMLIISWmGT 276
Cdd:PLN03130 469 --KEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSFILNS-IPVLVTVVSF-GV 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 277 KQIVGSHNNAAVGLTTGDLTALVTYAmqilmsLNMVSMIIVMVVISRADAERICQV-LNEVSTVRDNadPIMDVPDGSIT 355
Cdd:PLN03130 545 FTLLGGDLTPARAFTSLSLFAVLRFP------LFMLPNLITQAVNANVSLKRLEELlLAEERVLLPN--PPLEPGLPAIS 616
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 356 FNDVSFRYDVGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQ-LIPRLYDVSSGSLevggrdvreydleTLRDAVAM 434
Cdd:PLN03130 617 IKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASV-------------VIRGTVAY 683
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 435 VLQKNVLFAGTIADNIRWGNPNATD--EDVRRVCKLAQAdgfIREFPKGYDTYIEEGGSNVSGGQRQRLCIARALLKKPK 512
Cdd:PLN03130 684 VPQVSWIFNATVRDNILFGSPFDPEryERAIDVTALQHD---LDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSD 760
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 705456738 513 ILILDDSTSAVDTKTDR-LIRGAFKTEIPDTTKIIIAQRVASVQESDEIIVMDGGRILDRGTHDQL 577
Cdd:PLN03130 761 VYIFDDPLSALDAHVGRqVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
354-578 |
2.08e-31 |
|
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: 121.92 E-value: 2.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRY-DVGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDV---REYDLETLR 429
Cdd:cd03258 2 IELKNVSKVFgDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 430 DAVAMVLQK-NVLFAGTIADNIR-----WGNPNAT-DEDVRRVCKLAQADGFIREFPkgydtyieeggSNVSGGQRQRLC 502
Cdd:cd03258 82 RRIGMIFQHfNLLSSRTVFENVAlpleiAGVPKAEiEERVLELLELVGLEDKADAYP-----------AQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 503 IARALLKKPKILILDDSTSAVDTKTDRLIRGAFKtEIPDT---TKIIIAQRVASVQE-SDEIIVMDGGRILDRGTHDQLL 578
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLR-DINRElglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVF 229
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
354-584 |
5.28e-31 |
|
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: 120.68 E-value: 5.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDvgsERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVR---EYDLETLRD 430
Cdd:cd03261 1 IELRGLTKSFG---GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglsEAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 431 AVAMVLQKNVLFAG-TIADNIrwGNP-----NATDEDVRRVC--KLAQA--DGFIREFPkgydtyieeggSNVSGGQRQR 500
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENV--AFPlrehtRLSEEEIREIVleKLEAVglRGAEDLYP-----------AELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 501 LCIARALLKKPKILILDDSTSAVD----TKTDRLIRGAFKTeiPDTTKIIIAQRVASVQE-SDEIIVMDGGRILDRGTHD 575
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDpiasGVIDDLIRSLKKE--LGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPE 222
|
....*....
gi 705456738 576 QLLQTCDEY 584
Cdd:cd03261 223 ELRASDDPL 231
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
354-578 |
1.07e-30 |
|
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: 120.10 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYdvGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVA 433
Cdd:cd03295 1 IEFENVTKRY--GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 MVLQKNVLFAG-TIADNI-------RWGNPNAtDEDVRRVCKLAQADgfirefPKGY-DTYIEEggsnVSGGQRQRLCIA 504
Cdd:cd03295 79 YVIQQIGLFPHmTVEENIalvpkllKWPKEKI-RERADELLALVGLD------PAEFaDRYPHE----LSGGQQQRVGVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 505 RALLKKPKILILDDSTSAVDTKTD--------RLIRGAFKTEIPDTTKIIIAQRVAsvqesDEIIVMDGGRILDRGTHDQ 576
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPITRdqlqeefkRLQQELGKTIVFVTHDIDEAFRLA-----DRIAIMKNGEIVQVGTPDE 222
|
..
gi 705456738 577 LL 578
Cdd:cd03295 223 IL 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
354-569 |
1.37e-30 |
|
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: 119.16 E-value: 1.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDvgsERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVreYDLETLRDAVA 433
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV--TGVPPERRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 MVLQKNVLFAG-TIADNIRWG-----NPNATDED-VRRVCKLAQADGFIREFPkgydtyieeggSNVSGGQRQRLCIARA 506
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGlklrgVPKAEIRArVRELLELVGLEGLLNRYP-----------HELSGGQQQRVALARA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 705456738 507 LLKKPKILILDDSTSAVDTKTDRLIRGAFKtEIPDTTKIII---------AQRVAsvqesDEIIVMDGGRIL 569
Cdd:cd03259 145 LAREPSLLLLDEPLSALDAKLREELREELK-ELQRELGITTiyvthdqeeALALA-----DRIAVMNEGRIV 210
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
354-578 |
3.06e-29 |
|
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: 116.30 E-value: 3.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDvgsERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVA 433
Cdd:COG1120 2 LEAENLSVGYG---GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 MVLQKNVL-FAGTIADNI---------RWGNPNATDED-VRRVCKLAQADGFIrefpkgyDTYIEEggsnVSGGQRQRLC 502
Cdd:COG1120 79 YVPQEPPApFGLTVRELValgryphlgLFGRPSAEDREaVEEALERTGLEHLA-------DRPVDE----LSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 503 IARALLKKPKILILDDSTSAVD----TKTDRLIRGAFKTEipDTTKIII------AQRVAsvqesDEIIVMDGGRILDRG 572
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDlahqLEVLELLRRLARER--GRTVVMVlhdlnlAARYA-----DRLVLLKDGRIVAQG 220
|
....*.
gi 705456738 573 THDQLL 578
Cdd:COG1120 221 PPEEVL 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
354-568 |
1.43e-28 |
|
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: 113.35 E-value: 1.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDVGSER-PVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETL---- 428
Cdd:cd03255 1 IELKNLSKTYGGGGEKvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 429 RDAVAMVLQ-----------KNVLFAGTIAdnirwGNPNATDED-VRRVCKLAQADGFIREFPkgydtyieeggSNVSGG 496
Cdd:cd03255 81 RRHIGFVFQsfnllpdltalENVELPLLLA-----GVPKKERRErAEELLERVGLGDRLNHYP-----------SELSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 705456738 497 QRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFK--TEIPDTTkIIIA---QRVASvqESDEIIVMDGGRI 568
Cdd:cd03255 145 QQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRelNKEAGTT-IVVVthdPELAE--YADRIIELRDGKI 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
354-571 |
1.51e-28 |
|
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: 113.34 E-value: 1.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDVGSER-PVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREydletLRDAV 432
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 433 AMVLQKNVLFA-GTIADNI------RWGNPNATDEDVRRVCKLAQADGFIREFPKgydtyieeggsNVSGGQRQRLCIAR 505
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNValglelQGVPKAEARERAEELLELVGLSGFENAYPH-----------QLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 705456738 506 ALLKKPKILILDDSTSAVDTKTDRLIRGafkteipDTTKIIIAQRVA------SVQE----SDEIIVMDG--GRILDR 571
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQE-------ELLDIWRETGKTvllvthDIDEavflADRVVVLSArpGRIVAE 215
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
33-329 |
1.79e-28 |
|
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: 115.22 E-value: 1.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 33 ILAPTFVIVESVLEILIPTVMASMIDQGVAGGS-MPAIWKFGLILLGCAVVSLFAGFMSGRyaaiASAGFAKNLRHDLFE 111
Cdd:cd18551 2 ILALLLSLLGTAASLAQPLLVKNLIDALSAGGSsGGLLALLVALFLLQAVLSALSSYLLGR----TGERVVLDLRRRLWR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 112 KVQSFSFTNIDHFSTGSIITRITTDVTNIQYAFQMCIRVAVRAPLMVVVAWLFSFRISPSISMIFLIIIPILGVTLTGLA 191
Cdd:cd18551 78 RLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 192 LSVNPVFEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEHVLAFNWPILNTCIYGAMLII 271
Cdd:cd18551 158 RRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 705456738 272 SWMGTKQIvgshnnaAVG-LTTGDLTALVTYAMQILMSLNMVSMIIVMVVISRADAERI 329
Cdd:cd18551 238 LGVGGARV-------ASGaLTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
355-567 |
1.88e-28 |
|
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: 111.18 E-value: 1.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 355 TFNDVSFRYDvgsERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVAM 434
Cdd:cd00267 1 EIENLSFRYG---GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 435 VLQknvlfagtiadnirwgnpnatdedvrrvcklaqadgfirefpkgydtyieeggsnVSGGQRQRLCIARALLKKPKIL 514
Cdd:cd00267 78 VPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 705456738 515 ILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIA-QRVASVQE-SDEIIVMDGGR 567
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEEGRTVIIVtHDPELAELaADRVIVLKDGK 157
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
354-584 |
2.48e-28 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 113.54 E-value: 2.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDvgsERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDV---REYDLETLRD 430
Cdd:COG1127 6 IEVRNLTKSFG---DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglSEKELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 431 AVAMVLQKNVLFAG-TIADNIRWG---NPNATDEDVRRV--CKLAQA--DGFIREFPkgydtyieeggSNVSGGQRQRLC 502
Cdd:COG1127 83 RIGMLFQGGALFDSlTVFENVAFPlreHTDLSEAEIRELvlEKLELVglPGAADKMP-----------SELSGGMRKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 503 IARALLKKPKILILDDSTSAVD----TKTDRLIRgafktEIPD---TTKIIIAQRVASVQE-SDEIIVMDGGRILDRGTH 574
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDpitsAVIDELIR-----ELRDelgLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTP 226
|
250
....*....|
gi 705456738 575 DQLLQTCDEY 584
Cdd:COG1127 227 EELLASDDPW 236
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
354-587 |
2.88e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 114.34 E-value: 2.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDvGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVA 433
Cdd:PRK13635 6 IRVEHISFRYP-DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 MVLQK--NVLFAGTIADNIRWGNPN---ATDEDVRRVcklaqaDGFIREFpkGYDTYIEEGGSNVSGGQRQRLCIARALL 508
Cdd:PRK13635 85 MVFQNpdNQFVGATVQDDVAFGLENigvPREEMVERV------DQALRQV--GMEDFLNREPHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 509 KKPKILILDDSTSAVDTktdrliRGafKTEIPDTTKIIIAQRVASV----------QESDEIIVMDGGRILDRGTHDQLL 578
Cdd:PRK13635 157 LQPDIIILDEATSMLDP------RG--RREVLETVRQLKEQKGITVlsithdldeaAQADRVIVMNKGEILEEGTPEEIF 228
|
....*....
gi 705456738 579 QTCDEYRSI 587
Cdd:PRK13635 229 KSGHMLQEI 237
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
29-329 |
6.37e-28 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 113.73 E-value: 6.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 29 KKDTILAPTFVIVESVLEILIPTVMASMIDQGVAGGSMPAIWKFGLILLGCAVVSLFAGFMSGRYAAIASAGFAKNLRHD 108
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 109 LFEKVQSFSFTNIDHFSTGSIITRITTDVTNIQ-----YAFQMcirvaVRAPLMVVVAWLFSFRISPSISMIFLIIIPIL 183
Cdd:cd18540 81 AFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGeiiswGLVDL-----VWGITYMIGILIVMLILNWKLALIVLAVVPVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 184 GVtltglalsVNPVFEKVFHtydHLNNIV-----------DENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEHV 252
Cdd:cd18540 156 AV--------VSIYFQKKIL---KAYRKVrkinsritgafNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARL 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 705456738 253 LAFNWPILNTCIYGAMLIISWMGTKQIVGShnnaavGLTTGDLTALVTYAMQILMSLNMVSMIIVMVVISRADAERI 329
Cdd:cd18540 225 SALFLPIVLFLGSIATALVLWYGGILVLAG------AITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
354-567 |
1.07e-27 |
|
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: 109.58 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYdvgSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLET--LRDA 431
Cdd:cd03229 1 LELKNVSKRY---GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 432 VAMVLQKNVLFAG-TIADNIRWGnpnatdedvrrvcklaqadgfirefpkgydtyieeggsnVSGGQRQRLCIARALLKK 510
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 511 PKILILDDSTSAVDTKTDRLIRGAFKT--EIPDTTKIIIAQRVASVQE-SDEIIVMDGGR 567
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSlqAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
352-568 |
1.58e-27 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 118.47 E-value: 1.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 352 GSITFNDVSFRYDVGSeRPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDvSSGSLEVGGRDVREYDLETLRDA 431
Cdd:TIGR01271 1216 GQMDVQGLTAKYTEAG-RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKA 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 432 VAMVLQKNVLFAGTIADNI----RWgnpnaTDEDVRRVCKLAQADGFIREFPKGYDTYIEEGGSNVSGGQRQRLCIARAL 507
Cdd:TIGR01271 1294 FGVIPQKVFIFSGTFRKNLdpyeQW-----SDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSI 1368
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 705456738 508 LKKPKILILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIAQRVASVQESDEIIVMDGGRI 568
Cdd:TIGR01271 1369 LSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSV 1429
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
354-568 |
1.63e-27 |
|
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: 110.42 E-value: 1.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDvgsERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVReyDLETLRDAVA 433
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPPKDRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 MVLQKNVLFAG-TIADNIRWG------NPNATDEDVRRVCKLAQADGFIREFPKgydtyieeggsNVSGGQRQRLCIARA 506
Cdd:cd03301 76 MVFQNYALYPHmTVYDNIAFGlklrkvPKDEIDERVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 705456738 507 LLKKPKILILDDSTSAVDTKtdrlIRGAFKTEIP------DTTKIIIAQ-RVASVQESDEIIVMDGGRI 568
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAK----LRVQMRAELKrlqqrlGTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
347-587 |
1.74e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 112.42 E-value: 1.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 347 MDvpdgsITFNDVSFRYDVGS--ERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGR----DV 420
Cdd:PRK13634 1 MD-----ITFQKVEHRYQYKTpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERvitaGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 421 REYDLETLRDAVAMVLQ--KNVLFAGTIADNIRWGNPN--ATDEDV-RRVCKLAQADGFIREfpkgydtYIEEGGSNVSG 495
Cdd:PRK13634 76 KNKKLKPLRKKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEEDAkQKAREMIELVGLPEE-------LLARSPFELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 496 GQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKT---EIPDTTKIIIAQRVASVQESDEIIVMDGGRILDRG 572
Cdd:PRK13634 149 GQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKlhkEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQG 228
|
250
....*....|....*
gi 705456738 573 THDQLLQTCDEYRSI 587
Cdd:PRK13634 229 TPREIFADPDELEAI 243
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
353-587 |
1.88e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 112.45 E-value: 1.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 353 SITFNDVSFRYDVGS--ERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDV--REYDLETL 428
Cdd:PRK13637 2 SIKIENLTHIYMEGTpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 429 RDAVAMVLQ--KNVLFAGTIADNIRWG--NPNATDEDV-RRVCKLAQADGFirefpkGYDTYIEEGGSNVSGGQRQRLCI 503
Cdd:PRK13637 82 RKKVGLVFQypEYQLFEETIEKDIAFGpiNLGLSEEEIeNRVKRAMNIVGL------DYEDYKDKSPFELSGGQKRRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 504 ARALLKKPKILILDDSTSAVDTKTDRLIRGAFKT--EIPDTTKIIIAQRVASVQE-SDEIIVMDGGRILDRGTHDQLLQT 580
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGRDEILNKIKElhKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREVFKE 235
|
....*..
gi 705456738 581 CDEYRSI 587
Cdd:PRK13637 236 VETLESI 242
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
347-570 |
2.03e-27 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 111.33 E-value: 2.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 347 MDVPDGSITFNDVSFRYDVGS-ERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDL 425
Cdd:COG1116 1 MSAAAPALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 426 EtlrdaVAMVLQKNVLFA-GTIADNIRWGNPNA---TDEDVRRVCKLAQA---DGFIREFPKgydtyieeggsNVSGGQR 498
Cdd:COG1116 81 D-----RGVVFQEPALLPwLTVLDNVALGLELRgvpKAERRERARELLELvglAGFEDAYPH-----------QLSGGMR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 499 QRLCIARALLKKPKILILDDSTSAVDTKT-----DRLIRgafkteipdttkIIIAQRVA------SVQE----SDEIIVM 563
Cdd:COG1116 145 QRVAIARALANDPEVLLMDEPFGALDALTrerlqDELLR------------LWQETGKTvlfvthDVDEavflADRVVVL 212
|
....*....
gi 705456738 564 DG--GRILD 570
Cdd:COG1116 213 SArpGRIVE 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
354-531 |
2.32e-27 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 110.95 E-value: 2.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDvgsERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVR------------ 421
Cdd:COG1121 7 IELENLTVSYG---GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRrarrrigyvpqr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 422 -EYDLE---TLRDAVAMVLQKNVLFagtiadnirWGNPNATD-EDVRRVCKLAQADGFIrefpkgyDTYIeeggSNVSGG 496
Cdd:COG1121 84 aEVDWDfpiTVRDVVLMGRYGRRGL---------FRRPSRADrEAVDEALERVGLEDLA-------DRPI----GELSGG 143
|
170 180 190
....*....|....*....|....*....|....*
gi 705456738 497 QRQRLCIARALLKKPKILILDDSTSAVDTKTDRLI 531
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEAL 178
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
352-568 |
2.50e-27 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 111.48 E-value: 2.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 352 GSITFNDVSFRYDVGSErPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDvSSGSLEVGGRDVREYDLETLRDA 431
Cdd:cd03289 1 GQMTVKDLTAKYTEGGN-AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 432 VAMVLQKNVLFAGTIADNIrwgNPNA--TDEDVRRVCKLAQADGFIREFPKGYDTYIEEGGSNVSGGQRQRLCIARALLK 509
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNL---DPYGkwSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 705456738 510 KPKILILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIAQRVASVQESDEIIVMDGGRI 568
Cdd:cd03289 156 KAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
353-577 |
2.66e-27 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 110.51 E-value: 2.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 353 SITFNDVSFRYDvgsERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLEtlRDAV 432
Cdd:cd03296 2 SIEVRNVSKRFG---DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 433 AMVLQKNVLFAG-TIADNIRWG--------NPNAT--DEDVRRVCKLAQADGFIREFPkgydtyieeggSNVSGGQRQRL 501
Cdd:cd03296 77 GFVFQHYALFRHmTVFDNVAFGlrvkprseRPPEAeiRAKVHELLKLVQLDWLADRYP-----------AQLSGGQRQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 705456738 502 CIARALLKKPKILILDDSTSAVDTKTDRLIRG---AFKTEIPDTTKIIIAQRVASVQESDEIIVMDGGRILDRGTHDQL 577
Cdd:cd03296 146 ALARALAVEPKVLLLDEPFGALDAKVRKELRRwlrRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
354-580 |
2.84e-27 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 110.57 E-value: 2.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYdvgSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVR--EYDLETLRDA 431
Cdd:PRK09493 2 IEFKNVSKHF---GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 432 VAMVLQKNVLFAGTIA-DNIRWGnPnatdEDVRRVCKlAQADGFIREFPK--GYDTYIEEGGSNVSGGQRQRLCIARALL 508
Cdd:PRK09493 79 AGMVFQQFYLFPHLTAlENVMFG-P----LRVRGASK-EEAEKQARELLAkvGLAERAHHYPSELSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 705456738 509 KKPKILILDDSTSAVDTKTDRLIRGAFK-------TEIPDTTKIIIAQRVASvqesdEIIVMDGGRILDRGTHDQLLQT 580
Cdd:PRK09493 153 VKPKLMLFDEPTSALDPELRHEVLKVMQdlaeegmTMVIVTHEIGFAEKVAS-----RLIFIDKGRIAEDGDPQVLIKN 226
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
43-318 |
7.63e-27 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 110.62 E-value: 7.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 43 SVLEILIPTVMASMIDQGVAGGSMPAIWKFGLILLGCAVVSLFAGFMSGRYAAIASAGFAKNLRHDLFEKVQSFSFTNID 122
Cdd:cd18549 15 AALDLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFEHLQKLSFSFFD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 123 HFSTGSIITRITTDVTNIQyafqmciRVAVRAP-------LMVVVAWLFSFRISPSISMIFLIIIPILGV--TLTGLALS 193
Cdd:cd18549 95 NNKTGQLMSRITNDLFDIS-------ELAHHGPedlfisiITIIGSFIILLTINVPLTLIVFALLPLMIIftIYFNKKMK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 194 VnpVFEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEHVLAFNWPILNTC---------I 264
Cdd:cd18549 168 K--AFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMNFFtnllnlvvlV 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 705456738 265 YGAMLIIswMGTkqivgshnnaavgLTTGDLTALVTYAMQILMSLNMVSMIIVM 318
Cdd:cd18549 246 AGGYFII--KGE-------------ITLGDLVAFLLYVNVFIKPIRRLVNFTEQ 284
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
353-573 |
9.24e-27 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 111.73 E-value: 9.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 353 SITFNDVSFRYDvgsERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVReyDLETLRDAV 432
Cdd:COG3842 5 ALELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT--GLPPEKRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 433 AMVLQKNVLFAG-TIADNIRWG------NPNATDEDVRRVCKLAQADGFIREFPkgydtyieeggSNVSGGQRQRLCIAR 505
Cdd:COG3842 80 GMVFQDYALFPHlTVAENVAFGlrmrgvPKAEIRARVAELLELVGLEGLADRYP-----------HQLSGGQQQRVALAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 705456738 506 ALLKKPKILILDDSTSAVDTKTdrliRGAFKTEIpdtTKIIIAQRVASV-----QE-----SDEIIVMDGGRILDRGT 573
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAKL----REEMREEL---RRLQRELGITFIyvthdQEealalADRIAVMNDGRIEQVGT 219
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
354-587 |
9.65e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 109.70 E-value: 9.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDvGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVA 433
Cdd:PRK13632 8 IKVENVSFSYP-NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 MVLQK--NVLFAGTIADNIRWG--NPNATDEDVRRVcklaqadgfIREFPK--GYDTYIEEGGSNVSGGQRQRLCIARAL 507
Cdd:PRK13632 87 IIFQNpdNQFIGATVEDDIAFGleNKKVPPKKMKDI---------IDDLAKkvGMEDYLDKEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 508 LKKPKILILDDSTSAVDTKTDRLIRgAFKTEIPDTTK---IIIAQRVASVQESDEIIVMDGGRILDRGTHDQLLQTCDEY 584
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIK-KIMVDLRKTRKktlISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKEIL 236
|
...
gi 705456738 585 RSI 587
Cdd:PRK13632 237 EKA 239
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
354-591 |
1.15e-26 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 108.99 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDvgSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDA-- 431
Cdd:COG3638 3 LELRNLSKRYP--GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 432 -VAMVLQ-----------KNVLfAGTIAdniRWGNPNA-----TDEDVRRVCK-LAQ---ADgfirefpkgydtYIEEGG 490
Cdd:COG3638 81 rIGMIFQqfnlvprlsvlTNVL-AGRLG---RTSTWRSllglfPPEDRERALEaLERvglAD------------KAYQRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 491 SNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKtEIPDTTKIII---------AQRVAsvqesDEII 561
Cdd:COG3638 145 DQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLR-RIAREDGITVvvnlhqvdlARRYA-----DRII 218
|
250 260 270
....*....|....*....|....*....|
gi 705456738 562 VMDGGRILDRGTHDQLlqTCDEYRSIYQSQ 591
Cdd:COG3638 219 GLRDGRVVFDGPPAEL--TDAVLREIYGGE 246
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
354-573 |
1.21e-26 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 110.94 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDVGS-ERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDA- 431
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 432 --VAMVLQK-NVLFAGTIADNI-----RWGNPNATDEdvRRVCKL-------AQADgfirEFPkgydtyieeggSNVSGG 496
Cdd:COG1135 82 rkIGMIFQHfNLLSSRTVAENValpleIAGVPKAEIR--KRVAELlelvglsDKAD----AYP-----------SQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 497 QRQRLCIARALLKKPKILILDDSTSAVDTKTDR----LIRgafktEIPDTTKI----I---------IAQRVAsvqesde 559
Cdd:COG1135 145 QKQRVGIARALANNPKVLLCDEATSALDPETTRsildLLK-----DINRELGLtivlIthemdvvrrICDRVA------- 212
|
250
....*....|....
gi 705456738 560 iiVMDGGRILDRGT 573
Cdd:COG1135 213 --VLENGRIVEQGP 224
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
354-573 |
1.24e-26 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 111.05 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDVGS-ERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDA- 431
Cdd:PRK11153 2 IELKNISKVFPQGGrTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 432 --VAMVLQK-NVLFAGTIADNIRW-----GNPNAtdEDVRRVCKL-------AQADgfirEFPkgydtyieeggSNVSGG 496
Cdd:PRK11153 82 rqIGMIFQHfNLLSSRTVFDNVALplelaGTPKA--EIKARVTELlelvglsDKAD----RYP-----------AQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 497 QRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKtEIPDT---TKIIIAQRVASVQE-SDEIIVMDGGRILDRG 572
Cdd:PRK11153 145 QKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLK-DINRElglTIVLITHEMDVVKRiCDRVAVIDAGRLVEQG 223
|
.
gi 705456738 573 T 573
Cdd:PRK11153 224 T 224
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
353-579 |
1.48e-26 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 111.01 E-value: 1.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 353 SITFNDVSFRYDvgsERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVrEYDLETLRDAV 432
Cdd:COG1118 2 SIEVRNISKRFG---SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL-FTNLPPRERRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 433 AMVLQKNVLFAG-TIADNI------RWGNPNATDEDVRRVCKLAQADGFIREFPkgydtyieeggSNVSGGQRQRLCIAR 505
Cdd:COG1118 78 GFVFQHYALFPHmTVAENIafglrvRPPSKAEIRARVEELLELVQLEGLADRYP-----------SQLSGGQRQRVALAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 506 ALLKKPKILILDDSTSAVDTKTDRLIRgafkTEIpdtTKIIIAQRVASV-----QE-----SDEIIVMDGGRILDRGTHD 575
Cdd:COG1118 147 ALAVEPEVLLLDEPFGALDAKVRKELR----RWL---RRLHDELGGTTVfvthdQEealelADRVVVMNQGRIEQVGTPD 219
|
....
gi 705456738 576 QLLQ 579
Cdd:COG1118 220 EVYD 223
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
351-573 |
2.63e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 108.73 E-value: 2.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 351 DGSITFNDVSFRYDvGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLY---DVSSGSLEVGGRDVREYDLET 427
Cdd:PRK13640 3 DNIVEFKHVSFTYP-DSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 428 LRDAVAMVLQK--NVLFAGTIADNIRWG--NPNATDEDVRRVCKLAQADgfirefpKGYDTYIEEGGSNVSGGQRQRLCI 503
Cdd:PRK13640 82 IREKVGIVFQNpdNQFVGATVGDDVAFGleNRAVPRPEMIKIVRDVLAD-------VGMLDYIDSEPANLSGGQKQRVAI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 705456738 504 ARALLKKPKILILDDSTSAVD----TKTDRLIRGAFKTEipDTTKIIIAQRVASVQESDEIIVMDGGRILDRGT 573
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDpagkEQILKLIRKLKKKN--NLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
354-568 |
3.48e-26 |
|
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: 106.46 E-value: 3.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYdvgSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDV--REYDLETLRDA 431
Cdd:cd03262 1 IEIKNLHKSF---GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 432 VAMVLQKNVLFAG-TIADNI------RWGNPNATDED-----VRRVCKLAQADGFIREfpkgydtyieeggsnVSGGQRQ 499
Cdd:cd03262 78 VGMVFQQFNLFPHlTVLENItlapikVKGMSKAEAEEralelLEKVGLADKADAYPAQ---------------LSGGQQQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 705456738 500 RLCIARALLKKPKILILDDSTSAVDTKTDR----LIRGAFKTEIpdtTKIIIAQRVASVQE-SDEIIVMDGGRI 568
Cdd:cd03262 143 RVAIARALAMNPKVMLFDEPTSALDPELVGevldVMKDLAEEGM---TMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
352-573 |
4.26e-26 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 109.78 E-value: 4.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 352 GSITFNDVSFRYDvgsERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVreYDLETL-RD 430
Cdd:COG3839 2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV--TDLPPKdRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 431 aVAMVLQKNVLF-AGTIADNIRWG------NPNATDEDVRRVCKLAQADGFIREFPKgydtyieeggsNVSGGQRQRLCI 503
Cdd:COG3839 77 -IAMVFQSYALYpHMTVYENIAFPlklrkvPKAEIDRRVREAAELLGLEDLLDRKPK-----------QLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 504 ARALLKKPKILILDDSTSAVDTKtdrlIRGAFKTEIPD------TTKIII------AQRVAsvqesDEIIVMDGGRILDR 571
Cdd:COG3839 145 GRALVREPKVFLLDEPLSNLDAK----LRVEMRAEIKRlhrrlgTTTIYVthdqveAMTLA-----DRIAVMNDGRIQQV 215
|
..
gi 705456738 572 GT 573
Cdd:COG3839 216 GT 217
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
154-603 |
7.42e-26 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 113.50 E-value: 7.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 154 APLMVVVA-WLFSFRISPSIsmifliiipILGVTLTGLALSVNPVFEKVFHTY--------DHLNNIVDENLQGIRVVKS 224
Cdd:TIGR00957 441 APLQVILAlYFLWLNLGPSV---------LAGVAVMVLMVPLNAVMAMKTKTYqvahmkskDNRIKLMNEILNGIKVLKL 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 225 YDREEHESRKFGRVSERIYEYFCKAEHVLA---FNW---PILNTCIYGAMLIisWMGTKQIVGSHnnaavglttgdlTAL 298
Cdd:TIGR00957 512 YAWELAFLDKVEGIRQEELKVLKKSAYLHAvgtFTWvctPFLVALITFAVYV--TVDENNILDAE------------KAF 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 299 VTYAM-QIL-MSLNMVSMIIVMVVISRADAERICQVLNEVSTVRDNAD--PIMDVPDGSITFNDVSFRYdVGSERPVLDD 374
Cdd:TIGR00957 578 VSLALfNILrFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIErrTIKPGEGNSITVHNATFTW-ARDLPPTLNG 656
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 375 INLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLevggrdvreydleTLRDAVAMVLQKNVLFAGTIADNIRWGN 454
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV-------------HMKGSVAYVPQQAWIQNDSLRENILFGK 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 455 PNATD--EDVRRVCKLAqADgfIREFPKGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLI- 531
Cdd:TIGR00957 724 ALNEKyyQQVLEACALL-PD--LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIf 800
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 705456738 532 ------RGAFKTEipdtTKIIIAQRVASVQESDEIIVMDGGRILDRGTHDQLLQTCDEYRSIYQSQTKSQGEGSDDDE 603
Cdd:TIGR00957 801 ehvigpEGVLKNK----TRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEQQGHLEDS 874
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
354-570 |
8.68e-26 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 105.52 E-value: 8.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDVGseRPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDV---REYDLETLRD 430
Cdd:COG2884 2 IRFENVSKRYPGG--REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLsrlKRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 431 AVAMVLQ-----------KNVLFA----GTIADNIRwgnpnatdEDVRRVCKLAQADGFIREFPkgydtyieeggSNVSG 495
Cdd:COG2884 80 RIGVVFQdfrllpdrtvyENVALPlrvtGKSRKEIR--------RRVREVLDLVGLSDKAKALP-----------HELSG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 496 GQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKtEIPDT-TKIIIA-----------QRVasvqesdeiIVM 563
Cdd:COG2884 141 GEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLE-EINRRgTTVLIAthdlelvdrmpKRV---------LEL 210
|
....*..
gi 705456738 564 DGGRILD 570
Cdd:COG2884 211 EDGRLVR 217
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
354-568 |
1.35e-25 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 105.13 E-value: 1.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDVGS-ERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDV---REYDLETLR 429
Cdd:COG1136 5 LELRNLTKSYGTGEgEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslSERELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 430 -DAVAMVLQK-----------NVLFAGTIAdnirwGNPNAtdEDVRRVCKLAQA---DGFIREFPkgydtyieeggSNVS 494
Cdd:COG1136 85 rRHIGFVFQFfnllpeltaleNVALPLLLA-----GVSRK--ERRERARELLERvglGDRLDHRP-----------SQLS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 705456738 495 GGQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKtEIPDTTK--IIIA---QRVASvqESDEIIVMDGGRI 568
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLR-ELNRELGttIVMVthdPELAA--RADRVIRLRDGRI 222
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
66-329 |
4.47e-25 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 105.63 E-value: 4.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 66 MPAIWKFGLILLGCAVVSLFAGFMSGRYAAIASAGFAKNLRHDLFEKV--QSFSFTniDHFSTGSIITRITTDVTNIQYA 143
Cdd:cd18577 43 LDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALlrQDIAWF--DKNGAGELTSRLTSDTNLIQDG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 144 FQMCIRVAVRAPLMVVVAWLFSFRISPSISMIFLIIIPILGVTLTGLALSVNPVFEKVFHTYDHLNNIVDENLQGIRVVK 223
Cdd:cd18577 121 IGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 224 SYDREEHESRKFGRVSERIYEYFCKAEHVLAFNWPILNTCIYGAMLIISWMGTKQIVGSHNNAavglttGDLTALVTYAM 303
Cdd:cd18577 201 AFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISP------GDVLTVFFAVL 274
|
250 260
....*....|....*....|....*.
gi 705456738 304 QILMSLNMVSMIIVMVVISRADAERI 329
Cdd:cd18577 275 IGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
337-524 |
4.68e-25 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 104.35 E-value: 4.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 337 STVRDNADPIMDVpdgsitfNDVSFRYDvgsERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDV-----SSG 411
Cdd:COG1117 2 TAPASTLEPKIEV-------RNLNVYYG---DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLipgarVEG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 412 SLEVGGRDV--REYDLETLRDAVAMVLQKNVLFAGTIADNIRWG-------NPNATDEDVRRVckLAQA-------Dgfi 475
Cdd:COG1117 72 EILLDGEDIydPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgikSKSELDEIVEES--LRKAalwdevkD--- 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 705456738 476 RefpkgydtyIEEGGSNVSGGQRQRLCIARALLKKPKILILDDSTSAVD 524
Cdd:COG1117 147 R---------LKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
354-568 |
6.72e-25 |
|
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: 101.71 E-value: 6.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDvgsERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDaVA 433
Cdd:cd03230 1 IEVRNLSKRYG---KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR-IG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 MVLQKNVLFAG-TIADNIRwgnpnatdedvrrvcklaqadgfirefpkgydtyieeggsnVSGGQRQRLCIARALLKKPK 512
Cdd:cd03230 77 YLPEEPSLYENlTVRENLK-----------------------------------------LSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 705456738 513 ILILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIII-------AQRVAsvqesDEIIVMDGGRI 568
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEGKTILLsshileeAERLC-----DRVAILNNGRI 173
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
354-573 |
3.21e-24 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 101.54 E-value: 3.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDVGserPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVreYDLETLRDAVA 433
Cdd:cd03300 1 IELENVSKFYGGF---VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 MVLQKNVLFAG-TIADNIRWG------NPNATDEDVRRVCKLAQADGFIREFPkgydtyieeggSNVSGGQRQRLCIARA 506
Cdd:cd03300 76 TVFQNYALFPHlTVFENIAFGlrlkklPKAEIKERVAEALDLVQLEGYANRKP-----------SQLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 705456738 507 LLKKPKILILDDSTSAVDTKTDRLIRGAFKtEIPDTTKIIIAQrVASVQE-----SDEIIVMDGGRILDRGT 573
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELK-RLQKELGITFVF-VTHDQEealtmSDRIAVMNKGKIQQIGT 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
357-572 |
3.98e-24 |
|
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: 99.43 E-value: 3.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 357 NDVSFRYDvgsERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVAMVL 436
Cdd:cd03214 3 ENLSVGYG---GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 437 QknvlfagtiadnirwgnpnatdedvrrVCKLAQADGFIRefpKGYDTyieeggsnVSGGQRQRLCIARALLKKPKILIL 516
Cdd:cd03214 80 Q---------------------------ALELLGLAHLAD---RPFNE--------LSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 705456738 517 DDSTSAVDTKTDRLIRGAFKTEIPDTTKIII--------AQRVAsvqesDEIIVMDGGRILDRG 572
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARERGKTVVmvlhdlnlAARYA-----DRVILLKDGRIVAQG 180
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
354-578 |
6.63e-24 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 100.84 E-value: 6.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDvgsERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDV--REYDLETLRDA 431
Cdd:COG1126 2 IEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 432 VAMVLQK-NvLFAG-TIADNI--------RWGNPNATDEDVR---RVCKLAQADgfirEFPkgydtyieeggSNVSGGQR 498
Cdd:COG1126 79 VGMVFQQfN-LFPHlTVLENVtlapikvkKMSKAEAEERAMElleRVGLADKAD----AYP-----------AQLSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 499 QRLCIARALLKKPKILILDDSTSAVDTktdRLIRgafktEIPDT---------TKIII------AQRVAsvqesDEIIVM 563
Cdd:COG1126 143 QRVAIARALAMEPKVMLFDEPTSALDP---ELVG-----EVLDVmrdlakegmTMVVVthemgfAREVA-----DRVVFM 209
|
250
....*....|....*
gi 705456738 564 DGGRILDRGTHDQLL 578
Cdd:COG1126 210 DGGRIVEEGPPEEFF 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
354-583 |
8.54e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 101.35 E-value: 8.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDVGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVA 433
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 MVLQK--NVLFAGTIADNIRWGNPN---ATDEDVRRVcklAQADGFIrefpkGYDTYIEEGGSNVSGGQRQRLCIARALL 508
Cdd:PRK13650 85 MVFQNpdNQFVGATVEDDVAFGLENkgiPHEEMKERV---NEALELV-----GMQDFKEREPARLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 509 KKPKILILDDSTSAVDTK-------TDRLIRGAFkteipDTTKIIIAQRVASVQESDEIIVMDGGRILDRGTHDQLLQTC 581
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEgrlelikTIKGIRDDY-----QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRG 231
|
..
gi 705456738 582 DE 583
Cdd:PRK13650 232 ND 233
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
38-313 |
9.65e-24 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 101.41 E-value: 9.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 38 FVIVESVLEILIPTVMASMIDQGVAGGSMPAIWKFGLILLGCAVVSLFAGFMsgRYAAIASAG--FAKNLRHDLFEKVQS 115
Cdd:cd18575 4 ALLIAAAATLALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASAL--RFYLVSWLGerVVADLRKAVFAHLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 116 FSFTNIDHFSTGSIITRITTDVTNIQYAFQMCIRVAVRAPLMVVVAWLFSFRISPSISMIFLIIIPILGVTLTGLA---- 191
Cdd:cd18575 82 LSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGrrvr 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 192 -LSVNpvfekvfhTYDHLNNI---VDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEHVLAFNWPILNTCIYGA 267
Cdd:cd18575 162 rLSRA--------SQDRLADLsafAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGA 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 705456738 268 MLIISWMGTKQIV-GShnnaavgLTTGDLTALVTYAMQILMSLNMVS 313
Cdd:cd18575 234 IVFVLWLGAHDVLaGR-------MSAGELSQFVFYAVLAAGSVGALS 273
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
358-568 |
1.28e-23 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 98.87 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 358 DVSFRYDVGSErpVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLetlRDAVAMVLQ 437
Cdd:cd03226 4 NISFSYKKGTE--ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER---RKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 438 kNV---LFAGTIADNIRWGNPNATDedvrrvcKLAQADGFIREFpkGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKIL 514
Cdd:cd03226 79 -DVdyqLFTDSVREELLLGLKELDA-------GNEQAETVLKDL--DLYALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 705456738 515 ILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIII-------AQRVAsvqesDEIIVMDGGRI 568
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAAQGKAVIVithdyefLAKVC-----DRVLLLANGAI 204
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
354-588 |
1.69e-23 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 99.56 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYdvGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREY---DLETLRD 430
Cdd:cd03256 1 IEVENLSKTY--PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgkALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 431 AVAMVLQ-----------KNVLFAGTIADNIRWGNPNA-TDEDVRRVCKLAQADGFirefpkgyDTYIEEGGSNVSGGQR 498
Cdd:cd03256 79 QIGMIFQqfnlierlsvlENVLSGRLGRRSTWRSLFGLfPKEEKQRALAALERVGL--------LDKAYQRADQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 499 QRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFK---TEIPDTTKIIIAQRVASVQESDEIIVMDGGRILDRGTHD 575
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKrinREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPA 230
|
250
....*....|...
gi 705456738 576 QLlqTCDEYRSIY 588
Cdd:cd03256 231 EL--TDEVLDEIY 241
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
356-527 |
2.03e-23 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 98.76 E-value: 2.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 356 FNDVSFRYDvgsERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDV-------------RE 422
Cdd:cd03235 2 VEDLTVSYG---GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLekerkrigyvpqrRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 423 YDLE---TLRDAVAMVLQKNVLFagtiadnirWGNPNATD-EDVRRVCKLAQADGFI-REFpkgydtyieeggSNVSGGQ 497
Cdd:cd03235 79 IDRDfpiSVRDVVLMGLYGHKGL---------FRRLSKADkAKVDEALERVGLSELAdRQI------------GELSGGQ 137
|
170 180 190
....*....|....*....|....*....|
gi 705456738 498 RQRLCIARALLKKPKILILDDSTSAVDTKT 527
Cdd:cd03235 138 QQRVLLARALVQDPDLLLLDEPFAGVDPKT 167
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
38-313 |
5.91e-23 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 99.15 E-value: 5.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 38 FVIVESVLEILIPTVMASMIDQGVAGGSMPAIWKFGLILLGCAVVS-LFAGFMSGRYAaIASAGFAKNLRHDLFEKV--Q 114
Cdd:cd18572 4 FLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSgLFSGLRGGCFS-YAGTRLVRRLRRDLFRSLlrQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 115 SFSFtnIDHFSTGSIITRITTDVTNIQYAFQMCIRVAVRAPLMVVVAWLFSFRISPSISMIFLIIIPILGVtltglalsV 194
Cdd:cd18572 83 DIAF--FDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIAL--------I 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 195 NPVFEKVFH-----TYDHL---NNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYE--------YFCkaeHVLAFNwp 258
Cdd:cd18572 153 TKVYGRYYRklskeIQDALaeaNQVAEEALSNIRTVRSFATEEREARRYERALDKALKlsvrqalaYAG---YVAVNT-- 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 705456738 259 ILNTCIYGAMLiiswmgtkqIVGSHNNAAVGLTTGDLTALVTYAMQILMSLNMVS 313
Cdd:cd18572 228 LLQNGTQVLVL---------FYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLG 273
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
353-577 |
6.83e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 99.08 E-value: 6.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 353 SITFNDVSFRYDVGS--ERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDV----REYDLE 426
Cdd:PRK13646 2 TIRFDNVSYTYQKGTpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 427 TLRDAVAMVLQ--KNVLFAGTIADNIRWG--NPNATDEDVR-RVCKLAQADGFIREFpkgydtyIEEGGSNVSGGQRQRL 501
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVEREIIFGpkNFKMNLDEVKnYAHRLLMDLGFSRDV-------MSQSPFQMSGGQMRKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 502 CIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIII-----AQRVAsvQESDEIIVMDGGRILDRGTHDQ 576
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIIlvshdMNEVA--RYADEVIVMKEGSIVSQTSPKE 232
|
.
gi 705456738 577 L 577
Cdd:PRK13646 233 L 233
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
359-579 |
1.64e-22 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 98.59 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 359 VSFRYDVGSERpVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYD---VSSGSLEVGGRDVREYDLETLRDA---- 431
Cdd:COG0444 9 VYFPTRRGVVK-AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELRKIrgre 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 432 VAMVLQK-----NVLFagTIADNI-------RWGNPNATDEDVRRV---CKLAQADGFIREFPkgydtyieeggSNVSGG 496
Cdd:COG0444 88 IQMIFQDpmtslNPVM--TVGDQIaeplrihGGLSKAEARERAIELlerVGLPDPERRLDRYP-----------HELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 497 QRQRLCIARALLKKPKILILDDSTSAVDTkTDR-----LIRgAFKTEIpDTTKIIIAQRVASVQE-SDEIIVMDGGRILD 570
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDV-TIQaqilnLLK-DLQREL-GLAILFITHDLGVVAEiADRVAVMYAGRIVE 231
|
....*....
gi 705456738 571 RGTHDQLLQ 579
Cdd:COG0444 232 EGPVEELFE 240
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
370-579 |
2.57e-22 |
|
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: 95.58 E-value: 2.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 370 PVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLET-LRDAVAMVLQKNVLFAG-TIA 447
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 448 DNIRWG----NPNATDEDVRRVCKLaqadgfireFPKGYDTYIEEGGsNVSGGQRQRLCIARALLKKPKILILDDST--- 520
Cdd:cd03224 94 ENLLLGayarRRAKRKARLERVYEL---------FPRLKERRKQLAG-TLSGGEQQMLAIARALMSRPKLLLLDEPSegl 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 705456738 521 --SAVDTKTDRLIRgafkteIPD--TTKIIIAQRVASVQE-SDEIIVMDGGRILDRGTHDQLLQ 579
Cdd:cd03224 164 apKIVEEIFEAIRE------LRDegVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
290-550 |
7.72e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 99.50 E-value: 7.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 290 LTTGDLtalvtyaMQILMSLNMV----SMII-VMVVIS--RADAERI---CQVLNEVSTVRDNADPIMDVPDGSITFNDV 359
Cdd:COG4178 296 ITLGGL-------MQAASAFGQVqgalSWFVdNYQSLAewRATVDRLagfEEALEAADALPEAASRIETSEDGALALEDL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 360 SFRYDVGseRPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVggrdvreydletLRDAVAMVL-QK 438
Cdd:COG4178 369 TLRTPDG--RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR------------PAGARVLFLpQR 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 439 NVLFAGTIADNIRWGNP--NATDEDVRRVCKLAQADGFIREFpkgyDTyiEEGGSNV-SGGQRQRLCIARALLKKPKILI 515
Cdd:COG4178 435 PYLPLGTLREALLYPATaeAFSDAELREALEAVGLGHLAERL----DE--EADWDQVlSLGEQQRLAFARLLLHKPDWLF 508
|
250 260 270
....*....|....*....|....*....|....*
gi 705456738 516 LDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIAQR 550
Cdd:COG4178 509 LDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
39-301 |
8.12e-22 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 96.02 E-value: 8.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 39 VIVESVLEILIPTVMASMIDQGVAGGSMPAIWKFGLILLGCAVVSLFAGFMSGRYAAIASAGFAKNLRHDLFEKVQSFSF 118
Cdd:cd18546 8 VVVDTAASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 119 TNIDHFSTGSIITRITTDVTNIQYAFQMCIRVAVRAPLMVV--VAWLFSfrISPSISMIFLIIIPILgvtltgLALSV-- 194
Cdd:cd18546 88 DFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVgiAVVLLV--LDPRLALVALAALPPL------ALATRwf 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 195 ----NPVFEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEHVLAFNWPILNTCIYGAMLI 270
Cdd:cd18546 160 rrrsSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAA 239
|
250 260 270
....*....|....*....|....*....|.
gi 705456738 271 ISWmgtkqiVGSHNNAAVGLTTGDLTALVTY 301
Cdd:cd18546 240 VLL------VGAWRVAAGTLTVGVLVAFLLY 264
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
366-566 |
1.10e-21 |
|
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: 93.93 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 366 GSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETL----RDAVAMVLQKNVL 441
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 442 FAGTIADNIRWGNP--NATDEDVRRVCKLaQADgfIREFPKGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDS 519
Cdd:cd03290 91 LNATVEENITFGSPfnKQRYKAVTDACSL-QPD--IDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 705456738 520 TSAVDTK-TDRLIRGAFKTEIPDT--TKIIIAQRVASVQESDEIIVMDGG 566
Cdd:cd03290 168 FSALDIHlSDHLMQEGILKFLQDDkrTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
39-329 |
1.32e-21 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 95.24 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 39 VIVESVLEILIPTVMASMIDQGVAGGSMPAIWKFGLILLGCAVVSLFAGFMSGRYAAIASAGFAKNLRHDLFEKVQSFS- 117
Cdd:cd18550 8 ILLSALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 118 --FTNIdhfSTGSIITRITTDVTNIQYAFQMCIRVAVRAPLMVVVAWLFSFRISPSISMIFLIIIPILGVTLTGLALSVN 195
Cdd:cd18550 88 afFTRT---RTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 196 PVFEKVFHTYDHLNNIVDENL--QGIRVVKSYDREEHESRKFGRVSERIYEYFCKAehVLAFNWpilntcIYGAMLIISW 273
Cdd:cd18550 165 KLTREQQEKLAELNSIMQETLsvSGALLVKLFGREDDEAARFARRSRELRDLGVRQ--ALAGRW------FFAALGLFTA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 705456738 274 MGTKQI--VGSHNNAAVGLTTGDLTALVTYAMQILMSLNMVSMIIVMVVISRADAERI 329
Cdd:cd18550 237 IGPALVywVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
354-548 |
2.02e-21 |
|
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: 92.54 E-value: 2.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDvgsERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREyDLETLRDAVA 433
Cdd:COG4133 3 LEAENLSCRRG---ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 MVLQKNVLFAG-TIADNIRW----GNPNATDEDVRRVCKLAQADGFIREFPKGYdtyieeggsnvSGGQRQRLCIARALL 508
Cdd:COG4133 79 YLGHADGLKPElTVRENLRFwaalYGLRADREAIDEALEAVGLAGLADLPVRQL-----------SAGQKRRVALARLLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 705456738 509 KKPKILILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIA 548
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLT 187
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
353-577 |
2.41e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 95.92 E-value: 2.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 353 SITFNDVSFRYDvgsERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYdleTLRD-A 431
Cdd:PRK10851 2 SIEIANIKKSFG---RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL---HARDrK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 432 VAMVLQKNVLFAG-TIADNIRWG--------NPN--ATDEDVRRVCKLAQADGFIREFPkgydtyieeggSNVSGGQRQR 500
Cdd:PRK10851 76 VGFVFQHYALFRHmTVFDNIAFGltvlprreRPNaaAIKAKVTQLLEMVQLAHLADRYP-----------AQLSGGQKQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 501 LCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFK---TEIPDTTKIIIAQRVASVQESDEIIVMDGGRILDRGTHDQL 577
Cdd:PRK10851 145 VALARALAVEPQILLLDEPFGALDAQVRKELRRWLRqlhEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
353-582 |
2.97e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 94.04 E-value: 2.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 353 SITFNDVSFRYDVGS--ERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREY----DLE 426
Cdd:PRK13649 2 GINLQNVSYTYQAGTpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 427 TLRDAVAMVLQ--KNVLFAGTIADNIRWGNPN--ATDEDVRRVC--KLAQAdGFIREFpkgydtyIEEGGSNVSGGQRQR 500
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALAreKLALV-GISESL-------FEKNPFELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 501 LCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIAQR----VASVqeSDEIIVMDGGRILDRGTHDQ 576
Cdd:PRK13649 154 VAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHlmddVANY--ADFVYVLEKGKLVLSGKPKD 231
|
....*.
gi 705456738 577 LLQTCD 582
Cdd:PRK13649 232 IFQDVD 237
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
354-573 |
3.79e-21 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 95.40 E-value: 3.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDvgsERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETlRDaVA 433
Cdd:PRK09452 15 VELRGISKSFD---GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN-RH-VN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 MVLQKNVLFAG-TIADNIRWG-----NPNA-TDEDVRRVCKLAQADGFIREFPKgydtyieeggsNVSGGQRQRLCIARA 506
Cdd:PRK09452 90 TVFQSYALFPHmTVFENVAFGlrmqkTPAAeITPRVMEALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 507 LLKKPKILILDDSTSAVDTKtdrlIRGAFKTEIpdttKIIiaQR--------VASVQE-----SDEIIVMDGGRILDRGT 573
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYK----LRKQMQNEL----KAL--QRklgitfvfVTHDQEealtmSDRIVVMRDGRIEQDGT 228
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
353-579 |
8.17e-21 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 92.00 E-value: 8.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 353 SITFNDVSFRYdvgSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGG------RDVREYDLE 426
Cdd:COG4161 2 SIQLKNINCFY---GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 427 TLRDAVAMVLQKNVLFAG-TIADNIRwgnpnatdEDVRRVCKLAQADGFIR---------------EFPkgydtyieegg 490
Cdd:COG4161 79 LLRQKVGMVFQQYNLWPHlTVMENLI--------EAPCKVLGLSKEQAREKamkllarlrltdkadRFP----------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 491 SNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTD----RLIRGAFKTEIpdtTKIII------AQRVASvqesdEI 560
Cdd:COG4161 140 LHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITaqvvEIIRELSQTGI---TQVIVthevefARKVAS-----QV 211
|
250
....*....|....*....
gi 705456738 561 IVMDGGRILDRGTHDQLLQ 579
Cdd:COG4161 212 VYMEKGRIIEQGDASHFTQ 230
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
374-584 |
8.40e-21 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 92.32 E-value: 8.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 374 DINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETL----RDAVAMVLQKNVLFAG-TIAD 448
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPHrTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 449 NIRWG------NPNATDEDVRRVCKLAQADGFIrefpkgyDTYIEEggsnVSGGQRQRLCIARALLKKPKILILDDSTSA 522
Cdd:cd03294 122 NVAFGlevqgvPRAEREERAAEALELVGLEGWE-------HKYPDE----LSGGMQQRVGLARALAVDPDILLMDEAFSA 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 523 VDTktdrLIRG-------AFKTEIPDTTKIIIAQRVASVQESDEIIVMDGGRILDRGTHDQLLQT-CDEY 584
Cdd:cd03294 191 LDP----LIRRemqdellRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNpANDY 256
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
354-570 |
1.16e-20 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 92.18 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDVGS------ERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLET 427
Cdd:TIGR02769 3 LEVRDVTHTYRTGGlfgakqRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 428 ---LRDAVAMVLQkNVLFAGTIADNIRW--GNPNATDEDVRRVCKLAQADGFIREF---PKGYDTYIEEggsnVSGGQRQ 499
Cdd:TIGR02769 83 rraFRRDVQLVFQ-DSPSAVNPRMTVRQiiGEPLRHLTSLDESEQKARIAELLDMVglrSEDADKLPRQ----LSGGQLQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 705456738 500 RLCIARALLKKPKILILDDSTSAVD----TKTDRLIRgAFKTEIpDTTKIIIAQRVASVQE-SDEIIVMDGGRILD 570
Cdd:TIGR02769 158 RINIARALAVKPKLIVLDEAVSNLDmvlqAVILELLR-KLQQAF-GTAYLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
387-573 |
1.37e-20 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 92.94 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 387 IVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLEtlRDAVAMVLQKNVLFAG-TIADNIRWG-----NPNAT-D 459
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH--LRHINMVFQSYALFPHmTVEENVAFGlkmrkVPRAEiK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 460 EDVRRVCKLAQADGFIREFPkgydtyieeggSNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKT-- 537
Cdd:TIGR01187 79 PRVLEALRLVQLEEFADRKP-----------HQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTiq 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 705456738 538 -EIPDTTKIIIAQRVASVQESDEIIVMDGGRILDRGT 573
Cdd:TIGR01187 148 eQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGT 184
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
296-579 |
2.73e-20 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 94.37 E-value: 2.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 296 TAL-VTYAMQIL-----------MS-------LNMVSMI----IVM---VVISRADAERI---------CQVLN-----E 335
Cdd:COG4172 185 TALdVTVQAQILdllkdlqrelgMAlllithdLGVVRRFadrvAVMrqgEIVEQGPTAELfaapqhpytRKLLAaeprgD 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 336 VSTVRDNADPIMDVPDGSITFnDVS---FRYDVGSERPVlDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDvSSGS 412
Cdd:COG4172 265 PRPVPPDAPPLLEARDLKVWF-PIKrglFRRTVGHVKAV-DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 413 LEVGGRDV---REYDLETLRDAVAMVLQKNvlFAG-----TIADNIRWG----NPNATDEDVR-RVCKLAQADG------ 473
Cdd:COG4172 342 IRFDGQDLdglSRRALRPLRRRMQVVFQDP--FGSlsprmTVGQIIAEGlrvhGPGLSAAERRaRVAEALEEVGldpaar 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 474 --FIREFpkgydtyieeggsnvSGGQRQRLCIARALLKKPKILILDDSTSAVdtktDRLIRgafkteipdttKIIIA--- 548
Cdd:COG4172 420 hrYPHEF---------------SGGQRQRIAIARALILEPKLLVLDEPTSAL----DVSVQ-----------AQILDllr 469
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 705456738 549 --QR---------------VASVqeSDEIIVMDGGRILDRGTHDQLLQ 579
Cdd:COG4172 470 dlQRehglaylfishdlavVRAL--AHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
358-580 |
3.83e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.49 E-value: 3.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 358 DVSFRYDVGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGR------DVREYDLETLRDA 431
Cdd:PRK14246 12 NISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 432 VAMVLQKNVLFAG-TIADNIRWGNPNATDEDVRRVCKLAQAD----GFIREFpkgYDTyIEEGGSNVSGGQRQRLCIARA 506
Cdd:PRK14246 92 VGMVFQQPNPFPHlSIYDNIAYPLKSHGIKEKREIKKIVEEClrkvGLWKEV---YDR-LNSPASQLSGGQQQRLTIARA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 705456738 507 LLKKPKILILDDSTSAVDTKTDRLIRgAFKTEIPDTTKIIIA----QRVASVqeSDEIIVMDGGRILDRGTHDQLLQT 580
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDIVNSQAIE-KLITELKNEIAIVIVshnpQQVARV--ADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
353-569 |
3.86e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 91.04 E-value: 3.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 353 SITFNDVSFRYDVGS--ERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVR----EYDLE 426
Cdd:PRK13641 2 SIKFENVDYIYSPGTpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 427 TLRDAVAMVLQ--KNVLFAGTIADNIRWGNPN--ATDEDVRRvcklaQADGFIREFpkGYDT-YIEEGGSNVSGGQRQRL 501
Cdd:PRK13641 82 KLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAKE-----KALKWLKKV--GLSEdLISKSPFELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 502 CIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKT-EIPDTTKIIIAQRVASVQE-SDEIIVMDGGRIL 569
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDyQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLI 224
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
372-524 |
5.21e-20 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 91.33 E-value: 5.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 372 LDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDV---REYDLETLRDAVAMVLQKNvlFAG---- 444
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDItglSGRELRPLRRRMQMVFQDP--YASlnpr 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 445 -TIADNIRWG---NPNATDEDVR-RVCKLAQADGFIREFpkgYDTYIEEggsnVSGGQRQRLCIARALLKKPKILILDDS 519
Cdd:COG4608 112 mTVGDIIAEPlriHGLASKAERReRVAELLELVGLRPEH---ADRYPHE----FSGGQRQRIGIARALALNPKLIVCDEP 184
|
....*
gi 705456738 520 TSAVD 524
Cdd:COG4608 185 VSALD 189
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
354-573 |
6.17e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 90.15 E-value: 6.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRY---DVGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVR-EYDLETLR 429
Cdd:PRK13633 5 IKCKNVSYKYesnEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSdEENLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 430 DAVAMVLQK--NVLFAGTIADNIRWGNPN---ATDEDVRRVCKLAQADGfIREFpKGYDTYIeeggsnVSGGQRQRLCIA 504
Cdd:PRK13633 85 NKAGMVFQNpdNQIVATIVEEDVAFGPENlgiPPEEIRERVDESLKKVG-MYEY-RRHAPHL------LSGGQKQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 705456738 505 RALLKKPKILILDDSTSAVDTKTDRLIRGAFK--TEIPDTTKIIIAQRVASVQESDEIIVMDGGRILDRGT 573
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKelNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
371-580 |
7.31e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 91.32 E-value: 7.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 371 VLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETlRDaVAMVLQKNVLFAG-TIADN 449
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ-RD-ICMVFQSYALFPHmSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 450 IRWG------NPNATDEDVRRVCKLAQADGFirefpkgYDTYIEEggsnVSGGQRQRLCIARALLKKPKILILDDSTSAV 523
Cdd:PRK11432 99 VGYGlkmlgvPKEERKQRVKEALELVDLAGF-------EDRYVDQ----ISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 524 DTKTDRLIRgafkteipdtTKI--------IIAQRVASVQE-----SDEIIVMDGGRILDRGTHDQLLQT 580
Cdd:PRK11432 168 DANLRRSMR----------EKIrelqqqfnITSLYVTHDQSeafavSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
38-301 |
1.08e-19 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 89.88 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 38 FVIVESVLEILIPTVMASMIDQ---------------GVAGGSMPAIWKFGLILLGCAVVSLFAGFMSGRYAAIASAGFA 102
Cdd:cd18564 7 ALLLETALRLLEPWPLKVVIDDvlgdkplpgllglapLLGPDPLALLLLAAAALVGIALLRGLASYAGTYLTALVGQRVV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 103 KNLRHDLFEKVQSFSFTNIDHFSTGSIITRITTDVTNIQyafqmciRVAVRAPL-----------MVVVAwlfsFRISPS 171
Cdd:cd18564 87 LDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQ-------DLLVSGVLplltnlltlvgMLGVM----FWLDWQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 172 ISMIFLIIIPILGVTLTGLALSVNPVFEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEH 251
Cdd:cd18564 156 LALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAAR 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 705456738 252 VLAFNWPILNTCIYGAMLIISWMGTKQIVGSHnnaavgLTTGDLTALVTY 301
Cdd:cd18564 236 LQALLSPVVDVLVAVGTALVLWFGAWLVLAGR------LTPGDLLVFLAY 279
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
353-575 |
1.13e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 88.53 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 353 SITFNDVSFRYdvGSERpVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRdvrEYDLET----- 427
Cdd:PRK11124 2 SIQLNGINCFY--GAHQ-ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGN---HFDFSKtpsdk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 428 ----LRDAVAMVLQKNVLFAG-TIADN-------IRWGNPNATDEDVRRVCKLAQADGFIREFPKgydtyieeggsNVSG 495
Cdd:PRK11124 76 aireLRRNVGMVFQQYNLWPHlTVQQNlieapcrVLGLSKDQALARAEKLLERLRLKPYADRFPL-----------HLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 496 GQRQRLCIARALLKKPKILILDDSTSAVD----TKTDRLIRGAFKTEIpdtTKII------IAQRVASvqesdEIIVMDG 565
Cdd:PRK11124 145 GQQQRVAIARALMMEPQVLLFDEPTAALDpeitAQIVSIIRELAETGI---TQVIvtheveVARKTAS-----RVVYMEN 216
|
250
....*....|
gi 705456738 566 GRILDRGTHD 575
Cdd:PRK11124 217 GHIVEQGDAS 226
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
370-577 |
1.23e-19 |
|
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: 89.53 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 370 PVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRdvreydletlrdaVAMVLQKNVLFAGTIADN 449
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 450 IRWGNpnATDE-DVRRVCKLAQADGFIREFPKGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTD 528
Cdd:cd03291 118 IIFGV--SYDEyRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 705456738 529 RLIrgaFKTEI----PDTTKIIIAQRVASVQESDEIIVMDGGRILDRGTHDQL 577
Cdd:cd03291 196 KEI---FESCVcklmANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
347-587 |
2.27e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 88.27 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 347 MDVPDGSITFNDVSFRYDvGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLE 426
Cdd:PRK13648 1 MEDKNSIIVFKNVSFQYQ-SDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 427 TLRDAVAMVLQ--KNVLFAGTIADNIRWGNPN---ATDEDVRRVCK-LAQADGfirefpkgYDTYIEEGGSnVSGGQRQR 500
Cdd:PRK13648 80 KLRKHIGIVFQnpDNQFVGSIVKYDVAFGLENhavPYDEMHRRVSEaLKQVDM--------LERADYEPNA-LSGGQKQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 501 LCIARALLKKPKILILDDSTSAVDTKTD----RLIRGAFKTEipDTTKIIIAQRVASVQESDEIIVMDGGRILDRGTHDQ 576
Cdd:PRK13648 151 VAIAGVLALNPSVIILDEATSMLDPDARqnllDLVRKVKSEH--NITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTE 228
|
250
....*....|.
gi 705456738 577 LLQTCDEYRSI 587
Cdd:PRK13648 229 IFDHAEELTRI 239
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
354-572 |
2.33e-19 |
|
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: 86.78 E-value: 2.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYdvgSERPVldDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREydLETLRDAVA 433
Cdd:cd03298 1 VRLDKIRFSY---GEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTA--APPADRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 MVLQKNVLFAG-TIADNIRWG-NPNA--TDEDVRRVCK-LAQA--DGFIREFPKgydtyieeggsNVSGGQRQRLCIARA 506
Cdd:cd03298 74 MLFQENNLFAHlTVEQNVGLGlSPGLklTAEDRQAIEVaLARVglAGLEKRLPG-----------ELSGGERQRVALARV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 705456738 507 LLKKPKILILDDSTSAVDTktdrlirgAFKTEIPDTTKIIIAQR-------VASVQES----DEIIVMDGGRILDRG 572
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDP--------ALRAEMLDLVLDLHAETkmtvlmvTHQPEDAkrlaQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
354-578 |
5.25e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 87.35 E-value: 5.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDVGSerPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYD-LETLRDAV 432
Cdd:PRK13644 2 IRLENVSYSYPDGT--PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 433 AMVLQK-NVLFAG-TIADNIRWGNPNAT--DEDVRRVCKLAQADgfirefpKGYDTYIEEGGSNVSGGQRQRLCIARALL 508
Cdd:PRK13644 80 GIVFQNpETQFVGrTVEEDLAFGPENLClpPIEIRKRVDRALAE-------IGLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 705456738 509 KKPKILILDDSTSAVDTKTDR-LIRGAFKTEIPDTTKIIIAQRVASVQESDEIIVMDGGRILDRGTHDQLL 578
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIaVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
353-568 |
5.83e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 88.93 E-value: 5.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 353 SITFNDVSFRYDvgsERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRdvREYDLETLRDAV 432
Cdd:PRK11000 3 SVTLRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK--RMNDVPPAERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 433 AMVLQKNVLFAG-TIADNIRWG------NPNATDEDVRRVCKLAQADGFIREFPKGydtyieeggsnVSGGQRQRLCIAR 505
Cdd:PRK11000 78 GMVFQSYALYPHlSVAENMSFGlklagaKKEEINQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 506 ALLKKPKILILDDSTSAVDTKtdrlIRGAFKTEIP------DTTKIIIAQ-RVASVQESDEIIVMDGGRI 568
Cdd:PRK11000 147 TLVAEPSVFLLDEPLSNLDAA----LRVQMRIEISrlhkrlGRTMIYVTHdQVEAMTLADKIVVLDAGRV 212
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
354-579 |
6.03e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 85.96 E-value: 6.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDvgsERPVldDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVReyDLETLRDAVA 433
Cdd:COG3840 2 LRLDDLTYRYG---DFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLT--ALPPAERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 MVLQKNVLFAG-TIADNIRWG-NPNA--TDEDVRRVCKLAQA---DGFIREFPkgydtyieeggSNVSGGQRQRLCIARA 506
Cdd:COG3840 75 MLFQENNLFPHlTVAQNIGLGlRPGLklTAEQRAQVEQALERvglAGLLDRLP-----------GQLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 507 LLKKPKILILDDSTSAVDT--KTD--RLIRgafktEIPDTTKIII---------AQRVAsvqesDEIIVMDGGRILDRGT 573
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPalRQEmlDLVD-----ELCRERGLTVlmvthdpedAARIA-----DRVLLVADGRIAADGP 213
|
....*.
gi 705456738 574 HDQLLQ 579
Cdd:COG3840 214 TAALLD 219
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
37-314 |
8.92e-19 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 87.18 E-value: 8.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 37 TFVIVESVLEILIPTVMASMIDQGVAGGSMPAIW-----KFGLILLGCAVVSLFAGFmsGRYAAIASAG--FAKNLRHDL 109
Cdd:cd18573 3 ALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIFglslkTFALALLGVFVVGAAANF--GRVYLLRIAGerIVARLRKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 110 FEKV--QSFSFtnIDHFSTGSIITRITTDVTNIQYAFQMCIRVAVRAPLMVVVAWLFSFRISPSISMIFLIIIPILGVTL 187
Cdd:cd18573 81 FKSIlrQDAAF--FDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 188 TGLALSVNPVFEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEHVLAFNWPILNTCIYGA 267
Cdd:cd18573 159 VFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLS 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 705456738 268 MLIISWMGTKQIVGSHnnaavgLTTGDLTALVTYAmqILMSLNMVSM 314
Cdd:cd18573 239 LLSVLYYGGSLVASGE------LTVGDLTSFLMYA--VYVGSSVSGL 277
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
366-577 |
1.10e-18 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 85.25 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 366 GSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVReYDLETLRDAVAMVLQKNVLFAG- 444
Cdd:cd03263 12 KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLGYCPQFDALFDEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 445 TIADNIR-----WGNPNAT----DEDVRRVCKL-AQADGFIREFpkgydtyieeggsnvSGGQRQRLCIARALLKKPKIL 514
Cdd:cd03263 91 TVREHLRfyarlKGLPKSEikeeVELLLRVLGLtDKANKRARTL---------------SGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 705456738 515 ILDDSTSAVDTKTDRLIRGAFKTEIPDTTkIIIAQRvaSVQE----SDEIIVMDGGRILDRGTHDQL 577
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEVRKGRS-IILTTH--SMDEaealCDRIAIMSDGKLRCIGSPQEL 219
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
371-603 |
1.11e-18 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 90.61 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 371 VLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVggrdvreydletlRDAVAMVLQKNVLFAGTIADNI 450
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA-------------ERSIAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 451 RWGNP-NATD-EDVRRVCKLaQADgfIREFPKGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKT- 527
Cdd:PTZ00243 742 LFFDEeDAARlADAVRVSQL-EAD--LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVg 818
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 705456738 528 DRLIRGAFKTEIPDTTKIIIAQRVASVQESDEIIVMDGGRILDRGTHDQLLQTcdeyrSIYQSQTksqGEGSDDDE 603
Cdd:PTZ00243 819 ERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRT-----SLYATLA---AELKENKD 886
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
353-554 |
1.53e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 85.86 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 353 SITFNDVSFRYDVgseRPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSS-----GSLEVGGRDV--REYDL 425
Cdd:PRK14258 7 AIKVNNLSFYYDT---QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 426 ETLRDAVAMVLQKNVLFAGTIADNIRWGnpnatdedVRRVC---KLaQADGFIREFPKGYDTY------IEEGGSNVSGG 496
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVYDNVAYG--------VKIVGwrpKL-EIDDIVESALKDADLWdeikhkIHKSALDLSGG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 705456738 497 QRQRLCIARALLKKPKILILDDSTSAVD----TKTDRLIRG-AFKTEIpdtTKIIIAQRVASV 554
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSlRLRSEL---TMVIVSHNLHQV 214
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
345-580 |
2.27e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.59 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 345 PIMDVPDGSITFNDVsfrydvgserPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYD 424
Cdd:PRK09536 2 PMIDVSDLSVEFGDT----------TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 425 LETLRDAVAMVLQKNVL-FAGTIADNIRWG-NPNAT-----DEDVRRVCKLAQADGfirefpkGYDTYIEEGGSNVSGGQ 497
Cdd:PRK09536 72 ARAASRRVASVPQDTSLsFEFDVRQVVEMGrTPHRSrfdtwTETDRAAVERAMERT-------GVAQFADRPVTSLSGGE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 498 RQRLCIARALLKKPKILILDDSTSAVD----TKTDRLIRgafktEIPDTTKIIIAQ----RVASvQESDEIIVMDGGRIL 569
Cdd:PRK09536 145 RQRVLLARALAQATPVLLLDEPTASLDinhqVRTLELVR-----RLVDDGKTAVAAihdlDLAA-RYCDELVLLADGRVR 218
|
250
....*....|.
gi 705456738 570 DRGTHDQLLQT 580
Cdd:PRK09536 219 AAGPPADVLTA 229
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
371-573 |
2.55e-18 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 84.31 E-value: 2.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 371 VLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETlRDaVAMVLQKNVLFAG-TIADN 449
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK-RD-ISYVPQNYALFPHmTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 450 IRWG-----NPNAT-DEDVRRVCKLAQADGFIREFPKgydtyieeggsNVSGGQRQRLCIARALLKKPKILILDDSTSAV 523
Cdd:cd03299 92 IAYGlkkrkVDKKEiERKVLEIAEMLGIDHLLNRKPE-----------TLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 705456738 524 DTKTDRLIRGAFKT--EIPDTTKIIIAQRVASVQE-SDEIIVMDGGRILDRGT 573
Cdd:cd03299 161 DVRTKEKLREELKKirKEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGK 213
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
354-527 |
3.23e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 84.91 E-value: 3.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDVGSE-RPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLEtlRdav 432
Cdd:COG4525 4 LTVRHVSVRYPGGGQpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD--R--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 433 AMVLQKNVLFAG-TIADNIRWG------NPNATDEDVRRVCKLAQADGFIREFPkgydtyieeggSNVSGGQRQRLCIAR 505
Cdd:COG4525 79 GVVFQKDALLPWlNVLDNVAFGlrlrgvPKAERRARAEELLALVGLADFARRRI-----------WQLSGGMRQRVGIAR 147
|
170 180
....*....|....*....|..
gi 705456738 506 ALLKKPKILILDDSTSAVDTKT 527
Cdd:COG4525 148 ALAADPRFLLMDEPFGALDALT 169
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
310-577 |
3.66e-18 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 89.20 E-value: 3.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 310 NMVSMIIVMVVISRADAERICQVLNEVStvRDNADPIMDVPDGSITFNDVSFRYDvgserPVLDDINLTIASGSTIGIVG 389
Cdd:TIGR01271 387 NLTTTEVEMVNVTASWDEGIGELFEKIK--QNNKARKQPNGDDGLFFSNFSLYVT-----PVLKNISFKLEKGQLLAVAG 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 390 GTGSAKSSLVQLIPRLYDVSSGSLEVGGRdvreydletlrdaVAMVLQKNVLFAGTIADNIRWGNpnATDE-DVRRVCKL 468
Cdd:TIGR01271 460 STGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNIIFGL--SYDEyRYTSVIKA 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 469 AQADGFIREFPKGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLI-RGAFKTEIPDTTKIII 547
Cdd:TIGR01271 525 CQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIfESCLCKLMSNKTRILV 604
|
250 260 270
....*....|....*....|....*....|
gi 705456738 548 AQRVASVQESDEIIVMDGGRILDRGTHDQL 577
Cdd:TIGR01271 605 TSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
358-587 |
8.39e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 83.99 E-value: 8.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 358 DVSFRYDVGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVAMVLQ 437
Cdd:PRK13642 9 NLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 438 K--NVLFAGTIADNIRWGNPN---ATDEDVRRVCKLAQADGFIrefpkgydTYIEEGGSNVSGGQRQRLCIARALLKKPK 512
Cdd:PRK13642 89 NpdNQFVGATVEDDVAFGMENqgiPREEMIKRVDEALLAVNML--------DFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 705456738 513 ILILDDSTSAVD-TKTDRLIRgaFKTEIPDT---TKIIIAQRVASVQESDEIIVMDGGRILDRGTHDQLLQTCDEYRSI 587
Cdd:PRK13642 161 IIILDESTSMLDpTGRQEIMR--VIHEIKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDMVEI 237
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
343-573 |
1.88e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 83.75 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 343 ADPIMDVPDGSITFNDvsfryDVGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQ-----LIPRLYDVSSGSLEVGG 417
Cdd:PRK13631 18 DDIILRVKNLYCVFDE-----KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVGDIYIGD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 418 RDVREY-----------DLETLRDAVAMVLQ--KNVLFAGTIADNIRWGnPNAtdedvrrvckLAQADGFIREFPKGY-- 482
Cdd:PRK13631 93 KKNNHElitnpyskkikNFKELRRRVSMVFQfpEYQLFKDTIEKDIMFG-PVA----------LGVKKSEAKKLAKFYln 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 483 -----DTYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTDR----LIRGAFKTeipDTTKIIIAQRVAS 553
Cdd:PRK13631 162 kmgldDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHemmqLILDAKAN---NKTVFVITHTMEH 238
|
250 260
....*....|....*....|.
gi 705456738 554 VQE-SDEIIVMDGGRILDRGT 573
Cdd:PRK13631 239 VLEvADEVIVMDKGKILKTGT 259
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
350-573 |
1.97e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 82.97 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 350 PDGSITFNDVSFRYDVGSErpVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGR--DVREYDLET 427
Cdd:PRK13636 2 EDYILKVEELNYNYSDGTH--ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 428 LRDAVAMVLQK--NVLFAGTIADNIRWGNPN---ATDEDVRRVCKLAQADGF--IREFPKGYdtyieeggsnVSGGQRQR 500
Cdd:PRK13636 80 LRESVGMVFQDpdNQLFSASVYQDVSFGAVNlklPEDEVRKRVDNALKRTGIehLKDKPTHC----------LSFGQKKR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 705456738 501 LCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKT--EIPDTTKIIIAQRVASVQ-ESDEIIVMDGGRILDRGT 573
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEmqKELGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGN 225
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
353-573 |
2.30e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 83.74 E-value: 2.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 353 SITFNDVSFRYDVGseRPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVReyDLE-TLRDa 431
Cdd:PRK11650 3 GLKLQAVRKSYDGK--TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVN--ELEpADRD- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 432 VAMVLQKNVLFAG-TIADNIRWGNPNA---TDEDVRRVCKLAQadgfIREFpkgyDTYIEEGGSNVSGGQRQRLCIARAL 507
Cdd:PRK11650 78 IAMVFQNYALYPHmSVRENMAYGLKIRgmpKAEIEERVAEAAR----ILEL----EPLLDRKPRELSGGQRQRVAMGRAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 508 LKKPKILILDDSTSAVDTKtdrlIRGAFKTEIPD------TTKIII----------AQRVasvqesdeiIVMDGGRILDR 571
Cdd:PRK11650 150 VREPAVFLFDEPLSNLDAK----LRVQMRLEIQRlhrrlkTTSLYVthdqveamtlADRV---------VVMNGGVAEQI 216
|
..
gi 705456738 572 GT 573
Cdd:PRK11650 217 GT 218
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
357-524 |
2.45e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 81.30 E-value: 2.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 357 NDVSFRYDvgsERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVAMVL 436
Cdd:PRK10247 11 QNVGYLAG---DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 437 QKNVLFAGTIADNIR--WGNPNATDEDVRRVCKLAQadgFirEFPkgyDTYIEEGGSNVSGGQRQRLCIARALLKKPKIL 514
Cdd:PRK10247 88 QTPTLFGDTVYDNLIfpWQIRNQQPDPAIFLDDLER---F--ALP---DTILTKNIAELSGGEKQRISLIRNLQFMPKVL 159
|
170
....*....|
gi 705456738 515 ILDDSTSAVD 524
Cdd:PRK10247 160 LLDEITSALD 169
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
34-329 |
2.83e-17 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 83.00 E-value: 2.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 34 LAPTFVI---VESVL---EILIPTVMASMIDQGVAGgsmpAIWKFGLILLGCAVVSLFAGFMSGryaaIASAGFAKNLRH 107
Cdd:cd18565 16 LAPPLLIgvaIDAVFngeASFLPLVPASLGPADPRG----QLWLLGGLTVAAFLLESLFQYLSG----VLWRRFAQRVQH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 108 DL----FEKVQSFSFTNIDHFSTGSIITRITTDVTNIQYAFQMCIRVAVRAPLMVVVAWLFSFRISPSISMIFLIIIPIL 183
Cdd:cd18565 88 DLrtdtYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 184 GVTLTGLALSVNPVFEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEHVLAFNWPILNTC 263
Cdd:cd18565 168 IAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAFFPVIRLV 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 705456738 264 IYGAMLIISWMGTKQIVGSHNNAAVGLTTGDLTALVTYAMQILMSLNMVSMIIVMVVISRADAERI 329
Cdd:cd18565 248 AGAGFVATFVVGGYWVLDGPPLFTGTLTVGTLVTFLFYTQRLLWPLTRLGDLIDQYQRAMASAKRV 313
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
372-572 |
3.23e-17 |
|
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: 80.80 E-value: 3.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 372 LDDINLTIA---SGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGR---DVR-EYDLETLRDAVAMVLQKNVLFAG 444
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRkKINLPPQQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 445 -TIADNIRWGNPNATDEdVRRVCKLAQADGFirefpkGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDSTSAV 523
Cdd:cd03297 90 lNVRENLAFGLKRKRNR-EDRISVDELLDLL------GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 705456738 524 DTKTDRLIRGAFKT--EIPDTTKIII------AQRVAsvqesDEIIVMDGGRILDRG 572
Cdd:cd03297 163 DRALRLQLLPELKQikKNLNIPVIFVthdlseAEYLA-----DRIVVMEDGRLQYIG 214
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
354-550 |
3.70e-17 |
|
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: 79.12 E-value: 3.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDVGseRPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVggrdvreydleTLRDAVA 433
Cdd:cd03223 1 IELENLSLATPDG--RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM-----------PEGEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 MVLQKNVLFAGTIADNIR--WGnpnatdedvrrvcklaqadgfirefpkgydtyieeggSNVSGGQRQRLCIARALLKKP 511
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIypWD-------------------------------------DVLSGGEQQRLAFARLLLHKP 110
|
170 180 190
....*....|....*....|....*....|....*....
gi 705456738 512 KILILDDSTSAVDTKTDRLIRGAFKTEIpdTTKIIIAQR 550
Cdd:cd03223 111 KFVFLDEATSALDEESEDRLYQLLKELG--ITVISVGHR 147
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
354-568 |
4.50e-17 |
|
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: 80.14 E-value: 4.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDVGSerPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYD---LETLRD 430
Cdd:cd03292 1 IEFINVTKTYPNGT--AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 431 AVAMVLQKNVLFAG-TIADNIRWG------NPNATDEDVRRVCKLAQADGFIREFPKGydtyieeggsnVSGGQRQRLCI 503
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFAlevtgvPPREIRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 705456738 504 ARALLKKPKILILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIAQRVASVQE--SDEIIVMDGGRI 568
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDttRHRVIALERGKL 214
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
369-580 |
6.68e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 81.30 E-value: 6.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 369 RPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYD-VS----SGSLEVGGRDVREY-DLETLRDAVAMVLQKNVLF 442
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkVSgyrySGDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 443 AGTIADNIRWGNPNATDEDVRRVCKLAQADGFIREFPKGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDSTSA 522
Cdd:PRK14271 114 PMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 705456738 523 VDTKTDRLIRGAFKTEIPDTTKIIIAQRVASVQE-SDEIIVMDGGRILDRGTHDQLLQT 580
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
354-580 |
1.03e-16 |
|
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: 80.13 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDvgsERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPR-LYDVSSGSLEVGGRDVREYDLETLRDAV 432
Cdd:COG1119 4 LELRNVTVRRG---GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 433 AMV---LQ---------KNVL---FAGTIAdniRWGNPnaTDEDVRRvcklaqADGFIREFpkGYDTYIEEGGSNVSGGQ 497
Cdd:COG1119 81 GLVspaLQlrfprdetvLDVVlsgFFDSIG---LYREP--TDEQRER------ARELLELL--GLAHLADRPFGTLSQGE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 498 RQRLCIARALLKKPKILILDDSTSAVDTKT--------DRLIRGAFKT---------EIPDTTkiiiaqrvasvqesDEI 560
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDLGArelllallDKLAAEGAPTlvlvthhveEIPPGI--------------THV 213
|
250 260
....*....|....*....|
gi 705456738 561 IVMDGGRILDRGTHDQLLQT 580
Cdd:COG1119 214 LLLKDGRVVAAGPKEEVLTS 233
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
369-548 |
1.10e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 78.43 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 369 RPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLE----------TLRDAVAMvlqk 438
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQrsevpdslplTVRDLVAM---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 439 nvlfaGTIADNIRWGNPNAtdEDVRRVCKLAQADGfIREFPK-GYDTyieeggsnVSGGQRQRLCIARALLKKPKILILD 517
Cdd:NF040873 81 -----GRWARRGLWRRLTR--DDRAAVDDALERVG-LADLAGrQLGE--------LSGGQRQRALLAQGLAQEADLLLLD 144
|
170 180 190
....*....|....*....|....*....|.
gi 705456738 518 DSTSAVDTKTDRLIRGAFKTEIPDTTKIIIA 548
Cdd:NF040873 145 EPTTGLDAESRERIIALLAEEHARGATVVVV 175
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
376-526 |
2.01e-16 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 78.36 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 376 NLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREydLETLRDAVAMVLQKNVLFAG-TIADNIRWG- 453
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTG--LAPYQRPVSMLFQENNLFAHlTVRQNIGLGl 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 705456738 454 NPNA--TDEDVRRVCKLAQADGFirefpkgyDTYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTK 526
Cdd:TIGR01277 96 HPGLklNAEQQEKVVDAAQQVGI--------ADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPL 162
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
357-580 |
2.15e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 79.43 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 357 NDVSFRYdvgSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVAMVL 436
Cdd:PRK13548 6 RNLSVRL---GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 437 QKNVL-FAGTIADNIR-----WGNPNATDED-VRRVckLAQAD--GFI-REFPKgydtyieeggsnVSGGQRQRLCIARA 506
Cdd:PRK13548 83 QHSSLsFPFTVEEVVAmgrapHGLSRAEDDAlVAAA--LAQVDlaHLAgRDYPQ------------LSGGEQQRVQLARV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 507 LL------KKPKILILDDSTSAVDT----KTDRLIRgAFKTEIPDTTKII-----IAQRVAsvqesDEIIVMDGGRILDR 571
Cdd:PRK13548 149 LAqlwepdGPPRWLLLDEPTSALDLahqhHVLRLAR-QLAHERGLAVIVVlhdlnLAARYA-----DRIVLLHQGRLVAD 222
|
....*....
gi 705456738 572 GTHDQLLQT 580
Cdd:PRK13548 223 GTPAEVLTP 231
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
371-572 |
2.67e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 78.80 E-value: 2.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 371 VLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVS-----SGSLEVGGRDVREYDLETLRDAVAMVLQ-KNVLFAG 444
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRRVQMVFQiPNPIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 445 TIADNIRWG--------NPNATDEDVRRVCKLAQADGFIREfpkgydtYIEEGGSNVSGGQRQRLCIARALLKKPKILIL 516
Cdd:PRK14247 98 SIFENVALGlklnrlvkSKKELQERVRWALEKAQLWDEVKD-------RLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 705456738 517 DDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIA---QRVASVqeSDEIIVMDGGRILDRG 572
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDMTIVLVThfpQQAARI--SDYVAFLYKGQIVEWG 227
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
371-576 |
2.98e-16 |
|
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: 78.25 E-value: 2.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 371 VLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDV---REYdlETLRDAVAMVLQKNVLFAG-TI 446
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItglPPH--EIARLGIGRTFQIPRLFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 447 ADNIR-----------WGNPNATDEDVRRvcklAQADGFIREFpkGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKILI 515
Cdd:cd03219 93 LENVMvaaqartgsglLLARARREEREAR----ERAEELLERV--GLADLADRPAGELSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 705456738 516 LDDSTSAV-DTKTDRLIRgaFKTEIPD--TTKIIIAQRVASVQE-SDEIIVMDGGRILDRGTHDQ 576
Cdd:cd03219 167 LDEPAAGLnPEETEELAE--LIRELRErgITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDE 229
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
357-578 |
3.08e-16 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 78.49 E-value: 3.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 357 NDVSFRYDvgsERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETL-RDAVAMV 435
Cdd:COG0410 7 ENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 436 LQKNVLFAG-TIADNIRWG-----NPNATDEDVRRVCKLaqadgfireFPKgydtyIEE----GGSNVSGGQRQRLCIAR 505
Cdd:COG0410 84 PEGRRIFPSlTVEENLLLGayarrDRAEVRADLERVYEL---------FPR-----LKErrrqRAGTLSGGEQQMLAIGR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 506 ALLKKPKILILDDST-----SAVDTktdrlIRGAFKtEIPD--TTKIIIAQRVASVQE-SDEIIVMDGGRILDRGTHDQL 577
Cdd:COG0410 150 ALMSRPKLLLLDEPSlglapLIVEE-----IFEIIR-RLNRegVTILLVEQNARFALEiADRAYVLERGRIVLEGTAAEL 223
|
.
gi 705456738 578 L 578
Cdd:COG0410 224 L 224
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
374-582 |
3.11e-16 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 80.54 E-value: 3.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 374 DINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGR---DVRE-YDLETLRDAVAMVLQKNVLFAG-TIAD 448
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfDSRKgIFLPPEKRRIGYVFQEARLFPHlSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 449 NIRWGNPNATDEDVRrvcklAQADGFIREFpkGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTD 528
Cdd:TIGR02142 95 NLRYGMKRARPSERR-----ISFERVIELL--GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 705456738 529 RLIRgAFKTEIPDTTKIIIAQRVASVQE----SDEIIVMDGGRILDRGTHDQLLQTCD 582
Cdd:TIGR02142 168 YEIL-PYLERLHAEFGIPILYVSHSLQEvlrlADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
354-524 |
4.87e-16 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 77.70 E-value: 4.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDVGSERpvlddINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVReyDLETLRDAVA 433
Cdd:PRK10771 2 LKLTDITWLYHHLPMR-----FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHT--TTPPSRRPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 MVLQKNVLFAG-TIADNIRWG-NPNATDEDVRRvCKLAQADGFIrefpkGYDTYIEEGGSNVSGGQRQRLCIARALLKKP 511
Cdd:PRK10771 75 MLFQENNLFSHlTVAQNIGLGlNPGLKLNAAQR-EKLHAIARQM-----GIEDLLARLPGQLSGGQRQRVALARCLVREQ 148
|
170
....*....|...
gi 705456738 512 KILILDDSTSAVD 524
Cdd:PRK10771 149 PILLLDEPFSALD 161
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
341-577 |
5.68e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 79.37 E-value: 5.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 341 DNADPIMDVPDGSITFN---DVSFRYDVGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGG 417
Cdd:PRK15079 3 EGKKVLLEVADLKVHFDikdGKQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 418 RDVREYDLETLRDA---VAMVLQK-------NVLFAGTIADNIRWGNPNATDEDVR-RVCKLAQADGFIrefPKGYDTYI 486
Cdd:PRK15079 83 KDLLGMKDDEWRAVrsdIQMIFQDplaslnpRMTIGEIIAEPLRTYHPKLSRQEVKdRVKAMMLKVGLL---PNLINRYP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 487 EEggsnVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKT---EIpDTTKIIIAQRVASVQE-SDEIIV 562
Cdd:PRK15079 160 HE----FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQlqrEM-GLSLIFIAHDLAVVKHiSDRVLV 234
|
250
....*....|....*
gi 705456738 563 MDGGRILDRGTHDQL 577
Cdd:PRK15079 235 MYLGHAVELGTYDEV 249
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
354-524 |
5.77e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 78.19 E-value: 5.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDVGS------ERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLE- 426
Cdd:PRK10419 4 LNVSGLSHHYAHGGlsgkhqHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 427 --TLRDAVAMVLQknvlfagtiaDNIRWGNPNAT-----DEDVRRVCKLAQADGFIR--------EFPkgyDTYIEEGGS 491
Cdd:PRK10419 84 rkAFRRDIQMVFQ----------DSISAVNPRKTvreiiREPLRHLLSLDKAERLARasemlravDLD---DSVLDKRPP 150
|
170 180 190
....*....|....*....|....*....|...
gi 705456738 492 NVSGGQRQRLCIARALLKKPKILILDDSTSAVD 524
Cdd:PRK10419 151 QLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
354-582 |
6.48e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 78.62 E-value: 6.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDVGS--ERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDV----REYDLET 427
Cdd:PRK13643 2 IKFEKVNYTYQPNSpfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 428 LRDAVAMVLQ--KNVLFAGTIADNIRWGNPN---ATDEDVRRVCKLAQADGFIREFpkgydtyIEEGGSNVSGGQRQRLC 502
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGPQNfgiPKEKAEKIAAEKLEMVGLADEF-------WEKSPFELSGGQMRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 503 IARALLKKPKILILDDSTSAVDTKTDRLIRGAFKTeIPDT--TKIIIAQRVASVQE-SDEIIVMDGGRILDRGTHDQLLQ 579
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFES-IHQSgqTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQ 233
|
...
gi 705456738 580 TCD 582
Cdd:PRK13643 234 EVD 236
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
344-524 |
7.23e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 77.51 E-value: 7.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 344 DPIMDVPDGSITFNDvsfrydvgseRPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVS-----SGSLEVGGR 418
Cdd:PRK14239 3 EPILQVSDLSVYYNK----------KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 419 DV--REYDLETLRDAVAMVLQKNVLFAGTIADNIRWG-------NPNATDEDVRRVCKLAQADGFIREfpkgydtYIEEG 489
Cdd:PRK14239 73 NIysPRTDTVDLRKEIGMVFQQPNPFPMSIYENVVYGlrlkgikDKQVLDEAVEKSLKGASIWDEVKD-------RLHDS 145
|
170 180 190
....*....|....*....|....*....|....*
gi 705456738 490 GSNVSGGQRQRLCIARALLKKPKILILDDSTSAVD 524
Cdd:PRK14239 146 ALGLSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
353-572 |
7.31e-16 |
|
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: 76.05 E-value: 7.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 353 SITFNDVSF---RYDVGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQ-LIPRLYDVS-SGSLEVGGRDVreyDLET 427
Cdd:cd03213 3 TLSFRNLTVtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNaLAGRRTGLGvSGEVLINGRPL---DKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 428 LRDAVAMVLQKNVLFagtiadnirwgnPNAT-DEDVRRVCKLaqadgfirefpkgydtyieeggSNVSGGQRQRLCIARA 506
Cdd:cd03213 80 FRKIIGYVPQDDILH------------PTLTvRETLMFAAKL----------------------RGLSGGERKRVSIALE 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 507 LLKKPKILILDDSTSAVDTKTDRLIRGAFKtEIPDTTKIIIA---QRVASVQES-DEIIVMDGGRILDRG 572
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLR-RLADTGRTIICsihQPSSEIFELfDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
351-572 |
9.67e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 77.85 E-value: 9.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 351 DGSITFNDVSFRYDVGSErpVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRD 430
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTK--ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 431 AVAMVLQ--KNVLFAGTIADNIRWGNPN---ATDEDVRRVCKLAQADGFirefpkgYDtYIEEGGSNVSGGQRQRLCIAR 505
Cdd:PRK13647 80 KVGLVFQdpDDQVFSSTVWDDVAFGPVNmglDKDEVERRVEEALKAVRM-------WD-FRDKPPYHLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 705456738 506 ALLKKPKILILDDSTSAVDTKTDRLIRgafktEIPD------TTKIIIAQRVASVQE-SDEIIVMDGGRILDRG 572
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLM-----EILDrlhnqgKTVIVATHDVDLAAEwADQVIVLKEGRVLAEG 220
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
357-573 |
1.10e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 77.43 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 357 NDVSFRYDVGSErpVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVReYDLETL---RDAVA 433
Cdd:PRK13639 5 RDLKYSYPDGTE--ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLlevRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 MVLQK--NVLFAGTIADNIRWGNPN---ATDEDVRRVCKLAQADGFirefpKGYDtyiEEGGSNVSGGQRQRLCIARALL 508
Cdd:PRK13639 82 IVFQNpdDQLFAPTVEEDVAFGPLNlglSKEEVEKRVKEALKAVGM-----EGFE---NKPPHHLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 509 KKPKILILDDSTSAVD----TKTDRLIRGAFKTEIpdtTKIIIAQRVASVQE-SDEIIVMDGGRILDRGT 573
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDpmgaSQIMKLLYDLNKEGI---TIIISTHDVDLVPVyADKVYVMSDGKIIKEGT 220
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
342-524 |
1.55e-15 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 79.73 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 342 NADPIMDVPDGSITFNDVsfrydvGSERPVLDDINLTIASGSTIGIVGGTGSAKS----SLVQLIPRLYDVSSGSLEVGG 417
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQG------GGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 418 RDVREYDLETLR----DAVAMVLQK-----NVLFagTIADNI----RWGNPnATDEDVR-RVCKLAQADGfIREFPKGYD 483
Cdd:COG4172 76 QDLLGLSERELRrirgNRIAMIFQEpmtslNPLH--TIGKQIaevlRLHRG-LSGAAARaRALELLERVG-IPDPERRLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 705456738 484 TYIEEggsnVSGGQRQRLCIARALLKKPKILILDDSTSAVD 524
Cdd:COG4172 152 AYPHQ----LSGGQRQRVMIAMALANEPDLLIADEPTTALD 188
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
370-568 |
1.69e-15 |
|
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: 74.39 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 370 PVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVReydLETLRDA----VAMVLQknvlfagt 445
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS---FASPRDArragIAMVYQ-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 446 iadnirwgnpnatdedvrrvcklaqadgfirefpkgydtyieeggsnVSGGQRQRLCIARALLKKPKILILDDSTSAVDT 525
Cdd:cd03216 83 -----------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 705456738 526 K-TDRLIR--GAFKTEipDTTKIIIAQRVASVQE-SDEIIVMDGGRI 568
Cdd:cd03216 116 AeVERLFKviRRLRAQ--GVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
40-315 |
1.77e-15 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 77.20 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 40 IVESVLEILIPTVMASMID------QGVAGGSMPAIWKFGLILLGcaVVSLFAGFMSGRYAAIASAG--FAKNLRHDLFE 111
Cdd:cd18574 6 LAAALVNIQIPLLLGDLVNvisrslKETNGDFIEDLKKPALKLLG--LYLLQSLLTFAYISLLSVVGerVAARLRNDLFS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 112 KVQSFSFTNIDHFSTGSIITRITTDVTNIQYAFQMCIRVAVRApLMVVVAWLFS-FRISPSISMIFLIIIPILGVTLTGL 190
Cdd:cd18574 84 SLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRS-VTQTVGCVVSlYLISPKLTLLLLVIVPVVVLVGTLY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 191 A-----LSVNpVFEKVFHTydhlNNIVDENLQGIRVVKSYDREEHESRKFGRVSERiyeyFCKAEHVLAFNWPIL----N 261
Cdd:cd18574 163 GsflrkLSRR-AQAQVAKA----TGVADEALGNIRTVRAFAMEDRELELYEEEVEK----AAKLNEKLGLGIGIFqglsN 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 705456738 262 TCIYGAMLIISWMGTKQIVGSHnnaavgLTTGDLTALVTYAMQILMSLNMVSMI 315
Cdd:cd18574 234 LALNGIVLGVLYYGGSLVSRGE------LTAGDLMSFLVATQTIQRSLAQLSVL 281
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
354-572 |
1.91e-15 |
|
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: 75.31 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDvgsERPVLDDINLTIASGSTiGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREyDLETLRDAVA 433
Cdd:cd03264 1 LQLENLTKRYG---KKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 MVLQKNVLFAGTIA----DNIRW-GNPNATDEDvRRVCKLAQADGFIREfpkgYDTYIeeggSNVSGGQRQRLCIARALL 508
Cdd:cd03264 76 YLPQEFGVYPNFTVreflDYIAWlKGIPSKEVK-ARVDEVLELVNLGDR----AKKKI----GSLSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 705456738 509 KKPKILILDDSTSAVDTKTdrliRGAFKTEIPD--TTKIII--AQRVASVQES-DEIIVMDGGRILDRG 572
Cdd:cd03264 147 GDPSILIVDEPTAGLDPEE----RIRFRNLLSElgEDRIVIlsTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
369-592 |
1.99e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 78.34 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 369 RPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVReyDLETLRDAVAMVLQKNVLFAG-TIA 447
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPINMMFQSYALFPHmTVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 448 DNIRWG---NPNATDEDVRRVCK---LAQADGFIREFPKgydtyieeggsNVSGGQRQRLCIARALLKKPKILILDDSTS 521
Cdd:PRK11607 110 QNIAFGlkqDKLPKAEIASRVNEmlgLVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 705456738 522 AVDTKtdrlIRGAFKTEIPDTTKIIIAQRVASVQESDEIIVMdGGR--ILDRGTHDQLlqtcDEYRSIYQSQT 592
Cdd:PRK11607 179 ALDKK----LRDRMQLEVVDILERVGVTCVMVTHDQEEAMTM-AGRiaIMNRGKFVQI----GEPEEIYEHPT 242
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
342-573 |
2.18e-15 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 77.46 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 342 NADPIMDVPDGSITFN----DVSfrydvgserpVLDDINLTIASGSTIGIVGGTGSAKS----SLVQLIPRlYDVSSGSL 413
Cdd:PRK09473 8 QADALLDVKDLRVTFStpdgDVT----------AVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 414 EVGGRDV---REYDLETLR-DAVAMVLQK----------------NVLFAgtiadNIRWGNPNATDEDVRRV--CKLAQA 471
Cdd:PRK09473 77 TFNGREIlnlPEKELNKLRaEQISMIFQDpmtslnpymrvgeqlmEVLML-----HKGMSKAEAFEESVRMLdaVKMPEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 472 DGFIREFPKGYdtyieeggsnvSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIR---GAFKTEIpDTTKIIIA 548
Cdd:PRK09473 152 RKRMKMYPHEF-----------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMtllNELKREF-NTAIIMIT 219
|
250 260
....*....|....*....|....*.
gi 705456738 549 QRVASVQES-DEIIVMDGGRILDRGT 573
Cdd:PRK09473 220 HDLGVVAGIcDKVLVMYAGRTMEYGN 245
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
354-572 |
3.41e-15 |
|
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: 74.56 E-value: 3.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYdvgSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREydletLRDAVA 433
Cdd:cd03268 1 LKTNDLTKTY---GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-----NIEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 MVlqknvlfaGTIADNIRWgNPNAT-DEDVRRVCKLAQadgfIREfpKGYDTYIEEGG---------SNVSGGQRQRLCI 503
Cdd:cd03268 73 RI--------GALIEAPGF-YPNLTaRENLRLLARLLG----IRK--KRIDEVLDVVGlkdsakkkvKGFSLGMKQRLGI 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 705456738 504 ARALLKKPKILILDDSTSAVDTK----TDRLIRGAFKTEIpdtTKIIIAQRVASVQE-SDEIIVMDGGRILDRG 572
Cdd:cd03268 138 ALALLGNPDLLILDEPTNGLDPDgikeLRELILSLRDQGI---TVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
352-600 |
3.45e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 76.20 E-value: 3.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 352 GSITFNDVSFRYDVGS--ERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGG-------RDVRE 422
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 423 ydLETLRDAVAMVLQ--KNVLFAGTIADNIRWG--NPNATDEDV-RRVCKLAQADGFIREfpkgydtYIEEGGSNVSGGQ 497
Cdd:PRK13645 85 --VKRLRKEIGLVFQfpEYQLFQETIEKDIAFGpvNLGENKQEAyKKVPELLKLVQLPED-------YVKRSPFELSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 498 RQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKTEIPDTTK--IIIAQRVASV-QESDEIIVMDGGRILDRG-- 572
Cdd:PRK13645 156 KRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKriIMVTHNMDQVlRIADEVIVMHEGKVISIGsp 235
|
250 260 270
....*....|....*....|....*....|...
gi 705456738 573 ----THDQLLQTCD-EYRSIYQSQTKSQGEGSD 600
Cdd:PRK13645 236 feifSNQELLTKIEiDPPKLYQLMYKLKNKGID 268
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
368-570 |
3.52e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 75.89 E-value: 3.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 368 ERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDV---REYdletlRDA--VAMVLQkNVLf 442
Cdd:COG1101 18 EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtklPEY-----KRAkyIGRVFQ-DPM- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 443 AGT-----IADN------------IRWGNPNATDEDVRRvcKLAQADgfirefpKGYDTYIEEGGSNVSGGQRQRLCIAR 505
Cdd:COG1101 91 MGTapsmtIEENlalayrrgkrrgLRRGLTKKRRELFRE--LLATLG-------LGLENRLDTKVGLLSGGQRQALSLLM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 705456738 506 ALLKKPKILILDDSTSAVDTKTDRLIrgafkTEIpdTTKIIIAQRVAS----------VQESDEIIVMDGGRI-LD 570
Cdd:COG1101 162 ATLTKPKLLLLDEHTAALDPKTAALV-----LEL--TEKIVEENNLTTlmvthnmeqaLDYGNRLIMMHEGRIiLD 230
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
354-572 |
4.51e-15 |
|
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: 74.71 E-value: 4.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRY-DVGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLR--- 429
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRrlg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 430 ---DAVA----MVLQKNVLFAGTIADNIRwgnpnatDEDVRRVCKLAQADGFirefpkgyDTYIEEGGSNVSGGQRQRLC 502
Cdd:cd03266 82 fvsDSTGlydrLTARENLEYFAGLYGLKG-------DELTARLEELADRLGM--------EELLDRRVGGFSTGMRQKVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 705456738 503 IARALLKKPKILILDDSTSAVDTKTDRLIRGAFKtEIPDTTKII-----IAQRVASVqeSDEIIVMDGGRILDRG 572
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDVMATRALREFIR-QLRALGKCIlfsthIMQEVERL--CDRVVVLHRGRVVYEG 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
322-517 |
5.23e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.80 E-value: 5.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 322 SRADA-ERicqvLNEVSTVRDNADPIMDVPDGS------ITFNDVSFRYDvgsERPVLDDINLTIASGSTIGIVGGTGSA 394
Cdd:COG0488 281 SRIKAlEK----LEREEPPRRDKTVEIRFPPPErlgkkvLELEGLSKSYG---DKTLLDDLSLRIDRGDRIGLIGPNGAG 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 395 KSSLVQLIPRLYDVSSGSLEVGGRDVREY---DLETLRDavamvlQKNVLfagtiaDNIRWGNPNATDEDVRRVCKL--- 468
Cdd:COG0488 354 KSTLLKLLAGELEPDSGTVKLGETVKIGYfdqHQEELDP------DKTVL------DELRDGAPGGTEQEVRGYLGRflf 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 705456738 469 --AQADGFIREFpkgydtyieeggsnvSGGQRQRLCIARALLKKPKILILD 517
Cdd:COG0488 422 sgDDAFKPVGVL---------------SGGEKARLALAKLLLSPPNVLLLD 457
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
371-524 |
6.00e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 74.88 E-value: 6.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 371 VLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVS-----SGSLEVGGRDVREYDLETL--RDAVAMVLQ-KNVLF 442
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDPIevRREVGMVFQyPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 443 AGTIADNIRWG--------NPNATDEDVRRVCKLAQADGFIREFPKGYdtyieegGSNVSGGQRQRLCIARALLKKPKIL 514
Cdd:PRK14267 99 HLTIYDNVAIGvklnglvkSKKELDERVEWALKKAALWDEVKDRLNDY-------PSNLSGGQRQRLVIARALAMKPKIL 171
|
170
....*....|
gi 705456738 515 ILDDSTSAVD 524
Cdd:PRK14267 172 LMDEPTANID 181
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
71-339 |
1.20e-14 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 75.18 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 71 KFGLILLGCAVVSLFAGFMSGRYAAIASAGFAKNLRHDLFEKV----QSFsFTNIDHfSTGSIITRITTDVTNIQYAFQM 146
Cdd:cd18578 53 FWALMFLVLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAIlrqdIAW-FDDPEN-STGALTSRLSTDASDVRGLVGD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 147 CIRVAVRAPLMVVVAWLFSFRISPSISMIFLIIIPILGVT-------LTGLALSVNPVFEKVfhtydhlNNIVDENLQGI 219
Cdd:cd18578 131 RLGLILQAIVTLVAGLIIAFVYGWKLALVGLATVPLLLLAgylrmrlLSGFEEKNKKAYEES-------SKIASEAVSNI 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 220 RVVKSYDREEHESRKFGRVSERIYEYFCKAEHVLAFNWPILNTCIYGAMLIISWMGTKQIvgshnnaavglTTGDLTalV 299
Cdd:cd18578 204 RTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLV-----------ANGEYT--F 270
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 705456738 300 TYAMQILMSLNMVSMIIVMVV-----ISRAD--AERICQVLNEVSTV 339
Cdd:cd18578 271 EQFFIVFMALIFGAQSAGQAFsfapdIAKAKaaAARIFRLLDRKPEI 317
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
371-586 |
1.23e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 74.02 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 371 VLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVG------GRDVREYD--LETLRDAVAMVLQKNVLF 442
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGditidtARSLSQQKglIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 443 AG-TIADNIRWG----NPNATDEDVRRVCKLAQADGFIRE---FPKgydtyieeggsNVSGGQRQRLCIARALLKKPKIL 514
Cdd:PRK11264 98 PHrTVLENIIEGpvivKGEPKEEATARARELLAKVGLAGKetsYPR-----------RLSGGQQQRVAIARALAMRPEVI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 705456738 515 ILDDSTSAVDTK-------TDRLIRGAFKTEIPDTTKIIIAQRVAsvqesDEIIVMDGGRILDRGTHDQLLQTCDEYRS 586
Cdd:PRK11264 167 LFDEPTSALDPElvgevlnTIRQLAQEKRTMVIVTHEMSFARDVA-----DRAIFMDQGRIVEQGPAKALFADPQQPRT 240
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
371-580 |
1.46e-14 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 73.33 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 371 VLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVReyDLETLRDA---VAMVLQKNVLFAG-TI 446
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDIT--KLPPHERAragIAYVPQGREIFPRlTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 447 ADNIRWGNPNATDEDvRRVcklaqaDGFIRE-FPKGYDTYIEEGGsNVSGGQRQRLCIARALLKKPKILILDDSTSAvdt 525
Cdd:TIGR03410 93 EENLLTGLAALPRRS-RKI------PDEIYElFPVLKEMLGRRGG-DLSGGQQQQLAIARALVTRPKLLLLDEPTEG--- 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 705456738 526 ktdrlIRGAFKTEIPDTTKIIIAQRVASV-----------QESDEIIVMDGGRILDRGTHDQLLQT 580
Cdd:TIGR03410 162 -----IQPSIIKDIGRVIRRLRAEGGMAIllveqyldfarELADRYYVMERGRVVASGAGDELDED 222
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
372-593 |
1.67e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 74.05 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 372 LDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDV-----SSGSLEVGGRDVREYDLE--TLRDAVAMVLQKNVLFAG 444
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 445 TIADNIRWGN-----PNATDEDVRRvcKLAQADGFIREFPKgydtyIEEGGSNVSGGQRQRLCIARALLKKPKILILDDS 519
Cdd:PRK14243 106 SIYDNIAYGAringyKGDMDELVER--SLRQAALWDEVKDK-----LKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 705456738 520 TSAVDTKTDRLIRGAFKTEIPDTTKIIIAQRVASVQESDEIIVMDGGRILDRGTHDQLLQTCDEYRSIYQSQTK 593
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRYGYLVEFDRTEKIFNSPQQ 252
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
374-595 |
1.71e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 75.84 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 374 DINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDA----VAMVLQKNVLFAG-TIAD 448
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPHmTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 449 NIRWGNPNATDEDVRRVCKLAQAdgfIREFpkGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTktd 528
Cdd:PRK10070 126 NTAFGMELAGINAEERREKALDA---LRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP--- 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 705456738 529 rLIRGAFKTEI------PDTTKIIIAQRV-ASVQESDEIIVMDGGRILDRGTHDQLLQ--TCDEYRSIYQSQTKSQ 595
Cdd:PRK10070 198 -LIRTEMQDELvklqakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNnpANDYVRTFFRGVDISQ 272
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
368-578 |
1.72e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 73.85 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 368 ERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRD---VREYD----------LETLRDAVAM 434
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlVRDKDgqlkvadknqLRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 435 VLQK-NVLFAGTIADNIRwgnpnatdEDVRRVCKLAQADGFIREFPKGYDTYIEEGG-----SNVSGGQRQRLCIARALL 508
Cdd:PRK10619 97 VFQHfNLWSHMTVLENVM--------EAPIQVLGLSKQEARERAVKYLAKVGIDERAqgkypVHLSGGQQQRVSIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 705456738 509 KKPKILILDDSTSAVDTK-TDRLIRGAFKTEIPDTTKIIIAQRVASVQE-SDEIIVMDGGRILDRGTHDQLL 578
Cdd:PRK10619 169 MEPEVLLFDEPTSALDPElVGEVLRIMQQLAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
366-569 |
2.45e-14 |
|
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: 72.69 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 366 GSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLydVSSGSLeVGGR---DVREYDLETLRDAVAMVLQKNVLF 442
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR--VEGGGT-TSGQilfNGQPRKPDQFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 443 AG-TIADNIRWGN----PNATDEDVRR----VCKLAQ-ADGFIRefpkgyDTYIEeggsNVSGGQRQRLCIARALLKKPK 512
Cdd:cd03234 94 PGlTVRETLTYTAilrlPRKSSDAIRKkrveDVLLRDlALTRIG------GNLVK----GISGGERRRVSIAVQLLWDPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 705456738 513 ILILDDSTSAVDTKTDRLIrGAFKTEIPDTTKIIIA---QRVASV-QESDEIIVMDGGRIL 569
Cdd:cd03234 164 VLILDEPTSGLDSFTALNL-VSTLSQLARRNRIVILtihQPRSDLfRLFDRILLLSSGEIV 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
356-517 |
2.59e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 75.87 E-value: 2.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 356 FNDVSFRYDvgsERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGR--------DVREYDLET 427
Cdd:COG0488 1 LENLSKSFG---GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGlrigylpqEPPLDDDLT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 428 LRDAVAMVLQKnvlfAGTIADNIR--WGNPNATDEDVRRVCKL----AQADGFirefpkGYDTYIEE--GG--------- 490
Cdd:COG0488 78 VLDTVLDGDAE----LRALEAELEelEAKLAEPDEDLERLAELqeefEALGGW------EAEARAEEilSGlgfpeedld 147
|
170 180 190
....*....|....*....|....*....|
gi 705456738 491 ---SNVSGGQRQRLCIARALLKKPKILILD 517
Cdd:COG0488 148 rpvSELSGGWRRRVALARALLSEPDLLLLD 177
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
38-313 |
3.00e-14 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 73.82 E-value: 3.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 38 FVIVESVLEILIPTVMASMIDQGVAG------GSMPAIWKFGLILLGCAVVSLFAGFMSGRYAAIASAGFAKNLRHDLFE 111
Cdd:cd18780 4 ALLVSSGTNLALPYFFGQVIDAVTNHsgsggeEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 112 K--VQSFSFtnIDHFSTGSIITRITTDVTNIQYAFQMCIRVAVRAPLMVVVAWLFSFRISPSISMIFLIIIPILGV---- 185
Cdd:cd18780 84 AiiAQEIAF--FDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIgavi 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 186 -----------TLTGLALSvnpvfekvfhtydhlNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEHVLA 254
Cdd:cd18780 162 ygkyvrklskkFQDALAAA---------------STVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASG 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 705456738 255 FNWPILNTCIYGAMLIISWMGTKQIVGSHnnaavgLTTGDLTALVTYAMQILMSLNMVS 313
Cdd:cd18780 227 GFNGFMGAAAQLAIVLVLWYGGRLVIDGE------LTTGLLTSFLLYTLTVAMSFAFLS 279
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
372-524 |
3.14e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 74.23 E-value: 3.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 372 LDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLET---LRDAVAMVLQ---------KN 439
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqklLRQKIQIVFQnpygslnprKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 440 VlfaGTIAdnirwGNPNATDEDVRRVCKLAQADGFIREF---PKGYDTYIEEggsnVSGGQRQRLCIARALLKKPKILIL 516
Cdd:PRK11308 111 V---GQIL-----EEPLLINTSLSAAERREKALAMMAKVglrPEHYDRYPHM----FSGGQRQRIAIARALMLDPDVVVA 178
|
....*...
gi 705456738 517 DDSTSAVD 524
Cdd:PRK11308 179 DEPVSALD 186
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
369-527 |
4.26e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 72.42 E-value: 4.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 369 RPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETlrdavAMVLQKNVLFA-GTIA 447
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVFQNEGLLPwRNVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 448 DNIRW-----GNPNATDEDV-RRVCKLAQADGFIREFPkgydtyieeggSNVSGGQRQRLCIARALLKKPKILILDDSTS 521
Cdd:PRK11248 89 DNVAFglqlaGVEKMQRLEIaHQMLKKVGLEGAEKRYI-----------WQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
....*.
gi 705456738 522 AVDTKT 527
Cdd:PRK11248 158 ALDAFT 163
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
372-577 |
7.18e-14 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 71.25 E-value: 7.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 372 LDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREyDLETLRDAVAMVLQ-----------KNV 440
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQdlsvddeltgwENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 441 LFAGTIadnirWGNPNA-----TDEDVRRVCKLAQADGFIREFpkgydtyieeggsnvSGGQRQRLCIARALLKKPKILI 515
Cdd:cd03265 95 YIHARL-----YGVPGAerrerIDELLDFVGLLEAADRLVKTY---------------SGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 705456738 516 LDDSTSAVDTKTD----RLIRGAFKTEipDTTKIIIAQRVASVQE-SDEIIVMDGGRILDRGTHDQL 577
Cdd:cd03265 155 LDEPTIGLDPQTRahvwEYIEKLKEEF--GMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
342-580 |
9.33e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.97 E-value: 9.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 342 NADPIMDVPDGSITFNDVsfrydvGSERPVLDDINLTIASGSTIGIVGGTGSAKS----SLVQLIPR---LYdvSSGSLE 414
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQ------QTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppvVY--PSGDIR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 415 VGGRDVREYDLETLR----DAVAMVLQK-----NVLFagTIADNIR--------WGNPNATDEDVR---RVcKLAQADGF 474
Cdd:PRK15134 73 FHGESLLHASEQTLRgvrgNKIAMIFQEpmvslNPLH--TLEKQLYevlslhrgMRREAARGEILNcldRV-GIRQAAKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 475 IREFPKgydtyieeggsNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTD----RLIRgAFKTEIpDTTKIIIAQR 550
Cdd:PRK15134 150 LTDYPH-----------QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQaqilQLLR-ELQQEL-NMGLLFITHN 216
|
250 260 270
....*....|....*....|....*....|.
gi 705456738 551 VASVQE-SDEIIVMDGGRILDRGTHDQLLQT 580
Cdd:PRK15134 217 LSIVRKlADRVAVMQNGRCVEQNRAATLFSA 247
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
374-582 |
1.07e-13 |
|
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: 72.83 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 374 DINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGR----DVREYDLETLRDAVAMVLQKNVLFAG-TIAD 448
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdSARGIFLPPHRRRIGYVFQEARLFPHlSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 449 NIRWGnpnatdedVRRVCKLAQADGFirefpkgyDTYIEEGG---------SNVSGGQRQRLCIARALLKKPKILILDDS 519
Cdd:COG4148 97 NLLYG--------RKRAPRAERRISF--------DEVVELLGighlldrrpATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 705456738 520 TSAVDtktdrlirGAFKTEI-------PDTTKIII---------AQRVAsvqesDEIIVMDGGRILDRGTHDQLLQTCD 582
Cdd:COG4148 161 LAALD--------LARKAEIlpylerlRDELDIPIlyvshsldeVARLA-----DHVVLLEQGRVVASGPLAEVLSRPD 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
347-570 |
1.10e-13 |
|
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: 70.93 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 347 MDVPDGS-ITFNDVSFRYDVGSER-PVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYD 424
Cdd:COG4181 1 MSSSSAPiIELRGLTKTVGTGAGElTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 425 letlRDAVAMVLQKNVLF---------AGTIADNI-----RWGNPNATD---EDVRRVcKLAQadgfiRE--FPKGydty 485
Cdd:COG4181 81 ----EDARARLRARHVGFvfqsfqllpTLTALENVmlpleLAGRRDARArarALLERV-GLGH-----RLdhYPAQ---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 486 ieeggsnVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLI----------RGafkteipdTTKIII------AQ 549
Cdd:COG4181 147 -------LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIidllfelnreRG--------TTLVLVthdpalAA 211
|
250 260
....*....|....*....|.
gi 705456738 550 RvasvqeSDEIIVMDGGRILD 570
Cdd:COG4181 212 R------CDRVLRLRAGRLVE 226
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
25-518 |
1.13e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 73.85 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 25 LREYKKDTILAPTFVIVESVLEI-LIPTVMASMIDqgVAGGSMPAIWKFGLILLGCAVVSLFAGFmsgryaAIASAG--F 101
Cdd:PRK10522 8 WRQYRWPFISVMALSLASAALGIgLIAFINQRLIE--TADTSLLVLPEFLGLLLLLMAVTLGSQL------ALTTLGhhF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 102 AKNLRHDLFEKVQSFSFTNIDHFSTGSIITRITTDVTNIQYAFqmcirvaVRAPLMV-----------VVAWLfsfriSP 170
Cdd:PRK10522 80 VYRLRSEFIKRILDTHVERIEQLGSASLLASLTSDVRNITIAF-------VRLPELVqgiiltlgsaaYLAWL-----SP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 171 SIsmiFLIIIPILGVTLTGLALSVNPV---FEKVFHTYDHLNNivdeNLQGI------------RVVKSYDRE-EHESRK 234
Cdd:PRK10522 148 KM---LLVTAIWMAVTIWGGFVLVARVykhMATLRETEDKLYN----DYQTVlegrkeltlnreRAEYVFENEyEPDAQE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 235 FGRVSERIYEYfckaeHVLAFNWPilNTCIYGAMLIISWMgtkqivgshnnaAVGLTTGDLTALVTYAMQIL-MSLNMVS 313
Cdd:PRK10522 221 YRHHIIRADTF-----HLSAVNWS--NIMMLGAIGLVFYM------------ANSLGWADTNVAATYSLTLLfLRTPLLS 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 314 MIIVMVVISRAdaericQV-LNEVSTVrDNADPIMDVPDGS-------ITFNDVSFRYdvGSERPVLDDINLTIASGSTI 385
Cdd:PRK10522 282 AVGALPTLLSA------QVaFNKLNKL-ALAPYKAEFPRPQafpdwqtLELRNVTFAY--QDNGFSVGPINLTIKRGELL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 386 GIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVAMVLQKNVLFAGTIADNIRWGNPNATDEDVRRV 465
Cdd:PRK10522 353 FLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLLGPEGKPANPALVEKWLERL 432
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 705456738 466 ---CKLAQADGFIREFpkgydtyieeggsNVSGGQRQRLCIARALLKKPKILILDD 518
Cdd:PRK10522 433 kmaHKLELEDGRISNL-------------KLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
357-569 |
1.18e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 73.99 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 357 NDVSFRYDVGSER-PVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETL----RDA 431
Cdd:PRK10535 8 KDIRRSYPSGEEQvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 432 VAMVLQKNVLFAG-TIADNIRWGNPNATDEDVRRvckLAQADGFIREFpkGYDTYIEEGGSNVSGGQRQRLCIARALLKK 510
Cdd:PRK10535 88 FGFIFQRYHLLSHlTAAQNVEVPAVYAGLERKQR---LLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 705456738 511 PKILILDDSTSAVDTKTDRLIRGAFKtEIPDT--TKIIIAQRVASVQESDEIIVMDGGRIL 569
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILH-QLRDRghTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
345-568 |
2.59e-13 |
|
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: 69.48 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 345 PIMDVPDGSITFNDVSFRYDVGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRdvreyd 424
Cdd:cd03220 11 PTYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 425 letlrdaVAMVLQKNVLFagtiadnirwgNPNATDED-VRRVCKL-----AQADG---FIREFpKGYDTYIEEGGSNVSG 495
Cdd:cd03220 85 -------VSSLLGLGGGF-----------NPELTGREnIYLNGRLlglsrKEIDEkidEIIEF-SELGDFIDLPVKTYSS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 705456738 496 GQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIAQR-VASVQE-SDEIIVMDGGRI 568
Cdd:cd03220 146 GMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHdPSSIKRlCDRALVLEKGKI 220
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
369-579 |
5.53e-13 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 68.72 E-value: 5.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 369 RPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDL-ETLRDAVAMVLQKNVLFAG-TI 446
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLPQEASIFRKlTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 447 ADNIRWGNPNATDEDVRRVCKLaqaDGFIREFpkGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTK 526
Cdd:cd03218 93 EENILAVLEIRGLSKKEREEKL---EELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 705456738 527 TDRLIRGafkteipdttkiIIAQRVAS----------VQESDEII----VMDGGRILDRGTHDQLLQ 579
Cdd:cd03218 168 AVQDIQK------------IIKILKDRgigvlitdhnVRETLSITdrayIIYEGKVLAEGTPEEIAA 222
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
368-573 |
9.19e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 68.17 E-value: 9.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 368 ERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLI---PRlYDVSSGSLEVGGRDVREYDL-ETLRDAVAMVLQKNVLFA 443
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDILELSPdERARAGIFLAFQYPVEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 444 G-------TIADNIRWGNPNATDEDVRRVCKLAQADGFIREFPkgyDTYIEEGgsnVSGGQRQRLCIARALLKKPKILIL 516
Cdd:COG0396 91 GvsvsnflRTALNARRGEELSAREFLKLLKEKMKELGLDEDFL---DRYVNEG---FSGGEKKRNEILQMLLLEPKLAIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 517 DDSTSAVDTKTDRLIRGAFKTEI-PDTTKIIIA--QRVASVQESDEIIVMDGGRILDRGT 573
Cdd:COG0396 165 DETDSGLDIDALRIVAEGVNKLRsPDRGILIIThyQRILDYIKPDFVHVLVDGRIVKSGG 224
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
354-527 |
1.08e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 68.55 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYdvgSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGgrdvrEYDLETLRDAVA 433
Cdd:PRK11247 13 LLLNAVSKRY---GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-----TAPLAEAREDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 MVLQKNVLFA-GTIADNIRWGNPNATDEDVRRVCK---LAQADGfirEFPkgydtyieeggSNVSGGQRQRLCIARALLK 509
Cdd:PRK11247 85 LMFQDARLLPwKKVIDNVGLGLKGQWRDAALQALAavgLADRAN---EWP-----------AALSGGQKQRVALARALIH 150
|
170
....*....|....*...
gi 705456738 510 KPKILILDDSTSAVDTKT 527
Cdd:PRK11247 151 RPGLLLLDEPLGALDALT 168
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
354-518 |
1.38e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.60 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYdvgSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLI---PRlydVSSGSLEVGGRDVREYDL-ETLR 429
Cdd:PRK11614 6 LSFDKVSAHY---GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLcgdPR---ATSGRIVFDGKDITDWQTaKIMR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 430 DAVAMVLQKNVLFAG-TIADNIRWGNPNATDED----VRRVCKLaqadgfireFPKGYDTYIEEGGSnVSGGQRQRLCIA 504
Cdd:PRK11614 80 EAVAIVPEGRRVFSRmTVEENLAMGGFFAERDQfqerIKWVYEL---------FPRLHERRIQRAGT-MSGGEQQMLAIG 149
|
170
....*....|....
gi 705456738 505 RALLKKPKILILDD 518
Cdd:PRK11614 150 RALMSQPRLLLLDE 163
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
369-568 |
1.42e-12 |
|
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: 66.30 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 369 RPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDA-VAMVL---QKNVLFAG 444
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPedrKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 445 -TIADNIrwgnpnatdedvrrvcklaqadgFIREFpkgydtyieeggsnVSGGQRQRLCIARALLKKPKILILDDSTSAV 523
Cdd:cd03215 93 lSVAENI-----------------------ALSSL--------------LSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 705456738 524 DTKTDRLIRgafkteipdttKIIIAQR-------VAS------VQESDEIIVMDGGRI 568
Cdd:cd03215 136 DVGAKAEIY-----------RLIRELAdagkavlLISseldelLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
354-573 |
1.53e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 68.29 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDvgSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVA 433
Cdd:PRK13652 4 IETRDLCYSYS--GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 MVLQK--NVLFAGTIADNIRWGNPN-ATDEDV--RRVCKLAQADGFirefpkgyDTYIEEGGSNVSGGQRQRLCIARALL 508
Cdd:PRK13652 82 LVFQNpdDQIFSPTVEQDIAFGPINlGLDEETvaHRVSSALHMLGL--------EELRDRVPHHLSGGEKKRVAIAGVIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 509 KKPKILILDDSTSAVDTK-TDRLIRgaFKTEIPDT---TKIIIAQRVASVQE-SDEIIVMDGGRILDRGT 573
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQgVKELID--FLNDLPETygmTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGT 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
369-579 |
5.00e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.51 E-value: 5.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 369 RPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVReydLETLRDAVA--MVL-----QKNVL 441
Cdd:COG1129 265 GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR---IRSPRDAIRagIAYvpedrKGEGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 442 FAG-TIADNI---------RWGNPNATDEDvrrvcklAQADGFIREF---PKGYDTYIeeggSNVSGGQRQRLCIARALL 508
Cdd:COG1129 342 VLDlSIRENItlasldrlsRGGLLDRRRER-------ALAEEYIKRLrikTPSPEQPV----GNLSGGNQQKVVLAKWLA 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 509 KKPKILILDDSTSAVD--TKTD--RLIRgafktEIPDTTKIIIaqrVAS--VQE----SDEIIVMDGGRI---LDRG--T 573
Cdd:COG1129 411 TDPKVLILDEPTRGIDvgAKAEiyRLIR-----ELAAEGKAVI---VISseLPEllglSDRILVMREGRIvgeLDREeaT 482
|
....*.
gi 705456738 574 HDQLLQ 579
Cdd:COG1129 483 EEAIMA 488
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
372-527 |
5.05e-12 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 65.95 E-value: 5.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 372 LDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLrdavaMVLQKNVLFAG-TIADNI 450
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPWlTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 451 RWgnpnATDEdVRRVCKLAQADGFIRE------FPKGYDTYIEEggsnVSGGQRQRLCIARALLKKPKILILDDSTSAVD 524
Cdd:TIGR01184 76 AL----AVDR-VLPDLSKSERRAIVEEhialvgLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
...
gi 705456738 525 TKT 527
Cdd:TIGR01184 147 ALT 149
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
35-305 |
7.07e-12 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 66.59 E-value: 7.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 35 APTFVIVESVLEILIPTVMASMIDqgVAGGS------MPAIwkfGLILLGCAVVSLFAGFMSGRYAAIASAgFAKNLRHD 108
Cdd:cd18590 1 AFLFLTLAVICETFIPYYTGRVID--ILGGEyqhnafTSAI---GLMCLFSLGSSLSAGLRGGLFMCTLSR-LNLRLRHQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 109 LFEkvqsfSFTNID-HF----STGSIITRITTDVTNIQYAFQMCIRVAVRAPLMVVVAWLFSFRISPSISMIFLIIIPIL 183
Cdd:cd18590 75 LFS-----SLVQQDiGFfektKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 184 GVTltglalsvnpvfEKVFHTYD------------HLNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEH 251
Cdd:cd18590 150 AIA------------QKVYNTYHqklsqavqdsiaKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDT 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 705456738 252 VLAFNWPILNTCIYGAMLIISWMGTKQIVGSHnnaavgLTTGDLTALVTYAMQI 305
Cdd:cd18590 218 VRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGH------LTTGSLVSFILYQKNL 265
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
372-567 |
8.11e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 67.74 E-value: 8.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 372 LDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVReydLETLRDAVA----MVLQKNVLFAG-TI 446
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR---IRSPRDAIAlgigMVHQHFMLVPNlTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 447 ADNIRWGNPNATdedvRRVCKLAQADGFIREFPKGY------DTYIEEggsnVSGGQRQRLCIARALLKKPKILILDDST 520
Cdd:COG3845 98 AENIVLGLEPTK----GGRLDRKAARARIRELSERYgldvdpDAKVED----LSVGEQQRVEILKALYRGARILILDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 705456738 521 sAVDT--KTDRLIR--GAFKTEipDTTKIIIAQRVASVQE-SDEIIVMDGGR 567
Cdd:COG3845 170 -AVLTpqEADELFEilRRLAAE--GKSIIFITHKLREVMAiADRVTVLRRGK 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
341-524 |
8.97e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.81 E-value: 8.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 341 DNADPIMDVPDGSITF--NDVSFRYDVGsERPVLDDINLTIASGSTIGIVGGTGSAKSS----LVQLIPrlydvSSGSLE 414
Cdd:PRK15134 270 EPASPLLDVEQLQVAFpiRKGILKRTVD-HNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIW 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 415 VGGRDVREYD---LETLRDAVAMVLQK---------NVLfaGTIADNIRWGNPNATDEDV-RRVCKLAQADGFIREFPKG 481
Cdd:PRK15134 344 FDGQPLHNLNrrqLLPVRHRIQVVFQDpnsslnprlNVL--QIIEEGLRVHQPTLSAAQReQQVIAVMEEVGLDPETRHR 421
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 705456738 482 YDtyieeggSNVSGGQRQRLCIARALLKKPKILILDDSTSAVD 524
Cdd:PRK15134 422 YP-------AEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
335-572 |
1.32e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.57 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 335 EVSTVRDnADPIMDVPDGSITFNDVSFRYD-VGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSL 413
Cdd:PRK10261 303 EQDTVVD-GEPILQVRNLVTRFPLRSGLLNrVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEI 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 414 EVGGRDVreydlETLRDAVAMVLQKNVLF---------------AGTIADNIRWGNPNATDEDVRRVCKLAQADGFIREF 478
Cdd:PRK10261 382 IFNGQRI-----DTLSPGKLQALRRDIQFifqdpyasldprqtvGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEH 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 479 PKGYDtyieeggSNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKtdrlIRGAFKTEIPDTTK------IIIAQRVA 552
Cdd:PRK10261 457 AWRYP-------HEFSGGQRQRICIARALALNPKVIIADEAVSALDVS----IRGQIINLLLDLQRdfgiayLFISHDMA 525
|
250 260
....*....|....*....|.
gi 705456738 553 SVQE-SDEIIVMDGGRILDRG 572
Cdd:PRK10261 526 VVERiSHRVAVMYLGQIVEIG 546
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
354-527 |
1.40e-11 |
|
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: 62.47 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDvgsERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIprlydvssgslevggrdvreydletlrdava 433
Cdd:cd03221 1 IELENLSKTYG---GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLI------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 mvLQKNVLFAGTIadniRWGnpnatdeDVRRVCKLAQadgfirefpkgydtyieeggsnVSGGQRQRLCIARALLKKPKI 513
Cdd:cd03221 47 --AGELEPDEGIV----TWG-------STVKIGYFEQ----------------------LSGGEKMRLALAKLLLENPNL 91
|
170
....*....|....
gi 705456738 514 LILDDSTSAVDTKT 527
Cdd:cd03221 92 LLLDEPTNHLDLES 105
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
369-531 |
1.61e-11 |
|
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: 67.73 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 369 RPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVrEYDLETLRDAVAMVLQKNVLFAG-TIA 447
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 448 DNIR-WGNPNATDEDVRRVcklaQADGFIREfpKGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTK 526
Cdd:TIGR01257 1022 EHILfYAQLKGRSWEEAQL----EMEAMLED--TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY 1095
|
....*
gi 705456738 527 TDRLI 531
Cdd:TIGR01257 1096 SRRSI 1100
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
354-579 |
1.83e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 67.07 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYdvGSERpVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREydlETLRDAVA 433
Cdd:NF033858 2 ARLEGVSHRY--GKTV-ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD---ARHRRAVC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 -----M--VLQKNVLFAGTIADNIR-----WGNPNAtdEDVRRVCKLAQADG---FiREFPKGydtyieeggsNVSGGQR 498
Cdd:NF033858 76 priayMpqGLGKNLYPTLSVFENLDffgrlFGQDAA--ERRRRIDELLRATGlapF-ADRPAG----------KLSGGMK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 499 QRLCIARALLKKPKILILDDSTSAVDTktdrLIRGAFKTEIPDttkiIIAQRVA-SV----------QESDEIIVMDGGR 567
Cdd:NF033858 143 QKLGLCCALIHDPDLLILDEPTTGVDP----LSRRQFWELIDR----IRAERPGmSVlvataymeeaERFDWLVAMDAGR 214
|
250
....*....|..
gi 705456738 568 ILDRGTHDQLLQ 579
Cdd:NF033858 215 VLATGTPAELLA 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
370-575 |
2.12e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 66.58 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 370 PVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVReydLETLRDA----VAMVLQKNVLFAG- 444
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR---FRSPRDAqaagIAIIHQELNLVPNl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 445 TIADNI-------RWG--NPNATDEDVRRVCKLAQADgfIREfpkgyDTYIeeggSNVSGGQRQRLCIARALLKKPKILI 515
Cdd:COG1129 95 SVAENIflgreprRGGliDWRAMRRRARELLARLGLD--IDP-----DTPV----GDLSVAQQQLVEIARALSRDARVLI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 705456738 516 LDDSTSAVDTK-TDRL---IRgAFKTEipDTTKIIIAQRVASVQE-SDEIIVM-DGGRILDRGTHD 575
Cdd:COG1129 164 LDEPTASLTEReVERLfriIR-RLKAQ--GVAIIYISHRLDEVFEiADRVTVLrDGRLVGTGPVAE 226
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
354-524 |
2.97e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 63.36 E-value: 2.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDVGseRPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDV---REYDLETLRD 430
Cdd:PRK10908 2 IRFEHVSKAYLGG--RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 431 AVAMVLQKN-VLFAGTIADNIrwGNP----NATDEDVRRVCKLAQADGFIREFPKGYDTyieeggsNVSGGQRQRLCIAR 505
Cdd:PRK10908 80 QIGMIFQDHhLLMDRTVYDNV--AIPliiaGASGDDIRRRVSAALDKVGLLDKAKNFPI-------QLSGGEQQRVGIAR 150
|
170
....*....|....*....
gi 705456738 506 ALLKKPKILILDDSTSAVD 524
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLD 169
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
368-569 |
3.37e-11 |
|
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: 63.51 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 368 ERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVAMVLQKNVLF----- 442
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQLWwdlpv 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 443 AGTIADNIRWGN--PNATDEDVRRVCKLAQADGFIrefpkgyDTYIEeggsNVSGGQRQRLCIARALLKKPKILILDDST 520
Cdd:cd03267 113 IDSFYLLAAIYDlpPARFKKRLDELSELLDLEELL-------DTPVR----QLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 705456738 521 SAVDTKTDRLIRGAFKTEIPD--TTKIIIAQRVASVQE-SDEIIVMDGGRIL 569
Cdd:cd03267 182 IGLDVVAQENIRNFLKEYNRErgTTVLLTSHYMKDIEAlARRVLVIDKGRLL 233
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
321-578 |
3.59e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 64.85 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 321 ISRADAERICQVLNEVSTVRDN-------ADPIMDVPDGSITFNDVSFRYdvgSERPVLDDINLTIASGSTIGIVGGTGS 393
Cdd:PRK13536 2 LTRAVAEEAPRRLELSPIERKHqgiseakASIPGSMSTVAIDLAGVSKSY---GDKAVVNGLSFTVASGECFGLLGPNGA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 394 AKSSLVQLIPRLYDVSSGSLEVGGRDVREyDLETLRDAVAMVLQ-KNVLFAGTIADNI----RWGNPNATD-EDVrrVCK 467
Cdd:PRK13536 79 GKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQfDNLDLEFTVRENLlvfgRYFGMSTREiEAV--IPS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 468 LAQadgFIREFPKGyDTYIeeggSNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIII 547
Cdd:PRK13536 156 LLE---FARLESKA-DARV----SDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILL 227
|
250 260 270
....*....|....*....|....*....|...
gi 705456738 548 AQRVASVQES--DEIIVMDGGRILDRGTHDQLL 578
Cdd:PRK13536 228 TTHFMEEAERlcDRLCVLEAGRKIAEGRPHALI 260
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
368-572 |
4.36e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 62.54 E-value: 4.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 368 ERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLI---PRlYDVSSGSLEVGGRDVREYDL-ETLRDAVAMVLQKNVLFA 443
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImghPK-YEVTEGEILFKGEDITDLPPeERARLGIFLAFQYPPEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 444 G-TIADNIRWGNpnatdedvrrvcklaqaDGFirefpkgydtyieeggsnvSGGQRQRLCIARALLKKPKILILDDSTSA 522
Cdd:cd03217 91 GvKNADFLRYVN-----------------EGF-------------------SGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 705456738 523 VDTKTDRLIRGAFKTEI-PDTTKIIIA--QRVASVQESDEIIVMDGGRILDRG 572
Cdd:cd03217 135 LDIDALRLVAEVINKLReEGKSVLIIThyQRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
366-527 |
4.73e-11 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 62.84 E-value: 4.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 366 GSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEV--GGRDVreyDLETLRDAVAMVLQKNVL-- 441
Cdd:COG4778 21 GKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWV---DLAQASPREILALRRRTIgy 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 442 ---FAGTIadnirwgnPNATDEDVrrVCKLAQADGFIREfpkgydTYIEEGGS-----NV------------SGGQRQRL 501
Cdd:COG4778 98 vsqFLRVI--------PRVSALDV--VAEPLLERGVDRE------EARARAREllarlNLperlwdlppatfSGGEQQRV 161
|
170 180
....*....|....*....|....*.
gi 705456738 502 CIARALLKKPKILILDDSTSAVDTKT 527
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAAN 187
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
368-537 |
9.91e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.43 E-value: 9.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 368 ERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETL------RDAVamvlqKNVL 441
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAchylghRNAM-----KPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 442 fagTIADNIR-WGNPNATDE-DVRR-VCKLAQADgfIREFPKGYdtyieeggsnVSGGQRQRLCIARALLKKPKILILDD 518
Cdd:PRK13539 89 ---TVAENLEfWAAFLGGEElDIAAaLEAVGLAP--LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDE 153
|
170
....*....|....*....
gi 705456738 519 STSAVDTKTDRLIRGAFKT 537
Cdd:PRK13539 154 PTAALDAAAVALFAELIRA 172
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
353-591 |
1.58e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 61.64 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 353 SITFNDVSFRYDVGSERP-------------------VLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSL 413
Cdd:COG1134 4 MIEVENVSKSYRLYHEPSrslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 414 EVGGRdvreydletlrdaVAMVLQKNVLFAG--TIADNIR-----WGnpnATDEDVRRVCKlaqadgFIREF-------- 478
Cdd:COG1134 84 EVNGR-------------VSALLELGAGFHPelTGRENIYlngrlLG---LSRKEIDEKFD------EIVEFaelgdfid 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 479 -P-KGYdtyieeggsnvSGGQRQRLCIARALLKKPKILILDDSTSAVDT----KTDRLIRgAFKTEipDTTKIIIAQRVA 552
Cdd:COG1134 142 qPvKTY-----------SSGMRARLAFAVATAVDPDILLVDEVLAVGDAafqkKCLARIR-ELRES--GRTVIFVSHSMG 207
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 705456738 553 SVQE-SDEIIVMDGGRILDRGTHDqllQTCDEYRSIYQSQ 591
Cdd:COG1134 208 AVRRlCDRAIWLEKGRLVMDGDPE---EVIAAYEALLAGR 244
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
372-531 |
2.75e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 61.18 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 372 LDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLY--DVSSGS-LEVGGRDVREY-----DLETLRDAVAMVLQK-NVLF 442
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGShIELLGRTVQREgrlarDIRKSRANTGYIFQQfNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 443 AGTIADNIRWGNPNATDedVRRVC----KLAQADGFIREFPK-GYDTYIEEGGSNVSGGQRQRLCIARALLKKPKILILD 517
Cdd:PRK09984 100 RLSVLENVLIGALGSTP--FWRTCfswfTREQKQRALQALTRvGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170
....*....|....
gi 705456738 518 DSTSAVDTKTDRLI 531
Cdd:PRK09984 178 EPIASLDPESARIV 191
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
354-577 |
2.96e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 61.64 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDVGS--ERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRD--------VREY 423
Cdd:PRK13651 3 IKVKNIVKIFNKKLptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDeknkkktkEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 424 DLET----------------LRDAVAMVLQ--KNVLFAGTIADNIRWG------NPNATDEDVRRVCKLAQADgfirefp 479
Cdd:PRK13651 83 VLEKlviqktrfkkikkikeIRRRVGVVFQfaEYQLFEQTIEKDIIFGpvsmgvSKEEAKKRAAKYIELVGLD------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 480 kgyDTYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKtEIPDTTK--IIIAQRVASVQE- 556
Cdd:PRK13651 156 ---ESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFD-NLNKQGKtiILVTHDLDNVLEw 231
|
250 260
....*....|....*....|..
gi 705456738 557 SDEIIVMDGGRIL-DRGTHDQL 577
Cdd:PRK13651 232 TKRTIFFKDGKIIkDGDTYDIL 253
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
358-572 |
3.56e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 61.18 E-value: 3.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 358 DVSFRYdvgSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGR--DVREYDLETLRDAVAMV 435
Cdd:PRK13638 6 DLWFRY---QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 436 LQ--KNVLFAGTIADNIRWGNPN---ATDEDVRRV---CKLAQADGFiREFPKgydtyieeggSNVSGGQRQRLCIARAL 507
Cdd:PRK13638 83 FQdpEQQIFYTDIDSDIAFSLRNlgvPEAEITRRVdeaLTLVDAQHF-RHQPI----------QCLSHGQKKRVAIAGAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 705456738 508 LKKPKILILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIAQR-VASVQE-SDEIIVMDGGRILDRG 572
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHdIDLIYEiSDAVYVLRQGQILTHG 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
344-582 |
3.58e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 61.36 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 344 DPIMDVPdgsITFNDVSFRYDvgsERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREY 423
Cdd:PRK13537 1 GPMSVAP---IDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 424 DLETlRDAVAMVLQKNVL---FagTIADNIR-----WGNPNATDEdvRRVCKL-------AQADGFIREfpkgydtyiee 488
Cdd:PRK13537 75 ARHA-RQRVGVVPQFDNLdpdF--TVRENLLvfgryFGLSAAAAR--ALVPPLlefakleNKADAKVGE----------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 489 ggsnVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIAQRVASVQES--DEIIVMDGG 566
Cdd:PRK13537 139 ----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERlcDRLCVIEEG 214
|
250
....*....|....*....
gi 705456738 567 RILDRGTHDQLLQT---CD 582
Cdd:PRK13537 215 RKIAEGAPHALIESeigCD 233
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
368-536 |
4.53e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.97 E-value: 4.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 368 ERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYdvsSGSLEVGGRDVREYDLEtlRDAvamvlqknvlfagTIA 447
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL---KGTPVAGCVDVPDNQFG--REA-------------SLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 448 DNI-RWGNPNATDEdVRRVCKLAQADGFIREFpkgydtyieeggSNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTK 526
Cdd:COG2401 104 DAIgRKGDFKDAVE-LLNAVGLSDAVLWLRRF------------KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170
....*....|
gi 705456738 527 TDRliRGAFK 536
Cdd:COG2401 171 TAK--RVARN 178
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
354-524 |
5.19e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.13 E-value: 5.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYdvgSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEvggrdvREYDLEtlrdaVA 433
Cdd:PRK09544 5 VSLENVSVSF---GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------RNGKLR-----IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 MVLQKNVLFAG---TIADNIRWgNPNATDEDVRRVCKLAQAdGFIREFPKgydtyieeggSNVSGGQRQRLCIARALLKK 510
Cdd:PRK09544 71 YVPQKLYLDTTlplTVNRFLRL-RPGTKKEDILPALKRVQA-GHLIDAPM----------QKLSGGETQRVLLARALLNR 138
|
170
....*....|....
gi 705456738 511 PKILILDDSTSAVD 524
Cdd:PRK09544 139 PQLLVLDEPTQGVD 152
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
368-579 |
5.78e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 60.03 E-value: 5.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 368 ERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVAMVLQKNVLFAG-TI 446
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 447 ADNIRWG-NP------NATDEDVRRVCKLAQADGFirefpkgyDTYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDS 519
Cdd:PRK11231 94 RELVAYGrSPwlslwgRLSAEDNARVNQAMEQTRI--------NHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 705456738 520 TSAVD-------TKTDRLIRGAFKTEIPDTTKIIIAQRVAsvqesDEIIVMDGGRILDRGTHDQLLQ 579
Cdd:PRK11231 166 TTYLDinhqvelMRLMRELNTQGKTVVTVLHDLNQASRYC-----DHLVVLANGHVMAQGTPEEVMT 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
369-568 |
5.82e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 61.97 E-value: 5.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 369 RPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDA-VAMVL---QKNVLFAG 444
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPedrLGRGLVPD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 445 -TIADNI-----------RWG--NPNATDEDVRRVcklaqadgfIREF---PKGYDTYIeeggSNVSGGQRQRLCIARAL 507
Cdd:COG3845 351 mSVAENLilgryrrppfsRGGflDRKAIRAFAEEL---------IEEFdvrTPGPDTPA----RSLSGGNQQKVILAREL 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 705456738 508 LKKPKILILDDSTSAVDTKTDRLIRgafkteipdttKIIIAQR-------VASvQE-------SDEIIVMDGGRI 568
Cdd:COG3845 418 SRDPKLLIAAQPTRGLDVGAIEFIH-----------QRLLELRdagaavlLIS-EDldeilalSDRIAVMYEGRI 480
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
368-535 |
1.22e-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: 58.14 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 368 ERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREydletlrdaVAMVLQKNVLFAG--- 444
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE---------QRDEPHENILYLGhlp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 445 ------TIADNIRWGNPNATDEDvrRVCKLAQADGFIREF---PKGYdtyieeggsnVSGGQRQRLCIARALLKKPKILI 515
Cdd:TIGR01189 83 glkpelSALENLHFWAAIHGGAQ--RTIEDALAAVGLTGFedlPAAQ----------LSAGQQRRLALARLWLSRRPLWI 150
|
170 180
....*....|....*....|
gi 705456738 516 LDDSTSAVDTKTDRLIRGAF 535
Cdd:TIGR01189 151 LDEPTTALDKAGVALLAGLL 170
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
350-588 |
2.45e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 58.65 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 350 PDGSITFNDVSFRYdvgSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLR 429
Cdd:PRK10575 8 SDTTFALRNVSFRV---PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 430 DAVAMVLQKNvlfagtiadnirwgnPNATDEDVRRVCKLAQA--DGFIREFPKGYDTYIEEGGSNV-------------S 494
Cdd:PRK10575 85 RKVAYLPQQL---------------PAAEGMTVRELVAIGRYpwHGALGRFGAADREKVEEAISLVglkplahrlvdslS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 495 GGQRQRLCIARALLKKPKILILDDSTSAVDTK--------TDRLIRGAFKTEIPDTTKIIIAQRVAsvqesDEIIVMDGG 566
Cdd:PRK10575 150 GGERQRAWIAMLVAQDSRCLLLDEPTSALDIAhqvdvlalVHRLSQERGLTVIAVLHDINMAARYC-----DYLVALRGG 224
|
250 260
....*....|....*....|..
gi 705456738 567 RILDRGTHDQLLQTcDEYRSIY 588
Cdd:PRK10575 225 EMIAQGTPAELMRG-ETLEQIY 245
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
358-579 |
3.98e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.48 E-value: 3.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 358 DVSFRYDvGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGG-----RDVREYDLETLRDA- 431
Cdd:PRK10261 19 NIAFMQE-QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrRSRQVIELSEQSAAq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 432 --------VAMVLQK-----NVLFA--GTIADNIRWGNPNATDEDVRRV------CKLAQADGFIREFPKgydtyieegg 490
Cdd:PRK10261 98 mrhvrgadMAMIFQEpmtslNPVFTvgEQIAESIRLHQGASREEAMVEAkrmldqVRIPEAQTILSRYPH---------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 491 sNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKTEIPDTTK--IIIAQRVASVQE-SDEIIVMDGGR 567
Cdd:PRK10261 168 -QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgvIFITHDMGVVAEiADRVLVMYQGE 246
|
250
....*....|..
gi 705456738 568 ILDRGTHDQLLQ 579
Cdd:PRK10261 247 AVETGSVEQIFH 258
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
353-572 |
4.59e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 57.59 E-value: 4.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 353 SITFNDVSFRYDVGseRPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREydletlrdav 432
Cdd:PRK15056 6 GIVVNDVTVTWRNG--HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 433 amVLQKNVLFAGTIADNIRWGNPNATdEDVRRVCKLAQAdGFIREfPKGYDTYIEEGG--------------SNVSGGQR 498
Cdd:PRK15056 74 --ALQKNLVAYVPQSEEVDWSFPVLV-EDVVMMGRYGHM-GWLRR-AKKRDRQIVTAAlarvdmvefrhrqiGELSGGQK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 705456738 499 QRLCIARALLKKPKILILDDSTSAVDTKTD-RLIrgAFKTEIPDT--TKIIIAQRVASVQESDEIIVMDGGRILDRG 572
Cdd:PRK15056 149 KRVFLARAIAQQGQVILLDEPFTGVDVKTEaRII--SLLRELRDEgkTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
40-304 |
4.93e-09 |
|
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: 57.84 E-value: 4.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 40 IVESVLEILIPTVMASMIDQGVAGGSMPAIWKFGLILLGCAVVSLFAGFMSGRYAAIASAGFAKNLRHDLFEKVQSFSFT 119
Cdd:cd18570 12 LLITLLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 120 NIDHFSTGSIITRITtDVTNIQYAFqmcIRVAVRAPL---MVVVAWLFSFRISPSISMIFLIIIPILGVtltgLALSVNP 196
Cdd:cd18570 92 FFETRKTGEIISRFN-DANKIREAI---SSTTISLFLdllMVIISGIILFFYNWKLFLITLLIIPLYIL----IILLFNK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 197 VFEKVFH----TYDHLNNIVDENLQGIRVVKSYDREEHESRKFgrvsERIYEYFCKAEHVLAfNWPILNTCIYGA----- 267
Cdd:cd18570 164 PFKKKNRevmeSNAELNSYLIESLKGIETIKSLNAEEQFLKKI----EKKFSKLLKKSFKLG-KLSNLQSSIKGLislig 238
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 705456738 268 MLIISWMGTKQIVGSHnnaavgLTTGDL---TALVTYAMQ 304
Cdd:cd18570 239 SLLILWIGSYLVIKGQ------LSLGQLiafNALLGYFLG 272
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
368-535 |
5.31e-09 |
|
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: 56.35 E-value: 5.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 368 ERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVreydletlrDAVAMVLQKNVLFAG--- 444
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL---------DFQRDSIARGLLYLGhap 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 445 ------TIADNIRWGNPNATDEDVRRVckLAQAD-GFIREFPKGYdtyieeggsnVSGGQRQRLCIARALLKKPKILILD 517
Cdd:cd03231 83 gikttlSVLENLRFWHADHSDEQVEEA--LARVGlNGFEDRPVAQ----------LSAGQQRRVALARLLLSGRPLWILD 150
|
170
....*....|....*...
gi 705456738 518 DSTSAVDTKTDRLIRGAF 535
Cdd:cd03231 151 EPTTALDKAGVARFAEAM 168
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
53-241 |
6.73e-09 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 57.42 E-value: 6.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 53 MASMIDQGVAGG-SMPAIWKFGLILLGCAVVSLFAGFMSGRYAAIASAGFAKNLRHDLFEKVQSFSFTNIDHFSTGSIIT 131
Cdd:cd18584 19 LARIIAGVFLEGaGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARLLALGPALLRRQSSGELAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 132 RITTDVTNI-----QYAFQMcIRVAVrAPLMVVVAwlfSFRISPSISMIFLIIIPILgvtltglalsvnPVF-------- 198
Cdd:cd18584 99 LLTEGVDALdgyfaRYLPQL-VLAAI-VPLLILVA---VFPLDWVSALILLVTAPLI------------PLFmiligkaa 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 705456738 199 ----EKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSER 241
Cdd:cd18584 162 qaasRRQWAALSRLSGHFLDRLRGLPTLKLFGRARAQAARIARASED 208
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
354-578 |
7.43e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 58.28 E-value: 7.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRY---DVGSERPVlDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEV--------------- 415
Cdd:TIGR03269 280 IKVRNVSKRYisvDRGVVKAV-DNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkpgpd 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 416 -GGRDVR-------EYDLETLRDAVamvlqknvlfaGTIADNIRWGNPnatDE-DVRRVCKLAQADGFIREFPKG-YDTY 485
Cdd:TIGR03269 359 gRGRAKRyigilhqEYDLYPHRTVL-----------DNLTEAIGLELP---DElARMKAVITLKMVGFDEEKAEEiLDKY 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 486 IEEggsnVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAF---KTEIpDTTKIIIAQRVASVQE-SDEII 561
Cdd:TIGR03269 425 PDE----LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkaREEM-EQTFIIVSHDMDFVLDvCDRAA 499
|
250
....*....|....*..
gi 705456738 562 VMDGGRILDRGTHDQLL 578
Cdd:TIGR03269 500 LMRDGKIVKIGDPEEIV 516
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
357-578 |
1.14e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 56.47 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 357 NDVSFRYDvgsERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDA----- 431
Cdd:PRK11701 10 RGLTKLYG---PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAerrrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 432 -----------VAMVLQKNVLFAGTIADNI------RWGNPNATDED-VRRVcKLAQADgfIREFPKGYdtyieeggsnv 493
Cdd:PRK11701 87 lrtewgfvhqhPRDGLRMQVSAGGNIGERLmavgarHYGDIRATAGDwLERV-EIDAAR--IDDLPTTF----------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 494 SGGQRQRLCIARALLKKPKILILDDSTSAVDTKT-----DrLIRGaFKTEIpDTTKIIIAQRVASVQE-SDEIIVMDGGR 567
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVqarllD-LLRG-LVREL-GLAVVIVTHDLAVARLlAHRLLVMKQGR 229
|
250
....*....|.
gi 705456738 568 ILDRGTHDQLL 578
Cdd:PRK11701 230 VVESGLTDQVL 240
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
381-579 |
1.58e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 57.36 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 381 SGSTIGIVGGTGSAKSSLV----QLIPRLYDVSsGSLEVGGRDVreyDLETLRDAVAMVLQKNvLFAGT--------IAD 448
Cdd:TIGR00955 50 PGELLAVMGSSGAGKTTLMnalaFRSPKGVKGS-GSVLLNGMPI---DAKEMRAISAYVQQDD-LFIPTltvrehlmFQA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 449 NIRWGNPNATDEDVRRVCKLAQADGFIrefpKGYDTYIEEGGS--NVSGGQRQRLCIARALLKKPKILILDDSTSAVDTK 526
Cdd:TIGR00955 125 HLRMPRRVTKKEKRERVDEVLQALGLR----KCANTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSF 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 705456738 527 TDRLIRGAFKtEIPDTTKIIIA---QRVASVQES-DEIIVMDGGRILDRGTHDQLLQ 579
Cdd:TIGR00955 201 MAYSVVQVLK-GLAQKGKTIICtihQPSSELFELfDKIILMAEGRVAYLGSPDQAVP 256
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
40-305 |
1.97e-08 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 56.27 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 40 IVESVLEILIPTVMASMIDQGVAGGSMPAIWKfgLILLGCAVVSLFAGFMSGRY---------AAIASAGFAKNLRHDLF 110
Cdd:cd18554 9 LVRFGIPLLLPLILKYIVDDVIQGSSLTLDEK--VYKLFTIIGIMFFIFLILRPpveyyrqyfAQWIANKILYDIRKDLF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 111 EKVQSFSFTNIDHFSTGSIITRITTDVTNIQYAFQMCIRVAVRAPLMVVVAWLFSFRISPSISMIFLIIIPILGVTLTGL 190
Cdd:cd18554 87 DHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 191 ALSVNPVFEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFgrvSERIYEYFCKAEHVLAFN---WPILNTCI-YG 266
Cdd:cd18554 167 FGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQF---DKRNGHFLTRALKHTRWNaktFSAVNTITdLA 243
|
250 260 270
....*....|....*....|....*....|....*....
gi 705456738 267 AMLIISWMGTKQIVGShnnaavgLTTGDLTALVTYAMQI 305
Cdd:cd18554 244 PLLVIGFAAYLVIEGN-------LTVGTLVAFVGYMERM 275
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
371-524 |
2.18e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 55.76 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 371 VLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVAMVLQkNVLFAGTIADN- 449
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQ-NATTPGDITVQe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 450 -------------IRWgnpnaTDEDVRRVCKLAQADGFIREFPKGYDTyieeggsnVSGGQRQRLCIARALLKKPKILIL 516
Cdd:PRK10253 101 lvargryphqplfTRW-----RKEDEEAVTKAMQATGITHLADQSVDT--------LSGGQRQRAWIAMVLAQETAIMLL 167
|
....*...
gi 705456738 517 DDSTSAVD 524
Cdd:PRK10253 168 DEPTTWLD 175
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
369-524 |
2.34e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 55.28 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 369 RPVLDDINLTIASGSTIGIVGGTGSAKSS----LVQLIPRlydvSSGSLEVGGRDVREYDL-ETLRDAVAMVLQKNVLFA 443
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTtfymVVGIVPR----DAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 444 G-TIADN------IRwgnpnatdEDVRRVCKLAQADGFIREFpkgYDTYIEEG-GSNVSGGQRQRLCIARALLKKPKILI 515
Cdd:PRK10895 92 RlSVYDNlmavlqIR--------DDLSAEQREDRANELMEEF---HIEHLRDSmGQSLSGGERRRVEIARALAANPKFIL 160
|
....*....
gi 705456738 516 LDDSTSAVD 524
Cdd:PRK10895 161 LDEPFAGVD 169
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
371-530 |
2.36e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.79 E-value: 2.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 371 VLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLE---TLR-DAVAMVLQKNVLFAGTI 446
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 447 A-DNI------RWGNPNATDEDVRRVCKLAQADGFIREFPkgydtyieeggSNVSGGQRQRLCIARALLKKPKILILDDS 519
Cdd:PRK10584 105 AlENVelpallRGESSRQSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170
....*....|..
gi 705456738 520 TSAVDTKT-DRL 530
Cdd:PRK10584 174 TGNLDRQTgDKI 185
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
354-577 |
3.31e-08 |
|
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: 56.35 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDvgsERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLI-------PR----LYDVS----SGSLEVGGR 418
Cdd:TIGR03269 1 IEVKNLTKKFD---GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgmdqyePTsgriIYHVAlcekCGYVERPSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 419 DVR------------EYDLETLRDAV--------AMVLQKNVLFAG--TIADNIRWGNPNA---TDEDVRRVCKLaqadg 473
Cdd:TIGR03269 78 VGEpcpvcggtlepeEVDFWNLSDKLrrrirkriAIMLQRTFALYGddTVLDNVLEALEEIgyeGKEAVGRAVDL----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 474 fIREFPKGYD-TYIeegGSNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKTEIPDT-TKIIIAQRV 551
Cdd:TIGR03269 153 -IEMVQLSHRiTHI---ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgISMVLTSHW 228
|
250 260
....*....|....*....|....*...
gi 705456738 552 ASVQE--SDEIIVMDGGRILDRGTHDQL 577
Cdd:TIGR03269 229 PEVIEdlSDKAIWLENGEIKEEGTPDEV 256
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
370-575 |
3.91e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.21 E-value: 3.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 370 PVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRdvreyDLETLRDAVA------MVLQKNVLFA 443
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN-----PCARLTPAKAhqlgiyLVPQEPLLFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 444 G-TIADNIRWGNPNaTDEDVRRVCKLaqadgfIREFPKGYDTYIEEGGSNVSggQRQRLCIARALLKKPKILILDDSTSA 522
Cdd:PRK15439 100 NlSVKENILFGLPK-RQASMQKMKQL------LAALGCQLDLDSSAGSLEVA--DRQIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 705456738 523 VD-TKTDRLIRGAFKTEIPDTTKIIIAQRVASV-QESDEIIVM-DGGRILDRGTHD 575
Cdd:PRK15439 171 LTpAETERLFSRIRELLAQGVGIVFISHKLPEIrQLADRISVMrDGTIALSGKTAD 226
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
72-280 |
4.22e-08 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 55.36 E-value: 4.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 72 FGLILLGCAVVSLFAGFMSGRYAAIASAGFAKNLRHDLFEKVQSFSFTNIDHFSTGSIITRITTDVTNIQYAFQMCIRVA 151
Cdd:cd18558 61 YAYYYLIIGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 152 VRAPLMVVVAWLFSFRISPSISMIFLIIIPILGVTLTGLALSVNPVFEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHE 231
Cdd:cd18558 141 FQNIATFGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKE 220
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 705456738 232 SRKFGRVSERIYEYFCKAEHVLAFNWPILNTCIYGAMLIISWMGTKQIV 280
Cdd:cd18558 221 ETRYAQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVT 269
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
354-568 |
5.44e-08 |
|
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: 53.44 E-value: 5.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYdvgSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETL----- 428
Cdd:cd03269 1 LEVENVTKRF---GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIgylpe 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 429 -----RDavaMVLQKNVLFAGTIAdnirwgnpNATDEDVRRvcklaQADGFIREFpkGYDTYIEEGGSNVSGGQRQRLCI 503
Cdd:cd03269 78 erglyPK---MKVIDQLVYLAQLK--------GLKKEEARR-----RIDEWLERL--ELSEYANKRVEELSKGNQQKVQF 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 705456738 504 ARALLKKPKILILDDSTSAVDTKTDRLirgaFKTEIPD-----TTKIIIAQRVASVQE-SDEIIVMDGGRI 568
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGLDPVNVEL----LKDVIRElaragKTVILSTHQMELVEElCDRVLLLNKGRA 206
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
370-568 |
6.00e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.39 E-value: 6.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 370 PVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVreyDLETLRDAVA---------------- 433
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEV---VTRSPQDGLAngivyisedrkrdglv 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 --MVLQKNVLFAGTIADNIRWGNPNATDEdvrrvcKLAQADgFIREF----PKgydtyIEEGGSNVSGGQRQRLCIARAL 507
Cdd:PRK10762 343 lgMSVKENMSLTALRYFSRAGGSLKHADE------QQAVSD-FIRLFniktPS-----MEQAIGLLSGGNQQKVAIARGL 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 705456738 508 LKKPKILILDDSTSAVDTktdrlirGAfKTEI--------PDTTKIIIaqrVAS-----VQESDEIIVMDGGRI 568
Cdd:PRK10762 411 MTRPKVLILDEPTRGVDV-------GA-KKEIyqlinqfkAEGLSIIL---VSSempevLGMSDRILVMHEGRI 473
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
360-578 |
8.18e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 54.03 E-value: 8.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 360 SFRYDVGSER----PVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVAMV 435
Cdd:PRK15112 13 TFRYRTGWFRrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 436 LQ--KNVLFA----GTIAD-NIRWGNPNATDEDVRRVCKLAQADGFIREFPKGYDTYIeeggsnvSGGQRQRLCIARALL 508
Cdd:PRK15112 93 FQdpSTSLNPrqriSQILDfPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHML-------APGQKQRLGLARALI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 705456738 509 KKPKILILDDSTSAVD-TKTDRLIRGAFK-TEIPDTTKIIIAQRVASVQE-SDEIIVMDGGRILDRGTHDQLL 578
Cdd:PRK15112 166 LRPKVIIADEALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
374-524 |
8.28e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 54.50 E-value: 8.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 374 DINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRdvreydleTLRDA------------VAMVLQKNVL 441
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGR--------VLFDAekgiclppekrrIGYVFQDARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 442 FAG-TIADNIRWGNPNATDEDVRRVCKLAQADGFIREFPkgydtyieeggSNVSGGQRQRLCIARALLKKPKILILDDST 520
Cdd:PRK11144 88 FPHyKVRGNLRYGMAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPL 156
|
....
gi 705456738 521 SAVD 524
Cdd:PRK11144 157 ASLD 160
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
346-580 |
1.10e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 53.98 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 346 IMDVPDGSITFND--VSFRydvgserpVLDDINLTIASGSTIGIVGGTGSAKS----SLVQLIPRLYDVSSGSLEVGGRD 419
Cdd:PRK11022 3 LLNVDKLSVHFGDesAPFR--------AVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 420 VREYDLETLRD----AVAMVLQK---------NVLFAGTIADNIRWGNPNATDEDvrRVCKLAQADGfIREFPKGYDTYI 486
Cdd:PRK11022 75 LQRISEKERRNlvgaEVAMIFQDpmtslnpcyTVGFQIMEAIKVHQGGNKKTRRQ--RAIDLLNQVG-IPDPASRLDVYP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 487 EEggsnVSGGQRQRLCIARALLKKPKILILDDSTSAVD-TKTDRLIRGAFKTEIPDTTK-IIIAQRVASVQES-DEIIVM 563
Cdd:PRK11022 152 HQ----LSGGMSQRVMIAMAIACRPKLLIADEPTTALDvTIQAQIIELLLELQQKENMAlVLITHDLALVAEAaHKIIVM 227
|
250
....*....|....*..
gi 705456738 564 DGGRILDRGTHDQLLQT 580
Cdd:PRK11022 228 YAGQVVETGKAHDIFRA 244
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
365-527 |
1.44e-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: 54.17 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 365 VGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSG------SLEVG----------GRDVREYDLETL 428
Cdd:TIGR03719 14 VPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGearpqpGIKVGylpqepqldpTKTVRENVEEGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 429 RDAVAMVLQKNVLFAgtiadniRWGNPNA-----TDEDVRRVCKLAQADGFIRE-----------FPKGyDTYIEeggsN 492
Cdd:TIGR03719 94 AEIKDALDRFNEISA-------KYAEPDAdfdklAAEQAELQEIIDAADAWDLDsqleiamdalrCPPW-DADVT----K 161
|
170 180 190
....*....|....*....|....*....|....*
gi 705456738 493 VSGGQRQRLCIARALLKKPKILILDDSTSAVDTKT 527
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
330-523 |
1.88e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 53.98 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 330 CQVLNEVSTVR-DNADPImdVPDGSITFNDVSFRydvgserpvlddinltIASGSTIGIVGGTGSAKSSLVQLIPRLYDV 408
Cdd:TIGR00954 443 GIVEYQDNGIKfENIPLV--TPNGDVLIESLSFE----------------VPSGNNLLICGPNGCGKSSLFRILGELWPV 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 409 SSGSLEVGGRDV------REY-DLETLRDavamvlqkNVLFAGTIADNIRWGnpnATDEDVRRVCKLAQADgFIREFPKG 481
Cdd:TIGR00954 505 YGGRLTKPAKGKlfyvpqRPYmTLGTLRD--------QIIYPDSSEDMKRRG---LSDKDLEQILDNVQLT-HILEREGG 572
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 705456738 482 YDTyIEEGGSNVSGGQRQRLCIARALLKKPKILILDDSTSAV 523
Cdd:TIGR00954 573 WSA-VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAV 613
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
357-527 |
3.52e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 51.36 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 357 NDVSFRYDVGS-ERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDvreydLETLRDAVAMV 435
Cdd:PRK11629 9 DNLCKRYQEGSvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQP-----MSKLSSAAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 436 LQKNVL-----FAGTIADNirwgnpNATdEDVRRVC-----KLAQADGFIREFPK--GYDTYIEEGGSNVSGGQRQRLCI 503
Cdd:PRK11629 84 LRNQKLgfiyqFHHLLPDF------TAL-ENVAMPLligkkKPAEINSRALEMLAavGLEHRANHRPSELSGGERQRVAI 156
|
170 180
....*....|....*....|....
gi 705456738 504 ARALLKKPKILILDDSTSAVDTKT 527
Cdd:PRK11629 157 ARALVNNPRLVLADEPTGNLDARN 180
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
368-526 |
4.46e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 50.57 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 368 ERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREydletLRDAvamvLQKNVLFAG--- 444
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR-----QRDE----YHQDLLYLGhqp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 445 ------TIADNIRW---GNPNATDEDVRRVckLAQA--DGFiREFPKGYdtyieeggsnVSGGQRQRLCIARALLKKPKI 513
Cdd:PRK13538 84 giktelTALENLRFyqrLHGPGDDEALWEA--LAQVglAGF-EDVPVRQ----------LSAGQQRRVALARLWLTRAPL 150
|
170
....*....|...
gi 705456738 514 LILDDSTSAVDTK 526
Cdd:PRK13538 151 WILDEPFTAIDKQ 163
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
368-573 |
5.13e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.18 E-value: 5.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 368 ERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLI---PRlYDVSSGSLEVGGRDVREYDLEtLRDAVAMVL--QKNVLF 442
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIaghPA-YKILEGDILFKGESILDLEPE-ERAHLGIFLafQYPIEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 443 AG-TIADNIRwgnpnATDEDVRRVCKLAQAD-----GFIREF-------PKGYDTYIEEGgsnVSGGQRQRLCIARALLK 509
Cdd:CHL00131 97 PGvSNADFLR-----LAYNSKRKFQGLPELDpleflEIINEKlklvgmdPSFLSRNVNEG---FSGGEKKRNEILQMALL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 705456738 510 KPKILILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIA---QRVASVQESDEIIVMDGGRILDRGT 573
Cdd:CHL00131 169 DSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILIthyQRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
374-568 |
7.54e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.98 E-value: 7.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 374 DINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDAVAMVL----QKNVLF------- 442
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLpedrQSSGLYldaplaw 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 443 ---AGTIADNIRWGNP---NATDEDVRRV--CKLAQADGFIRefpkgydtyieeggsNVSGGQRQRLCIARALLKKPKIL 514
Cdd:PRK15439 361 nvcALTHNRRGFWIKPareNAVLERYRRAlnIKFNHAEQAAR---------------TLSGGNQQKVLIAKCLEASPQLL 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 705456738 515 ILDDSTSAVDTktdrlirGAfKTEIPDTTKIIIAQRVAS----------VQESDEIIVMDGGRI 568
Cdd:PRK15439 426 IVDEPTRGVDV-------SA-RNDIYQLIRSIAAQNVAVlfissdleeiEQMADRVLVMHQGEI 481
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
35-305 |
1.22e-06 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 50.39 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 35 APTFVIVESVLEILIPTVMASMIDQGVAGGSMP----AIWKFGLIllgCAVVSLFAGFMSGRYAaIASAGFAKNLRHDLF 110
Cdd:cd18784 1 AFFFLLAAAVGEIFIPYYTGQVIDGIVIEKSQDkfsrAIIIMGLL---AIASSVAAGIRGGLFT-LAMARLNIRIRNLLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 111 EKV--QSFSFtnIDHFSTGSIITRITTDVTNIQYAFQMCIRVAVRAPLMVVVAWLFSFRISPSISMIFLIIIPIL----- 183
Cdd:cd18784 77 RSIvsQEIGF--FDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIaivsk 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 184 --GVTLTGLALSVNPVFEKVfhtydhlNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEHVLA-FNWP-- 258
Cdd:cd18784 155 vyGDYYKKLSKAVQDSLAKA-------NEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGgYVWSne 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 705456738 259 ------ILNTCIYGAMLIIswmgTKQIVGshnnaavglttGDLTALVTYAMQI 305
Cdd:cd18784 228 ltelalTVSTLYYGGHLVI----TGQISG-----------GNLISFILYQLEL 265
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
461-577 |
1.29e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.89 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 461 DVRRVCKLAQADGFIREFpkgydTYIEEGG---SNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKT 537
Cdd:NF000106 115 DLSRKDARARADELLERF-----SLTEAAGraaAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRS 189
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 705456738 538 EIPDTTKIIIAQRVASVQE--SDEIIVMDGGRILDRGTHDQL 577
Cdd:NF000106 190 MVRDGATVLLTTQYMEEAEqlAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
365-568 |
1.62e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.08 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 365 VGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYD-VSSGSLEVGGRDVreyDLETLRDAV----AMV---- 435
Cdd:PRK13549 271 VNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPV---KIRNPQQAIaqgiAMVpedr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 436 ----------LQKNVlfagTIADNIRWGNPNATDEDVrrvcKLAQADGFIREFpKGYDTYIEEGGSNVSGGQRQRLCIAR 505
Cdd:PRK13549 348 krdgivpvmgVGKNI----TLAALDRFTGGSRIDDAA----ELKTILESIQRL-KVKTASPELAIARLSGGNQQKAVLAK 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 705456738 506 ALLKKPKILILDDSTSAVDTktdrlirGAfKTEIpdtTKII--IAQRVASV----QE-------SDEIIVMDGGRI 568
Cdd:PRK13549 419 CLLLNPKILILDEPTRGIDV-------GA-KYEI---YKLInqLVQQGVAIivisSElpevlglSDRVLVMHEGKL 483
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
372-567 |
2.37e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.31 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 372 LDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSS--GSLEVGGRDVREYDL-ETLRDAVAMVLQKNVLFAG-TIA 447
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIrDTERAGIAIIHQELALVKElSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 448 DNIRWGN---PNAT---DEDVRRVCKLaqadgfIREFPKGYDTYIEEGgsNVSGGQRQRLCIARALLKKPKILILDDSTS 521
Cdd:PRK13549 101 ENIFLGNeitPGGImdyDAMYLRAQKL------LAQLKLDINPATPVG--NLGLGQQQLVEIAKALNKQARLLILDEPTA 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 705456738 522 AV-DTKTD---RLIRGaFKT----------------EIPDTTKII-----IAQRVASVQESDEIIVMDGGR 567
Cdd:PRK13549 173 SLtESETAvllDIIRD-LKAhgiaciyishklnevkAISDTICVIrdgrhIGTRPAAGMTEDDIITMMVGR 242
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
33-329 |
3.25e-06 |
|
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: 49.05 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 33 ILAPTFVIVesVLEILIPTVMASMIDQGVAGGSMPAIWKFGLILLGCAVVSLFAGFMSGRYAAIASAGFAKNLRHDLFEK 112
Cdd:cd18555 7 ILLLSLLLQ--LLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 113 VQSFSFTNIDHFSTGSIITRITTDVTnIQyafQMCIRVAVRA---PLMVVVAWLFSFRISPSISMIFLIIIPILGVTLTg 189
Cdd:cd18555 85 LLKLPYSFFENRSSGDLLFRANSNVY-IR---QILSNQVISLiidLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLL- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 190 lalsvnpVFEKVFHTYDH--------LNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEHVLAFNWPILN 261
Cdd:cd18555 160 -------LTRKKIKKLNQeeivaqtkVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISS 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 705456738 262 TCIYGAMLIISWMGTKQIVGSHnnaavgLTTGDLTALVTYAMQILMSLNMVSMIIVMVVISRADAERI 329
Cdd:cd18555 233 SIQFIAPLLILWIGAYLVINGE------LTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
38-225 |
3.58e-06 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350041 [Multi-domain] Cd Length: 293 Bit Score: 48.99 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 38 FVIVESVLEILIPTVMASMID---QGVAGGSMPAIWK-FGLILlGCAVVSLFAGFMSGR--YAAIASAGFAKN-LRHDLF 110
Cdd:cd18597 5 LKLLADVLQVLSPLLLKYLINfveDAYLGGPPPSIGYgIGYAI-GLFLLQLLSSLLLNHffYRSMLTGAQVRAaLTKAIY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 111 EKvqSFSFTNIDH--FSTGSIITRITTDVTNIQYAFQMCIRVAVrAPLMVVvawlfsfrispsISMIFLIIipILGVT-L 187
Cdd:cd18597 84 RK--SLRLSGKSRheFPNGKITNLMSTDLSRIDFALGFFHFLWT-APIQII------------IAIALLIV--NLGPSaL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 705456738 188 TGLALSV--NPV----FEKVFHTYDHLNNIVD-------ENLQGIRVVKSY 225
Cdd:cd18597 147 VGIGVLIlsIPLqgflMKKLFKLRKKANKITDkrvkltqEILQGIRVIKFY 197
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
53-244 |
4.60e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 48.82 E-value: 4.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 53 MASMIDQGVAGGSMPAIWKFGLILLGCAVVSlfAGFMSGRYAAIASAGFA--KNLRHDLFEKVQSFSFTNIDHFSTGSII 130
Cdd:cd18561 19 LARALARIFAGGPWEDIMPPLAGIAGVIVLR--AALLWLRERVAHRAAQRvkQHLRRRLFAKLLKLGPGYLEGERTGELQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 131 TRITTDVTNIQ-----YAFQMCIrvAVRAPlMVVVAWLFSfrISPSISMIFLIIIPILGVTLTGLALSVNPVFEKVFHTY 205
Cdd:cd18561 97 TTVVDGVEALEayygrYLPQLLV--ALLGP-LLILIYLFF--LDPLVALILLVFALLIPLSPALWDRLAKDTGRRHWAAY 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 705456738 206 DHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYE 244
Cdd:cd18561 172 GRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQ 210
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
365-524 |
5.82e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.35 E-value: 5.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 365 VGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSG------SLEVG----------GRDVREYDLETL 428
Cdd:PRK11819 16 VPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGearpapGIKVGylpqepqldpEKTVRENVEEGV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 429 RDAVAMVLQKNVLFAgtiadniRWGNPNA-TDEDVRRVCKL----AQADGF------------IReFPKGyDTYIeeggS 491
Cdd:PRK11819 96 AEVKAALDRFNEIYA-------AYAEPDAdFDALAAEQGELqeiiDAADAWdldsqleiamdaLR-CPPW-DAKV----T 162
|
170 180 190
....*....|....*....|....*....|...
gi 705456738 492 NVSGGQRQRLCIARALLKKPKILILDDSTSAVD 524
Cdd:PRK11819 163 KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
372-567 |
6.35e-06 |
|
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: 49.05 E-value: 6.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 372 LDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLY-------DVSSGSLEVGGRDVREydleTLRDAVAMVLQKNVLFAG 444
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphgtwdgEIYWSGSPLKASNIRD----TERAGIVIIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 445 -TIADNIRWGNP-------NATDEDVRRVCKLaqadgfIREFpKGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKILIL 516
Cdd:TIGR02633 93 lSVAENIFLGNEitlpggrMAYNAMYLRAKNL------LREL-QLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLIL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 705456738 517 DDSTSAVDTKTDR----LIRG-----------AFKTE----IPDTTKII-----IAQRVASVQESDEIIVMDGGR 567
Cdd:TIGR02633 166 DEPSSSLTEKETEilldIIRDlkahgvacvyiSHKLNevkaVCDTICVIrdgqhVATKDMSTMSEDDIITMMVGR 240
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
354-529 |
7.19e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 48.78 E-value: 7.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDvgsERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGgrdvreydlETLRdaVA 433
Cdd:TIGR03719 323 IEAENLTKAFG---DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG---------ETVK--LA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 434 MVLQ--------KNV---LFAGTiaDNIRWGNpnatdedvRRVCKLAQADGFirEFpKGYDTyiEEGGSNVSGGQRQRLC 502
Cdd:TIGR03719 389 YVDQsrdaldpnKTVweeISGGL--DIIKLGK--------REIPSRAYVGRF--NF-KGSDQ--QKKVGQLSGGERNRVH 453
|
170 180
....*....|....*....|....*..
gi 705456738 503 IARALLKKPKILILDDSTSAVDTKTDR 529
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLDVETLR 480
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
358-518 |
9.04e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 47.84 E-value: 9.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 358 DVSFRYdvgSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYD---LETLRDAVAM 434
Cdd:PRK11831 12 GVSFTR---GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrLYTVRKRMSM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 435 VLQKNVLFAG-TIADNIRWgnpnATDEDVRRVCKLAQADGFIREFPKGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKI 513
Cdd:PRK11831 89 LFQSGALFTDmNVFDNVAY----PLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDL 164
|
....*
gi 705456738 514 LILDD 518
Cdd:PRK11831 165 IMFDE 169
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
372-566 |
9.50e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.63 E-value: 9.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 372 LDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGrdvREYDLETLRDA----VAMVLQK-NVLFAGTI 446
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN---INYNKLDHKLAaqlgIGIIYQElSVIDELTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 447 ADNIRWGNpnatdEDVRRVCKLAQAD-GFIREFPK------GYDTYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDS 519
Cdd:PRK09700 98 LENLYIGR-----HLTKKVCGVNIIDwREMRVRAAmmllrvGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 705456738 520 TSAV-DTKTDRL--IRGAFKTEipDTTKIIIAQRVASVQE-SDEIIVMDGG 566
Cdd:PRK09700 173 TSSLtNKEVDYLflIMNQLRKE--GTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
368-531 |
9.68e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 48.72 E-value: 9.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 368 ERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIP-RLYDVS-SGSLEVGGRDVREydlETLRdAVAMVLQKNVLFAG- 444
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANNRKPTK---QILK-RTGFVTQDDILYPHl 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 445 TIADNIRWGN----PNATDEDVrrvcKLAQADGFIREF--PKGYDTYIeeGGS---NVSGGQRQRLCIARALLKKPKILI 515
Cdd:PLN03211 156 TVRETLVFCSllrlPKSLTKQE----KILVAESVISELglTKCENTII--GNSfirGISGGERKRVSIAHEMLINPSLLI 229
|
170
....*....|....*..
gi 705456738 516 LDDSTSAVD-TKTDRLI 531
Cdd:PLN03211 230 LDEPTSGLDaTAAYRLV 246
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
358-524 |
1.07e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 46.48 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 358 DVSFRYdvgSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREyDLETLrdavamvlQ 437
Cdd:PRK13540 6 ELDFDY---HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTY--------Q 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 438 KNVLFAGTiadniRWG-NPNATDE-----DVRRVCKLAQADGFIREFPKGYdtYIEEGGSNVSGGQRQRLCIARALLKKP 511
Cdd:PRK13540 74 KQLCFVGH-----RSGiNPYLTLRenclyDIHFSPGAVGITELCRLFSLEH--LIDYPCGLLSSGQKRQVALLRLWMSKA 146
|
170
....*....|...
gi 705456738 512 KILILDDSTSAVD 524
Cdd:PRK13540 147 KLWLLDEPLVALD 159
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
38-304 |
1.78e-05 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 47.08 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 38 FVIVESVLEILIPTVMASMID----QGVAGGSMPAIWKFGLILLGCAVVSL-----FAGFMSGRYAAIASAGFAKNLRhd 108
Cdd:cd18589 4 LVVLSSLGEMAIPYYTGRMTDwimnKDAPEAFTAAITVMSLLTIASAVSEFvcdliYNITMSRIHSRLQGLVFAAVLR-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 109 lfekvQSFSFtnIDHFSTGSIITRITTDVTNIQYAFQMCIRVAVRAPLMVVVAWLFSFRISPSISMIFLIIIPILGVTLT 188
Cdd:cd18589 82 -----QEIAF--FDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 189 GLALSVNPVFEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEHVLAFN-WP------ILN 261
Cdd:cd18589 155 FVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSmWTssfsglALK 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 705456738 262 TCI--YGAMLIISwmGTkqivgshnnaavgLTTGDLTALVTYAMQ 304
Cdd:cd18589 235 VGIlyYGGQLVTA--GT-------------VSSGDLVTFVLYELQ 264
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
493-579 |
1.94e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.80 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 493 VSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKT--EIPDTTKIiiaqrVASVQES-------DEIIVM 563
Cdd:TIGR00956 210 VSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTsaNILDTTPL-----VAIYQCSqdayelfDKVIVL 284
|
90
....*....|....*.
gi 705456738 564 DGGRILDRGTHDQLLQ 579
Cdd:TIGR00956 285 YEGYQIYFGPADKAKQ 300
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
372-526 |
2.12e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.42 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 372 LDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVR-EYDLETLRDAVAMVLQK-NVLFAGTIADN 449
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 450 IRWGN-PNA---TDED-VRRVCKLAQADGFIREFPKgydtyieEGGSNVSGGQRQRLCIARALLKKPKILILDDSTSAVD 524
Cdd:PRK10982 94 MWLGRyPTKgmfVDQDkMYRDTKAIFDELDIDIDPR-------AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT 166
|
..
gi 705456738 525 TK 526
Cdd:PRK10982 167 EK 168
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
365-579 |
2.37e-05 |
|
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: 47.13 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 365 VGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVS-SGSLEVGGR--DVREyDLETLRDAVAMVLQknvl 441
Cdd:TIGR02633 269 INPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvDIRN-PAQAIRAGIAMVPE---- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 442 fagtiaDNIRWG-------NPNATDEDVRRVCKLAQAD----------GFIREFPKGYDTYIEEGGsnVSGGQRQRLCIA 504
Cdd:TIGR02633 344 ------DRKRHGivpilgvGKNITLSVLKSFCFKMRIDaaaelqiigsAIQRLKVKTASPFLPIGR--LSGGNQQKAVLA 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 505 RALLKKPKILILDDSTSAVDTktdrlirGAfKTEIPDTTKIIIAQRVASVQES----------DEIIVMDGGRILDRGTH 574
Cdd:TIGR02633 416 KMLLTNPRVLILDEPTRGVDV-------GA-KYEIYKLINQLAQEGVAIIVVSselaevlglsDRVLVIGEGKLKGDFVN 487
|
....*
gi 705456738 575 DQLLQ 579
Cdd:TIGR02633 488 HALTQ 492
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
369-568 |
2.42e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.03 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 369 RPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYD-LETLRDAVAMVLQK--------- 438
Cdd:PRK10982 261 QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAINHGFALVTEErrstgiyay 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 439 -NVLFAGTIADNIRWGNPNATDEDVRRVCKLAQADGFIREFPKGYDTYIeegGSnVSGGQRQRLCIARALLKKPKILILD 517
Cdd:PRK10982 341 lDIGFNSLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQI---GS-LSGGNQQKVIIGRWLLTQPEILMLD 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 705456738 518 DSTSAVDTktdrlirGAfKTEI---------PDTTKIIIAQRVASVQE-SDEIIVMDGGRI 568
Cdd:PRK10982 417 EPTRGIDV-------GA-KFEIyqliaelakKDKGIIIISSEMPELLGiTDRILVMSNGLV 469
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
38-225 |
2.66e-05 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 46.32 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 38 FVIVESVLEILIPTVMASMIdQGVAGGSMPAIWKfGLILLGC-AVVSLFAGFMSGRY------------AAIASAgfakn 104
Cdd:cd18579 5 LKLLEDLLSLAQPLLLGLLI-SYLSSYPDEPLSE-GYLLALAlFLVSLLQSLLLHQYfflsfrlgmrvrSALSSL----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 105 lrhdLFEKVQSFSFTNIDHFSTGSIITRITTDVTNIQYAFQMCIrVAVRAPLMVVVA-WLFSFRISPSIsmifliiipIL 183
Cdd:cd18579 78 ----IYRKALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLH-YLWSAPLQIIVAlYLLYRLLGWAA---------LA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 705456738 184 GVTLTGLALSVNPVFEKVFHTY--------DHLNNIVDENLQGIRVVKSY 225
Cdd:cd18579 144 GLGVLLLLIPLQAFLAKLISKLrkklmkatDERVKLTNEILSGIKVIKLY 193
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
354-568 |
2.91e-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: 45.33 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 354 ITFNDVSFRYDVG-SERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLI---PRLYDVSSGSLEVGGRDVREyDLETLR 429
Cdd:cd03233 4 LSWRNISFTTGKGrSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKE-FAEKYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 430 DAVAMVLQKNVLFagtiadnirwgnPNATdedVRRVCKLA---QADGFIRefpkgydtyieeggsNVSGGQRQRLCIARA 506
Cdd:cd03233 83 GEIIYVSEEDVHF------------PTLT---VRETLDFAlrcKGNEFVR---------------GISGGERKRVSIAEA 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 705456738 507 LLKKPKILILDDSTSAVDTKTdrlirgAFK--TEIPDTTKIIIAQRVASV-QESDEI-------IVMDGGRI 568
Cdd:cd03233 133 LVSRASVLCWDNSTRGLDSST------ALEilKCIRTMADVLKTTTFVSLyQASDEIydlfdkvLVLYEGRQ 198
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
358-576 |
3.98e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.44 E-value: 3.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 358 DVSFRYDVGSERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVReydLETLRDAVA--MV 435
Cdd:PRK11288 255 EVRLRLDGLKGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID---IRSPRDAIRagIM 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 436 L------QKNVLFAGTIADNI-----RWGNPNATDEDVRRVCKLAqaDGFIREF----PKGyDTYIeeggSNVSGGQRQR 500
Cdd:PRK11288 332 LcpedrkAEGIIPVHSVADNInisarRHHLRAGCLINNRWEAENA--DRFIRSLniktPSR-EQLI----MNLSGGNQQK 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 501 LCIARALLKKPKILILDDSTSAVDTktdrlirGAfKTEIPDTTKIIIAQRVASVQES----------DEIIVMDGGRILD 570
Cdd:PRK11288 405 AILGRWLSEDMKVILLDEPTRGIDV-------GA-KHEIYNVIYELAAQGVAVLFVSsdlpevlgvaDRIVVMREGRIAG 476
|
....*.
gi 705456738 571 RGTHDQ 576
Cdd:PRK11288 477 ELAREQ 482
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
372-597 |
4.49e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.58 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 372 LDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEvggrdvreydletlRDAVAMVLQKNVLFAGTIA--DN 449
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD--------------RNGEVSVIAISAGLSGQLTgiEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 450 IRWG------NPNATDEDVRRVCKLAQADGFIREFPKGYdtyieeggsnvSGGQRQRLCIARALLKKPKILILDDSTSAV 523
Cdd:PRK13546 106 IEFKmlcmgfKRKEIKAMTPKIIEFSELGEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVG 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 705456738 524 D-TKTDRLIRGAFKTEIPDTTKIIIAQRVASVQE-SDEIIVMDGGRILDRGTHDQLLQTCDEYRSIYQSQTKSQGE 597
Cdd:PRK13546 175 DqTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPKYEAFLNDFKKKSKAEQK 250
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
368-574 |
4.71e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.17 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 368 ERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIP--RLYDVSSGSLEVGGRDVREYDLETLR-DAVAMVLQKNVLFAG 444
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPEDRAgEGIFMAFQYPVEIPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 445 TIADNIRWGNPNAtdedVRRVCKLAQADGFirefpkGYDTYIEEG-------------GSNV--SGGQRQRLCIARALLK 509
Cdd:PRK09580 93 VSNQFFLQTALNA----VRSYRGQEPLDRF------DFQDLMEEKiallkmpedlltrSVNVgfSGGEKKRNDILQMAVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 705456738 510 KPKILILDDSTSAVDTKTDRLIRGAFKTEIPDTTKIIIA---QRVASVQESDEIIVMDGGRILDRGTH 574
Cdd:PRK09580 163 EPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVthyQRILDYIKPDYVHVLYQGRIVKSGDF 230
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
496-524 |
4.98e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.27 E-value: 4.98e-05
10 20
....*....|....*....|....*....
gi 705456738 496 GQRQRLCIARALLKKPKILILDDSTSAVD 524
Cdd:NF033858 401 GIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
38-328 |
1.55e-04 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 44.03 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 38 FVIVESVLEILIPTVMASMIDQgVAGGSMPAIWKFGLILLGCAVVSLFAGFMSG-RYAAIA--SAGFAKNLRHDLFEKVQ 114
Cdd:cd18582 4 LLVLAKLLNVAVPFLLKYAVDA-LSAPASALLAVPLLLLLAYGLARILSSLFNElRDALFArvSQRAVRRLALRVFRHLH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 115 --SFSFtnidHFS--TGSIitriTTDVTNIQYAFQMCIRVAVR--APL---MVVVAWLFSFRISPSISMIFLIIIpILGV 185
Cdd:cd18582 83 slSLRF----HLSrkTGAL----SRAIERGTRGIEFLLRFLLFniLPTileLLLVCGILWYLYGWSYALITLVTV-ALYV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 186 TLTGLALS-VNPVFEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEHVLAFnwpiLN--- 261
Cdd:cd18582 154 AFTIKVTEwRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLAL----LNigq 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 705456738 262 TCIYGA-MLIISWMGTKQIVGSHnnaavgLTTGDLTALVTYAMQILMSLNMVSMIIVMVVISRADAER 328
Cdd:cd18582 230 ALIISLgLTAIMLLAAQGVVAGT------LTVGDFVLVNTYLLQLYQPLNFLGFVYREIRQSLIDMEK 291
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
352-527 |
1.55e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.56 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 352 GSITF--NDVSFRYDvgsERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGR-DVREYDletl 428
Cdd:PRK11147 316 GKIVFemENVNYQID---GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVAYFD---- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 429 RDAVAMVLQKnvlfagTIADNIRWGNPNATDEDVRRvcklaQADGFIREF---PKGYDTYIEEggsnVSGGQRQRLCIAR 505
Cdd:PRK11147 389 QHRAELDPEK------TVMDNLAEGKQEVMVNGRPR-----HVLGYLQDFlfhPKRAMTPVKA----LSGGERNRLLLAR 453
|
170 180
....*....|....*....|..
gi 705456738 506 ALLKKPKILILDDSTSAVDTKT 527
Cdd:PRK11147 454 LFLKPSNLLILDEPTNDLDVET 475
|
|
| ABC_6TM_AarD_CydDC_like |
cd18781 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ... |
47-241 |
3.33e-04 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; This subgroup belongs to the ABC_6TM_AarD_CydDC_like subgroup of the ABC_6TM exporter family. The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs). The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350054 [Multi-domain] Cd Length: 290 Bit Score: 42.91 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 47 ILIPTVMASMIDQGVAGGSMPA-IWKFGLILLGCAVVSLFAGFMSGRYAAIASAGFAKNLRHDLFEKVQSFSFTNIDHFS 125
Cdd:cd18781 13 IAFVFSIANLLQKLLEGKLTTAsLLIVLGILAIAIIVRFICTRLASRASYRASADVKKTLREKIYDKLLRLGPSYQEKVS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 126 TGSIITRITTDVTNI---------QYAFqmcirvAVRAP--LMVVVAWlfsfrISPSISMIFLIIIPILGVTLTGLALSV 194
Cdd:cd18781 93 TAEVVQLSVEGVEQLeiyfgrylpQFFY------SMLAPltLFVVLAP-----INWKAALVLLICVPLIPISIIAVQKIA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 705456738 195 NPVFEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSER 241
Cdd:cd18781 162 KKLLSKYWGSYTDLGDSFLENLQGLTTLKIYQADERRHEEMNEEAED 208
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
372-532 |
3.36e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.45 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 372 LDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVREYDLETLRDA-VAMVLQK-NVLFAGTIADN 449
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgIGIIHQElNLIPQLTIAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 450 IRWGNpnatdEDVRRVCKL------AQADGFIREFPKGYDTYIEEGgsNVSGGQRQRLCIARALLKKPKILILDDSTSAV 523
Cdd:PRK10762 100 IFLGR-----EFVNRFGRIdwkkmyAEADKLLARLNLRFSSDKLVG--ELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
170
....*....|
gi 705456738 524 -DTKTDRLIR 532
Cdd:PRK10762 173 tDTETESLFR 182
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
157-328 |
4.96e-04 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 42.52 E-value: 4.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 157 MVVVAWLFSFRISPSISMIFLIIIpILGVTLTGLALSVNPVFEKVFHTYDH-LNNIVDENLQGIRVVKSYDREEHESRKF 235
Cdd:cd18583 124 LVIAIVYLYYLFDPYMGLIVAVVM-VLYVWSTIKLTSWRTKLRRDMIDADReERSILTESLLNWETVKYFNREPYEKERY 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 236 GR-VSERIyeyfcKAEHVLAFNWPILNTC----IYGAMLIISWMGTKQIvgSHNNAAVGlttgDLTALVTYAMQILMSLN 310
Cdd:cd18583 203 REaVKNYQ-----KAERKYLFSLNLLNAVqsliLTLGLLAGCFLAAYQV--SQGQATVG----DFVTLLTYWAQLSGPLN 271
|
170
....*....|....*...
gi 705456738 311 MVSMIIVMVVISRADAER 328
Cdd:cd18583 272 FFATLYRSIQSDLIDAER 289
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
381-532 |
5.38e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.82 E-value: 5.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 381 SGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGslevggrDVREYDLETLRDAVAMVLQKnvlfagtiadnirwgnpnatde 460
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG-------GVIYIDGEDILEEVLDQLLL---------------------- 51
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 705456738 461 dvrrvcklaqadgfirefpkgydTYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDSTSAVDTKTDRLIR 532
Cdd:smart00382 52 -----------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLL 100
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
372-565 |
5.44e-04 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 42.01 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 372 LDDINLTIASGS-----TIGIVGGTGSAKSSLVQLIprlydvsSGSLEVGGRDVreydlETLRDAVAMVLQK-NVLFAGT 445
Cdd:cd03237 10 LGEFTLEVEGGSiseseVIGILGPNGIGKTTFIKML-------AGVLKPDEGDI-----EIELDTVSYKPQYiKADYEGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 446 IADNIRwgnpnatdEDVRRVCKLAQadgFIREF--PKGYDTYIEEGGSNVSGGQRQRLCIARALLKKPKILILDDSTSAV 523
Cdd:cd03237 78 VRDLLS--------SITKDFYTHPY---FKTEIakPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 705456738 524 DTKT--------DRLIRGAFKTEIPDTTKIIIAQRVAsvqesDEIIVMDG 565
Cdd:cd03237 147 DVEQrlmaskviRRFAENNEKTAFVVEHDIIMIDYLA-----DRLIVFEG 191
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
369-524 |
6.16e-04 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 41.55 E-value: 6.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 369 RPVLDDINLTIASGSTIGIVGGTGSAKS----SLVQLIPrlydVSSGSLEVGGRDVREYDL-ETLRDAVAMVLQKNVLFA 443
Cdd:COG1137 16 RTVVKDVSLEVNQGEIVGLLGPNGAGKTttfyMIVGLVK----PDSGRIFLDGEDITHLPMhKRARLGIGYLPQEASIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 444 G-TIADNIRwgnpnA------TDEDVRRvcklAQADGFIREFpkgydtYIEE----GGSNVSGGQRQRLCIARALLKKPK 512
Cdd:COG1137 92 KlTVEDNIL-----AvlelrkLSKKERE----ERLEELLEEF------GITHlrksKAYSLSGGERRRVEIARALATNPK 156
|
170
....*....|..
gi 705456738 513 ILILDDSTSAVD 524
Cdd:COG1137 157 FILLDEPFAGVD 168
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
222-329 |
9.61e-04 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 41.44 E-value: 9.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 222 VKSYDREEHESRKFGRVSERIYEYFCKAEHVLAF-NWP---ILNTCIYGAMLIISWMGTKQivgshnnaavGLTTGDLTA 297
Cdd:cd18560 191 VKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLlNVGqqlIIQLGLTLGLLLAGYRVVDG----------GLSVGDFVA 260
|
90 100 110
....*....|....*....|....*....|..
gi 705456738 298 LVTYAMQILMSLNMVSMIIVMVVISRADAERI 329
Cdd:cd18560 261 VNTYIFQLFQPLNFLGTIYRMIIQSLTDMENL 292
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
492-577 |
1.55e-03 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 40.74 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 492 NVSGGQRQRLCIARALLKKPKILILDDSTSAVDTK-TDRL------IRGAFKTEIpdttkIIIAQRVASVQE-SDEIIVM 563
Cdd:PRK11300 153 NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKeTKELdeliaeLRNEHNVTV-----LLIEHDMKLVMGiSDRIYVV 227
|
90
....*....|....
gi 705456738 564 DGGRILDRGTHDQL 577
Cdd:PRK11300 228 NQGTPLANGTPEEI 241
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
40-235 |
2.17e-03 |
|
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: 40.27 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 40 IVESVLEILIPTVMASMIDQGVAGGSMPAIWKFGLILLGCAVVS-LFAGFMSGRYAAIASAgFAKNLRHDLFEKVQSFSF 118
Cdd:cd18782 12 FVVQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEaVLTALRTYLFTDTANR-IDLELGGTIIDHLLRLPL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 119 TNIDHFSTGSIITRItTDVTNI-QYAFQMCIRVAVRAPLMVV-VAWLFSfrISPSISMIFLIIIPILGvtltGLALSVNP 196
Cdd:cd18782 91 GFFDKRPVGELSTRI-SELDTIrGFLTGTALTTLLDVLFSVIyIAVLFS--YSPLLTLVVLATVPLQL----LLTFLFGP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 705456738 197 VFEKVFH--------TYDHLNnivdENLQGIRVVKSYDREEHESRKF 235
Cdd:cd18782 164 ILRRQIRrraeasakTQSYLV----ESLTGIQTVKAQNAELKARWRW 206
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
368-547 |
3.27e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.26 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 368 ERPVLDDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSG--SLEVGGR------DVREYDLETLRDAVAM----- 434
Cdd:PRK15064 13 AKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGnvSLDPNERlgklrqDQFAFEEFTVLDTVIMghtel 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 435 --VLQKNvlfagtiaDNIrWGNPNATDEDVRRVCKL----AQADGFIREFPKGyDTYIEEG-------G--SNVSGGQRQ 499
Cdd:PRK15064 93 weVKQER--------DRI-YALPEMSEEDGMKVADLevkfAEMDGYTAEARAG-ELLLGVGipeeqhyGlmSEVAPGWKL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 705456738 500 RLCIARALLKKPKILILDDSTSAVDTKTDRLIRGAFKTEipDTTKIII 547
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNER--NSTMIII 208
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
362-583 |
5.59e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 39.77 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 362 RYDVGSERpvldDINLTIASGSTIGIVGGTGSAKSSLVQLIPRLYDVSSGSLEVGGRDVR-EYDLETLRDAVAMVLQ--- 437
Cdd:PRK09700 273 SRDRKKVR----DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAYITEsrr 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 438 KNVLFAG-TIADNIR-------------WGNPNATDEDvrrvcKLAQADgfiREFPKGYDTYIEEGGSNVSGGQRQRLCI 503
Cdd:PRK09700 349 DNGFFPNfSIAQNMAisrslkdggykgaMGLFHEVDEQ-----RTAENQ---RELLALKCHSVNQNITELSGGNQQKVLI 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 504 ARALLKKPKILILDDSTSAVDTKTdrlirgafKTEI-------PDTTKIIIAqrVAS-----VQESDEIIVMDGGRIldr 571
Cdd:PRK09700 421 SKWLCCCPEVIIFDEPTRGIDVGA--------KAEIykvmrqlADDGKVILM--VSSelpeiITVCDRIAVFCEGRL--- 487
|
250
....*....|..
gi 705456738 572 gthDQLLQTCDE 583
Cdd:PRK09700 488 ---TQILTNRDD 496
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
104-309 |
6.89e-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: 39.00 E-value: 6.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 104 NLRHDLFEKVQSFSFTNIDHFSTGSIITRITTDVTNIQYAFqmcIRV---AVRAPLMVVVAWLFSFRISPSISMIFLIII 180
Cdd:cd18585 69 NLRVWFYRKLEPLAPARLQKYRSGDLLNRIVADIDTLDNLY---LRVlspPVVALLVILATILFLAFFSPALALILLAGL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 181 PILGVTLTGLALSV-NPVFEKVFHTYDHLNNIVDENLQGIRVVKSYDREEHESRKFGRVSERIYEYFCKAEHVLAFNWPI 259
Cdd:cd18585 146 LLAGVVIPLLFYRLgKKIGQQLVQLRAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGLSQAL 225
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 705456738 260 LNTCIYGAMLIISWMGTKQIvgshnnaavglTTGDLTAlVTYAMQILMSL 309
Cdd:cd18585 226 MILLSGLTVWLVLWLGAPLV-----------QNGALDG-ALLAMLVFAVL 263
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
32-241 |
9.75e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 38.33 E-value: 9.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 32 TILAPTFVIveSVLEILIPTVMASMIDQGVAGGSMPAIWkfgLILLGCAVVSLFAGFMSG---RYAAIASAGFAKNLRHD 108
Cdd:cd18566 6 QVLLASLFI--NILALATPLFILQVYDRVIPNESIPTLQ---VLVIGVVIAILLESLLRLlrsYILAWIGARFDHRLSNA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 109 LFEKVQSFSFTNIDHFSTGSIITRITtDVTNI--QYAFQMcirvavrapLMVVVAWLFSFrispsismIFLIIIPILGVT 186
Cdd:cd18566 81 AFEHLLSLPLSFFEREPSGAHLERLN-SLEQIreFLTGQA---------LLALLDLPFVL--------IFLGLIWYLGGK 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 705456738 187 LT-----------GLALSVNPVFEKVF-HTYDHL---NNIVDENLQGIRVVKSYDREEHESRKFGRVSER 241
Cdd:cd18566 143 LVlvplvllglfvLVAILLGPILRRALkERSRADerrQNFLIETLTGIHTIKAMAMEPQMLRRYERLQAN 212
|
|
| |
