|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-668 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 592.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 1 MKIGKTLWRYALLYRKLLITAVLLLTVAVGAELTGPFIGKKMIDDHILGiektwyeaaekdknavqfhgvsyvredrlqe 80
Cdd:COG1132 6 RKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAG------------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 81 pvskakeahiyqvgmafyfvdqavsfdgnrtvsdgkltitngdksrtyaaekltkqelfqfyqPEIKGMVLLICLYGGLL 160
Cdd:COG1132 55 ---------------------------------------------------------------GDLSALLLLLLLLLGLA 71
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 161 VFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVTVLSTFVTSGIYMFG 240
Cdd:COG1132 72 LLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIG 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 241 IFTALFLLDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTIIQAFRHQKETMREFEELNE 320
Cdd:COG1132 152 ALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANE 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 321 SHFYFQNRMLNLNSLMShNLVNVIRNLAFVCLIWhfGGASLNAAGIVSIGVLYAFVDYLNRLFQPITGIVNQFSKLELAR 400
Cdd:COG1132 232 ELRRANLRAARLSALFF-PLMELLGNLGLALVLL--VGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRAL 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 401 VSAGRVFELLEEKN--TEEAGQPAKERALGRVEFRDVSFAYQEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFR 478
Cdd:COG1132 309 ASAERIFELLDEPPeiPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLR 388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 479 FYDAQKGDVLIDGKSIYNMSRQELRSHMGIVLQDPYLFSGTIGSNVSLDDERMTEEEIKNALRQVGAEPLLKKLPKGINE 558
Cdd:COG1132 389 FYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDT 468
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 559 PVIEKGSTLSSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQKALDVVKQGRTTFVIAHRLSTIRNADQILVLD 638
Cdd:COG1132 469 VVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLD 548
|
650 660 670
....*....|....*....|....*....|
gi 1718055426 639 KGEIVEKGNHEELMALEGQYYQMYELQKGQ 668
Cdd:COG1132 549 DGRIVEQGTHEELLARGGLYARLYRLQFGE 578
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
148-665 |
1.93e-149 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 446.09 E-value: 1.93e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 148 GMVL-LICLYGGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVT 226
Cdd:PRK10790 62 GLVAgLAAAYVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 227 VLSTFVTSGIYMFGIFTALFLLDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTIIQAFR 306
Cdd:PRK10790 142 VVATVLRSAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 307 HQketMREFEELNE-SHFYFQNRM--LNLNSLMSHNLVNVIRNLAFVCLIWHFGgasLNAAGIVSIGVLYAFVDYLNRLF 383
Cdd:PRK10790 222 QQ---ARFGERMGEaSRSHYMARMqtLRLDGFLLRPLLSLFSALILCGLLMLFG---FSASGTIEVGVLYAFISYLGRLN 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 384 QPITGIVNQFSKLELARVSAGRVFELLEEKNtEEAGQPAKERALGRVEFRDVSFAYQEGEEVLKHISFTAQKGETVALVG 463
Cdd:PRK10790 296 EPLIELTTQQSMLQQAVVAGERVFELMDGPR-QQYGNDDRPLQSGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVG 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 464 HTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGIVLQDPYLFSGTIGSNVSLDDErMTEEEIKNALRQV 543
Cdd:PRK10790 375 HTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD-ISEEQVWQALETV 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 544 GAEPLLKKLPKGINEPVIEKGSTLSSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQKALDVVKQGRTTFVIAH 623
Cdd:PRK10790 454 QLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAH 533
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1718055426 624 RLSTIRNADQILVLDKGEIVEKGNHEELMALEGQYYQMYELQ 665
Cdd:PRK10790 534 RLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQ 575
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
149-665 |
5.42e-149 |
|
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: 448.90 E-value: 5.42e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 149 MVLLICLYGGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARItNDTEAIRDLYVTVL 228
Cdd:COG2274 195 LWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 229 STFVTSGIYMFGIFTALFLLDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTIIQAFRHQ 308
Cdd:COG2274 274 LTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 309 KETMREFEELNESHFYFQNRMLNLNSLMShNLVNVIRNLAFVCLIWhfGGASLNAAGIVSIGVLYAFVDYLNRLFQPITG 388
Cdd:COG2274 354 SRFRRRWENLLAKYLNARFKLRRLSNLLS-TLSGLLQQLATVALLW--LGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQ 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 389 IVNQFSKLELARVSAGRVFELLEEK--NTEEAGQPAKERALGRVEFRDVSFAY-QEGEEVLKHISFTAQKGETVALVGHT 465
Cdd:COG2274 431 LIGLLQRFQDAKIALERLDDILDLPpeREEGRSKLSLPRLKGDIELENVSFRYpGDSPPVLDNISLTIKPGERVAIVGRS 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 466 GSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGIVLQDPYLFSGTIGSNVSLDDERMTEEEIKNALRQVGA 545
Cdd:COG2274 511 GSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGL 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 546 EPLLKKLPKGINEPVIEKGSTLSSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQKALDVVKQGRTTFVIAHRL 625
Cdd:COG2274 591 HDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRL 670
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1718055426 626 STIRNADQILVLDKGEIVEKGNHEELMALEGQYYQMYELQ 665
Cdd:COG2274 671 STIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQ 710
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
158-668 |
4.60e-120 |
|
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: 369.82 E-value: 4.60e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 158 GLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVTVLSTFVTSGIY 237
Cdd:TIGR02203 62 GLAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 238 MFGIFTALFLLDVKLAFVCLAIVPII-WLWSVIYRRYASYyNQKIRSINSDINAKMNESIQGMTIIQAFRHQKETMREFE 316
Cdd:TIGR02203 142 VIGLFIVLLYYSWQLTLIVVVMLPVLsILMRRVSKRLRRI-SKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 317 ELNESHFYFQNRMLNLNSLMShNLVNVIRNLAFVCLIwhFGGASLNAAGIVSIGVLYAFVDYLNRLFQPITGIVNQFSKL 396
Cdd:TIGR02203 221 AVSNRNRRLAMKMTSAGSISS-PITQLIASLALAVVL--FIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPM 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 397 ELARVSAGRVFELLEEKNTEEAGQPAKERALGRVEFRDVSFAYQ-EGEEVLKHISFTAQKGETVALVGHTGSGKSSILNL 475
Cdd:TIGR02203 298 QRGLAAAESLFTLLDSPPEKDTGTRAIERARGDVEFRNVTFRYPgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNL 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 476 LFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGIVLQDPYLFSGTIGSNVSLDD-ERMTEEEIKNALRQVGAEPLLKKLPK 554
Cdd:TIGR02203 378 IPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPL 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 555 GINEPVIEKGSTLSSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQKALDVVKQGRTTFVIAHRLSTIRNADQI 634
Cdd:TIGR02203 458 GLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRI 537
|
490 500 510
....*....|....*....|....*....|....
gi 1718055426 635 LVLDKGEIVEKGNHEELMALEGQYYQMYELQKGQ 668
Cdd:TIGR02203 538 VVMDDGRIVERGTHNELLARNGLYAQLHNMQFRE 571
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
428-656 |
1.51e-114 |
|
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: 343.05 E-value: 1.51e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 428 GRVEFRDVSFAYQEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMG 507
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 508 IVLQDPYLFSGTIGSNVSLDDERMTEEEIKNALRQVGAEPLLKKLPKGINEPVIEKGSTLSSGERQLISFARALAFDPAI 587
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1718055426 588 LILDEATAHIDTETEAVIQKALDVVKQGRTTFVIAHRLSTIRNADQILVLDKGEIVEKGNHEELMALEG 656
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
142-406 |
6.87e-110 |
|
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: 333.59 E-value: 6.87e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 142 YQPEIKGMVLLICLYGGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIR 221
Cdd:cd18544 33 GQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 222 DLYVTVLSTFVTSGIYMFGIFTALFLLDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTI 301
Cdd:cd18544 113 ELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 302 IQAFRHQKETMREFEELNESHFYFQNRMLNLNSLmSHNLVNVIRNLAFVCLIWHFGGASLNaaGIVSIGVLYAFVDYLNR 381
Cdd:cd18544 193 IQLFNREKREFEEFDEINQEYRKANLKSIKLFAL-FRPLVELLSSLALALVLWYGGGQVLS--GAVTLGVLYAFIQYIQR 269
|
250 260
....*....|....*....|....*
gi 1718055426 382 LFQPITGIVNQFSKLELARVSAGRV 406
Cdd:cd18544 270 FFRPIRDLAEKFNILQSAMASAERI 294
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
180-664 |
8.25e-110 |
|
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: 342.90 E-value: 8.25e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 180 RIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVTVLSTFVTSGIYMFGIFTALFLLDVKLA---FVC 256
Cdd:COG4987 85 RLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALAlvlALG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 257 LAIVPIIWLWsVIYRRYASYyNQKIRSINSDINAKMNESIQGMTIIQAFRHQKETMREFEELNESHFYFQNRMLNLNSLm 336
Cdd:COG4987 165 LLLAGLLLPL-LAARLGRRA-GRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSAL- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 337 SHNLVNVIRNLAFVCLIWhFGGASLNAAGI----VSIGVLYAFVdylnrLFQPITGIVNQFSKLELARVSAGRVFELLEE 412
Cdd:COG4987 242 AQALLQLAAGLAVVAVLW-LAAPLVAAGALsgplLALLVLAALA-----LFEALAPLPAAAQHLGRVRAAARRLNELLDA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 413 K-NTEEAGQPAKERALGRVEFRDVSFAY-QEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLID 490
Cdd:COG4987 316 PpAVTEPAEPAPAPGGPSLELEDVSFRYpGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLG 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 491 GKSIYNMSRQELRSHMGIVLQDPYLFSGTIGSNVSLDDERMTEEEIKNALRQVGAEPLLKKLPKGINEPVIEKGSTLSSG 570
Cdd:COG4987 396 GVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGG 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 571 ERQLISFARALAFDPAILILDEATAHIDTETEAVIQKALDVVKQGRTTFVIAHRLSTIRNADQILVLDKGEIVEKGNHEE 650
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEE 555
|
490
....*....|....
gi 1718055426 651 LMALEGQYYQMYEL 664
Cdd:COG4987 556 LLAQNGRYRQLYQR 569
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
158-668 |
2.76e-106 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 334.29 E-value: 2.76e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 158 GLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVTVLSTFVTSGIY 237
Cdd:PRK11176 73 GLMILRGITSFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGAS 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 238 MFGIFTALFLLDVKLAFVCLAIVPII-WLWSVIYRRYasyynqkiRSINSDINAKMNE-------SIQGMTIIQAFRHQK 309
Cdd:PRK11176 153 IIGLFIMMFYYSWQLSLILIVIAPIVsIAIRVVSKRF--------RNISKNMQNTMGQvttsaeqMLKGHKEVLIFGGQE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 310 ETMREFEELneSHFYFQNRM-LNLNSLMSHNLVNVIRNLAFVCLIWhfgGASLNA------AGivSIGVLYAFVDYLNRL 382
Cdd:PRK11176 225 VETKRFDKV--SNRMRQQGMkMVSASSISDPIIQLIASLALAFVLY---AASFPSvmdtltAG--TITVVFSSMIALMRP 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 383 FQPITGIVNQFSKlelARVSAGRVFELLEEKNTEEAGQPAKERALGRVEFRDVSFAYQEGEE-VLKHISFTAQKGETVAL 461
Cdd:PRK11176 298 LKSLTNVNAQFQR---GMAACQTLFAILDLEQEKDEGKRVIERAKGDIEFRNVTFTYPGKEVpALRNINFKIPAGKTVAL 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 462 VGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGIVLQDPYLFSGTIGSNVSL-DDERMTEEEIKNAL 540
Cdd:PRK11176 375 VGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYaRTEQYSREQIEEAA 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 541 RQVGAEPLLKKLPKGINEPVIEKGSTLSSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQKALDVVKQGRTTFV 620
Cdd:PRK11176 455 RMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLV 534
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1718055426 621 IAHRLSTIRNADQILVLDKGEIVEKGNHEELMALEGQYYQMYELQKGQ 668
Cdd:PRK11176 535 IAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQFGQ 582
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
152-656 |
1.89e-104 |
|
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: 329.03 E-value: 1.89e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 152 LICLYGGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVTVLSTF 231
Cdd:COG4988 60 LLGLLLAVLLLRALLAWLRERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 232 VTSGIYMFGIFTALFLLDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTIIQAF---RHQ 308
Cdd:COG4988 140 FLAALVPLLILVAVFPLDWLSGLILLVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFgraKAE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 309 KETMREfeelnESHFYFQNRM----LNLNSLMShnlvnvirnLAFVcliwhfggASLNAA-GIVSIGV--LYAFVDYLNR 381
Cdd:COG4988 220 AERIAE-----ASEDFRKRTMkvlrVAFLSSAV---------LEFF--------ASLSIAlVAVYIGFrlLGGSLTLFAA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 382 L---------FQPITGIVNQF-SKLElARVSAGRVFELLEEKN--TEEAGQPAKERALGRVEFRDVSFAYQEGEEVLKHI 449
Cdd:COG4988 278 LfvlllapefFLPLRDLGSFYhARAN-GIAAAEKIFALLDAPEpaAPAGTAPLPAAGPPSIELEDVSFSYPGGRPALDGL 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 450 SFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGIVLQDPYLFSGTIGSNVSLDDE 529
Cdd:COG4988 357 SLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRP 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 530 RMTEEEIKNALRQVGAEPLLKKLPKGINEPVIEKGSTLSSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQKAL 609
Cdd:COG4988 437 DASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQAL 516
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1718055426 610 DVVKQGRTTFVIAHRLSTIRNADQILVLDKGEIVEKGNHEELMALEG 656
Cdd:COG4988 517 RRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
430-662 |
4.88e-100 |
|
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: 305.69 E-value: 4.88e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQ-EGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGI 508
Cdd:cd03251 1 VEFKNVTFRYPgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 509 VLQDPYLFSGTIGSNVSLDDERMTEEEIKNALRQVGAEPLLKKLPKGINEPVIEKGSTLSSGERQLISFARALAFDPAIL 588
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1718055426 589 ILDEATAHIDTETEAVIQKALDVVKQGRTTFVIAHRLSTIRNADQILVLDKGEIVEKGNHEELMALEGQYYQMY 662
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
150-671 |
1.15e-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: 317.53 E-value: 1.15e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 150 VLLICLYGGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDL--YV-- 225
Cdd:COG5265 78 VGLLLAYGLLRLLSVLFGELRDALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGGLSRDIERGTKGIEFLlrFLlf 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 226 ----TVLSTFVTSGI--YMFGIFTALFlldvklafVCLAIVPIIWL------WSVIYRRYASYYNQKI--RSINSDINA- 290
Cdd:COG5265 158 nilpTLLEIALVAGIllVKYDWWFALI--------TLVTVVLYIAFtvvvteWRTKFRREMNEADSEAntRAVDSLLNYe 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 291 --KM--NEsiqgmtiiqAFRHQK--ETMREFEELneshfyfqnRMLNLNSLMSHNLV-NVIRNLAFVCLIWHfgGASLNA 363
Cdd:COG5265 230 tvKYfgNE---------AREARRydEALARYERA---------AVKSQTSLALLNFGqALIIALGLTAMMLM--AAQGVV 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 364 AGIVSIGVLYAFVDYLNRLFQP--ITGIVnqFSKLELARVSAGRVFELLEEkNTEEAGQP-AKERAL--GRVEFRDVSFA 438
Cdd:COG5265 290 AGTMTVGDFVLVNAYLIQLYIPlnFLGFV--YREIRQALADMERMFDLLDQ-PPEVADAPdAPPLVVggGEVRFENVSFG 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 439 YQEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGIVLQDPYLFSG 518
Cdd:COG5265 367 YDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFND 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 519 TIGSNVSLDDERMTEEEIKNALRQVGAEPLLKKLPKGINEPVIEKGSTLSSGERQLISFARALAFDPAILILDEATAHID 598
Cdd:COG5265 447 TIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALD 526
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1718055426 599 TETEAVIQKALDVVKQGRTTFVIAHRLSTIRNADQILVLDKGEIVEKGNHEELMALEGQYYQMYELQKGQKHS 671
Cdd:COG5265 527 SRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEA 599
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
430-665 |
1.12e-96 |
|
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: 297.14 E-value: 1.12e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQE--GEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMG 507
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 508 IVLQDPYLFSGTIGSNVSLDDERMTEEEIKNALRQVGAEPLLKKLPKGINEPVIEKGSTLSSGERQLISFARALAFDPAI 587
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718055426 588 LILDEATAHIDTETEAVIQKALDVVKQGRTTFVIAHRLSTIRNADQILVLDKGEIVEKGNHEELMALEGQYYQMYELQ 665
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
430-665 |
2.12e-92 |
|
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: 286.05 E-value: 2.12e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGIV 509
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 510 LQDPYLFSGTIGSNVSLDDERMTEEEIKNALRQVGAEPLLKKLPKGINEPVIEKGSTLSSGERQLISFARALAFDPAILI 589
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1718055426 590 LDEATAHIDTETEAVIQKALDVVKQGRTTFVIAHRLSTIRNADQILVLDKGEIVEKGNHEELMALEGQYYQMYELQ 665
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
173-661 |
1.32e-91 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 296.10 E-value: 1.32e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 173 LLQMSANRIIQKMRQDV----FSHIQRMPIRYFDNLPAGKVVARITNDTEAI--------RDLYVTVLSTFVTsgiymfg 240
Cdd:PRK13657 75 LVARHADRLAHRRRLAVlteyFERIIQLPLAWHSQRGSGRALHTLLRGTDALfglwlefmREHLATLVALVVL------- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 241 IFTALFLlDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTIIQAF---RHQKETMREF-E 316
Cdd:PRK13657 148 LPLALFM-NWRLSLVLVVLGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYnriEAETQALRDIaD 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 317 ELNEShfyfQNRMLNLNSLmshnlVNVIRNLA--FVCLIWHFGGASLNAAGIVSIGVLYAFVDYLNRLFQPITGIVNQFS 394
Cdd:PRK13657 227 NLLAA----QMPVLSWWAL-----ASVLNRAAstITMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFIN 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 395 KLELARVSAGRVFELLEEKNT--EEAGQPAKERALGRVEFRDVSFAYQEGEEVLKHISFTAQKGETVALVGHTGSGKSSI 472
Cdd:PRK13657 298 QVFMAAPKLEEFFEVEDAVPDvrDPPGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTL 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 473 LNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGIVLQDPYLFSGTIGSNVSLDDERMTEEEIKNALRQVGAEPLLKKL 552
Cdd:PRK13657 378 INLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERK 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 553 PKGINEPVIEKGSTLSSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQKALDVVKQGRTTFVIAHRLSTIRNAD 632
Cdd:PRK13657 458 PDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNAD 537
|
490 500
....*....|....*....|....*....
gi 1718055426 633 QILVLDKGEIVEKGNHEELMALEGQYYQM 661
Cdd:PRK13657 538 RILVFDNGRVVESGSFDELVARGGRFAAL 566
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
150-661 |
8.32e-89 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 292.01 E-value: 8.32e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 150 VLLICLYGGLLVFSVFFQYGQhYLLQMSanRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVTVLS 229
Cdd:TIGR00958 204 IFFMCLLSIASSVSAGLRGGS-FNYTMA--RINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVN 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 230 TFVTSGIYMFGIFTALFLLDVKLAFVCLAIVPIIWLwsvIYRRYASYYnQKIRSINSDINAKMN----ESIQGMTIIQAF 305
Cdd:TIGR00958 281 VLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFL---AEKVFGKRY-QLLSEELQEAVAKANqvaeEALSGMRTVRSF 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 306 RHQKETMREFEElneshfyFQNRMLNLNSLMS----HNLVN--VIRNLAFVCLIWHfgGASLNAAGIVSIGVLYAFVDYL 379
Cdd:TIGR00958 357 AAEEGEASRFKE-------ALEETLQLNKRKAlayaGYLWTtsVLGMLIQVLVLYY--GGQLVLTGKVSSGNLVSFLLYQ 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 380 NRLFQPITGIVNQFSKLELARVSAGRVFELLEEK-NTEEAGQPAKERALGRVEFRDVSFAY--QEGEEVLKHISFTAQKG 456
Cdd:TIGR00958 428 EQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKpNIPLTGTLAPLNLEGLIEFQDVSFSYpnRPDVPVLKGLTFTLHPG 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 457 ETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGIVLQDPYLFSGTIGSNVSLDDERMTEEEI 536
Cdd:TIGR00958 508 EVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEI 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 537 KNALRQVGAEPLLKKLPKGINEPVIEKGSTLSSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQKalDVVKQGR 616
Cdd:TIGR00958 588 MAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASR 665
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1718055426 617 TTFVIAHRLSTIRNADQILVLDKGEIVEKGNHEELMALEGQYYQM 661
Cdd:TIGR00958 666 TVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
428-647 |
7.42e-82 |
|
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: 258.19 E-value: 7.42e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 428 GRVEFRDVSFAYQEGEE-VLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHM 506
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 507 GIVLQDPYLFSGTIGSNvsLD-DERMTEEEIKNALRQVGAEPLLKKLPKGINEPVIEKGSTLSSGERQLISFARALAFDP 585
Cdd:cd03244 81 SIIPQDPVLFSGTIRSN--LDpFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1718055426 586 AILILDEATAHIDTETEAVIQKALDVVKQGRTTFVIAHRLSTIRNADQILVLDKGEIVEKGN 647
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
152-658 |
1.61e-80 |
|
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: 269.89 E-value: 1.61e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 152 LICLYGGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDtEAIRDLYVTVLSTF 231
Cdd:TIGR03796 196 LLLGMGLTALLQGVLTWLQLYYLRRLEIKLAVGMSARFLWHILRLPVRFFAQRHAGDIASRVQLN-DQVAEFLSGQLATT 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 232 VTSGIYMFGIFTALFLLDVKLAFVCLAIVPI-IWLWSVIYRRYASYyNQKIRSinsDINAKMNESIQGMTIIqafrhqkE 310
Cdd:TIGR03796 275 ALDAVMLVFYALLMLLYDPVLTLIGIAFAAInVLALQLVSRRRVDA-NRRLQQ---DAGKLTGVAISGLQSI-------E 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 311 TMREfeELNESHFY-----FQNRMLN-------LNSLMShNLVNVIRNLAFVCLIWhFGGAsLNAAGIVSIGVLYAFVDY 378
Cdd:TIGR03796 344 TLKA--SGLESDFFsrwagYQAKLLNaqqelgvLTQILG-VLPTLLTSLNSALILV-VGGL-RVMEGQLTIGMLVAFQSL 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 379 LNRLFQPITGIVNQFSKL-----ELAR---VSAGRVFELLEEKNTEEAGQPAKERALGRVEFRDVSFAYQEGEE-VLKHI 449
Cdd:TIGR03796 419 MSSFLEPVNNLVGFGGTLqelegDLNRlddVLRNPVDPLLEEPEGSAATSEPPRRLSGYVELRNITFGYSPLEPpLIENF 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 450 SFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGIVLQDPYLFSGTIGSNVSLDDE 529
Cdd:TIGR03796 499 SLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDP 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 530 RMTEEEIKNALRQVGAEPLLKKLPKGINEPVIEKGSTLSSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQKAL 609
Cdd:TIGR03796 579 TIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL 658
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1718055426 610 DvvKQGRTTFVIAHRLSTIRNADQILVLDKGEIVEKGNHEELMALEGQY 658
Cdd:TIGR03796 659 R--RRGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAY 705
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
430-641 |
4.07e-76 |
|
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: 241.13 E-value: 4.07e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGE-EVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGI 508
Cdd:cd03228 1 IEFKNVSFSYPGRPkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 509 VLQDPYLFSGTIGSNVslddermteeeiknalrqvgaepllkklpkginepviekgstLSSGERQLISFARALAFDPAIL 588
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1718055426 589 ILDEATAHIDTETEAVIQKALDVVKQGRTTFVIAHRLSTIRNADQILVLDKGE 641
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
430-665 |
8.75e-75 |
|
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: 240.08 E-value: 8.75e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQ-EGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGI 508
Cdd:cd03252 1 ITFEHVRFRYKpDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 509 VLQDPYLFSGTIGSNVSLDDERMTEEEIKNALRQVGAEPLLKKLPKGINEPVIEKGSTLSSGERQLISFARALAFDPAIL 588
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1718055426 589 ILDEATAHIDTETEAVIQKALDVVKQGRTTFVIAHRLSTIRNADQILVLDKGEIVEKGNHEELMALEGQYYQMYELQ 665
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
173-661 |
4.70e-73 |
|
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: 246.72 E-value: 4.70e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 173 LLQMSANRIIQKMRQDV----FSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVTVLSTFVTSGIYMFGIFTALFLL 248
Cdd:TIGR01192 75 LVAREADRLAHGRRATLlteaFGRIISMPLSWHQQRGTSNALHTLLRATETLFGLWLEFMRQHLATFVALFLLIPTAFAM 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 249 DVKLAFVCLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTIIQAFRHQKETMREFEELNESHFYFQNR 328
Cdd:TIGR01192 155 DWRLSIVLMVLGILYILIAKLVMQRTKNGQAAVEHHYHNVFKHVSDSISNVSVVHSYNRIEAETSALKQFTNNLLSAQYP 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 329 MLNLNSLMShNLVNVIRNLAFVCLIwhFGGASLNAAGIVSIGVLYAFVDYLN----RLFQpITGIVNQFSKlelARVSAG 404
Cdd:TIGR01192 235 VLDWWALAS-GLNRMASTISMMCIL--VIGTVLVIKGELSVGEVIAFIGFANlligRLDQ-MSGFITQIFE---ARAKLE 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 405 RVFELleEKNTEEAGQPAKERAL----GRVEFRDVSFAYQEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFY 480
Cdd:TIGR01192 308 DFFDL--EDSVFQREEPADAPELpnvkGAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVY 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 481 DAQKGDVLIDGKSIYNMSRQELRSHMGIVLQDPYLFSGTIGSNVSLDDERMTEEEIKNALRQVGAEPLLKKLPKGINEPV 560
Cdd:TIGR01192 386 DPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLV 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 561 IEKGSTLSSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQKALDVVKQGRTTFVIAHRLSTIRNADQILVLDKG 640
Cdd:TIGR01192 466 GERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQG 545
|
490 500
....*....|....*....|.
gi 1718055426 641 EIVEKGNHEELMALEGQYYQM 661
Cdd:TIGR01192 546 RLIEKGSFQELIQKDGRFYKL 566
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
168-637 |
3.04e-71 |
|
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: 240.27 E-value: 3.04e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 168 YGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVTVLSTFVTSGIYMFGIFTALFL 247
Cdd:TIGR02857 62 WLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 248 LDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTIIQAFRHQKETMREFEELNEShfYFQN 327
Cdd:TIGR02857 142 QDWISGLILLLTAPLIPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEE--YRER 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 328 RMlnlnslmshnlvNVIRnLAFVC-LIWHFGgASLNAAGI-VSIGV--LYAFVDYLNRLF---------QPITGIVNQFS 394
Cdd:TIGR02857 220 TM------------RVLR-IAFLSsAVLELF-ATLSVALVaVYIGFrlLAGDLDLATGLFvlllapefyLPLRQLGAQYH 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 395 KLELARVSAGRVFELLEEKNTEEAGQ-PAKERALGRVEFRDVSFAYQEGEEVLKHISFTAQKGETVALVGHTGSGKSSIL 473
Cdd:TIGR02857 286 ARADGVAAAEALFAVLDAAPRPLAGKaPVTAAPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 474 NLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGIVLQDPYLFSGTIGSNVSLDDERMTEEEIKNALRQVGAEPLLKKLP 553
Cdd:TIGR02857 366 NLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALP 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 554 KGINEPVIEKGSTLSSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQKALDVVKQGRTTFVIAHRLSTIRNADQ 633
Cdd:TIGR02857 446 QGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADR 525
|
....
gi 1718055426 634 ILVL 637
Cdd:TIGR02857 526 IVVL 529
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
161-662 |
1.73e-70 |
|
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: 242.72 E-value: 1.73e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 161 VFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVTVLSTFVTSGIY-MF 239
Cdd:TIGR01193 207 IIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILvIV 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 240 GIFtaLFLLDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTIIQAFRHQKETMREFEELN 319
Cdd:TIGR01193 287 GLF--LVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEF 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 320 EShfYFQNRMLNLNSLMSHNLVNVIRNLAF-VCLIWhfGGASLNAAGIVSIGVLYAFVDYLNRLFQPITGIVNQFSKLEL 398
Cdd:TIGR01193 365 GD--YLNKSFKYQKADQGQQAIKAVTKLILnVVILW--TGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 399 ARVSAGRVFE--LLEEKNTEEAGQPAKERALGRVEFRDVSFAYQEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLL 476
Cdd:TIGR01193 441 ARVANNRLNEvyLVDSEFINKKKRTELNNLNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLL 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 477 FRFYDAQKGDVLIDGKSIYNMSRQELRSHMGIVLQDPYLFSGTIGSNVSL-DDERMTEEEIKNALRQVGAEPLLKKLPKG 555
Cdd:TIGR01193 521 VGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLgAKENVSQDEIWAACEIAEIKDDIENMPLG 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 556 INEPVIEKGSTLSSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQKALdVVKQGRTTFVIAHRLSTIRNADQIL 635
Cdd:TIGR01193 601 YQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNL-LNLQDKTIIFVAHRLSVAKQSDKII 679
|
490 500
....*....|....*....|....*..
gi 1718055426 636 VLDKGEIVEKGNHEELMALEGQYYQMY 662
Cdd:TIGR01193 680 VLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
155-661 |
2.80e-70 |
|
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: 249.48 E-value: 2.80e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 155 LYGGLLVFSVFFQYGqhYLLQMSANRII--QKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVTVLSTFV 232
Cdd:TIGR00957 1010 VYGALGILQGFAVFG--YSMAVSIGGIQasRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFM 1087
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 233 TSgiyMFGIFTALFLLDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQ--KIRSIN-SDINAKMNESIQGMTIIQAFRHQK 309
Cdd:TIGR00957 1088 GS---LFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQlkRLESVSrSPVYSHFNETLLGVSVIRAFEEQE 1164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 310 ETMREFE---ELNESHFY---FQNRMLNLNSLMSHNLVnvirnLAFVCLIWHFGGASLNAaGIVSIGVLYAF--VDYLNR 381
Cdd:TIGR00957 1165 RFIHQSDlkvDENQKAYYpsiVANRWLAVRLECVGNCI-----VLFAALFAVISRHSLSA-GLVGLSVSYSLqvTFYLNW 1238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 382 LfqpitgiVNQFSKLELARVSAGRVFELLE-EKNT----EEAGQPAKERALGRVEFRDVSFAYQEGEE-VLKHISFTAQK 455
Cdd:TIGR00957 1239 L-------VRMSSEMETNIVAVERLKEYSEtEKEApwqiQETAPPSGWPPRGRVEFRNYCLRYREDLDlVLRHINVTIHG 1311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 456 GETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGIVLQDPYLFSGTIGSNvsLDD-ERMTEE 534
Cdd:TIGR00957 1312 GEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMN--LDPfSQYSDE 1389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 535 EIKNALRQVGAEPLLKKLPKGINEPVIEKGSTLSSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQKALDVVKQ 614
Cdd:TIGR00957 1390 EVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFE 1469
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1718055426 615 GRTTFVIAHRLSTIRNADQILVLDKGEIVEKGNHEELMALEGQYYQM 661
Cdd:TIGR00957 1470 DCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
212-663 |
7.37e-70 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 237.80 E-value: 7.37e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 212 RITNDTEAIRDLYVTVLSTFVTSGIYMFGIFTALFLLDVKLAFVCLAIVPIIWL-WSVIYRRYASYYNQKIRSINSDINA 290
Cdd:PRK11160 122 RLVADVDTLDHLYLRLISPLVAALVVILVLTIGLSFFDLTLALTLGGILLLLLLlLPLLFYRLGKKPGQDLTHLRAQYRV 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 291 KMNESIQGMTIIQAFRHQKETMREFEELNESHFYFQNRMLNLNSLmSHNLVNVIRNLAFVCLIW----HFGGASLNAAGI 366
Cdd:PRK11160 202 QLTEWLQGQAELTLFGAEDRYRQQLEQTEQQWLAAQRRQANLTGL-SQALMILANGLTVVLMLWlaagGVGGNAQPGALI 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 367 --VSIGVLYAFvdylnRLFQPITGivnQFSKLELARVSAGRVFELLEEKN----TEEAGQPAKERALgrvEFRDVSFAYQ 440
Cdd:PRK11160 281 alFVFAALAAF-----EALMPVAG---AFQHLGQVIASARRINEITEQKPevtfPTTSTAAADQVSL---TLNNVSFTYP 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 441 EGEE-VLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGIVLQDPYLFSGT 519
Cdd:PRK11160 350 DQPQpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSAT 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 520 IGSNVSLDDERMTEEEIKNALRQVGAEPLLKKlPKGINEPVIEKGSTLSSGERQLISFARALAFDPAILILDEATAHIDT 599
Cdd:PRK11160 430 LRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDA 508
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1718055426 600 ETEAVIQKALDVVKQGRTTFVIAHRLSTIRNADQILVLDKGEIVEKGNHEELMALEGQYYQMYE 663
Cdd:PRK11160 509 ETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQ 572
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
428-646 |
6.31e-66 |
|
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: 216.30 E-value: 6.31e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 428 GRVEFRDVSFAYQEGE-EVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHM 506
Cdd:cd03245 1 GRIEFRNVSFSYPNQEiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 507 GIVLQDPYLFSGTIGSNVSLDDERMTEEEIKNALRQVGAEPLLKKLPKGINEPVIEKGSTLSSGERQLISFARALAFDPA 586
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 587 ILILDEATAHIDTETEAVIQKALDVVKQGRTTFVIAHRLSTIRNADQILVLDKGEIVEKG 646
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
165-625 |
3.50e-65 |
|
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: 224.16 E-value: 3.50e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 165 FFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVTVLSTFVTSGIYMFGIFTA 244
Cdd:TIGR02868 68 VFRYLERLVGHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 245 LFLLDVKLAFVCLAIVPII-WLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTIIQAFRHQKETMREFEELNESHF 323
Cdd:TIGR02868 148 IAVLSVPAALILAAGLLLAgFVAPLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELT 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 324 YFQNRMLNLNSLmSHNLVNVIRNLAFVCLIWHFGGASlnAAGIVSIGVLYAFVDYLNRLFQPITGIVNQFSKLELARVSA 403
Cdd:TIGR02868 228 RAERRAAAATAL-GAALTLLAAGLAVLGALWAGGPAV--ADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 404 GRVFELLEEKNTEEAGQPAKERALG----RVEFRDVSFAYQEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRF 479
Cdd:TIGR02868 305 ERIVEVLDAAGPVAEGSAPAAGAVGlgkpTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGL 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 480 YDAQKGDVLIDGKSIYNMSRQELRSHMGIVLQDPYLFSGTIGSNVSLDDERMTEEEIKNALRQVGAEPLLKKLPKGINEP 559
Cdd:TIGR02868 385 LDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTV 464
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1718055426 560 VIEKGSTLSSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQKALDVVKQGRTTFVIAHRL 625
Cdd:TIGR02868 465 LGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
146-406 |
6.50e-65 |
|
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: 216.18 E-value: 6.50e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 146 IKGMVLLICLYGGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYV 225
Cdd:cd18545 36 LSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 226 TVLSTFVTSGIYMFGIFTALFLLDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTIIQAF 305
Cdd:cd18545 116 NGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSF 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 306 RHQKETMREFEELNESHFYFQNRMLNLNSLMShNLVNVIRNLAFVCLIWHfgGASLNAAGIVSIGVLYAFVDYLNRLFQP 385
Cdd:cd18545 196 AREDENEEIFDELNRENRKANMRAVRLNALFW-PLVELISALGTALVYWY--GGKLVLGGAITVGVLVAFIGYVGRFWQP 272
|
250 260
....*....|....*....|.
gi 1718055426 386 ITGIVNQFSKLELARVSAGRV 406
Cdd:cd18545 273 IRNLSNFYNQLQSAMASAERI 293
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
143-406 |
3.26e-63 |
|
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: 211.64 E-value: 3.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 143 QPEIKGMVLLICLYGGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRD 222
Cdd:cd07346 32 AGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 223 LYVTVLSTFVTSGIYMFGIFTALFLLDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTII 302
Cdd:cd07346 112 LVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 303 QAFRHQKETMREFEELNESHFYFQNRMLNLNSLMShNLVNVIRNLAFVCLIWhFGGaSLNAAGIVSIGVLYAFVDYLNRL 382
Cdd:cd07346 192 KAFAAEEREIERFREANRDLRDANLRAARLSALFS-PLIGLLTALGTALVLL-YGG-YLVLQGSLTIGELVAFLAYLGML 268
|
250 260
....*....|....*....|....
gi 1718055426 383 FQPITGIVNQFSKLELARVSAGRV 406
Cdd:cd07346 269 FGPIQRLANLYNQLQQALASLERI 292
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
428-642 |
1.33e-62 |
|
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: 207.71 E-value: 1.33e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 428 GRVEFRDVSFAY--QEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSH 505
Cdd:cd03248 10 GIVKFQNVTFAYptRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 506 MGIVLQDPYLFSGTIGSNVSLDDERMTEEEIKNALRQVGAEPLLKKLPKGINEPVIEKGSTLSSGERQLISFARALAFDP 585
Cdd:cd03248 90 VSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1718055426 586 AILILDEATAHIDTETEAVIQKALDVVKQGRTTFVIAHRLSTIRNADQILVLDKGEI 642
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
150-653 |
7.35e-60 |
|
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: 210.37 E-value: 7.35e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 150 VLLICLYGGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRyfdnlpagkvvARITNDTEAIRDLyvTVLS 229
Cdd:COG4618 60 LMLTLLALGLYAVMGLLDAVRSRILVRVGARLDRRLGPRVFDAAFRAALR-----------GGGGAAAQALRDL--DTLR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 230 TFVTSGIyMFGIFTA---------LFLLDVKLAFVCLAIVPIIWLWSVIyrryasyyNQkiRSINSDINAKMNESIQGMT 300
Cdd:COG4618 127 QFLTGPG-LFALFDLpwapiflavLFLFHPLLGLLALVGALVLVALALL--------NE--RLTRKPLKEANEAAIRANA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 301 IIQAFRHQKET-----MRE-----FEELNESHFYFQNRMLNLNSLMShNLVNVIRNLAFVCLIwhfG-GASLNAAGIVSI 369
Cdd:COG4618 196 FAEAALRNAEVieamgMLPalrrrWQRANARALALQARASDRAGGFS-ALSKFLRLLLQSAVL---GlGAYLVIQGEITP 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 370 GVLYAFVDYLNRLFQPITGIVNQFSKLELARVSAGRVFELLEEKNTEEAG--QPakeRALGRVEFRDVSFAYQEGEE-VL 446
Cdd:COG4618 272 GAMIAASILMGRALAPIEQAIGGWKQFVSARQAYRRLNELLAAVPAEPERmpLP---RPKGRLSVENLTVVPPGSKRpIL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 447 KHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGIVLQDPYLFSGTIGSNVSl 526
Cdd:COG4618 349 RGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIA- 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 527 ddeRMTE---EEIKNALRQVGAEPLLKKLPKGINEPVIEKGSTLSSGERQLISFARALAFDPAILILDEATAHIDTETEA 603
Cdd:COG4618 428 ---RFGDadpEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEA 504
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1718055426 604 VIQKALDVVKQ-GRTTFVIAHRLSTIRNADQILVLDKGEIVEKGNHEELMA 653
Cdd:COG4618 505 ALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
428-646 |
3.54e-58 |
|
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: 195.32 E-value: 3.54e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 428 GRVEFRDVSFAYQ-EGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHM 506
Cdd:cd03369 5 GEIEVENLSVRYApDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 507 GIVLQDPYLFSGTIGSNVSLDDErMTEEEIKNALRqvgaepllkklpkginepVIEKGSTLSSGERQLISFARALAFDPA 586
Cdd:cd03369 85 TIIPQDPTLFSGTIRSNLDPFDE-YSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 587 ILILDEATAHIDTETEAVIQKALDVVKQGRTTFVIAHRLSTIRNADQILVLDKGEIVEKG 646
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
144-656 |
1.91e-55 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 205.36 E-value: 1.91e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 144 PEIKGMVLLICLYGGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIrDL 223
Cdd:PLN03130 947 PKTHGPLFYNLIYALLSFGQVLVTLLNSYWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDI-DR 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 224 YVTVLSTfvtsgIYMFGIFTALFlldvklAFVCLAIVPIIWLWSVI------YRRYASYYN-----QKIRSIN-SDINAK 291
Cdd:PLN03130 1026 NVAVFVN-----MFLGQIFQLLS------TFVLIGIVSTISLWAIMpllvlfYGAYLYYQStarevKRLDSITrSPVYAQ 1094
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 292 MNESIQGMTIIQAFRHQketmrefeelneshfyfqNRMLNLN-SLMSHN----LVNVIRN------LAFV--CLIW---- 354
Cdd:PLN03130 1095 FGEALNGLSTIRAYKAY------------------DRMAEINgRSMDNNirftLVNMSSNrwlairLETLggLMIWltas 1156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 355 ----HFGGASLNAAGIVSIGVLYAFVDYLNRLfqpITGIVNQFSKLELARVSAGRVFELLE---------EKNTEEAGQP 421
Cdd:PLN03130 1157 favmQNGRAENQAAFASTMGLLLSYALNITSL---LTAVLRLASLAENSLNAVERVGTYIDlpseaplviENNRPPPGWP 1233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 422 AKeralGRVEFRDVSFAYQ-EGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQ 500
Cdd:PLN03130 1234 SS----GSIKFEDVVLRYRpELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLM 1309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 501 ELRSHMGIVLQDPYLFSGTIGSNVSLDDERmTEEEIKNALRQVGAEPLLKKLPKGINEPVIEKGSTLSSGERQLISFARA 580
Cdd:PLN03130 1310 DLRKVLGIIPQAPVLFSGTVRFNLDPFNEH-NDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARA 1388
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1718055426 581 LAFDPAILILDEATAHIDTETEAVIQKALDVVKQGRTTFVIAHRLSTIRNADQILVLDKGEIVEKGNHEELMALEG 656
Cdd:PLN03130 1389 LLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
357-666 |
5.74e-54 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 194.55 E-value: 5.74e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 357 GGASLNAAGIVSIGVLYAFVDYLNRLFQPITGIVNQFSKLELARVSAGRVFELLEEKNTEEAGQPA--KERALGRVEFRd 434
Cdd:PRK10789 241 GGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVKDGSEPvpEGRGELDVNIR- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 435 vSFAY-QEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGIVLQDP 513
Cdd:PRK10789 320 -QFTYpQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTP 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 514 YLFSGTIGSNVSLDDERMTEEEIKNALRQVGAEPLLKKLPKGINEPVIEKGSTLSSGERQLISFARALAFDPAILILDEA 593
Cdd:PRK10789 399 FLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDA 478
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1718055426 594 TAHIDTETEAVIQKALDVVKQGRTTFVIAHRLSTIRNADQILVLDKGEIVEKGNHEELMALEGQYYQMYELQK 666
Cdd:PRK10789 479 LSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQQ 551
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
134-661 |
7.54e-54 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 200.20 E-value: 7.54e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 134 TKQELFQFYQPEikgmvLLICLYGGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARI 213
Cdd:PLN03232 939 TDQSTPKSYSPG-----FYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRF 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 214 TNDTEAIRDLYVTVLSTFVTSGIYMFGIFTalfLLDVKLAFVCLAIVPIIWLWSVIYRRYASYyNQKIRSINS----DIN 289
Cdd:PLN03232 1014 SKDIGDIDRNVANLMNMFMNQLWQLLSTFA---LIGTVSTISLWAIMPLLILFYAAYLYYQST-SREVRRLDSvtrsPIY 1089
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 290 AKMNESIQGMTIIQAFRHQKETMREFEELNESHFYFQNRMLNLNSLMSHNLVNVirNLAFVCLIWHFG----GASLNAAG 365
Cdd:PLN03232 1090 AQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETL--GGVMIWLTATFAvlrnGNAENQAG 1167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 366 IVSI-GVLYAFVDYLNRLfqpITGIVNQFSKLELARVSAGRVFELLE---------EKNTEEAGQPAKeralGRVEFRDV 435
Cdd:PLN03232 1168 FASTmGLLLSYTLNITTL---LSGVLRQASKAENSLNSVERVGNYIDlpseataiiENNRPVSGWPSR----GSIKFEDV 1240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 436 SFAYQEG-EEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGIVLQDPY 514
Cdd:PLN03232 1241 HLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPV 1320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 515 LFSGTIGSNVSLDDERmTEEEIKNALRQVGAEPLLKKLPKGINEPVIEKGSTLSSGERQLISFARALAFDPAILILDEAT 594
Cdd:PLN03232 1321 LFSGTVRFNIDPFSEH-NDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEAT 1399
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718055426 595 AHIDTETEAVIQKALDVVKQGRTTFVIAHRLSTIRNADQILVLDKGEIVEKGNHEELMALEGQ-YYQM 661
Cdd:PLN03232 1400 ASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSaFFRM 1467
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
441-668 |
2.28e-50 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 184.66 E-value: 2.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 441 EGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRF--YdaqKGDVLIDGKSIYNMSRQELRSHMGIVLQDPYLFSG 518
Cdd:PRK11174 361 DGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpY---QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 519 TIGSNVSLDDERMTEEEIKNALRQVGAEPLLKKLPKGINEPVIEKGSTLSSGERQLISFARALAFDPAILILDEATAHID 598
Cdd:PRK11174 438 TLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 599 TETEAVIQKALDVVKQGRTTFVIAHRLSTIRNADQILVLDKGEIVEKGNHEELMALEGQYYQMYELQKGQ 668
Cdd:PRK11174 518 AHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQEE 587
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
146-406 |
4.69e-50 |
|
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: 176.44 E-value: 4.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 146 IKGMVLLICLYGGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYV 225
Cdd:cd18547 41 FSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 226 TVLSTFVTSGIYMFGIFTALFLLDVKLAFVCLAIVPI-IWLWSVIYRRYASYYNQKIRSInSDINAKMNESIQGMTIIQA 304
Cdd:cd18547 121 QSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLsLLVTKFIAKRSQKYFRKQQKAL-GELNGYIEEMISGQKVVKA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 305 FRHQKETMREFEELNEShFYFQNRMLNLNSLMSHNLVNVIRNLAFVCLIwhFGGASLNAAGIVSIGVLYAFVDYLNRLFQ 384
Cdd:cd18547 200 FNREEEAIEEFDEINEE-LYKASFKAQFYSGLLMPIMNFINNLGYVLVA--VVGGLLVINGALTVGVIQAFLQYSRQFSQ 276
|
250 260
....*....|....*....|..
gi 1718055426 385 PITGIVNQFSKLELARVSAGRV 406
Cdd:cd18547 277 PINQISQQINSLQSALAGAERV 298
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
148-406 |
4.57e-49 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 173.44 E-value: 4.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 148 GMVLLICL-YGGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVT 226
Cdd:cd18546 36 GVLLLAAAaYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 227 VLSTFVTSGIYMFGIFTALFLLDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTIIQAFR 306
Cdd:cd18546 116 GLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 307 HQKETMREFEELNESHFYFQNRMLNLNSLMShNLVNVIRNLAFVCLIWHfgGASLNAAGIVSIGVLYAFVDYLNRLFQPI 386
Cdd:cd18546 196 RERRNAERFAELSDDYRDARLRAQRLVAIYF-PGVELLGNLATAAVLLV--GAWRVAAGTLTVGVLVAFLLYLRRFFAPI 272
|
250 260
....*....|....*....|
gi 1718055426 387 TGIVNQFSKLELARVSAGRV 406
Cdd:cd18546 273 QQLSQVFDSYQQARAALEKI 292
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
428-655 |
2.21e-47 |
|
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: 167.78 E-value: 2.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 428 GRVEFRDVSFAYQEG-EEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHM 506
Cdd:cd03288 18 GEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 507 GIVLQDPYLFSGTIGSNvsLDDERM-TEEEIKNALRQVGAEPLLKKLPKGINEPVIEKGSTLSSGERQLISFARALAFDP 585
Cdd:cd03288 98 SIILQDPILFSGSIRFN--LDPECKcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKS 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 586 AILILDEATAHIDTETEAVIQKALDVVKQGRTTFVIAHRLSTIRNADQILVLDKGEIVEKGNHEELMALE 655
Cdd:cd03288 176 SILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQE 245
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
431-641 |
2.49e-47 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 166.10 E-value: 2.49e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 431 EFRDVSFAYQEGEE-VLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGIV 509
Cdd:cd03225 1 ELKNLSFSYPDGARpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 510 LQDP--YLFSGTIGS-------NVSLDDERMtEEEIKNALRQVGAEPLLKKLPkginepviekgSTLSSGERQLISFARA 580
Cdd:cd03225 81 FQNPddQFFGPTVEEevafgleNLGLPEEEI-EERVEEALELVGLEGLRDRSP-----------FTLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1718055426 581 LAFDPAILILDEATAHIDTETEAVIQKAL-DVVKQGRTTFVIAHRLSTIRN-ADQILVLDKGE 641
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLkKLKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
149-663 |
2.61e-44 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 171.50 E-value: 2.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 149 MVLLICLYGGLLV-FSVFFQYgqhYLLQMSANRiiqkMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTE----AIRDL 223
Cdd:PTZ00243 1003 VYLGIVLLGTFSVpLRFFLSY---EAMRRGSRN----MHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDildnTLPMS 1075
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 224 YVTVLStfvtsgiYMFGIFTALFLLDVKLAFVCLAIVPIIWLWSVIYRRYASYyNQKIRSINSDINAK----MNESIQGM 299
Cdd:PTZ00243 1076 YLYLLQ-------CLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSA-NREIRRIKSVAKSPvftlLEEALQGS 1147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 300 TIIQAFRHQKETMRE-FEELN--ESHFYFQN---RMLNLN-SLMSHNLVNVIrnlAFVCLIWHFGGASLNAAGIVSIGVL 372
Cdd:PTZ00243 1148 ATITAYGKAHLVMQEaLRRLDvvYSCSYLENvanRWLGVRvEFLSNIVVTVI---ALIGVIGTMLRATSQEIGLVSLSLT 1224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 373 YAF--VDYLNRLfqpitgiVNQFSKLELARVSAGRVF------------ELLEEKNT--EEAGQPAK-------ERA--- 426
Cdd:PTZ00243 1225 MAMqtTATLNWL-------VRQVATVEADMNSVERLLyytdevphedmpELDEEVDAleRRTGMAADvtgtvviEPAspt 1297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 427 --------LGRVEFRDVSFAYQEGEE-VLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNM 497
Cdd:PTZ00243 1298 saaphpvqAGSLVFEGVQMRYREGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAY 1377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 498 SRQELRSHMGIVLQDPYLFSGTIGSNVSLDDErMTEEEIKNALRQVGAEPLLKKLPKGINEPVIEKGSTLSSGERQLISF 577
Cdd:PTZ00243 1378 GLRELRRQFSMIPQDPVLFDGTVRQNVDPFLE-ASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCM 1456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 578 ARA-LAFDPAILILDEATAHIDTETEAVIQKALDVVKQGRTTFVIAHRLSTIRNADQILVLDKGEIVEKGNHEEL-MALE 655
Cdd:PTZ00243 1457 ARAlLKKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQ 1536
|
....*...
gi 1718055426 656 GQYYQMYE 663
Cdd:PTZ00243 1537 SIFHSMVE 1544
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
430-644 |
6.68e-43 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 154.05 E-value: 6.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQE---LRSHM 506
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 507 GIVLQDPYLFSG-TIGSNVSL------DDERMTEEEIKNALRQVGAEPLLKKLPkginepviekgSTLSSGERQLISFAR 579
Cdd:COG2884 82 GVVFQDFRLLPDrTVYENVALplrvtgKSRKEIRRRVREVLDLVGLSDKAKALP-----------HELSGGEQQRVAIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1718055426 580 ALAFDPAILILDEATAHIDTETEAVIQKALDVVKQGRTTFVIA-HRLSTIRNADQ-ILVLDKGEIVE 644
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
149-406 |
8.32e-43 |
|
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: 156.43 E-value: 8.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 149 MVLLICLyGGLLVFSV--FFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVT 226
Cdd:cd18552 37 ALLLVPL-AIIGLFLLrgLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 227 VLSTFVTSGIYMFGIFTALFLLDVKLAFVCLAIVPIIwLWSVIY-----RRYAsyynQKIRSINSDINAKMNESIQGMTI 301
Cdd:cd18552 116 ALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLA-ALPIRRigkrlRKIS----RRSQESMGDLTSVLQETLSGIRV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 302 IQAFRHQKETMREFEELNESHFYFQNRMLNLNSLMShNLVNVIRNLAFVCLIWhFGGaSLNAAGIVSIGVLYAFVDYLNR 381
Cdd:cd18552 191 VKAFGAEDYEIKRFRKANERLRRLSMKIARARALSS-PLMELLGAIAIALVLW-YGG-YQVISGELTPGEFISFITALLL 267
|
250 260
....*....|....*....|....*
gi 1718055426 382 LFQPITGIVNQFSKLELARVSAGRV 406
Cdd:cd18552 268 LYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
430-653 |
3.55e-42 |
|
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: 160.07 E-value: 3.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGE----EVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQ---EL 502
Cdd:COG1123 261 LEVRNLSKRYPVRGkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRslrEL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 503 RSHMGIVLQDPY--LFSG-TIGSNVS-------LDDERMTEEEIKNALRQVG-AEPLLKKLPkginepviekgSTLSSGE 571
Cdd:COG1123 341 RRRVQMVFQDPYssLNPRmTVGDIIAeplrlhgLLSRAERRERVAELLERVGlPPDLADRYP-----------HELSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 572 RQLISFARALAFDPAILILDEATAHIDTETEAVIQKAL-DVVKQ-GRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKGNH 648
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLrDLQRElGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPT 489
|
....*
gi 1718055426 649 EELMA 653
Cdd:COG1123 490 EEVFA 494
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
429-652 |
5.63e-42 |
|
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: 152.89 E-value: 5.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 429 RVEFRDVSFAYQeGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGI 508
Cdd:COG1120 1 MLEAENLSVGYG-GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 509 VLQDPYL-FSGTIGSNVSL--------------DDERMTEEeiknALRQVGAEPLLKKlpkginePViekgSTLSSGERQ 573
Cdd:COG1120 80 VPQEPPApFGLTVRELVALgryphlglfgrpsaEDREAVEE----ALERTGLEHLADR-------PV----DELSGGERQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 574 LISFARALAFDPAILILDEATAHIDteteavI---QKALDVVK-----QGRTTFVIAHRLS-TIRNADQILVLDKGEIVE 644
Cdd:COG1120 145 RVLIARALAQEPPLLLLDEPTSHLD------LahqLEVLELLRrlareRGRTVVMVLHDLNlAARYADRLVLLKDGRIVA 218
|
....*...
gi 1718055426 645 KGNHEELM 652
Cdd:COG1120 219 QGPPEEVL 226
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
149-406 |
5.67e-42 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 154.59 E-value: 5.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 149 MVLLICLYGGLLVFSV---FFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYV 225
Cdd:cd18564 50 LALLLLAAAALVGIALlrgLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 226 TVLSTFVTSGIYMFGIFTALFLLDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTIIQAF 305
Cdd:cd18564 130 SGVLPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAF 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 306 RHQKETMREFEELNESHFYFQNRMLNLNSLMShNLVNVIRNLAFVCLIWHfgGASLNAAGIVSIGVLYAFVDYLNRLFQP 385
Cdd:cd18564 210 GREEHEERRFARENRKSLRAGLRAARLQALLS-PVVDVLVAVGTALVLWF--GAWLVLAGRLTPGDLLVFLAYLKNLYKP 286
|
250 260
....*....|....*....|.
gi 1718055426 386 ITGIVNQFSKLELARVSAGRV 406
Cdd:cd18564 287 VRDLAKLTGRIAKASASAERV 307
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
431-642 |
5.82e-42 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 150.06 E-value: 5.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 431 EFRDVSFAYQEGEE-VLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGIV 509
Cdd:cd03246 2 EVENVSFRYPGAEPpVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 510 LQDPYLFSGTIGSNVslddermteeeiknalrqvgaepllkklpkginepviekgstLSSGERQLISFARALAFDPAILI 589
Cdd:cd03246 82 PQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1718055426 590 LDEATAHIDTETEAVIQKAL-DVVKQGRTTFVIAHRLSTIRNADQILVLDKGEI 642
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIaALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
431-642 |
1.34e-41 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 150.35 E-value: 1.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 431 EFRDVSFAYQeGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGIVL 510
Cdd:COG4619 2 ELEGLSFRVG-GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 511 QDPYLFSGTIGSNV----SLDDERMTEEEIKNALRQVGAEP-LLKKlpkginePViekgSTLSSGERQLISFARALAFDP 585
Cdd:COG4619 81 QEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLGLPPdILDK-------PV----ERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 586 AILILDEATAHIDTETEAVIQKALD--VVKQGRTTFVIAHRLSTI-RNADQILVLDKGEI 642
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLReyLAEEGRAVLWVSHDPEQIeRVADRVLTLEAGRL 209
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
161-641 |
2.20e-41 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 162.51 E-value: 2.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 161 VFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVTVLSTFVTSGIYMFG 240
Cdd:PTZ00265 108 IFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLG 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 241 IFTALFLLDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTIIQAFRHQKETMREFeelNE 320
Cdd:PTZ00265 188 LYIWSLFKNARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKF---NL 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 321 SHFYFQNRMLNLNSLMS-H-NLVNVIRNLAFVCLIWH------------FGGASLNAAGIVSI--GVLYAFvdYLNRLFQ 384
Cdd:PTZ00265 265 SEKLYSKYILKANFMESlHiGMINGFILASYAFGFWYgtriiisdlsnqQPNNDFHGGSVISIllGVLISM--FMLTIIL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 385 PitGIVNQFSKLElarvSAGRVFELLEEKNTEEAGQPAKE-RALGRVEFRDVSFAY--QEGEEVLKHISFTAQKGETVAL 461
Cdd:PTZ00265 343 P--NITEYMKSLE----ATNSLYEIINRKPLVENNDDGKKlKDIKKIQFKNVRFHYdtRKDVEIYKDLNFTLTEGKTYAF 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 462 VGHTGSGKSSILNLLFRFYDAQKGDVLI-DGKSIYNMSRQELRSHMGIVLQDPYLFSGTIGSNV-----SLDD-ERMTEE 534
Cdd:PTZ00265 417 VGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIkyslySLKDlEALSNY 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 535 ---------------------------------------------------EIKNALRQVGAEPLLKKLPKGINEPVIEK 563
Cdd:PTZ00265 497 ynedgndsqenknkrnscrakcagdlndmsnttdsneliemrknyqtikdsEVVDVSKKVLIHDFVSALPDKYETLVGSN 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 564 GSTLSSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQKALDVVK--QGRTTFVIAHRLSTIRNADQILVLDKGE 641
Cdd:PTZ00265 577 ASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSNRE 656
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
170-662 |
2.55e-41 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 162.51 E-value: 2.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 170 QHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFD---NLPaGKVVARITNDteairdlyVTVLSTFVTSGIYMFGIFTALF 246
Cdd:PTZ00265 886 KNYYNNVIGEKVEKTMKRRLFENILYQEISFFDqdkHAP-GLLSAHINRD--------VHLLKTGLVNNIVIFTHFIVLF 956
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 247 LLDVKLAFVCLAIVPIIWlwSVIYrryasYYNQKIRSINSDINAkmNESIQGMTIIQ---AFRHQKETmrefEELNESHF 323
Cdd:PTZ00265 957 LVSMVMSFYFCPIVAAVL--TGTY-----FIFMRVFAIRARLTA--NKDVEKKEINQpgtVFAYNSDD----EIFKDPSF 1023
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 324 YFQNRMLNLNSLMSHNL----VNVI------------RNLAFVCLIWHFG--------------GASLNAAGIVSIGvly 373
Cdd:PTZ00265 1024 LIQEAFYNMNTVIIYGLedyfCNLIekaidysnkgqkRKTLVNSMLWGFSqsaqlfinsfaywfGSFLIRRGTILVD--- 1100
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 374 afvDYLNRLFQPI-TG-----IVNQFSKLELARVSAGRVFELLEEKNT----EEAGQPAKERAL--GRVEFRDVSFAYQE 441
Cdd:PTZ00265 1101 ---DFMKSLFTFLfTGsyagkLMSLKGDSENAKLSFEKYYPLIIRKSNidvrDNGGIRIKNKNDikGKIEIMDVNFRYIS 1177
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 442 GEEV--LKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQK----------------------------------- 484
Cdd:PTZ00265 1178 RPNVpiYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNdhhivfknehtndmtneqdyqgdeeqnvgmknvne 1257
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 485 -------------------GDVLIDGKSIYNMSRQELRSHMGIVLQDPYLFSGTIGSNVSLDDERMTEEEIKNALRQVGA 545
Cdd:PTZ00265 1258 fsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAI 1337
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 546 EPLLKKLPKGINEPVIEKGSTLSSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQKALDVVKQ--GRTTFVIAH 623
Cdd:PTZ00265 1338 DEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAH 1417
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1718055426 624 RLSTIRNADQILVLDK----GEIVE-KGNHEELMALEGQYYQMY 662
Cdd:PTZ00265 1418 RIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLSVQDGVYKKY 1461
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
430-653 |
1.20e-40 |
|
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: 148.42 E-value: 1.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYqEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSR---QELRSHM 506
Cdd:cd03261 1 IELRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 507 GIVLQDPYLFSG-TIGSNVSL-------DDERMTEEEIKNALRQVGAEPLLKKLPkginepviekgSTLSSGERQLISFA 578
Cdd:cd03261 80 GMLFQSGALFDSlTVFENVAFplrehtrLSEEEIREIVLEKLEAVGLRGAEDLYP-----------AELSGGMKKRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 579 RALAFDPAILILDEATAHIDTETEAVI-------QKALDVvkqgrTTFVIAHRLSTIRN-ADQILVLDKGEIVEKGNHEE 650
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDPIASGVIddlirslKKELGL-----TSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEE 223
|
...
gi 1718055426 651 LMA 653
Cdd:cd03261 224 LRA 226
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
146-406 |
1.40e-40 |
|
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: 150.32 E-value: 1.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 146 IKGMVLLICLYGGLLVFSVFFQYGQHYL---LQMSANRiiqKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRD 222
Cdd:cd18540 38 LDGLTGFILLYLGLILIQALSVFLFIRLagkIEMGVSY---DLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 223 LYVTVLSTFVTSGIYMFGIFTALFLLDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTII 302
Cdd:cd18540 115 IISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSIYFQKKILKAYRKVRKINSRITGAFNEGITGAKTT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 303 QAFRHQKETMREFEELNESHFYFQNRMLNLNSLMShNLVNVIRNLAFVCLIWhFGGASLnAAGIVSIGVLYAFVDYLNRL 382
Cdd:cd18540 195 KTLVREEKNLREFKELTEEMRRASVRAARLSALFL-PIVLFLGSIATALVLW-YGGILV-LAGAITIGTLVAFISYATQF 271
|
250 260
....*....|....*....|....
gi 1718055426 383 FQPITGIVNQFSKLELARVSAGRV 406
Cdd:cd18540 272 FEPIQQLARVLAELQSAQASAERV 295
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
430-642 |
2.62e-40 |
|
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: 146.87 E-value: 2.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGEE---VLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQEL---- 502
Cdd:cd03255 1 IELKNLSKTYGGGGEkvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 503 RSHMGIVLQDPYLFSG-TIGSNVSL------DDERMTEEEIKNALRQVGAEPLLKKLPkginepviekgSTLSSGERQLI 575
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELplllagVPKKERRERAEELLERVGLGDRLNHYP-----------SELSGGQQQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1718055426 576 SFARALAFDPAILILDEATAHIDTET-EAVIQKALDVVKQGRTTFVIA-HRLSTIRNADQILVLDKGEI 642
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETgKEVMELLRELNKEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
430-646 |
5.51e-40 |
|
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: 144.76 E-value: 5.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGEE-VLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMsRQELRSHMGI 508
Cdd:cd03247 1 LSINNVSFSYPEQEQqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 509 VLQDPYLFSGTIGSNVslddermteeeiknalrqvgaepllkklpkginepviekGSTLSSGERQLISFARALAFDPAIL 588
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1718055426 589 ILDEATAHIDTETEAVIQKALDVVKQGRTTFVIAHRLSTIRNADQILVLDKGEIVEKG 646
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
430-653 |
5.58e-40 |
|
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: 146.66 E-value: 5.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYqEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMS---RQELRSHM 506
Cdd:COG1127 6 IEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 507 GIVLQDPYLFSG-TIGSNVSL-DDE--RMTEEEIKN----ALRQVGAEPLLKKLPkginepviekgSTLSSGERQLISFA 578
Cdd:COG1127 85 GMLFQGGALFDSlTVFENVAFpLREhtDLSEAEIRElvleKLELVGLPGAADKMP-----------SELSGGMRKRVALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 579 RALAFDPAILILDEATAHIDTETEAVI-------QKALDVvkqgrTTFVIAHRLSTIRN-ADQILVLDKGEIVEKGNHEE 650
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDPITSAVIdelirelRDELGL-----TSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEE 228
|
...
gi 1718055426 651 LMA 653
Cdd:COG1127 229 LLA 231
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
430-646 |
1.40e-39 |
|
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: 145.34 E-value: 1.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGE---EVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQEL---R 503
Cdd:cd03257 2 LEVKNLSVSFPTGGgsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 504 SHMGIVLQDPYL---FSGTIG--------SNVSLDDERMTEEEIKNALRQVGAEP-LLKKLPkginepviekgSTLSSGE 571
Cdd:cd03257 82 KEIQMVFQDPMSslnPRMTIGeqiaeplrIHGKLSKKEARKEAVLLLLVGVGLPEeVLNRYP-----------HELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718055426 572 RQLISFARALAFDPAILILDEATAHIDTETEAVIQKAL-DVVKQGRTTFV-IAHRLSTIRN-ADQILVLDKGEIVEKG 646
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLkKLQEELGLTLLfITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
149-406 |
1.02e-38 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 144.96 E-value: 1.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 149 MVLLICLYGGLL---VFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYV 225
Cdd:cd18563 39 TSLLLLLVLGLAgayVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 226 TVLSTFVTSGIYMFGIFTALFLLDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTIIQAF 305
Cdd:cd18563 119 DGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAF 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 306 -RHQKETMReFEELNEsHFYFQNRMLNLNSLMSHNLVNVIRNLaFVCLIWHFGGASLnAAGIVSIGVLYAFVDYLNRLFQ 384
Cdd:cd18563 199 gQEKREIKR-FDEANQ-ELLDANIRAEKLWATFFPLLTFLTSL-GTLIVWYFGGRQV-LSGTMTLGTLVAFLSYLGMFYG 274
|
250 260
....*....|....*....|..
gi 1718055426 385 PITGIVNQFSKLELARVSAGRV 406
Cdd:cd18563 275 PLQWLSRLNNWITRALTSAERI 296
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
430-653 |
1.33e-38 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 150.05 E-value: 1.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGE-EVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQ---KGDVLIDGKSIYNMSRQELRSH 505
Cdd:COG1123 5 LEVRDLSVRYPGGDvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 506 MGIVLQDPY--LFSGTIGSNV--SLDDERMTEEEIK----NALRQVGAEPLLKKLPkginepviekgSTLSSGERQLISF 577
Cdd:COG1123 85 IGMVFQDPMtqLNPVTVGDQIaeALENLGLSRAEARarvlELLEAVGLERRLDRYP-----------HQLSGGQRQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1718055426 578 ARALAFDPAILILDEATAHIDTETEAVIQKALDVVKQ--GRTTFVIAHRLSTI-RNADQILVLDKGEIVEKGNHEELMA 653
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
151-406 |
1.70e-38 |
|
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: 144.11 E-value: 1.70e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 151 LLICLyGGLLVFSVF---FQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVTV 227
Cdd:cd18542 38 LWLLA-LLILGVALLrgvFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 228 LSTFVTSGIYMFGIFTALFLLDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTIIQAFRH 307
Cdd:cd18542 117 LVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAR 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 308 QKETMREFEELNEShfyFQNRMLNLNSLMS--HNLVNVIRNLAFVCLIWhFGGAsLNAAGIVSIGVLYAFVDYLNRLFQP 385
Cdd:cd18542 197 EDYEIEKFDKENEE---YRDLNIKLAKLLAkyWPLMDFLSGLQIVLVLW-VGGY-LVINGEITLGELVAFISYLWMLIWP 271
|
250 260
....*....|....*....|....
gi 1718055426 386 I--TG-IVNQFSKlelARVSAGRV 406
Cdd:cd18542 272 VrqLGrLINDMSR---ASASAERI 292
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
430-651 |
3.05e-38 |
|
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: 141.55 E-value: 3.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYqEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQK-----GDVLIDGKSIY--NMSRQEL 502
Cdd:cd03260 1 IELRDLNVYY-GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIYdlDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 503 RSHMGIVLQDPYLFSGTIGSNVSL-------DDERMTEEEIKNALRQVGAEPLLK-KLpkginepvieKGSTLSSGERQL 574
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYglrlhgiKLKEELDERVEEALRKAALWDEVKdRL----------HALGLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718055426 575 ISFARALAFDPAILILDEATAHIDTETEAVIQKALDVVKQGRTTFVIAHRLS-TIRNADQILVLDKGEIVEKGNHEEL 651
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQqAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
138-406 |
1.43e-37 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 141.52 E-value: 1.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 138 LFQFYQPEIKGMV-------------LLICLYGGLLVFSV--FFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFD 202
Cdd:cd18778 13 LLGLVPPWLIRELvdlvtigskslglLLGLALLLLGAYLLraLLNFLRIYLNHVAEQKVVADLRSDLYDKLQRLSLRYFD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 203 NLPAGKVVARITNDTEAIRDLYVTVLSTFVTSGIYMFGIFTALFLLDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQKIR 282
Cdd:cd18778 93 DRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 283 SINSDINAKMNESIQGMTIIQAFRHQKETMREFEELNESHFYFQNRMLNLNSlMSHNLVNVIRNLAFVCLIWHfgGASLN 362
Cdd:cd18778 173 EALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWA-IFHPLMEFLTSLGTVLVLGF--GGRLV 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1718055426 363 AAGIVSIGVLYAFVDYLNRLFQPITGIVNQFSKLELARVSAGRV 406
Cdd:cd18778 250 LAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
446-595 |
2.14e-37 |
|
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: 136.24 E-value: 2.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 446 LKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGIVLQDPYLFSG-TIGSNV 524
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1718055426 525 sldDERMTEEEIKNALRQVGAEPLLKKLPKG--INEPVIEKGSTLSSGERQLISFARALAFDPAILILDEATA 595
Cdd:pfam00005 81 ---RLGLLLKGLSKREKDARAEEALEKLGLGdlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
146-406 |
2.17e-37 |
|
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: 141.03 E-value: 2.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 146 IKGMVLLIClygGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYV 225
Cdd:cd18551 35 SGGLLALLV---ALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELIT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 226 TVLSTFVTSGIYMFGIFTALFLLDVKLAFVCLAIVP-----IIWLWSVIYRRYASYYNQkirsiNSDINAKMNESIQGMT 300
Cdd:cd18551 112 SGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPlafliILPLGRRIRKASKRAQDA-----LGELSAALERALSAIR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 301 IIQAFRHQKETMREFEELNESHFYFQNRMLNLNSLMShNLVNVIRNLAFVCLIWhFGGASLnAAGIVSIGVLYAFVDYLN 380
Cdd:cd18551 187 TVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIG-PLMGLAVQLALLVVLG-VGGARV-ASGALTVGTLVAFLLYLF 263
|
250 260
....*....|....*....|....*.
gi 1718055426 381 RLFQPITGIVNQFSKLELARVSAGRV 406
Cdd:cd18551 264 QLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
149-386 |
3.13e-37 |
|
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: 140.09 E-value: 3.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 149 MVLLICLYGGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVTVL 228
Cdd:pfam00664 40 LNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 229 STFVTSGIYMFGIFTALFLLDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTIIQAFRHQ 308
Cdd:pfam00664 120 GLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGRE 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718055426 309 KETMREFEELNESHFYFQNRMLNLNSLMShNLVNVIRNLAFVCLIWHfgGASLNAAGIVSIGVLYAFVDYLNRLFQPI 386
Cdd:pfam00664 200 EYELEKYDKALEEALKAGIKKAVANGLSF-GITQFIGYLSYALALWF--GAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
430-653 |
4.69e-37 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 138.78 E-value: 4.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGEE---VLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHM 506
Cdd:COG1124 2 LEVRNLSVSYGQGGRrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 507 GIVLQDPYLfsgtigsnvSLDdERMT-----------------EEEIKNALRQVGAEP-LLKKLPkginepviekgSTLS 568
Cdd:COG1124 82 QMVFQDPYA---------SLH-PRHTvdrilaeplrihglpdrEERIAELLEQVGLPPsFLDRYP-----------HQLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 569 SGERQLISFARALAFDPAILILDEATAHIDTETEAVIQKALDVVKQ--GRTTFVIAHRLSTI-RNADQILVLDKGEIVEK 645
Cdd:COG1124 141 GGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEE 220
|
....*...
gi 1718055426 646 GNHEELMA 653
Cdd:COG1124 221 LTVADLLA 228
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
430-652 |
1.67e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 138.20 E-value: 1.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGEE-VLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGI 508
Cdd:PRK13632 8 IKVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 509 VLQDPYlfSGTIGSNV------SLDDERMTEEEIK----NALRQVGAEPLLKKLPkginepviekgSTLSSGERQLISFA 578
Cdd:PRK13632 88 IFQNPD--NQFIGATVeddiafGLENKKVPPKKMKdiidDLAKKVGMEDYLDKEP-----------QNLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1718055426 579 RALAFDPAILILDEATAHIDTETEAVIQKAL-DVVKQGRTTFV-IAHRLSTIRNADQILVLDKGEIVEKGNHEELM 652
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMvDLRKTRKKTLIsITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
431-646 |
7.94e-36 |
|
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: 132.94 E-value: 7.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 431 EFRDVSFAYQeGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGIVL 510
Cdd:cd03214 1 EVENLSVGYG-GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 511 QdpylfsgtigsnvslddermteeeiknALRQVGAEPLLKKlpkGINEpviekgstLSSGERQLISFARALAFDPAILIL 590
Cdd:cd03214 80 Q---------------------------ALELLGLAHLADR---PFNE--------LSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1718055426 591 DEATAHIDTETEAVIqkaLDVVKQ-----GRTTFVIAHRLS-TIRNADQILVLDKGEIVEKG 646
Cdd:cd03214 122 DEPTSHLDIAHQIEL---LELLRRlarerGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
171-638 |
2.73e-35 |
|
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: 143.90 E-value: 2.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 171 HYLLQMSaNRIIQKMRQDVFshiqRMPIRYFDNLPAGKVVARITNDTEAIRDLYVTVLSTFVTSGIYMFGiftALFLLDV 250
Cdd:TIGR01271 951 HTLLTVS-KRLHEQMLHSVL----QAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLG---AIFVVSV 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 251 KLAFVCLAIVPIIWLWsVIYRRYASYYNQKIRSINSD----INAKMNESIQGMTIIQAFRHQKEtmreFEELneshFYfq 326
Cdd:TIGR01271 1023 LQPYIFIAAIPVAVIF-IMLRAYFLRTSQQLKQLESEarspIFSHLITSLKGLWTIRAFGRQSY----FETL----FH-- 1091
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 327 nRMLNLNSLMSHNLVNVIRNLAFVC---LIWHFGGASL-----NAAGIVSIGVLYAFVDYLNRLFQpitGIVNQFSKLEL 398
Cdd:TIGR01271 1092 -KALNLHTANWFLYLSTLRWFQMRIdiiFVFFFIAVTFiaigtNQDGEGEVGIILTLAMNILSTLQ---WAVNSSIDVDG 1167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 399 ARVSAGRVFELL-------EEKNTEEAGQPAKERAL------------GRVEFRDVSFAYQE-GEEVLKHISFTAQKGET 458
Cdd:TIGR01271 1168 LMRSVSRVFKFIdlpqeepRPSGGGGKYQLSTVLVIenphaqkcwpsgGQMDVQGLTAKYTEaGRAVLQDLSFSVEGGQR 1247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 459 VALVGHTGSGKSSILNLLFRFYDAQkGDVLIDGKSIYNMSRQELRSHMGIVLQDPYLFSGTIGSNvsLDD-ERMTEEEIK 537
Cdd:TIGR01271 1248 VGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKN--LDPyEQWSDEEIW 1324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 538 NALRQVGAEPLLKKLPKGINEPVIEKGSTLSSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQKALDVVKQGRT 617
Cdd:TIGR01271 1325 KVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCT 1404
|
490 500
....*....|....*....|.
gi 1718055426 618 TFVIAHRLSTIRNADQILVLD 638
Cdd:TIGR01271 1405 VILSEHRVEALLECQQFLVIE 1425
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
431-641 |
6.55e-35 |
|
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: 129.67 E-value: 6.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 431 EFRDVSFAYQEGEeVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGIVL 510
Cdd:cd00267 1 EIENLSFRYGGRT-ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 511 QdpylfsgtigsnvslddermteeeiknalrqvgaepllkklpkginepviekgstLSSGERQLISFARALAFDPAILIL 590
Cdd:cd00267 80 Q-------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1718055426 591 DEATAHIDTET-EAVIQKALDVVKQGRTTFVIAHRLSTIRNA-DQILVLDKGE 641
Cdd:cd00267 105 DEPTSGLDPASrERLLELLRELAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
430-644 |
1.52e-34 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 130.67 E-value: 1.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGE---EVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIynmsrQELRSHM 506
Cdd:cd03293 1 LEVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV-----TGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 507 GIVLQDPYLFS-GTIGSNVSL--------DDERmtEEEIKNALRQVGAEPLLKKLPKginepviekgsTLSSGERQLISF 577
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALglelqgvpKAEA--RERAEELLELVGLSGFENAYPH-----------QLSGGMRQRVAL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1718055426 578 ARALAFDPAILILDEATAHIDTETEAVIQKAL-DVV-KQGRTTFVIAHRLS-TIRNADQILVLDK--GEIVE 644
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELlDIWrETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
145-395 |
1.68e-34 |
|
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: 132.96 E-value: 1.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 145 EIKGMVLLICLYGGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLY 224
Cdd:cd18549 37 NLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISELA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 225 VTVLSTFVTSGIYMFGIFTALFLLDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTIIQA 304
Cdd:cd18549 117 HHGPEDLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 305 FRHQKETMREFEELNESHFYFQNRMLNLNSLMsHNLVNVIRNLAFVCLIwhFGGASLNAAGIVSIGVLYAFVDYLNRLFQ 384
Cdd:cd18549 197 FANEEYEIEKFDEGNDRFLESKKKAYKAMAYF-FSGMNFFTNLLNLVVL--VAGGYFIIKGEITLGDLVAFLLYVNVFIK 273
|
250
....*....|....
gi 1718055426 385 PITGIVN---QFSK 395
Cdd:cd18549 274 PIRRLVNfteQYQK 287
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
428-642 |
2.00e-34 |
|
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: 132.29 E-value: 2.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 428 GRVEFRDVSFAYQE-GEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQkGDVLIDGKSIYNMSRQELRSHM 506
Cdd:cd03289 1 GQMTVKDLTAKYTEgGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 507 GIVLQDPYLFSGTIGSNvsLDD-ERMTEEEIKNALRQVGAEPLLKKLPKGINEPVIEKGSTLSSGERQLISFARALAFDP 585
Cdd:cd03289 80 GVIPQKVFIFSGTFRKN--LDPyGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1718055426 586 AILILDEATAHIDTETEAVIQKALDVVKQGRTTFVIAHRLSTIRNADQILVLDKGEI 642
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
430-653 |
2.07e-34 |
|
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: 130.78 E-value: 2.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGE---EVLKHISFTAQKGETVALVGHTGSGKSSIL---NLLFRfYDAqkGDVLIDGKSIYNMSRQEL- 502
Cdd:cd03258 2 IELKNVSKVFGDTGgkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIrciNGLER-PTS--GSVLVDGTDLTLLSGKELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 503 --RSHMGIVLQDPYLFSG-TIGSNVSL--------DDERmtEEEIKNALRQVGAEPLLKKLPkginepviekgSTLSSGE 571
Cdd:cd03258 79 kaRRRIGMIFQHFNLLSSrTVFENVALpleiagvpKAEI--EERVLELLELVGLEDKADAYP-----------AQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 572 RQLISFARALAFDPAILILDEATAHIDTE-TEAVIQKALDVVKQ-GRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKGNH 648
Cdd:cd03258 146 KQRVGIARALANNPKVLLCDEATSALDPEtTQSILALLRDINRElGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTV 225
|
....*
gi 1718055426 649 EELMA 653
Cdd:cd03258 226 EEVFA 230
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
430-646 |
2.41e-34 |
|
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: 129.95 E-value: 2.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQeGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQelRSHMGIV 509
Cdd:cd03259 1 LELKGLSKTYG-SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 510 LQDPYLFSG-TIGSNVS--LDDERMTEEEIKN----ALRQVGAEPLLKKLPkginepviekgSTLSSGERQLISFARALA 582
Cdd:cd03259 78 FQDYALFPHlTVAENIAfgLKLRGVPKAEIRArvreLLELVGLEGLLNRYP-----------HELSGGQQQRVALARALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1718055426 583 FDPAILILDEATAHIDTETEAVIQKALDVV--KQGRTTFVIAHRLS-TIRNADQILVLDKGEIVEKG 646
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELREELKELqrELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
430-641 |
3.38e-34 |
|
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: 129.13 E-value: 3.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGEE----VLKHISFTAQKGETVALVGHTGSGKSSILNLLFrfydaqkGDV-LIDGKSIYNmsrqelrS 504
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALL-------GELeKLSGSVSVP-------G 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 505 HMGIVLQDPYLFSGTIGSNVsLDDERMTEEEIKNALRQVGAEPLLKKLPKGINEPVIEKGSTLSSGERQLISFARALAFD 584
Cdd:cd03250 67 SIAYVSQEPWIQNGTIRENI-LFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1718055426 585 PAILILDEATAHIDTETEA-----VIQKALdvvKQGRTTFVIAHRLSTIRNADQILVLDKGE 641
Cdd:cd03250 146 ADIYLLDDPLSAVDAHVGRhifenCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
430-653 |
3.47e-34 |
|
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: 130.50 E-value: 3.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGIV 509
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 510 LQDPYLFSG-TIGSNVSL-------DDERMtEEEIKNALRQVGAEP--LLKKLPkginepviekgSTLSSGERQLISFAR 579
Cdd:cd03295 81 IQQIGLFPHmTVEENIALvpkllkwPKEKI-RERADELLALVGLDPaeFADRYP-----------HELSGGQQQRVGVAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1718055426 580 ALAFDPAILILDEATAHIDTETEAVIQKALDVVKQ--GRTTFVIAHRL-STIRNADQILVLDKGEIVEKGNHEELMA 653
Cdd:cd03295 149 ALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
430-661 |
2.39e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 129.36 E-value: 2.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGEE-VLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGI 508
Cdd:PRK13635 6 IRVEHISFRYPDAATyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 509 VLQDP-YLFSG-TIGSNV--SLDDERMTEEE----IKNALRQVGAEPLLKKlpkginEPviekgSTLSSGERQLISFARA 580
Cdd:PRK13635 86 VFQNPdNQFVGaTVQDDVafGLENIGVPREEmverVDQALRQVGMEDFLNR------EP-----HRLSGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 581 LAFDPAILILDEATAHIDTE-TEAVIQKALDVVKQGRTTFV-IAHRLSTIRNADQILVLDKGEIVEKGNHEELMALEGQY 658
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRgRREVLETVRQLKEQKGITVLsITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGHML 234
|
...
gi 1718055426 659 YQM 661
Cdd:PRK13635 235 QEI 237
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
129-406 |
4.76e-33 |
|
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: 128.68 E-value: 4.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 129 AAEKLTKQELFQFyqpeikgmVLLIClygGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGK 208
Cdd:cd18541 30 TAGTLTASQLLRY--------ALLIL---LLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 209 VVARITNDTEAIRDLYVTVLSTFVTSGIYMFGIFTALFLLDVKLAFVCLAIVPII-----WLWSVIYRRYasyynQKIRS 283
Cdd:cd18541 99 LMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLallvyRLGKKIHKRF-----RKVQE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 284 INSDINAKMNESIQGMTIIQAFRHQKETMREFEELNESHFYFQNRMLNLNSLMsHNLVNVIRNLAFVCLIWhFGGaSLNA 363
Cdd:cd18541 174 AFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALF-FPLIGLLIGLSFLIVLW-YGG-RLVI 250
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1718055426 364 AGIVSIGVLYAFVDYLNRLFQPITGIVNQFSKLELARVSAGRV 406
Cdd:cd18541 251 RGTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
429-644 |
5.20e-33 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 127.90 E-value: 5.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 429 RVEFRDVSFAYQEGE---EVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIynmsrQELRSH 505
Cdd:COG1116 7 ALELRGVSKRFPTGGggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV-----TGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 506 MGIVLQDPYLFs-gTIGSNVSL--------DDERmtEEEIKNALRQVGAEPLLKKLPKginepviekgsTLSSGERQLIS 576
Cdd:COG1116 82 RGVVFQEPALLpwlTVLDNVALglelrgvpKAER--RERARELLELVGLAGFEDAYPH-----------QLSGGMRQRVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718055426 577 FARALAFDPAILILDEATAHIDTETEAVIQK-ALDVVKQGRTTFV-IAH------RLstirnADQILVLDK--GEIVE 644
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDALTRERLQDeLLRLWQETGKTVLfVTHdvdeavFL-----ADRVVVLSArpGRIVE 221
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
150-406 |
3.15e-32 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 126.44 E-value: 3.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 150 VLLICLYGGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVTVLS 229
Cdd:cd18550 39 VLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 230 TFVTSGIYMFGIFTALFLLDVKLAFVCLAIVPI-IWLWSVIYRRYASYYNQKIRSiNSDINAKMNE--SIQGMTIIQAFR 306
Cdd:cd18550 119 SVVSNVVTLVATLVAMLALDWRLALLSLVLLPLfVLPTRRVGRRRRKLTREQQEK-LAELNSIMQEtlSVSGALLVKLFG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 307 HQKETMREFEELNEshfyfQNRMLNLNSLMSHNLVNVIRNLAFVC---LIWHFGGAsLNAAGIVSIGVLYAFVDYLNRLF 383
Cdd:cd18550 198 REDDEAARFARRSR-----ELRDLGVRQALAGRWFFAALGLFTAIgpaLVYWVGGL-LVIGGGLTIGTLVAFTALLGRLY 271
|
250 260
....*....|....*....|...
gi 1718055426 384 QPITGIVNQFSKLELARVSAGRV 406
Cdd:cd18550 272 GPLTQLLNIQVDLMTSLALFERI 294
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
430-642 |
3.62e-32 |
|
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: 122.51 E-value: 3.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGEeVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNmSRQELRSHMGIV 509
Cdd:cd03230 1 IEVRNLSKRYGKKT-ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 510 LQDPYLFsgtigsnvslddERMTEEEiknalrqvgaepLLKklpkginepviekgstLSSGERQLISFARALAFDPAILI 589
Cdd:cd03230 79 PEEPSLY------------ENLTVRE------------NLK----------------LSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1718055426 590 LDEATAHIDTETEAVIQKAL-DVVKQGRTTFVIAHRLSTIRN-ADQILVLDKGEI 642
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLrELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
430-651 |
5.45e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 125.23 E-value: 5.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGIV 509
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 510 LQDP--YLFSGTIGSNVSLD--DERMTEEEIKN----ALRQVGAEPLLKKLPkginepviekgSTLSSGERQLISFARAL 581
Cdd:PRK13647 85 FQDPddQVFSSTVWDDVAFGpvNMGLDKDEVERrveeALKAVRMWDFRDKPP-----------YHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1718055426 582 AFDPAILILDEATAHIDTETEAVIQKALDVV-KQGRTTFVIAHRLS-TIRNADQILVLDKGEIVEKGNHEEL 651
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLL 225
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
430-642 |
7.11e-32 |
|
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: 123.29 E-value: 7.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQE---LRSHM 506
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 507 GIVLQDPYLFSG-TIGSNVSLDDE------RMTEEEIKNALRQVGAEPLLKKLPKGinepviekgstLSSGERQLISFAR 579
Cdd:cd03292 81 GVVFQDFRLLPDrNVYENVAFALEvtgvppREIRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1718055426 580 ALAFDPAILILDEATAHIDTETEAVIQKALDVVKQGRTTFVIAHRLSTIRNADQ--ILVLDKGEI 642
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRhrVIALERGKL 214
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
430-655 |
8.53e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 123.66 E-value: 8.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYqEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIynmsrQELRSHMGIV 509
Cdd:COG1121 7 IELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----RRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 510 LQ----DPYL-----------FSGTIGSNVSLDDERmtEEEIKNALRQVGAEPLLKKlpkginePViekgSTLSSGERQL 574
Cdd:COG1121 81 PQraevDWDFpitvrdvvlmgRYGRRGLFRRPSRAD--REAVDEALERVGLEDLADR-------PI----GELSGGQQQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 575 ISFARALAFDPAILILDEATAHIDTETEAVIQKAL-DVVKQGRTTFVIAHRLSTIR-NADQILVLDKGEIVEkGNHEELM 652
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLrELRREGKTILVVTHDLGAVReYFDRVLLLNRGLVAH-GPPEEVL 226
|
...
gi 1718055426 653 ALE 655
Cdd:COG1121 227 TPE 229
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
430-651 |
1.53e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 123.71 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGEE-VLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGI 508
Cdd:PRK13648 8 IVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 509 VLQDP-YLFSGTIGS--------NVSLDDERMtEEEIKNALRQVGAepllkkLPKGINEPviekgSTLSSGERQLISFAR 579
Cdd:PRK13648 88 VFQNPdNQFVGSIVKydvafgleNHAVPYDEM-HRRVSEALKQVDM------LERADYEP-----NALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1718055426 580 ALAFDPAILILDEATAHIDTETEAVIQKALDVVKQGR--TTFVIAHRLSTIRNADQILVLDKGEIVEKGNHEEL 651
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
430-642 |
6.49e-31 |
|
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: 120.33 E-value: 6.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQeGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQ--ELRSHMG 507
Cdd:cd03262 1 IEIKNLHKSFG-DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 508 IVLQDPYLFSG-TIGSNVSLD-------DERMTEEEIKNALRQVGAEPLLKKLPkginepviekgSTLSSGERQLISFAR 579
Cdd:cd03262 80 MVFQQFNLFPHlTVLENITLApikvkgmSKAEAEERALELLEKVGLADKADAYP-----------AQLSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718055426 580 ALAFDPAILILDEATAHIDTEteaVIQKALDVVKQ----GRTTFVIAHRLSTIRN-ADQILVLDKGEI 642
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPE---LVGEVLDVMKDlaeeGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
158-406 |
7.22e-31 |
|
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: 122.59 E-value: 7.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 158 GLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVTVLSTFVTSGIY 237
Cdd:cd18576 44 GLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 238 MFGIFTALFLLDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTIIQAF-RHQKETMReFE 316
Cdd:cd18576 124 LIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFtREDYEIER-YR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 317 ELNESHFYFQNRMLNLNSLMshnlVNVIRNLAFVCLI---WHfgGASLNAAGIVSIGVLYAFVDYLNRLFQPITGIVNQF 393
Cdd:cd18576 203 KALERVVKLALKRARIRALF----SSFIIFLLFGAIVavlWY--GGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLY 276
|
250
....*....|...
gi 1718055426 394 SKLELARVSAGRV 406
Cdd:cd18576 277 GQLQKALGASERV 289
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
430-651 |
3.13e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 120.68 E-value: 3.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGEE-VLKHISFTAQKGETVALVGHTGSGKSSI---LNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSH 505
Cdd:PRK13640 6 VEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTIsklINGLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 506 MGIVLQDP-YLFSG-TIGSNVS--LDDERMTEEE----IKNALRQVGAEPLLKKLPkginepviekgSTLSSGERQLISF 577
Cdd:PRK13640 86 VGIVFQNPdNQFVGaTVGDDVAfgLENRAVPRPEmikiVRDVLADVGMLDYIDSEP-----------ANLSGGQKQRVAI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1718055426 578 ARALAFDPAILILDEATAHIDTETEaviQKALDVVKQ-----GRTTFVIAHRLSTIRNADQILVLDKGEIVEKGNHEEL 651
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGK---EQILKLIRKlkkknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
430-651 |
1.41e-29 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 119.39 E-value: 1.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGEEVLK---HISFTAQKGETVALVGHTGSGKS----SILNLLFRFYDAqKGDVLIDGKSIYNMSRQEL 502
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKavdGVSFDVRRGETLGLVGESGSGKStlarAILGLLPPPGIT-SGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 503 R----SHMGIVLQDPY-----LFsgTIGSNVS-------LDDERMTEEEIKNALRQVG---AEPLLKKLPkginepviek 563
Cdd:COG0444 81 RkirgREIQMIFQDPMtslnpVM--TVGDQIAeplrihgGLSKAEARERAIELLERVGlpdPERRLDRYP---------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 564 gSTLSSGERQLISFARALAFDPAILILDEATAhidteteaviqkALDVVKQG-------------RTTFV-IAHRLSTIR 629
Cdd:COG0444 149 -HELSGGMRQRVMIARALALEPKLLIADEPTT------------ALDVTIQAqilnllkdlqrelGLAILfITHDLGVVA 215
|
250 260
....*....|....*....|...
gi 1718055426 630 N-ADQILVLDKGEIVEKGNHEEL 651
Cdd:COG0444 216 EiADRVAVMYAGRIVEEGPVEEL 238
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
430-653 |
1.70e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 118.17 E-value: 1.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGEEVLKHISFTAQKGETVALVGHTGSGKSSI---LNLLFRfydAQKGDVLIDGKSIYNMSR-QELRSH 505
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLalhLNGLLR---PQKGKVLVSGIDTGDFSKlQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 506 MGIVLQDPYL-FSG-TIGSNVSLDDERM------TEEEIKNALRQVGAEPLLKKLPKginepviekgsTLSSGERQLISF 577
Cdd:PRK13644 79 VGIVFQNPETqFVGrTVEEDLAFGPENLclppieIRKRVDRALAEIGLEKYRHRSPK-----------TLSGGQGQCVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1718055426 578 ARALAFDPAILILDEATAHIDTET-EAVIQKALDVVKQGRTTFVIAHRLSTIRNADQILVLDKGEIVEKGNHEELMA 653
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
445-653 |
2.02e-29 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 116.77 E-value: 2.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 445 VLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQElRSHMGIV--LQDPYLFSG---- 518
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHE-IARLGIGrtFQIPRLFPEltvl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 519 -------------TIGSNVSLDDERMTEEEIKNALRQVGAEPLLkklpkgiNEPViekgSTLSSGERQLISFARALAFDP 585
Cdd:cd03219 94 envmvaaqartgsGLLLARARREEREARERAEELLERVGLADLA-------DRPA----GELSYGQQRRLEIARALATDP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 586 AILILDEATAHI-DTETEAVIQKALDVVKQGRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKGNHEELMA 653
Cdd:cd03219 163 KLLLLDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
153-406 |
4.01e-29 |
|
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: 117.50 E-value: 4.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 153 ICLYGGLL----VFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVTVL 228
Cdd:cd18548 38 ILRTGLLMlllaLLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 229 STFVTSGIYMFGIFTALFLLDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTIIQAFRHQ 308
Cdd:cd18548 118 RMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNRE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 309 KETMREFEELNESHFYFQNRMLNLNSLMShNLVNVIRNLAFVCLIWhFGGASLNaAGIVSIGVLYAFVDYLNRLFQPITG 388
Cdd:cd18548 198 DYEEERFDKANDDLTDTSLKAGRLMALLN-PLMMLIMNLAIVAILW-FGGHLIN-AGSLQVGDLVAFINYLMQILMSLMM 274
|
250
....*....|....*...
gi 1718055426 389 IVNQFSKLELARVSAGRV 406
Cdd:cd18548 275 LSMVFVMLPRASASAKRI 292
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
430-651 |
6.48e-29 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 118.28 E-value: 6.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQeGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQElRsHMGIV 509
Cdd:COG3842 6 LELENVSKRYG-DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK-R-NVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 510 LQD----PYLfsgTIGSNV--SLDDERMTEEEIK----NALRQVGAEPLLKKLPkginepviekgSTLSSGERQLISFAR 579
Cdd:COG3842 83 FQDyalfPHL---TVAENVafGLRMRGVPKAEIRarvaELLELVGLEGLADRYP-----------HQLSGGQQQRVALAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 580 ALAFDPAILILDEATAHIDTET-EAV------IQKALDvvkqgrTTFVIA-HRLS---TIrnADQILVLDKGEIVEKGNH 648
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAKLrEEMreelrrLQRELG------ITFIYVtHDQEealAL--ADRIAVMNDGRIEQVGTP 220
|
...
gi 1718055426 649 EEL 651
Cdd:COG3842 221 EEI 223
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
448-653 |
6.72e-29 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 117.91 E-value: 6.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 448 HISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQEL---RSHMGIVLQDPYlfsgtigsnV 524
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplRRRMQMVFQDPY---------A 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 525 SLdDERMT--------------------EEEIKNALRQVGAEP-LLKKLPKginepviekgsTLSSGERQLISFARALAF 583
Cdd:COG4608 107 SL-NPRMTvgdiiaeplrihglaskaerRERVAELLELVGLRPeHADRYPH-----------EFSGGQRQRIGIARALAL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 584 DPAILILDEATAhidteteaviqkALDVVKQ--------------GRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKGNH 648
Cdd:COG4608 175 NPKLIVCDEPVS------------ALDVSIQaqvlnlledlqdelGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPR 242
|
....*
gi 1718055426 649 EELMA 653
Cdd:COG4608 243 DELYA 247
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
430-653 |
1.87e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 115.17 E-value: 1.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSI-Y-NMSRQELRSHMG 507
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkYdKKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 508 IVLQDP--YLFSGTIGSNVSLD------DERMTEEEIKNALRQVGAEPLLKKLPKginepviekgsTLSSGERQLISFAR 579
Cdd:PRK13639 82 IVFQNPddQLFAPTVEEDVAFGplnlglSKEEVEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1718055426 580 ALAFDPAILILDEATAHIDTETEAVIQKAL-DVVKQGRTTFVIAHRLSTI-RNADQILVLDKGEIVEKGNHEELMA 653
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLyDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
442-650 |
5.48e-28 |
|
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: 112.81 E-value: 5.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 442 GEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRshMGIVLQDPYLFSG-TI 520
Cdd:cd03299 11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRD--ISYVPQNYALFPHmTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 521 GSNVS--LDDERMTEEEIKNALRQVgAEPLlkklpkGINEPVIEKGSTLSSGERQLISFARALAFDPAILILDEATAHID 598
Cdd:cd03299 89 YKNIAygLKKRKVDKKEIERKVLEI-AEML------GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1718055426 599 TETEAVIQKAL-DVVKQGRTTFV-IAHRLSTIRN-ADQILVLDKGEIVEKGNHEE 650
Cdd:cd03299 162 VRTKEKLREELkKIRKEFGVTVLhVTHDFEEAWAlADKVAIMLNGKLIQVGKPEE 216
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
446-653 |
6.03e-28 |
|
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: 118.63 E-value: 6.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 446 LKHISFTAQKGETVALVGHTGSGKSS----ILNLLfrfydAQKGDVLIDGKSIYNMSRQE---LRSHMGIVLQDPYlfsg 518
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLDGLSRRAlrpLRRRMQVVFQDPF---- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 519 tiGSnvsLDdERMTEEEI---------------------KNALRQVGAEP-LLKKLPkgiNEpviekgstLSSGERQLIS 576
Cdd:COG4172 373 --GS---LS-PRMTVGQIiaeglrvhgpglsaaerrarvAEALEEVGLDPaARHRYP---HE--------FSGGQRQRIA 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 577 FARALAFDPAILILDEATAhidteteaviqkALDV--------------VKQGRTTFVIAHRLSTIRN-ADQILVLDKGE 641
Cdd:COG4172 436 IARALILEPKLLVLDEPTS------------ALDVsvqaqildllrdlqREHGLAYLFISHDLAVVRAlAHRVMVMKDGK 503
|
250
....*....|..
gi 1718055426 642 IVEKGNHEELMA 653
Cdd:COG4172 504 VVEQGPTEQVFD 515
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
430-652 |
1.23e-27 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 112.10 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYqEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRF-YDAQKGDVLIDGKSIYNMSRQELRSHMGI 508
Cdd:COG1119 4 LELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlPPTYGNDVRLFGERRGGEDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 509 V---LQDPYL------------FSGTIGSNVSLDDErmTEEEIKNALRQVGAEPLLKKLPkginepviekgSTLSSGERQ 573
Cdd:COG1119 83 VspaLQLRFPrdetvldvvlsgFFDSIGLYREPTDE--QRERARELLELLGLAHLADRPF-----------GTLSQGEQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 574 LISFARALAFDPAILILDEATAHIDTE-TEAVIQkALD-VVKQGRTTFV-IAHRLSTIRNA-DQILVLDKGEIVEKGNHE 649
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGaRELLLA-LLDkLAAEGAPTLVlVTHHVEEIPPGiTHVLLLKDGRVVAAGPKE 228
|
...
gi 1718055426 650 ELM 652
Cdd:COG1119 229 EVL 231
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
151-406 |
3.57e-27 |
|
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: 112.13 E-value: 3.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 151 LLICLYGGLLVFSVF---FQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLyvtV 227
Cdd:cd18554 44 LFTIIGIMFFIFLILrppVEYYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDF---I 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 228 LSTFVTSGIYMFGIFTAL---FLLDVKLAFVCLAIVPI-IWLWSVIYRRYASYYNQKIRSInSDINAKMNESIQGMTIIQ 303
Cdd:cd18554 121 TTGLMNIWLDMITIIIAIcimLVLNPKLTFVSLVIFPFyILAVKYFFGRLRKLTKERSQAL-AEVQGFLHERIQGMSVIK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 304 AFRHQKETMREFEELNESHFYFQNRMLNLNSLmSHNLVNVIRNLAFVCLIwhFGGASLNAAGIVSIGVLYAFVDYLNRLF 383
Cdd:cd18554 200 SFALEKHEQKQFDKRNGHFLTRALKHTRWNAK-TFSAVNTITDLAPLLVI--GFAAYLVIEGNLTVGTLVAFVGYMERMY 276
|
250 260
....*....|....*....|...
gi 1718055426 384 QPITGIVNQFSKLELARVSAGRV 406
Cdd:cd18554 277 SPLRRLVNSFTTLTQSFASMDRV 299
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
152-406 |
4.05e-27 |
|
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: 111.50 E-value: 4.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 152 LICLYGGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVTVLSTF 231
Cdd:cd18557 38 LALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 232 VTSGIYMFGIFTALFLLDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTIIQAFRHQKET 311
Cdd:cd18557 118 LRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 312 MREF-EELNESHFYFQNRMLNLNSLMShnLVNVIRNLAFVCLIWHfgGASLNAAGIVSIGVLYAFVDYLNRLFQPITGIV 390
Cdd:cd18557 198 IRRYsEALDRSYRLARKKALANALFQG--ITSLLIYLSLLLVLWY--GGYLVLSGQLTVGELTSFILYTIMVASSVGGLS 273
|
250
....*....|....*.
gi 1718055426 391 NQFSKLELARVSAGRV 406
Cdd:cd18557 274 SLLADIMKALGASERV 289
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
151-406 |
4.26e-27 |
|
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: 111.77 E-value: 4.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 151 LLICLYGGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARItNDTEAIRDLYVTVLST 230
Cdd:cd18570 43 IISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISSTTIS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 231 FVTSGIYMFGIFTALFLLDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTIIQAFRHQKE 310
Cdd:cd18570 122 LFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQ 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 311 TMREFEELNeSHFYFQNRMLNLNSLMSHNLVNVIRNLAFVCLIWhfGGASLNAAGIVSIGVLYAFVDYLNRLFQPITGIV 390
Cdd:cd18570 202 FLKKIEKKF-SKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILW--IGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLI 278
|
250
....*....|....*.
gi 1718055426 391 NQFSKLELARVSAGRV 406
Cdd:cd18570 279 NLQPKIQEAKVAADRL 294
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
430-641 |
6.02e-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: 107.66 E-value: 6.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEgEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQ--ELRSHMG 507
Cdd:cd03229 1 LELKNVSKRYGQ-KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 508 IVLQDPYLFSG-TIGSNVSLddermteeeiknalrqvgaepllkklpkginepviekgsTLSSGERQLISFARALAFDPA 586
Cdd:cd03229 80 MVFQDFALFPHlTVLENIAL---------------------------------------GLSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1718055426 587 ILILDEATAHIDTETEAVIQKALDVVKQ--GRTTFVIAHRLS-TIRNADQILVLDKGE 641
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAqlGITVVLVTHDLDeAARLADRVVVLRDGK 178
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
431-653 |
8.59e-27 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 108.68 E-value: 8.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 431 EFRDVSFAYqeGE-EVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQElRSHMGI- 508
Cdd:cd03224 2 EVENLNAGY--GKsQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE-RARAGIg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 509 -VLQDPYLFSgtigsnvslddeRMTEEEikNaLRqVGAEPLLKKLPKGINEPVIE-----------KGSTLSSGERQLIS 576
Cdd:cd03224 79 yVPEGRRIFP------------ELTVEE--N-LL-LGAYARRRAKRKARLERVYElfprlkerrkqLAGTLSGGEQQMLA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 577 FARALAFDPAILILDEATA----HIDTETEAVIQKaldVVKQGRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKGNHEEL 651
Cdd:cd03224 143 IARALMSRPKLLLLDEPSEglapKIVEEIFEAIRE---LRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAEL 219
|
..
gi 1718055426 652 MA 653
Cdd:cd03224 220 LA 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
414-659 |
9.50e-27 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 114.80 E-value: 9.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 414 NTEEAGQP----AKERALGRVEFRDVSFAYQEG--------EEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYD 481
Cdd:PRK15134 258 NSEPSGDPvplpEPASPLLDVEQLQVAFPIRKGilkrtvdhNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 482 AQkGDVLIDGKSIYNMSRQEL---RSHMGIVLQDPYlfsgtiGS-NVSLDDERMTEE----------------EIKNALR 541
Cdd:PRK15134 338 SQ-GEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPN------SSlNPRLNVLQIIEEglrvhqptlsaaqreqQVIAVME 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 542 QVGAEPLLK-KLPkginepviekgSTLSSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQKALDVVKQGR--TT 618
Cdd:PRK15134 411 EVGLDPETRhRYP-----------AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHqlAY 479
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1718055426 619 FVIAHRLSTIRN-ADQILVLDKGEIVEKGNHEELMALEGQYY 659
Cdd:PRK15134 480 LFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
431-640 |
1.21e-26 |
|
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: 108.00 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 431 EFRDVSFAYQeGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMsrqelRSHMGIVL 510
Cdd:cd03235 1 EVEDLTVSYG-GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 511 Q----DP--------------YLFSGTIGSNVSLDDERMTEeeiknALRQVGAEPLLKKLpkgInepviekgSTLSSGER 572
Cdd:cd03235 75 QrrsiDRdfpisvrdvvlmglYGHKGLFRRLSKADKAKVDE-----ALERVGLSELADRQ---I--------GELSGGQQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 573 QLISFARALAFDPAILILDEATAHIDTETEAVIQKALDVVKQ-GRTTFVIAHRLSTI-RNADQILVLDKG 640
Cdd:cd03235 139 QRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRReGMTILVVTHDLGLVlEYFDRVLLLNRT 208
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
430-651 |
1.31e-26 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 111.32 E-value: 1.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGE---EVLKHISFTAQKGETVALVGHTGSGKSS---ILNLLFRfydAQKGDVLIDGKSIYNMSRQEL- 502
Cdd:COG1135 2 IELENLSKTFPTKGgpvTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLER---PTSGSVLVDGVDLTALSERELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 503 --RSHMGIVLQDPYLFSG-TIGSNVS--LDDERMTEEEIKNA----LRQVGAEPLLKKLPkginepviekgSTLSSGERQ 573
Cdd:COG1135 79 aaRRKIGMIFQHFNLLSSrTVAENVAlpLEIAGVPKAEIRKRvaelLELVGLSDKADAYP-----------SQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 574 LISFARALAFDPAILILDEATAHIDTETEAVIqkaLDVVKQ-----GRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKGN 647
Cdd:COG1135 148 RVGIARALANNPKVLLCDEATSALDPETTRSI---LDLLKDinrelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
|
....
gi 1718055426 648 HEEL 651
Cdd:COG1135 225 VLDV 228
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
430-652 |
2.24e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 108.26 E-value: 2.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEgEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQE--LRSHMG 507
Cdd:PRK09493 2 IEFKNVSKHFGP-TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 508 IVLQDPYLFSG-TIGSNVSLDDERMTEEEIKNALRQvgAEPLLKKLpkGINEPVIEKGSTLSSGERQLISFARALAFDPA 586
Cdd:PRK09493 81 MVFQQFYLFPHlTALENVMFGPLRVRGASKEEAEKQ--ARELLAKV--GLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718055426 587 ILILDEATAHIDTE-TEAVIQKALDVVKQGRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKGNHEELM 652
Cdd:PRK09493 157 LMLFDEPTSALDPElRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
430-646 |
4.90e-26 |
|
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: 106.42 E-value: 4.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGEevlKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMgiV 509
Cdd:cd03298 1 VRLDKIRFSYGEQP---MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSM--L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 510 LQDPYLFSG-TIGSNVSLDDE---RMTEEE---IKNALRQVGAEPLLKKLPKginepviekgsTLSSGERQLISFARALA 582
Cdd:cd03298 76 FQENNLFAHlTVEQNVGLGLSpglKLTAEDrqaIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 583 FDPAILILDEATAHIDTeteAVIQKALDVV-----KQGRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKG 646
Cdd:cd03298 145 RDKPVLLLDEPFAALDP---ALRAEMLDLVldlhaETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
429-634 |
5.03e-26 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 106.02 E-value: 5.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 429 RVEFRDVSFAYQEgEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIyNMSRQELRSHMGI 508
Cdd:COG4133 2 MLEAENLSCRRGE-RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI-RDAREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 509 VLQDPYLFSG-TIGSNV----SLDDERMTEEEIKNALRQVGAEPLLkklpkgiNEPViekgSTLSSGERQLISFARALAF 583
Cdd:COG4133 80 LGHADGLKPElTVRENLrfwaALYGLRADREAIDEALEAVGLAGLA-------DLPV----RQLSAGQKRRVALARLLLS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1718055426 584 DPAILILDEATAHIDTETEAVIQKAL-DVVKQGRTTFVIAHRLSTIRNADQI 634
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIaAHLARGGAVLLTTHQPLELAAARVL 200
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
430-651 |
6.48e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 112.03 E-value: 6.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVS--FAyqeGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHmG 507
Cdd:COG1129 5 LEMRGISksFG---GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAA-G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 508 IVL--QDPYLFSG-TIGSNVSLDDERMTEEEI-KNALRQvGAEPLLKKLpkGINEPVIEKGSTLSSGERQLISFARALAF 583
Cdd:COG1129 81 IAIihQELNLVPNlSVAENIFLGREPRRGGLIdWRAMRR-RARELLARL--GLDIDPDTPVGDLSVAQQQLVEIARALSR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1718055426 584 DPAILILDEATAHI-DTETEAViqkaLDVVK----QGRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKGNHEEL 651
Cdd:COG1129 158 DARVLILDEPTASLtEREVERL----FRIIRrlkaQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
446-653 |
1.02e-25 |
|
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: 106.96 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 446 LKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQEL----RSHMGIVLQDPYLFSG-TI 520
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPHrTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 521 GSNVSLD------DERMTEEEIKNALRQVGAEPLLKKLPKginepviekgsTLSSGERQLISFARALAFDPAILILDEAT 594
Cdd:cd03294 120 LENVAFGlevqgvPRAEREERAAEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1718055426 595 AHIDTETEAVIQKALD--VVKQGRTTFVIAHRLS-TIRNADQILVLDKGEIVEKGNHEELMA 653
Cdd:cd03294 189 SALDPLIRREMQDELLrlQAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
389-640 |
2.30e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 111.05 E-value: 2.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 389 IVNQFSklELARVSAG--RVFEL---LEEKNTEEAGQPAKERALG-RVEFRDVSFAYQEGEEVLKHISFTAQKGETVALV 462
Cdd:COG4178 318 FVDNYQ--SLAEWRATvdRLAGFeeaLEAADALPEAASRIETSEDgALALEDLTLRTPDGRPLLEDLSLSLKPGERLLIT 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 463 GHTGSGKSSilnlLFR----FYDAQKGDVlidgksiynmSRQELRSHMgiVL-QDPYLFSGTIGSNVS--LDDERMTEEE 535
Cdd:COG4178 396 GPSGSGKST----LLRaiagLWPYGSGRI----------ARPAGARVL--FLpQRPYLPLGTLREALLypATAEAFSDAE 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 536 IKNALRQVGAEPLLKKLpkginEPVIEKGSTLSSGERQLISFARALAFDPAILILDEATAHIDTETEA----VIQKALDv 611
Cdd:COG4178 460 LREALEAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAalyqLLREELP- 533
|
250 260 270
....*....|....*....|....*....|
gi 1718055426 612 vkqgRTTFV-IAHRLSTIRNADQILVLDKG 640
Cdd:COG4178 534 ----GTTVIsVGHRSTLAAFHDRVLELTGD 559
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
430-651 |
2.36e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 106.04 E-value: 2.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGIV 509
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 510 LQDP--YLFSGTIGSNVSLD------DERMTEEEIKNALRQVGAEPLLKKLPKginepviekgsTLSSGERQLISFARAL 581
Cdd:PRK13652 84 FQNPddQIFSPTVEQDIAFGpinlglDEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1718055426 582 AFDPAILILDEATAHIDTETEAVIQKALD--VVKQGRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKGNHEEL 651
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNdlPETYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEI 225
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
430-653 |
3.82e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 105.58 E-value: 3.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGEE--VLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMG 507
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 508 IVLQDP-YLFSG-TIGSNVS--LDDERMTEEEIKN----ALRQVGAEPLLKKLPkginepviekgSTLSSGERQLISFAR 579
Cdd:PRK13650 85 MVFQNPdNQFVGaTVEDDVAfgLENKGIPHEEMKErvneALELVGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1718055426 580 ALAFDPAILILDEATAHIDTETEAVIQKALDVVKQ--GRTTFVIAHRLSTIRNADQILVLDKGEIVEKGNHEELMA 653
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
155-406 |
8.97e-25 |
|
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: 105.34 E-value: 8.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 155 LYGGLLVFS----VFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITND--------TEAIRD 222
Cdd:cd18565 55 LLGGLTVAAflleSLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDvnqlerflDDGANS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 223 LyVTVLSTFVTSGIYMfgiftalFLLDVKLAFVCLAIVPIIWLWSVIY-RRYASYYnQKIRSINSDINAKMNESIQGMTI 301
Cdd:cd18565 135 I-IRVVVTVLGIGAIL-------FYLNWQLALVALLPVPLIIAGTYWFqRRIEPRY-RAVREAVGDLNARLENNLSGIAV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 302 IQAFRHQKetmREFEELNE-SHFYFQNRMLNLN-SLMSHNLVNVIRNLAFVCLI-----WHFGGASLNAAGIvSIGVLYA 374
Cdd:cd18565 206 IKAFTAED---FERERVADaSEEYRDANWRAIRlRAAFFPVIRLVAGAGFVATFvvggyWVLDGPPLFTGTL-TVGTLVT 281
|
250 260 270
....*....|....*....|....*....|....*
gi 1718055426 375 FVDYLNRLFQPITG---IVNQFsklELARVSAGRV 406
Cdd:cd18565 282 FLFYTQRLLWPLTRlgdLIDQY---QRAMASAKRV 313
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
430-646 |
3.01e-24 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 104.50 E-value: 3.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGE---EVLKHISFTAQKGETVALVGHTGSGKSSIL---NLLFRfydAQKGDVLIDGKSIYNMSRQELR 503
Cdd:PRK11153 2 IELKNISKVFPQGGrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIrciNLLER---PTSGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 504 S---HMGIVLQDPYLFSG-TIGSNVSLDDE--RMTEEEIKNA----LRQVGAEPLLKKLPkginepviekgSTLSSGERQ 573
Cdd:PRK11153 79 KarrQIGMIFQHFNLLSSrTVFDNVALPLElaGTPKAEIKARvtelLELVGLSDKADRYP-----------AQLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1718055426 574 LISFARALAFDPAILILDEATAHIDTETEAVIqkaLDVVKQ-----GRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKG 646
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSI---LELLKDinrelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQG 223
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
429-651 |
4.63e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 101.91 E-value: 4.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 429 RVEFRDVSFAYQEgEEVLKHISFTAQKGETVALVGHTGSGKSSIL---NLLFRFYDAQK--GDVLIDGKSIYNMSRQELR 503
Cdd:PRK14247 3 KIEIRDLKVSFGQ-VEVLDGVNLEIPDNTITALMGPSGSGKSTLLrvfNRLIELYPEARvsGEVYLDGQDIFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 504 SHMGIVLQDPYLFSG-TIGSNVSL--------DDERMTEEEIKNALRQVgaePLLKKLPKGINEPviekGSTLSSGERQL 574
Cdd:PRK14247 82 RRVQMVFQIPNPIPNlSIFENVALglklnrlvKSKKELQERVRWALEKA---QLWDEVKDRLDAP----AGKLSGGQQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718055426 575 ISFARALAFDPAILILDEATAHIDTETEAVIQKALDVVKQGRTTFVIAH-RLSTIRNADQILVLDKGEIVEKGNHEEL 651
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
429-646 |
5.06e-24 |
|
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: 99.93 E-value: 5.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 429 RVEFRDVSFAYQEG-----EEVLKHISFTAQKGETVALVGHTGSGKSSILNLL--FRFYDAQKGDVLIDGKSIYnmsRQE 501
Cdd:cd03213 3 TLSFRNLTVTVKSSpsksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLD---KRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 502 LRSHMGIVLQDPYLFsgtigsnvslddERMTEEEiknALrQVGAEplLKKlpkginepviekgstLSSGERQLISFARAL 581
Cdd:cd03213 80 FRKIIGYVPQDDILH------------PTLTVRE---TL-MFAAK--LRG---------------LSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718055426 582 AFDPAILILDEATAHIDTETEAVIQKAL-DVVKQGRTTFVIAHRLST--IRNADQILVLDKGEIVEKG 646
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLrRLADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
430-653 |
5.29e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 102.60 E-value: 5.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGEEV----LKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIY----NMSRQE 501
Cdd:PRK13641 3 IKFENVDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 502 LRSHMGIVLQDP--YLFSGTIGSNVSLDDERM--TEEEIKNAlrqvgAEPLLKKLpkGINEPVIEKGS-TLSSGERQLIS 576
Cdd:PRK13641 83 LRKKVSLVFQFPeaQLFENTVLKDVEFGPKNFgfSEDEAKEK-----ALKWLKKV--GLSEDLISKSPfELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1718055426 577 FARALAFDPAILILDEATAHIDTET-EAVIQKALDVVKQGRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKGNHEELMA 653
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFS 234
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
157-378 |
9.77e-24 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 101.82 E-value: 9.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 157 GGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVTVLSTFVTSGI 236
Cdd:cd18573 48 LGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 237 YMFGIFTALFLLDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTIIQAFRHQKETMREFE 316
Cdd:cd18573 128 SGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYA 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1718055426 317 ELNESHFYFQNRMLNLNSLMsHNLVNVIRNLAFVCLIWHfgGASLNAAGIVSIGVLYAFVDY 378
Cdd:cd18573 208 KKVDEVFDLAKKEALASGLF-FGSTGFSGNLSLLSVLYY--GGSLVASGELTVGDLTSFLMY 266
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
430-653 |
1.10e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 101.64 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEG----EEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQE---- 501
Cdd:PRK13634 3 ITFQKVEHRYQYKtpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKklkp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 502 LRSHMGIVLQDP--YLFSGTIGSNVSLDDER--MTEEEiknalrqvgAEPLLKKLPK--GINEPVIEKGS-TLSSGERQL 574
Cdd:PRK13634 83 LRKKVGIVFQFPehQLFEETVEKDICFGPMNfgVSEED---------AKQKAREMIElvGLPEELLARSPfELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 575 ISFARALAFDPAILILDEATAHID-------TETEAVIQKaldvvKQGRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKG 646
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDpkgrkemMEMFYKLHK-----EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQG 228
|
....*..
gi 1718055426 647 NHEELMA 653
Cdd:PRK13634 229 TPREIFA 235
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
430-653 |
1.40e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 101.08 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIyNMSRQ---ELRSHM 506
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKglmKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 507 GIVLQDP--YLFSGTIGSNVSLD------DERMTEEEIKNALRQVGAEPLLKKlpkginePViekgSTLSSGERQLISFA 578
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYQDVSFGavnlklPEDEVRKRVDNALKRTGIEHLKDK-------PT----HCLSFGQKKRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718055426 579 RALAFDPAILILDEATAHIDTETEAVIQKAL-DVVKQGRTTFVIA-HRLSTIR-NADQILVLDKGEIVEKGNHEELMA 653
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLvEMQKELGLTIIIAtHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
144-655 |
1.69e-23 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 105.05 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 144 PEIKGMVLLiclyggLLVFSVFFQYGQHYLLQmsanRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDL 223
Cdd:PRK10522 52 PEFLGLLLL------LMAVTLGSQLALTTLGH----HFVYRLRSEFIKRILDTHVERIEQLGSASLLASLTSDVRNITIA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 224 YVTvLSTFVTSGIYMFGIFTALFLLDVKLAFVCLA-IVPIIW----LWSVIYRRYAsyynqKIRSINSDINAKMNESIQG 298
Cdd:PRK10522 122 FVR-LPELVQGIILTLGSAAYLAWLSPKMLLVTAIwMAVTIWggfvLVARVYKHMA-----TLRETEDKLYNDYQTVLEG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 299 MTIIQAFRHQKETMREFEELNESHFYFQNRML-NLNSLMSHNLVNVIRnLAFVCLIWH----FGGASLNAAGIVSIGVLY 373
Cdd:PRK10522 196 RKELTLNRERAEYVFENEYEPDAQEYRHHIIRaDTFHLSAVNWSNIMM-LGAIGLVFYmansLGWADTNVAATYSLTLLF 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 374 afvdylnrLFQPITGIVNQFSKLELARVSAGRVFELLEEKNTEEAGQPAKERALGRVEFRDVSFAYQEGEEVLKHISFTA 453
Cdd:PRK10522 275 --------LRTPLLSAVGALPTLLSAQVAFNKLNKLALAPYKAEFPRPQAFPDWQTLELRNVTFAYQDNGFSVGPINLTI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 454 QKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGIVLQDPYLFSGTIGSNvslddermtE 533
Cdd:PRK10522 347 KRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLLGPE---------G 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 534 EEIKNALrqvgAEPLLKKLpkGINEPVIEKGST-----LSSGERQLISFARALAFDPAILILDEATAHIDTETEAVI-QK 607
Cdd:PRK10522 418 KPANPAL----VEKWLERL--KMAHKLELEDGRisnlkLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFyQV 491
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1718055426 608 ALDVVKQ-GRTTFVIAHRLSTIRNADQILVLDKGEIVE-KGNHEELMALE 655
Cdd:PRK10522 492 LLPLLQEmGKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERDAASRD 541
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
150-378 |
2.55e-23 |
|
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: 100.64 E-value: 2.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 150 VLLICLYGGLLVFSVFFQYgqhYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVTVLS 229
Cdd:cd18575 39 FLLLLAVALVLALASALRF---YLVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 230 TFVTSGIYMFGIFTALFLLDVKLAFVCLAIVPIIWLWSVIY----RRYASYYNQKIrsinSDINAKMNESIQGMTIIQAF 305
Cdd:cd18575 116 IALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFgrrvRRLSRASQDRL----ADLSAFAEETLSAIKTVQAF 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1718055426 306 RHQKETMREFEELNESHFYFQNRMLNLNSLMShNLVNVIRNLAFVCLIWhFGGASLnAAGIVSIGVLYAFVDY 378
Cdd:cd18575 192 TREDAERQRFATAVEAAFAAALRRIRARALLT-ALVIFLVFGAIVFVLW-LGAHDV-LAGRMSAGELSQFVFY 261
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
445-653 |
3.28e-23 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 99.34 E-value: 3.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 445 VLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQElRSHMGIV--LQDPYLFSG-TIG 521
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHR-IARLGIArtFQNPRLFPElTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 522 SNV---------------------SLDDERMTEEEIKNALRQVGAEPLLkklpkgiNEPViekgSTLSSGERQLISFARA 580
Cdd:COG0411 98 ENVlvaaharlgrgllaallrlprARREEREARERAEELLERVGLADRA-------DEPA----GNLSYGQQRRLEIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718055426 581 LAFDPAILILDEATA-HIDTETE---AVIQKALDvvKQGRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKGNHEELMA 653
Cdd:COG0411 167 LATEPKLLLLDEPAAgLNPEETEelaELIRRLRD--ERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAEVRA 242
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
430-651 |
3.34e-23 |
|
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: 98.85 E-value: 3.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYqEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQelRSHMGIV 509
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 510 LQDPYLFSG-TIGSNVS--LDDERMTEEEIK----NALRQVGAEPLLKKLPkginepviekgSTLSSGERQLISFARALA 582
Cdd:cd03300 78 FQNYALFPHlTVFENIAfgLRLKKLPKAEIKervaEALDLVQLEGYANRKP-----------SQLSGGQQQRVAIARALV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1718055426 583 FDPAILILDEATAHIDTETEAVIQKALDVV-KQGRTTFV-IAHRLS-TIRNADQILVLDKGEIVEKGNHEEL 651
Cdd:cd03300 147 NEPKVLLLDEPLGALDLKLRKDMQLELKRLqKELGITFVfVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
437-651 |
3.52e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 99.35 E-value: 3.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 437 FAYQEGEEVLKHISFTAQKGETVALVGHTGSGKSS---ILNLLFRFYDAQ---KGDVLIDGKSIYNMSRQELRSHMGIVL 510
Cdd:PRK14246 17 YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTllkVLNRLIEIYDSKikvDGKVLYFGKDIFQIDAIKLRKEVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 511 QDPYLFSG-TIGSNVS-------LDDERMTEEEIKNALRQVGaepLLKKLPKGINEPviekGSTLSSGERQLISFARALA 582
Cdd:PRK14246 97 QQPNPFPHlSIYDNIAyplkshgIKEKREIKKIVEECLRKVG---LWKEVYDRLNSP----ASQLSGGQQQRLTIARALA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 583 FDPAILILDEATAHIDTETEAVIQKALDVVKQGRTTFVIAHRLSTI-RNADQILVLDKGEIVEKGNHEEL 651
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
428-651 |
7.17e-23 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 100.53 E-value: 7.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 428 GRVEFRDVSFAYQeGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQElRsHMG 507
Cdd:COG3839 2 ASLELENVSKSYG-GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-R-NIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 508 IVLQDPYLF-SGTIGSNVS--LDDERMTEEEIK----NALRQVGAEPLLKKLPKginepviekgsTLSSGERQLISFARA 580
Cdd:COG3839 79 MVFQSYALYpHMTVYENIAfpLKLRKVPKAEIDrrvrEAAELLGLEDLLDRKPK-----------QLSGGQRQRVALGRA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1718055426 581 LAFDPAILILDEATAHID----TETEAVIQKaldVVKQGRTTFVIA-HRLS---TIrnADQILVLDKGEIVEKGNHEEL 651
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDaklrVEMRAEIKR---LHRRLGTTTIYVtHDQVeamTL--ADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
445-643 |
8.53e-23 |
|
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: 97.19 E-value: 8.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 445 VLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIyNMSRQELRSHMGIVLQDPYLFSGTIGS-- 522
Cdd:cd03263 17 AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQSLGYCPQFDALFDELTVReh 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 523 --------NVSLDDERmteEEIKNALRQVGAEPLLKKLPKginepviekgsTLSSGERQLISFARALAFDPAILILDEAT 594
Cdd:cd03263 96 lrfyarlkGLPKSEIK---EEVELLLRVLGLTDKANKRAR-----------TLSGGMKRKLSLAIALIGGPSVLLLDEPT 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1718055426 595 AHIDTETEAVIQKALDVVKQGRTTFVIAHRLSTIRN-ADQILVLDKGEIV 643
Cdd:cd03263 162 SGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
430-646 |
9.32e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 98.66 E-value: 9.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGE----EVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSR----QE 501
Cdd:PRK13649 3 INLQNVSYTYQAGTpfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 502 LRSHMGIVLQDP--YLFSGTIGSNVSLDDER--MTEEEIKNALRQvgaepllKKLPKGINEPVIEKGS-TLSSGERQLIS 576
Cdd:PRK13649 83 IRKKVGLVFQFPesQLFEETVLKDVAFGPQNfgVSQEEAEALARE-------KLALVGISESLFEKNPfELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1718055426 577 FARALAFDPAILILDEATAHIDTETEaviQKALDVVKQ----GRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKG 646
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGR---KELMTLFKKlhqsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSG 227
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
146-406 |
9.63e-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: 98.77 E-value: 9.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 146 IKGMVLLICLYGgllVFSvFFQYGqhyLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYV 225
Cdd:cd18572 39 VLLLLLLSVLSG---LFS-GLRGG---CFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 226 TVLSTFVTSGIYMFGIFTALFLLDVKLAFVCLAIVPIIWLwsvIYRRYASYY---NQKIRSINSDINAKMNESIQGMTII 302
Cdd:cd18572 112 TNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIAL---ITKVYGRYYrklSKEIQDALAEANQVAEEALSNIRTV 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 303 QAFRHQKETMREFEELNEsHFYFQNRMLNLNSLMSHNLVNVIRNLAFVCLIWHfgGASLNAAGIVSIGVLYAFVDYLNRL 382
Cdd:cd18572 189 RSFATEEREARRYERALD-KALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFY--GGHLVLSGRMSAGQLVTFMLYQQQL 265
|
250 260
....*....|....*....|....
gi 1718055426 383 FQPITGIVNQFSKLELARVSAGRV 406
Cdd:cd18572 266 GEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
430-651 |
1.56e-22 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 99.45 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYqEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIY-NMSRQElRsHMGI 508
Cdd:COG1118 3 IEVRNISKRF-GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPRE-R-RVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 509 VLQDPYLFSG-TIGSNVS--LDDERMTEEEIK----NALRQVGAEPLLKKLPkginepviekgSTLSSGERQLISFARAL 581
Cdd:COG1118 80 VFQHYALFPHmTVAENIAfgLRVRPPSKAEIRarveELLELVQLEGLADRYP-----------SQLSGGQRQRVALARAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 582 AFDPAILILDEATAHIDT----ETEAVIQKALDvvKQGRTT-FVI-----AHRLstirnADQILVLDKGEIVEKGNHEEL 651
Cdd:COG1118 149 AVEPEVLLLDEPFGALDAkvrkELRRWLRRLHD--ELGGTTvFVThdqeeALEL-----ADRVVVMNQGRIEQVGTPDEV 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
435-653 |
1.59e-22 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 101.68 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 435 VSFAYQEGE-EVLKHISFTAQKGETVALVGHTGSGKS----SILNLLFRFYDAQKGDVLIDGKSIYNMSRQELR----SH 505
Cdd:COG4172 14 VAFGQGGGTvEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRrirgNR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 506 MGIVLQDPY-----LFsgTIGSNVSlddE------RMTEEEIKN----ALRQVG---AEPLLKKLPkginepviekgSTL 567
Cdd:COG4172 94 IAMIFQEPMtslnpLH--TIGKQIA---EvlrlhrGLSGAAARAraleLLERVGipdPERRLDAYP-----------HQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 568 SSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQKALDVVKQGRTTFV--IAHRLSTIRN-ADQILVLDKGEIVE 644
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALllITHDLGVVRRfADRVAVMRQGEIVE 237
|
....*....
gi 1718055426 645 KGNHEELMA 653
Cdd:COG4172 238 QGPTAELFA 246
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
431-653 |
1.69e-22 |
|
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: 96.59 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 431 EFRDVSFAYqeGE-EVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQElRSHMGI- 508
Cdd:COG0410 5 EVENLHAGY--GGiHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHR-IARLGIg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 509 -VLQDPYLFSgtigsnvslddeRMT-EEEIKNALRQVGAEPLLKKLPKGINE--PVIE-----KGSTLSSGERQLISFAR 579
Cdd:COG0410 82 yVPEGRRIFP------------SLTvEENLLLGAYARRDRAEVRADLERVYElfPRLKerrrqRAGTLSGGEQQMLAIGR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 580 ALAFDPAILILDEATAHIdteteA--VIQKALDVVK----QGRTTFVI---AHRLSTIrnADQILVLDKGEIVEKGNHEE 650
Cdd:COG0410 150 ALMSRPKLLLLDEPSLGL-----AplIVEEIFEIIRrlnrEGVTILLVeqnARFALEI--ADRAYVLERGRIVLEGTAAE 222
|
...
gi 1718055426 651 LMA 653
Cdd:COG0410 223 LLA 225
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
430-643 |
1.74e-22 |
|
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: 94.42 E-value: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYqEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSH-MGI 508
Cdd:cd03216 1 LELRGITKRF-GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAgIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 509 VLQdpylfsgtigsnvslddermteeeiknalrqvgaepllkklpkginepviekgstLSSGERQLISFARALAFDPAIL 588
Cdd:cd03216 80 VYQ-------------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1718055426 589 ILDEATAHI-DTETEAVIQKALDVVKQGRTTFVIAHRLSTIRN-ADQILVLDKGEIV 643
Cdd:cd03216 105 ILDEPTAALtPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
433-652 |
2.00e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 97.15 E-value: 2.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 433 RDVSFAYQeGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGIVLQD 512
Cdd:PRK13548 6 RNLSVRLG-GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 513 PYL---FS--------GTIGSNVSLDDERMTEEeiknALRQVGAEPLLKKL-PkginepviekgsTLSSGERQLISFARA 580
Cdd:PRK13548 85 SSLsfpFTveevvamgRAPHGLSRAEDDALVAA----ALAQVDLAHLAGRDyP------------QLSGGEQQRVQLARV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 581 LA------FDPAILILDEATAHIDteteavIQKALDVV--------KQGRTTFVIAHRLS-TIRNADQILVLDKGEIVEK 645
Cdd:PRK13548 149 LAqlwepdGPPRWLLLDEPTSALD------LAHQHHVLrlarqlahERGLAVIVVLHDLNlAARYADRIVLLHQGRLVAD 222
|
....*..
gi 1718055426 646 GNHEELM 652
Cdd:PRK13548 223 GTPAEVL 229
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
445-654 |
2.26e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 96.69 E-value: 2.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 445 VLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGK--------SIYNMS---RQELRshmgivlqdp 513
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsallelgAGFHPEltgRENIY---------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 514 ylFSGTI-GsnvsldderMTEEEIKNALRQVG--AEpllkkLPKGINEPViekgSTLSSGERQLISFARALAFDPAILIL 590
Cdd:COG1134 111 --LNGRLlG---------LSRKEIDEKFDEIVefAE-----LGDFIDQPV----KTYSSGMRARLAFAVATAVDPDILLV 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1718055426 591 DEATAHIDtetEAVIQKALD----VVKQGRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKGNHEELMAL 654
Cdd:COG1134 171 DEVLAVGD---AAFQKKCLArireLRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
430-651 |
2.91e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 97.08 E-value: 2.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGEE-----VLKHISFTAQKGETVALVGHTGSGKSSI---LNLLFRfydAQKGDVLIDGKSIYNMSRQ- 500
Cdd:PRK13633 5 IKCKNVSYKYESNEEsteklALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALLI---PSEGKVYVDGLDTSDEENLw 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 501 ELRSHMGIVLQDP--YLFSGTIGSNVSLDDERM--TEEEIK----NALRQVGAEPLLKKLPKginepviekgsTLSSGER 572
Cdd:PRK13633 82 DIRNKAGMVFQNPdnQIVATIVEEDVAFGPENLgiPPEEIRervdESLKKVGMYEYRRHAPH-----------LLSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 573 QLISFARALAFDPAILILDEATAHID-TETEAVIQKALDVVKQ-GRTTFVIAHRLSTIRNADQILVLDKGEIVEKGNHEE 650
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDpSGRREVVNTIKELNKKyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKE 230
|
.
gi 1718055426 651 L 651
Cdd:PRK13633 231 I 231
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
430-650 |
3.96e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 97.04 E-value: 3.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEG----EEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIY--NMSRQELR 503
Cdd:PRK13637 3 IKIENLTHIYMEGtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 504 SHMGIVLQDP--YLFSGTIGSNVSLDDERM--TEEEIKN----ALRQVG--AEPLLKKLPkginepviekgSTLSSGERQ 573
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDIAFGPINLglSEEEIENrvkrAMNIVGldYEDYKDKSP-----------FELSGGQKR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 574 LISFARALAFDPAILILDEATAHIDTET-EAVIQKALDVVKQ-GRTTFVIAHRLSTI-RNADQILVLDKGEIVEKGNHEE 650
Cdd:PRK13637 152 RVAIAGVVAMEPKILILDEPTAGLDPKGrDEILNKIKELHKEyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE 231
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
430-653 |
4.17e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 96.77 E-value: 4.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEG----EEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSR----QE 501
Cdd:PRK13646 3 IRFDNVSYTYQKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyiRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 502 LRSHMGIVLQDP--YLFSGTIGSNVSLDDE--RMTEEEIKNAlrqvgAEPLLKKLpkGINEPVIEKGS-TLSSGERQLIS 576
Cdd:PRK13646 83 VRKRIGMVFQFPesQLFEDTVEREIIFGPKnfKMNLDEVKNY-----AHRLLMDL--GFSRDVMSQSPfQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 577 FARALAFDPAILILDEATAHIDTETEAVIQKALDV--VKQGRTTFVIAHRLSTI-RNADQILVLDKGEIVEKGNHEELMA 653
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
157-406 |
1.02e-21 |
|
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: 96.01 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 157 GGLLVFSV---FFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLyVTVLSTFVT 233
Cdd:cd18543 43 LLLLALGVaeaVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRF-LAFGPFLLG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 234 SGIYMFGIFTALFLLDVKLAFVCLAIVPIIWLWSVIYRRyaSYY--NQKIRSINSDINAKMNESIQGMTIIQAF-RHQKE 310
Cdd:cd18543 122 NLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRR--RYFpaSRRAQDQAGDLATVVEESVTGIRVVKAFgRERRE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 311 TmREFEELNESHFYFQNRMLNLNSLMShNLVNVIRNLAFVCLIWhfGGASLNAAGIVSIGVLYAFVDYLNRLFQPITGIV 390
Cdd:cd18543 200 L-DRFEAAARRLRATRLRAARLRARFW-PLLEALPELGLAAVLA--LGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLG 275
|
250
....*....|....*.
gi 1718055426 391 NQFSKLELARVSAGRV 406
Cdd:cd18543 276 WLLAMAQRARAAAERV 291
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
439-626 |
1.79e-21 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 93.73 E-value: 1.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 439 YQEGE---EVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMS---RQELRSH-MGIVLQ 511
Cdd:PRK11629 15 YQEGSvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaaKAELRNQkLGFIYQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 512 DPYLfsgtigsnvsLDDermteeeiKNALRQVgAEPLL--KKLPKGINEPVIE-------------KGSTLSSGERQLIS 576
Cdd:PRK11629 95 FHHL----------LPD--------FTALENV-AMPLLigKKKPAEINSRALEmlaavglehranhRPSELSGGERQRVA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1718055426 577 FARALAFDPAILILDEATAHIDTETEAVIQKALDV--VKQGRTTFVIAHRLS 626
Cdd:PRK11629 156 IARALVNNPRLVLADEPTGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQ 207
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
152-406 |
2.44e-21 |
|
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: 94.85 E-value: 2.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 152 LICLYGGLLVFsvFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRD-------LY 224
Cdd:cd18577 51 LYFVYLGIGSF--VLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDgigeklgLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 225 VTVLSTFVTsgiymfGIFTAlFLLDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTIIQA 304
Cdd:cd18577 129 IQSLSTFIA------GFIIA-FIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 305 FRHQKETMREFEELNESHFYFQNRMLNLNSLMShNLVNVIRNLAFVCLIWhfGGASLNAAGIVSIG----VLYAFVDyln 380
Cdd:cd18577 202 FGGEEKEIKRYSKALEKARKAGIKKGLVSGLGL-GLLFFIIFAMYALAFW--YGSRLVRDGEISPGdvltVFFAVLI--- 275
|
250 260
....*....|....*....|....*.
gi 1718055426 381 rLFQPITGIVNQFSKLELARVSAGRV 406
Cdd:cd18577 276 -GAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
442-653 |
3.34e-21 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 93.28 E-value: 3.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 442 GEEVLKHISFTAQKGETVALVGHTGSGKSSIL---NLLFRFYDA--QKGDVLIDG-KSIYNMSRQ--ELRSHMGIVLQDP 513
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLrciNLLEQPEAGtiRVGDITIDTaRSLSQQKGLirQLRQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 514 YLFSG-TIGSNVsLDDERMTEEEIKNALRQVGAEpLLKKLPKGINEPVIEKgsTLSSGERQLISFARALAFDPAILILDE 592
Cdd:PRK11264 95 NLFPHrTVLENI-IEGPVIVKGEPKEEATARARE-LLAKVGLAGKETSYPR--RLSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1718055426 593 ATAHIDTEteaVIQKALDVVKQ----GRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKGNHEELMA 653
Cdd:PRK11264 171 PTSALDPE---LVGEVLNTIRQlaqeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
429-651 |
3.71e-21 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 93.56 E-value: 3.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 429 RVEFRDVSFAYQEgEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQ-----KGDVLIDGKSIY--NMSRQE 501
Cdd:COG1117 11 KIEVRNLNVYYGD-KQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIpgarvEGEILLDGEDIYdpDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 502 LRSHMGIVLQDPYLFSGTIGSNVS-------LDDERMTEEEIKNALRQVGaepL---LK-KLpkgiNEPviekGSTLSSG 570
Cdd:COG1117 90 LRRRVGMVFQKPNPFPKSIYDNVAyglrlhgIKSKSELDEIVEESLRKAA---LwdeVKdRL----KKS----ALGLSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 571 ERQLISFARALAFDPAILILDEATAHIDTETEAVIQKALDVVKQgRTTFVI-------AHRLStirnaDQILVLDKGEIV 643
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK-DYTIVIvthnmqqAARVS-----DYTAFFYLGELV 232
|
....*...
gi 1718055426 644 EKGNHEEL 651
Cdd:COG1117 233 EFGPTEQI 240
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
430-653 |
4.36e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 93.62 E-value: 4.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGEEV--LKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMG 507
Cdd:PRK13642 5 LEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 508 IVLQDP--YLFSGTIGSNVSLDDERM---TEEEIKNALRQVGAEPLLKKLPKginEPviekgSTLSSGERQLISFARALA 582
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQgipREEMIKRVDEALLAVNMLDFKTR---EP-----ARLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1718055426 583 FDPAILILDEATAHIDTETEAVIQKALDVVKQGR--TTFVIAHRLSTIRNADQILVLDKGEIVEKGNHEELMA 653
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
430-651 |
6.54e-21 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 92.40 E-value: 6.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYqEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQElrSHMGIV 509
Cdd:cd03296 3 IEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 510 LQDPYLFSG-TIGSNVSLD------DERMTEEEIK----NALRQVGAEPLLKKLPkginepviekgSTLSSGERQLISFA 578
Cdd:cd03296 80 FQHYALFRHmTVFDNVAFGlrvkprSERPPEAEIRakvhELLKLVQLDWLADRYP-----------AQLSGGQRQRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1718055426 579 RALAFDPAILILDEATAHIDTETEAVIQKALDVV--KQGRTT-FVIAHRLSTIRNADQILVLDKGEIVEKGNHEEL 651
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLhdELHVTTvFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
445-646 |
6.86e-21 |
|
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: 91.83 E-value: 6.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 445 VLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGK-------------------------SIYNMSR 499
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvssllglgggfnpeltgreniylngRLLGLSR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 500 QELRSHMGIVLQdpylFSGtigsnvslddermteeeiknalrqvgaepllkkLPKGINEPViekgSTLSSGERQLISFAR 579
Cdd:cd03220 117 KEIDEKIDEIIE----FSE---------------------------------LGDFIDLPV----KTYSSGMKARLAFAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1718055426 580 ALAFDPAILILDEATAHIDtetEAVIQKALDV----VKQGRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKG 646
Cdd:cd03220 156 ATALEPDILLIDEVLAVGD---AAFQEKCQRRlrelLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
445-651 |
1.16e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 93.38 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 445 VLKHISFTAQKGETVALVGHTGSGKSSILN-----LLFRFYDAQKGDVLIDGK------SIYNMSRQ-----ELRSHMGI 508
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVGDIYIGDKknnhelITNPYSKKiknfkELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 509 VLQDP--YLFSGTIGSNVSLDDERMTEEeiKNALRQVGAEPLLKKlpkGINEPVIEKGS-TLSSGERQLISFARALAFDP 585
Cdd:PRK13631 121 VFQFPeyQLFKDTIEKDIMFGPVALGVK--KSEAKKLAKFYLNKM---GLDDSYLERSPfGLSGGQKRRVAIAGILAIQP 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718055426 586 AILILDEATAHIDTETEA-VIQKALDVVKQGRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKGNHEEL 651
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEI 263
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
433-644 |
1.53e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 92.06 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 433 RDVSFAYQEG--------EEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQE--- 501
Cdd:PRK10419 7 SGLSHHYAHGglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrka 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 502 LRSHMGIVLQDPylFSG-----TIGSNV--------SLDDERmTEEEIKNALRQVGAEP-LLKKLPkginepviekgSTL 567
Cdd:PRK10419 87 FRRDIQMVFQDS--ISAvnprkTVREIIreplrhllSLDKAE-RLARASEMLRAVDLDDsVLDKRP-----------PQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 568 SSGERQLISFARALAFDPAILILDEATAHIDTETEA-VIQKALDVVKQGRTTFV-IAHRLSTI-RNADQILVLDKGEIVE 644
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAgVIRLLKKLQQQFGTACLfITHDLRLVeRFCQRVMVMDNGQIVE 232
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
430-653 |
2.47e-20 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 91.39 E-value: 2.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVS--FAYQEG------EEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSI----YNM 497
Cdd:PRK15112 5 LEVRNLSktFRYRTGwfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 498 SRQELRshmgIVLQDP-----------YLFSGTIGSNVSLDDERmTEEEIKNALRQVGAEPllkklpkginEPVIEKGST 566
Cdd:PRK15112 85 RSQRIR----MIFQDPstslnprqrisQILDFPLRLNTDLEPEQ-REKQIIETLRQVGLLP----------DHASYYPHM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 567 LSSGERQLISFARALAFDPAILILDEATAHIDTETEA-VIQKALDVV-KQGRTTFVIAHRLSTIRN-ADQILVLDKGEIV 643
Cdd:PRK15112 150 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSqLINLMLELQeKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVV 229
|
250
....*....|
gi 1718055426 644 EKGNHEELMA 653
Cdd:PRK15112 230 ERGSTADVLA 239
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
430-651 |
2.70e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 94.73 E-value: 2.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQeGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSrqELRSH-MGI 508
Cdd:PRK15439 12 LCARSISKQYS-GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT--PAKAHqLGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 509 VL--QDPYLFSG-TIGSNVSLddeRMTeeeiKNALRQVGAEPLLKKLPKGINEPVieKGSTLSSGERQLISFARALAFDP 585
Cdd:PRK15439 89 YLvpQEPLLFPNlSVKENILF---GLP----KRQASMQKMKQLLAALGCQLDLDS--SAGSLEVADRQIVEILRGLMRDS 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718055426 586 AILILDEATAHID-TETEAVIQKALDVVKQGRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKGNHEEL 651
Cdd:PRK15439 160 RILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
432-646 |
2.80e-20 |
|
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: 89.73 E-value: 2.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 432 FRDVSFAYQegeeVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIyNMSRQELRSHMGIVLQ 511
Cdd:cd03266 11 FRDVKKTVQ----AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-VKEPAEARRRLGFVSD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 512 DPYLFsgtigsnvslddERMTEEEIK------NALRQVGAEPLLKKLPK--GINEPVIEKGSTLSSGERQLISFARALAF 583
Cdd:cd03266 86 STGLY------------DRLTARENLeyfaglYGLKGDELTARLEELADrlGMEELLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718055426 584 DPAILILDEATAHIDTETEAVIqkaLDVVKQ----GRTTFVIAHRLSTI-RNADQILVLDKGEIVEKG 646
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRAL---REFIRQlralGKCILFSTHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
379-658 |
2.92e-20 |
|
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: 96.17 E-value: 2.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 379 LNRLFQPITGIVNqfSKLELARVSAGRVFELLEEKNTEEagQPAKERALGRVEFRDVSFAYQEGEE-VLKHISFTAQKGE 457
Cdd:TIGR00957 590 LNILPMVISSIVQ--ASVSLKRLRIFLSHEELEPDSIER--RTIKPGEGNSITVHNATFTWARDLPpTLNGITFSIPEGA 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 458 TVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYnmsrqelrshmgiVLQDPYLFSGTIGSNVsLDDERMTEEEIK 537
Cdd:TIGR00957 666 LVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAY-------------VPQQAWIQNDSLRENI-LFGKALNEKYYQ 731
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 538 NALRQVGAEPLLKKLPKGINEPVIEKGSTLSSGERQLISFARALAFDPAILILDEATAHIDTET-----EAVIqkALDVV 612
Cdd:TIGR00957 732 QVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVgkhifEHVI--GPEGV 809
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1718055426 613 KQGRTTFVIAHRLSTIRNADQILVLDKGEIVEKGNHEELMALEGQY 658
Cdd:TIGR00957 810 LKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
155-651 |
4.53e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 95.43 E-value: 4.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 155 LYGGLLVFSVFF------QYGQHYLlqmsanRIIQKMRQDVFSHIQRMPIRYFD----NLPAGKVVARITNDTEAIRDLY 224
Cdd:PLN03232 342 VYAFLIFFGVTFgvlcesQYFQNVG------RVGFRLRSTLVAAIFHKSLRLTHearkNFASGKVTNMITTDANALQQIA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 225 VTVlstfvtSGIYM--FGIFTALFLLDVKLA----FVCLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAkMNESIQG 298
Cdd:PLN03232 416 EQL------HGLWSapFRIIVSMVLLYQQLGvaslFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGI-INEILAS 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 299 MTIIQAFRHQKETMREFEEL-NESHFYFQNRML--NLNSLMSHNLVNVIRNLAFVCLIWhFGGASLNAAGIVSIGvLYAF 375
Cdd:PLN03232 489 MDTVKCYAWEKSFESRIQGIrNEELSWFRKAQLlsAFNSFILNSIPVVVTLVSFGVFVL-LGGDLTPARAFTSLS-LFAV 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 376 VDYlnrlfqPITGIVNQFSKLELARVSAGRVFELLEEKNTEEAGQPAKERALGRVEFRDVSFAYQEGEE--VLKHISFTA 453
Cdd:PLN03232 567 LRS------PLNMLPNLLSQVVNANVSLQRIEELLLSEERILAQNPPLQPGAPAISIKNGYFSWDSKTSkpTLSDINLEI 640
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 454 QKGETVALVGHTGSGKSSILN-LLFRFYDAQKGDVLIDGKSIYnmsrqelrshmgiVLQDPYLFSGTIGSNVsLDDERMT 532
Cdd:PLN03232 641 PVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGSVAY-------------VPQVSWIFNATVRENI-LFGSDFE 706
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 533 EEEIKNALRQVGAEPLLKKLPKGINEPVIEKGSTLSSGERQLISFARALAFDPAILILDEATAHIDTE-TEAVIQKALDV 611
Cdd:PLN03232 707 SERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKD 786
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1718055426 612 VKQGRTTFVIAHRLSTIRNADQILVLDKGEIVEKGNHEEL 651
Cdd:PLN03232 787 ELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
430-664 |
5.13e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 90.95 E-value: 5.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQE----GEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQE---- 501
Cdd:PRK13643 2 IKFEKVNYTYQPnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 502 LRSHMGIVLQDP--YLFSGTIGSNVSLDDER--MTEEEIKnalrQVGAEPLLKklpKGINEPVIEKGS-TLSSGERQLIS 576
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQNfgIPKEKAE----KIAAEKLEM---VGLADEFWEKSPfELSGGQMRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 577 FARALAFDPAILILDEATAHIDTETEAVIQKALDVVKQ-GRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKGNHEELMAl 654
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQ- 233
|
250
....*....|
gi 1718055426 655 EGQYYQMYEL 664
Cdd:PRK13643 234 EVDFLKAHEL 243
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
394-655 |
6.74e-20 |
|
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: 94.98 E-value: 6.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 394 SKLELARVSA------GRVFELLEEKNTEEaGQPAKERALGrveFRDVSFayqEGEEVLKHISFTAQKGETVALVGHTGS 467
Cdd:TIGR01271 391 TEVEMVNVTAswdegiGELFEKIKQNNKAR-KQPNGDDGLF---FSNFSL---YVTPVLKNISFKLEKGQLLAVAGSTGS 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 468 GKSSILNLLFRFYDAQKGDVLIDGKSIYNMsrqelrshmgivlQDPYLFSGTIGSN----VSLDDERMTeeeikNALRQV 543
Cdd:TIGR01271 464 GKSSLLMMIMGELEPSEGKIKHSGRISFSP-------------QTSWIMPGTIKDNiifgLSYDEYRYT-----SVIKAC 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 544 GAEPLLKKLPKGINEPVIEKGSTLSSGERQLISFARALAFDPAILILDEATAHIDTETEAVI-QKALDVVKQGRTTFVIA 622
Cdd:TIGR01271 526 QLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIfESCLCKLMSNKTRILVT 605
|
250 260 270
....*....|....*....|....*....|...
gi 1718055426 623 HRLSTIRNADQILVLDKGEIVEKGNHEELMALE 655
Cdd:TIGR01271 606 SKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
446-652 |
1.26e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 91.63 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 446 LKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRS----HMGIVLQDPYLFSG-TI 520
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 521 GSNVSLDDE------RMTEEEIKNALRQVGAEPLLKKLPkginepviekgSTLSSGERQLISFARALAFDPAILILDEAT 594
Cdd:PRK10070 124 LDNTAFGMElaginaEERREKALDALRQVGLENYAHSYP-----------DELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1718055426 595 AHIDTETEAVIQKALDVV--KQGRTTFVIAHRL-STIRNADQILVLDKGEIVEKGNHEELM 652
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLqaKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
442-653 |
1.34e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 89.38 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 442 GEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDA-----QKGDVLIDGKSIYNMSR-QELRSHMGIVLQDPYL 515
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRDvLEFRRRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 516 FSGTIGSNVsLDDERMTEEEIKNALRQVGAEPLLK-KLPKGINEPVIEKGSTLSSGERQLISFARALAFDPAILILDEAT 594
Cdd:PRK14271 113 FPMSIMDNV-LAGVRAHKLVPRKEFRGVAQARLTEvGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 595 AHIDTETEAVIQKALDVVKQGRTTFVIAHRLS-TIRNADQILVLDKGEIVEKGNHEELMA 653
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
147-406 |
1.71e-19 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 89.48 E-value: 1.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 147 KGMVLLICLYGGLLVFSVF---FQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARItNDTEAIRDl 223
Cdd:cd18588 36 RSLSTLDVLAIGLLVVALFeavLSGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFESRQVGDTVARV-RELESIRQ- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 224 YVTvlSTFVTS---GIYMFGIFTALFLLDVKLAFVCLAIVP---IIWLWSV-IYRRYAsyyNQKIRSiNSDINAKMNESI 296
Cdd:cd18588 114 FLT--GSALTLvldLVFSVVFLAVMFYYSPTLTLIVLASLPlyaLLSLLVTpILRRRL---EEKFQR-GAENQSFLVETV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 297 QGMTIIQAFRHQKETMREFEEL--NESHFYFQNRMLnlnSLMSHNLVNVIRNLAFVCLIWHfgGASLNAAGIVSIGVLYA 374
Cdd:cd18588 188 TGIETVKSLAVEPQFQRRWEELlaRYVKASFKTANL---SNLASQIVQLIQKLTTLAILWF--GAYLVMDGELTIGQLIA 262
|
250 260 270
....*....|....*....|....*....|..
gi 1718055426 375 FVDYLNRLFQPITGIVNQFSKLELARVSAGRV 406
Cdd:cd18588 263 FNMLAGQVSQPVLRLVQLWQDFQQAKVSVERL 294
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
445-643 |
1.73e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 88.60 E-value: 1.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 445 VLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGIVLQDPYLfsGTIGSnv 524
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDPMM--GTAPS-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 525 sldderMTEEE-----------------IKNALRQVGAEpLLKKLPKG----INEPViekgSTLSSGERQLISFARALAF 583
Cdd:COG1101 97 ------MTIEEnlalayrrgkrrglrrgLTKKRRELFRE-LLATLGLGlenrLDTKV----GLLSGGQRQALSLLMATLT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1718055426 584 DPAILILDEATAHIDTET-EAVIQKALDVVKQGR-TTFVIAHRLS-TIRNADQILVLDKGEIV 643
Cdd:COG1101 166 KPKLLLLDEHTAALDPKTaALVLELTEKIVEENNlTTLMVTHNMEqALDYGNRLIMMHEGRII 228
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
430-639 |
1.75e-19 |
|
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: 86.05 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGksiynmsrqelRSHMGIV 509
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 510 LQDPYLFSGTigsnvslddermteeeiknaLRQVGAEPLlkklpkginepviekGSTLSSGERQLISFARALAFDPAILI 589
Cdd:cd03223 70 PQRPYLPLGT--------------------LREQLIYPW---------------DDVLSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1718055426 590 LDEATAHIDTETEAviqKALDVVKQGRTTFV-IAHRLSTIRNADQILVLDK 639
Cdd:cd03223 115 LDEATSALDEESED---RLYQLLKELGITVIsVGHRPSLWKFHDRVLDLDG 162
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
449-653 |
2.63e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 89.64 E-value: 2.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 449 ISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQE---LRSHMGIVLQDPYlfsG------T 519
Cdd:PRK11308 34 VSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqklLRQKIQIVFQNPY---GslnprkK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 520 IGS--------NVSLD-DERmtEEEIKNALRQVGAEP-LLKKLPKginepviekgsTLSSGERQLISFARALAFDPAILI 589
Cdd:PRK11308 111 VGQileeplliNTSLSaAER--REKALAMMAKVGLRPeHYDRYPH-----------MFSGGQRQRIAIARALMLDPDVVV 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1718055426 590 LDEATAHIDTETEA-VIQKALDVVKQGRTTFV-IAHRLSTIRN-ADQILVLDKGEIVEKGNHEELMA 653
Cdd:PRK11308 178 ADEPVSALDVSVQAqVLNLMMDLQQELGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFN 244
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
149-406 |
2.82e-19 |
|
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: 88.72 E-value: 2.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 149 MVLLICLYGGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARItNDTEAIRDLYVTVL 228
Cdd:cd18555 41 LNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFENRSSGDLLFRA-NSNVYIRQILSNQV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 229 STFVTSGIYMFGIFTALFLLDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTIIQAFRHQ 308
Cdd:cd18555 120 ISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 309 KETMREFEELNESHFYFQNRMLNLNSLMShNLVNVIRNLAFVCLIWHfgGASLNAAGIVSIGVLYAFVDYLNRLFQPITG 388
Cdd:cd18555 200 KNIYKKWENLFKKQLKAFKKKERLSNILN-SISSSIQFIAPLLILWI--GAYLVINGELTLGELIAFSSLAGSFLTPIVS 276
|
250
....*....|....*...
gi 1718055426 389 IVNQFSKLELARVSAGRV 406
Cdd:cd18555 277 LINSYNQFILLKSYLERL 294
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
430-648 |
3.22e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 86.85 E-value: 3.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQE---LRSHM 506
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 507 GIVLQDPYLF-SGTIGSNV---------SLDDERmteEEIKNALRQVGAepllkkLPKGINEPViekgsTLSSGERQLIS 576
Cdd:PRK10908 82 GMIFQDHHLLmDRTVYDNVaipliiagaSGDDIR---RRVSAALDKVGL------LDKAKNFPI-----QLSGGEQQRVG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1718055426 577 FARALAFDPAILILDEATAHIDTE-TEAVIQKALDVVKQGRTTFVIAHRLSTI-RNADQILVLDKGEIVekGNH 648
Cdd:PRK10908 148 IARAVVNKPAVLLADEPTGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLIsRRSYRMLTLSDGHLH--GGV 219
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
448-653 |
6.04e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 86.17 E-value: 6.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 448 HISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQelRSHMGIVLQDPYLFSG-TIGSNVSL 526
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFSHlTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 527 ---------DDERMTEEEIknaLRQVGAEPLLKKLPkginepviekgSTLSSGERQLISFARALAFDPAILILDEATAHI 597
Cdd:PRK10771 95 glnpglklnAAQREKLHAI---ARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1718055426 598 DTeteAVIQKALDVVKQ-----GRTTFVIAHRLS-TIRNADQILVLDKGEIVEKGNHEELMA 653
Cdd:PRK10771 161 DP---ALRQEMLTLVSQvcqerQLTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
445-659 |
1.20e-18 |
|
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: 85.29 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 445 VLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSI--YNMSRqelRSHMGIVL--QDPYLFSG-T 519
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItkLPMHK---RARLGIGYlpQEASIFRKlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 520 IGSNVSLDDERM--TEEEIKNALRQVGAEPLLKKLPKginepviEKGSTLSSGERQLISFARALAFDPAILILDEATAHI 597
Cdd:cd03218 92 VEENILAVLEIRglSKKEREEKLEELLEEFHITHLRK-------SKASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1718055426 598 DTETEAVIQKALDVVKQGRTTFVIA-HRLS-TIRNADQILVLDKGEIVEKGNHEELMALEG--QYY 659
Cdd:cd03218 165 DPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAANELvrKVY 230
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
441-655 |
1.75e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 84.12 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 441 EGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRF--YDAQKGDVLIDGKSIYNMSRQElRSHMGIVL--QDPYLF 516
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEE-RARLGIFLafQYPPEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 517 SGtigsnvslddermteeeIKNA--LRQVgaepllkklpkgiNEpviekgsTLSSGERQLISFARALAFDPAILILDEAT 594
Cdd:cd03217 90 PG-----------------VKNAdfLRYV-------------NE-------GFSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1718055426 595 AHIDTETEAVIQKALDVVK-QGRTTFVIAH--RLSTIRNADQILVLDKGEIVEKGNHEELMALE 655
Cdd:cd03217 133 SGLDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKELALEIE 196
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
141-413 |
2.19e-18 |
|
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: 86.74 E-value: 2.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 141 FYQP---EIKGMVLLICL-YGGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFD---NLPaGKVVARI 213
Cdd:cd18578 39 FSLPdddELRSEANFWALmFLVLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDdpeNST-GALTSRL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 214 TNDTEAIRDLYVTVLSTFVTSgiyMFGIFTAL---FLLDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINA 290
Cdd:cd18578 118 STDASDVRGLVGDRLGLILQA---IVTLVAGLiiaFVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 291 KMNESIQGMTIIQAFRHQKETMREFEELNESHFYFQNRMLNLNSL---MSHNLVNVIRNLAFvcliwhFGGASLNAAGIV 367
Cdd:cd18578 195 IASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLgfgLSQSLTFFAYALAF------WYGGRLVANGEY 268
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1718055426 368 SIG----VLYAFV---DYLNRLFqpitGIVNQFSKlelARVSAGRVFELLEEK 413
Cdd:cd18578 269 TFEqffiVFMALIfgaQSAGQAF----SFAPDIAK---AKAAAARIFRLLDRK 314
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
445-646 |
2.53e-18 |
|
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: 84.24 E-value: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 445 VLKHISFTAQKGETVALVGHTGSGKSSILNLL---FRFYDAQKGDVLIDGKSiynMSRQELRSHMGIVLQD----PYL-- 515
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNGQP---RKPDQFQKCVAYVRQDdillPGLtv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 516 -----FSGTIGSNVSLDDERMTEEEIKNALRQVGAEPLLKKLPKGInepviekgstlSSGERQLISFARALAFDPAILIL 590
Cdd:cd03234 99 retltYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGI-----------SGGERRRVSIAVQLLWDPKVLIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1718055426 591 DEATAHIDTETEAVIQKAL-DVVKQGRTTFVIAH--RLSTIRNADQILVLDKGEIVEKG 646
Cdd:cd03234 168 DEPTSGLDSFTALNLVSTLsQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
429-642 |
4.02e-18 |
|
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: 82.48 E-value: 4.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 429 RVEFRDVSFAYQegeevLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQEL------ 502
Cdd:cd03215 4 VLEVRGLSVKGA-----VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiragia 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 503 -----RSHMGIVLQDPylfsgtIGSNVSLddermteeeiknalrqvgaepllkklpkginepviekGSTLSSGERQLISF 577
Cdd:cd03215 79 yvpedRKREGLVLDLS------VAENIAL-------------------------------------SSLLSGGNQQKVVL 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1718055426 578 ARALAFDPAILILDEATAHIDTETEAVIQKAL-DVVKQGRTTFVIahrlST-----IRNADQILVLDKGEI 642
Cdd:cd03215 116 ARWLARDPRVLILDEPTRGVDVGAKAEIYRLIrELADAGKAVLLI----SSeldelLGLCDRILVMYEGRI 182
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
445-646 |
4.06e-18 |
|
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: 83.40 E-value: 4.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 445 VLKHISFTAQKGETvALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMsRQELRSHMGIVLQDPYLFSG------ 518
Cdd:cd03264 15 ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQ-PQKLRRRIGYLPQEFGVYPNftvref 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 519 ----TIGSNVSLDDERmteEEIKNALRQVGAEPLLKKlpkginepvieKGSTLSSGERQLISFARALAFDPAILILDEAT 594
Cdd:cd03264 93 ldyiAWLKGIPSKEVK---ARVDEVLELVNLGDRAKK-----------KIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1718055426 595 AHIDTETEAVIQKALDVVKQGRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKG 646
Cdd:cd03264 159 AGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
441-601 |
5.82e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 83.29 E-value: 5.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 441 EGEE---VLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNM---SRQELRS-HMGIVLQDp 513
Cdd:PRK10584 18 QGEHelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARAKLRAkHVGFVFQS- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 514 YLFSGTIGS--NVSL------DDERMTEEEIKNALRQVGAEPLLKKLPkginepviekgSTLSSGERQLISFARALAFDP 585
Cdd:PRK10584 97 FMLIPTLNAleNVELpallrgESSRQSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRP 165
|
170
....*....|....*.
gi 1718055426 586 AILILDEATAHIDTET 601
Cdd:PRK10584 166 DVLFADEPTGNLDRQT 181
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
433-651 |
6.34e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 84.06 E-value: 6.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 433 RDVSFAYQEgEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYD-----AQKGDVLIDGKSIY--NMSRQELRSH 505
Cdd:PRK14239 9 SDLSVYYNK-KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYspRTDTVDLRKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 506 MGIVLQDPYLFSGTIGSNV-------SLDDERMTEEEIKNALRQVGAEPLLKklpkginEPVIEKGSTLSSGERQLISFA 578
Cdd:PRK14239 88 IGMVFQQPNPFPMSIYENVvyglrlkGIKDKQVLDEAVEKSLKGASIWDEVK-------DRLHDSALGLSGGQQQRVCIA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1718055426 579 RALAFDPAILILDEATAHIDTETEAVIQKALDVVKQGRTTFVIAHRLSTI-RNADQILVLDKGEIVEKGNHEEL 651
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
434-653 |
6.43e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 84.29 E-value: 6.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 434 DVSFAYQEgEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIyNMSRQ---ELRSHMGIVL 510
Cdd:PRK13638 6 DLWFRYQD-EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRgllALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 511 QDP--YLFSGTIGSNV--SLDDERMTEEEIKnalRQVGAEPLLKKLPKGINEPViekgSTLSSGERQLISFARALAFDPA 586
Cdd:PRK13638 84 QDPeqQIFYTDIDSDIafSLRNLGVPEAEIT---RRVDEALTLVDAQHFRHQPI----QCLSHGQKKRVAIAGALVLQAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1718055426 587 ILILDEATAHID----TETEAVIQKaldVVKQGRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKGNHEELMA 653
Cdd:PRK13638 157 YLLLDEPTAGLDpagrTQMIAIIRR---IVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFA 225
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
444-653 |
6.93e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 83.87 E-value: 6.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 444 EVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIyNMSR--------------QELRSHMGIV 509
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTI-NLVRdkdgqlkvadknqlRLLRTRLTMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 510 LQDPYLFSGTigsnVSLDDERMTEEEIKNALRQVGAEPLLKKLPK-GINEPVIEK-GSTLSSGERQLISFARALAFDPAI 587
Cdd:PRK10619 98 FQHFNLWSHM----TVLENVMEAPIQVLGLSKQEARERAVKYLAKvGIDERAQGKyPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718055426 588 LILDEATAHIDTE-TEAVIQKALDVVKQGRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKGNHEELMA 653
Cdd:PRK10619 174 LLFDEPTSALDPElVGEVLRIMQQLAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
431-643 |
6.96e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 87.86 E-value: 6.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 431 EFRDVSFAYQEGEE---VLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQEL----R 503
Cdd:PRK10535 6 ELKDIRRSYPSGEEqveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 504 SHMGIVLQDPYLFSG-TIGSNVSLDderMTEEEIKNALRQVGAEPLLKKLpkGINEPVIEKGSTLSSGERQLISFARALA 582
Cdd:PRK10535 86 EHFGFIFQRYHLLSHlTAAQNVEVP---AVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1718055426 583 FDPAILILDEATAHIDTET-EAVIQKALDVVKQGRTTFVIAHRLSTIRNADQILVLDKGEIV 643
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSgEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
387-654 |
7.21e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.00 E-value: 7.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 387 TGIVNQFSKLELARVSAGRVFELLEEKNTEEAGQPAkeralgrVEFRDVSfayqeGEEVLKHISFTAQKGETVALVGHTG 466
Cdd:COG1129 221 TGPVAELTEDELVRLMVGRELEDLFPKRAAAPGEVV-------LEVEGLS-----VGGVVRDVSFSVRAGEILGIAGLVG 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 467 SGKSSILNLLFRFYDAQKGDVLIDGKSIYNMS-RQELRSHM----------GIVLQDPylfsgtIGSNVSL--------- 526
Cdd:COG1129 289 AGRTELARALFGADPADSGEIRLDGKPVRIRSpRDAIRAGIayvpedrkgeGLVLDLS------IRENITLasldrlsrg 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 527 ---DDERMTEEeiknalrqvgAEPLLKKL---PKGINEPViekgSTLSSGERQLISFARALAFDPAILILDEATAHIDTE 600
Cdd:COG1129 363 gllDRRRERAL----------AEEYIKRLrikTPSPEQPV----GNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVG 428
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1718055426 601 TEAVIQKAL-DVVKQGRTTFVIahrlST-----IRNADQILVLDKGEIV-----EKGNHEELMAL 654
Cdd:COG1129 429 AKAEIYRLIrELAAEGKAVIVI----SSelpelLGLSDRILVMREGRIVgeldrEEATEEAIMAA 489
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
442-654 |
7.93e-18 |
|
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: 84.14 E-value: 7.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 442 GEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMsrqelrshmgivlQDPYLFSGTIG 521
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSS-------------QFSWIMPGTIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 522 SN----VSLDDERMteeeiKNALRQVGAEPLLKKLPKGINEPVIEKGSTLSSGERQLISFARALAFDPAILILDEATAHI 597
Cdd:cd03291 116 ENiifgVSYDEYRY-----KSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1718055426 598 DTETEA-VIQKALDVVKQGRTTFVIAHRLSTIRNADQILVLDKGEIVEKGNHEELMAL 654
Cdd:cd03291 191 DVFTEKeIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSL 248
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
436-652 |
8.62e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 83.52 E-value: 8.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 436 SFAYQEgEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHM--------- 506
Cdd:PRK11231 9 TVGYGT-KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLallpqhhlt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 507 --GIVLQD-------PYLfsgTIGSNVSLDDERMTEEeiknALRQVGAEPLLKKlpkginePViekgSTLSSGERQLISF 577
Cdd:PRK11231 88 peGITVRElvaygrsPWL---SLWGRLSAEDNARVNQ----AMEQTRINHLADR-------RL----TDLSGGQRQRAFL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1718055426 578 ARALAFDPAILILDEATAHIDTETEAVIQKALDVVKQ-GRTTFVIAHRLS-TIRNADQILVLDKGEIVEKGNHEELM 652
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTqGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
430-646 |
1.08e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 82.33 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEgEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIynmsRQELRSHMGIV 509
Cdd:cd03269 1 LEVENVTKRFGR-VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL----DIAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 510 LQDPYLFSG-TIGSNV----SLDDerMTEEEIKNALRQvgaepLLKKLpkGINEPVIEKGSTLSSGERQLISFARALAFD 584
Cdd:cd03269 76 PEERGLYPKmKVIDQLvylaQLKG--LKKEEARRRIDE-----WLERL--ELSEYANKRVEELSKGNQQKVQFIAAVIHD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1718055426 585 PAILILDEATAHID-TETEAVIQKALDVVKQGRTTFVIAHRLSTI-RNADQILVLDKGEIVEKG 646
Cdd:cd03269 147 PELLILDEPFSGLDpVNVELLKDVIRELARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
446-646 |
1.11e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 87.22 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 446 LKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSR---QELRSHMGIVLQDPYLF---SGT 519
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPgklQALRRDIQFIFQDPYASldpRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 520 IGSNV-------SLDDERMTEEEIKNALRQVGAEPllkklpkginEPVIEKGSTLSSGERQLISFARALAFDPAILILDE 592
Cdd:PRK10261 420 VGDSImeplrvhGLLPGKAAAARVAWLLERVGLLP----------EHAWRYPHEFSGGQRQRICIARALALNPKVIIADE 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1718055426 593 ATAHIDTETEA-VIQKALDVVKQGRTTFV-IAHRLSTI-RNADQILVLDKGEIVEKG 646
Cdd:PRK10261 490 AVSALDVSIRGqIINLLLDLQRDFGIAYLfISHDMAVVeRISHRVAVMYLGQIVEIG 546
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
433-653 |
1.12e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 86.68 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 433 RDVSFAYQEGEE---VLKHISFTAQKGETVALVGHTGSGKS----SILNLLFR---FYDAqkGDVLIDGKSIYNMSRQEL 502
Cdd:PRK15134 9 ENLSVAFRQQQTvrtVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppvVYPS--GDIRFHGESLLHASEQTL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 503 R----SHMGIVLQDPYlfsgtigsnVSLDDERMTEEEIKNAL---RQVGAEPLLKKLPKGINEPVIEKGST--------L 567
Cdd:PRK15134 87 RgvrgNKIAMIFQEPM---------VSLNPLHTLEKQLYEVLslhRGMRREAARGEILNCLDRVGIRQAAKrltdyphqL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 568 SSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQKALDVVKQ--GRTTFVIAHRLSTIRN-ADQILVLDKGEIVE 644
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVE 237
|
....*....
gi 1718055426 645 KGNHEELMA 653
Cdd:PRK15134 238 QNRAATLFS 246
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
431-637 |
1.73e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 82.07 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 431 EFRDVSFAyQEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGIVL 510
Cdd:PRK10247 9 QLQNVGYL-AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 511 QDPYLFSGTIGSNV----SLDDERMTEEEIKNALRQVG-AEPLLKklpKGINEpviekgstLSSGERQLISFARALAFDP 585
Cdd:PRK10247 88 QTPTLFGDTVYDNLifpwQIRNQQPDPAIFLDDLERFAlPDTILT---KNIAE--------LSGGEKQRISLIRNLQFMP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1718055426 586 AILILDEATAHIDTETEAVIQKALD--VVKQGRTTFVIAHRLSTIRNADQILVL 637
Cdd:PRK10247 157 KVLLLDEITSALDESNKHNVNEIIHryVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
158-406 |
2.00e-17 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 83.33 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 158 GLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGkVVARITNDTEAIRDlYVT--VLSTFVTSg 235
Cdd:cd18783 50 IALLFEGILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAG-VLTKHMQQIERIRQ-FLTgqLFGTLLDA- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 236 IYMFGIFTALFLLDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTIIQAFRHQKETMREF 315
Cdd:cd18783 127 TSLLVFLPVLFFYSPTLALVVLAFSALIALIILAFLPPFRRRLQALYRAEGERQAFLVETVHGIRTVKSLALEPRQRREW 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 316 EELNESHFYFQNRMLNLnSLMSHNLVNVIRNLAFVCLIWHfgGASLNAAGIVSIGVLYAFVDYLNRLFQPITGIVNQFSK 395
Cdd:cd18783 207 DERVARAIRARFAVGRL-SNWPQTLTGPLEKLMTVGVIWV--GAYLVFAGSLTVGALIAFNMLAGRVAGPLVQLAGLVQE 283
|
250
....*....|.
gi 1718055426 396 LELARVSAGRV 406
Cdd:cd18783 284 YQEARLSVRML 294
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
433-652 |
3.10e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 82.14 E-value: 3.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 433 RDVSFAYqEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSR-----------QE 501
Cdd:PRK10575 15 RNVSFRV-PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSkafarkvaylpQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 502 LRSHMGIVLQD-----PYLFSGTIGSNVSLDDERMTEeeiknALRQVGAEPLLKKLPkginepviekgSTLSSGERQLIS 576
Cdd:PRK10575 94 LPAAEGMTVRElvaigRYPWHGALGRFGAADREKVEE-----AISLVGLKPLAHRLV-----------DSLSGGERQRAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 577 FARALAFDPAILILDEATAHID----TETEAVIQKaldvVKQGRTTFVIA--HRLS-TIRNADQILVLDKGEIVEKGNHE 649
Cdd:PRK10575 158 IAMLVAQDSRCLLLDEPTSALDiahqVDVLALVHR----LSQERGLTVIAvlHDINmAARYCDYLVALRGGEMIAQGTPA 233
|
...
gi 1718055426 650 ELM 652
Cdd:PRK10575 234 ELM 236
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
440-651 |
4.50e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 85.29 E-value: 4.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 440 QEGEEV--LKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQ--ELR------------ 503
Cdd:PRK10261 24 QEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQviELSeqsaaqmrhvrg 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 504 SHMGIVLQDP-------YLFSGTIGSNVSLDDERMTEE---EIKNALRQV---GAEPLLKKLPKginepviekgsTLSSG 570
Cdd:PRK10261 104 ADMAMIFQEPmtslnpvFTVGEQIAESIRLHQGASREEamvEAKRMLDQVripEAQTILSRYPH-----------QLSGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 571 ERQLISFARALAFDPAILILDEATAHIDTETEAVIQKALDVVKQGRTTFV--IAHRLSTIRN-ADQILVLDKGEIVEKGN 647
Cdd:PRK10261 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVifITHDMGVVAEiADRVLVMYQGEAVETGS 252
|
....
gi 1718055426 648 HEEL 651
Cdd:PRK10261 253 VEQI 256
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
439-651 |
5.84e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 81.04 E-value: 5.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 439 YQEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQ-----KGDVLIDGKSIYN--MSRQELRSHMGIVLQ 511
Cdd:PRK14267 13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSpdVDPIEVRREVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 512 DPYLFSG-TIGSNVSLDDERMTEEEIKNALRQVgAEPLLKK--LPKGINEPVIEKGSTLSSGERQLISFARALAFDPAIL 588
Cdd:PRK14267 93 YPNPFPHlTIYDNVAIGVKLNGLVKSKKELDER-VEWALKKaaLWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1718055426 589 ILDEATAHIDTETEAVIQKALDVVKQGRTTFVIAHR-LSTIRNADQILVLDKGEIVEKGNHEEL 651
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
430-653 |
7.45e-17 |
|
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: 84.08 E-value: 7.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYqEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLfRFYDAQKGDvliDGKSIYNMS----------- 498
Cdd:TIGR03269 1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVL-RGMDQYEPT---SGRIIYHVAlcekcgyverp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 499 ----------------------------RQELRSHMGIVLQDPYLFSGtigsnvsldDERMTEEEIkNALRQVG--AEPL 548
Cdd:TIGR03269 76 skvgepcpvcggtlepeevdfwnlsdklRRRIRKRIAIMLQRTFALYG---------DDTVLDNVL-EALEEIGyeGKEA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 549 LKKLPKGINEPVIEKGST-----LSSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQKALD--VVKQGRTTFVI 621
Cdd:TIGR03269 146 VGRAVDLIEMVQLSHRIThiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEeaVKASGISMVLT 225
|
250 260 270
....*....|....*....|....*....|...
gi 1718055426 622 AHRLSTIRN-ADQILVLDKGEIVEKGNHEELMA 653
Cdd:TIGR03269 226 SHWPEVIEDlSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
444-649 |
1.03e-16 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 80.06 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 444 EVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSiYNMSRQ-------ELRSHMGIVLQD---- 512
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNH-FDFSKTpsdkairELRRNVGMVFQQynlw 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 513 PYLfsgTIGSNVSLDDER---MTEEEIKNAlrqvgAEPLLKKL---PKGINEPViekgsTLSSGERQLISFARALAFDPA 586
Cdd:PRK11124 95 PHL---TVQQNLIEAPCRvlgLSKDQALAR-----AEKLLERLrlkPYADRFPL-----HLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1718055426 587 ILILDEATAHIDTETEAVIQKALDVVKQ-GRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKGNHE 649
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
420-651 |
1.21e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 82.19 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 420 QPAKERALGRV-EFRDVSFAYqEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMS 498
Cdd:PRK11607 9 QAKTRKALTPLlEIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 499 RQELRSHMgiVLQDPYLFSG-TIGSNVS--LDDERMTEEEIKNALRQVGAEPLLKKLPKginepviEKGSTLSSGERQLI 575
Cdd:PRK11607 88 PYQRPINM--MFQSYALFPHmTVEQNIAfgLKQDKLPKAEIASRVNEMLGLVHMQEFAK-------RKPHQLSGGQRQRV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1718055426 576 SFARALAFDPAILILDEATAHIDTETEAVIQ-KALDVVKQ-GRTTFVIAH-RLSTIRNADQILVLDKGEIVEKGNHEEL 651
Cdd:PRK11607 159 ALARSLAKRPKLLLLDEPMGALDKKLRDRMQlEVVDILERvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
434-652 |
1.52e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 82.20 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 434 DVSFAyqeGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGIVLQDP 513
Cdd:PRK09536 10 SVEFG---DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 514 YL-FSGTIGSNVSL--------------DDERMTEEeiknALRQVGAEPLlkklpkgINEPViekgSTLSSGERQLISFA 578
Cdd:PRK09536 87 SLsFEFDVRQVVEMgrtphrsrfdtwteTDRAAVER----AMERTGVAQF-------ADRPV----TSLSGGERQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1718055426 579 RALAFDPAILILDEATAHID----TETEAVIQkalDVVKQGRTTFVIAHRLS-TIRNADQILVLDKGEIVEKGNHEELM 652
Cdd:PRK09536 152 RALAQATPVLLLDEPTASLDinhqVRTLELVR---RLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
449-646 |
2.30e-16 |
|
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: 78.49 E-value: 2.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 449 ISFTAqKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGkSIYNMSRQEL-----RSHMGIVLQDPYLFSG-TIGS 522
Cdd:cd03297 17 IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG-TVLFDSRKKInlppqQRKIGLVFQQYALFPHlNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 523 NVSLDDERMTEEEIKNALRQV----GAEPLLKKLPkginepviekgSTLSSGERQLISFARALAFDPAILILDEATAHID 598
Cdd:cd03297 95 NLAFGLKRKRNREDRISVDELldllGLDHLLNRYP-----------AQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1718055426 599 TETEAVIQKALDVVKQ--GRTTFVIAHRLSTI-RNADQILVLDKGEIVEKG 646
Cdd:cd03297 164 RALRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
446-643 |
3.92e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 81.61 E-value: 3.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 446 LKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGK--SIYNmSRQELRSHMGIVLQDPYLFSG-TIGS 522
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRS-PRDAIALGIGMVHQHFMLVPNlTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 523 NVSLDDERMTEEEI--KNALRQVGAepLLKKLPKGIN--EPViekgSTLSSGERQLISFARALAFDPAILILDEATAHI- 597
Cdd:COG3845 100 NIVLGLEPTKGGRLdrKAARARIRE--LSERYGLDVDpdAKV----EDLSVGEQQRVEILKALYRGARILILDEPTAVLt 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1718055426 598 DTETEAVIQ--KALdvVKQGRTTFVIAHRLSTIR-NADQILVLDKGEIV 643
Cdd:COG3845 174 PQEADELFEilRRL--AAEGKSIIFITHKLREVMaIADRVTVLRRGKVV 220
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
149-406 |
4.76e-16 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 79.04 E-value: 4.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 149 MVLLICLYGGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARItNDTEAIRDLYVTVL 228
Cdd:cd18567 41 LTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFEKRHLGDIVSRF-GSLDEIQQTLTTGF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 229 STFVTSGIYMFGIFTALFLLDVKLAFVCLAIVpiiwlwsVIYR--RYASYynQKIRSINSDI---NAKMN----ESIQGM 299
Cdd:cd18567 120 VEALLDGLMAILTLVMMFLYSPKLALIVLAAV-------ALYAllRLALY--PPLRRATEEQivaSAKEQshflETIRGI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 300 TIIQAFrhQKETMRE-------FEELNEShfyFQNRMLNLNSLMSHNLVNVIRNLAFVCLiwhfgGASLNAAGIVSIGVL 372
Cdd:cd18567 191 QTIKLF--GREAEREarwlnllVDAINAD---IRLQRLQILFSAANGLLFGLENILVIYL-----GALLVLDGEFTVGML 260
|
250 260 270
....*....|....*....|....*....|....
gi 1718055426 373 YAFVDYLNRLFQPITGIVNQFSKLELARVSAGRV 406
Cdd:cd18567 261 FAFLAYKDQFSSRASSLIDKLFELRMLRLHLERL 294
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
440-601 |
5.52e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 77.14 E-value: 5.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 440 QEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQ---KGDVLIDGKSIYNMSrQELRsHMGIVLQDPYLF 516
Cdd:COG4136 11 LGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALP-AEQR-RIGILFQDDLLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 517 SG-TIGSNVSLD-------DERmtEEEIKNALRQVGAEPLLKKLPkginepviekgSTLSSGERQLISFARALAFDPAIL 588
Cdd:COG4136 89 PHlSVGENLAFAlpptigrAQR--RARVEQALEEAGLAGFADRDP-----------ATLSGGQRARVALLRALLAEPRAL 155
|
170
....*....|...
gi 1718055426 589 ILDEATAHIDTET 601
Cdd:COG4136 156 LLDEPFSKLDAAL 168
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
411-653 |
7.65e-16 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 81.75 E-value: 7.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 411 EEKNTEEAGqpAKERALGRVEFrdvsfaYQ-EGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLI 489
Cdd:PTZ00243 648 EATPTSERS--AKTPKMKTDDF------FElEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 490 DgKSIynmsrqelrshmGIVLQDPYLFSGTIGSNVSLDDERmTEEEIKNALRQVGAEPLLKKLPKGINEPVIEKGSTLSS 569
Cdd:PTZ00243 720 E-RSI------------AYVPQQAWIMNATVRGNILFFDEE-DAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSG 785
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 570 GERQLISFARALAFDPAILILDEATAHIDTET-EAVIQKALDVVKQGRTTFVIAHRLSTIRNADQILVLDKGEIVEKGNH 648
Cdd:PTZ00243 786 GQKARVSLARAVYANRDVYLLDDPLSALDAHVgERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSS 865
|
....*
gi 1718055426 649 EELMA 653
Cdd:PTZ00243 866 ADFMR 870
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
430-646 |
8.22e-16 |
|
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: 76.91 E-value: 8.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYqEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQElrSHMGIV 509
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 510 LQDPYLFSG-TIGSNVS--LDDERMTEEEIKNALRQV----GAEPLLKKLPKginepviekgsTLSSGERQLISFARALA 582
Cdd:cd03301 78 FQNYALYPHmTVYDNIAfgLKLRKVPKDEIDERVREVaellQIEHLLDRKPK-----------QLSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1718055426 583 FDPAILILDEATAHID------TETEAV-IQKALdvvkqGRTTFVIAH-RLSTIRNADQILVLDKGEIVEKG 646
Cdd:cd03301 147 REPKVFLMDEPLSNLDaklrvqMRAELKrLQQRL-----GTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
203-653 |
9.68e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 81.71 E-value: 9.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 203 NLPAGKVVARITNDTEAIRDLyVTVLSTFVTSGiymFGIFTALFLLDVKLA----FVCLAIVPIIWLWSVIYRRYASYYN 278
Cdd:PLN03130 394 KFTSGKITNLMTTDAEALQQI-CQQLHTLWSAP---FRIIIAMVLLYQQLGvaslIGSLMLVLMFPIQTFIISKMQKLTK 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 279 QKIRSINSDINAkMNESIQGMTII------QAFRHQKETMREfEELNeshfYFQNRML--NLNSLMSHNLVNVIRNLAFV 350
Cdd:PLN03130 470 EGLQRTDKRIGL-MNEVLAAMDTVkcyaweNSFQSKVQTVRD-DELS----WFRKAQLlsAFNSFILNSIPVLVTVVSFG 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 351 CLIWhFGGASLNAAGIVSIGvLYAFVDY-LNRLFQPITGIVNqfsklelARVSAGRVFELLEEKNTEEAGQPAKERALGR 429
Cdd:PLN03130 544 VFTL-LGGDLTPARAFTSLS-LFAVLRFpLFMLPNLITQAVN-------ANVSLKRLEELLLAEERVLLPNPPLEPGLPA 614
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGEE--VLKHISFTAQKGETVALVGHTGSGKSSILN-LLFRFYDAQKGDVLIDGKSIYnmsrqelrshm 506
Cdd:PLN03130 615 ISIKNGYFSWDSKAErpTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGTVAY----------- 683
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 507 giVLQDPYLFSGTIGSNVsLDDERMTEEEIKNALRQVGAEPLLKKLPKGINEPVIEKGSTLSSGERQLISFARALAFDPA 586
Cdd:PLN03130 684 --VPQVSWIFNATVRDNI-LFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSD 760
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718055426 587 ILILDEATAHIDTET-EAVIQKALDVVKQGRTTFVIAHRLSTIRNADQILVLDKGEIVEKGNHEELMA 653
Cdd:PLN03130 761 VYIFDDPLSALDAHVgRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSN 828
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
444-651 |
2.31e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 79.71 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 444 EVLKHISFTAQKGETVALVGHTGSGKSSILNLLfRFYDAQ----KGDVLIDGKSIynmSRQELRSHMGIVLQDPyLFSGT 519
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNAL-AFRSPKgvkgSGSVLLNGMPI---DAKEMRAISAYVQQDD-LFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 520 I--------------GSNVSlDDERMteEEIKNALRQVGaepLLKKLPKGINEPVIEKGstLSSGERQLISFARALAFDP 585
Cdd:TIGR00955 114 LtvrehlmfqahlrmPRRVT-KKEKR--ERVDEVLQALG---LRKCANTRIGVPGRVKG--LSGGERKRLAFASELLTDP 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1718055426 586 AILILDEATAHIDTETEA-VIQKALDVVKQGRTTFVIAHRLST--IRNADQILVLDKGEIVEKGNHEEL 651
Cdd:TIGR00955 186 PLLFCDEPTSGLDSFMAYsVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
152-408 |
2.61e-15 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 77.16 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 152 LICLYGGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAI-RDLYVTVLST 230
Cdd:cd18580 41 LGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIdEELPLALLDF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 231 FvtsgIYMFGIFTALFLLDVKLAFVCLAIVPIIwlwsVIYRRYASYYNQKIRSI-------NSDINAKMNESIQGMTIIQ 303
Cdd:cd18580 121 L----QSLFSVLGSLIVIAIVSPYFLIVLPPLL----VVYYLLQRYYLRTSRQLrrlesesRSPLYSHFSETLSGLSTIR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 304 AFRHQKETMREFEEL----NESHFYFQ--NRMLNLNSLMSHNLVNVIrnLAFVCLIWHfggASLNaAGIVSIGVLYA--F 375
Cdd:cd18580 193 AFGWQERFIEENLRLldasQRAFYLLLavQRWLGLRLDLLGALLALV--VALLAVLLR---SSIS-AGLVGLALTYAlsL 266
|
250 260 270
....*....|....*....|....*....|...
gi 1718055426 376 VDYLNRLfqpitgiVNQFSKLELARVSAGRVFE 408
Cdd:cd18580 267 TGSLQWL-------VRQWTELETSMVSVERILE 292
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
445-651 |
3.21e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 76.69 E-value: 3.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 445 VLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIynmsRQELRSHMGivlqdpYLfsgtigsnv 524
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL----DPEDRRRIG------YL--------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 525 slDDER--------------------MTEEEIKNALRQvgaepLLKKLpkGINEPVIEKGSTLSSGERQLISFARALAFD 584
Cdd:COG4152 77 --PEERglypkmkvgeqlvylarlkgLSKAEAKRRADE-----WLERL--GLGDRANKKVEELSKGNQQKVQLIAALLHD 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1718055426 585 PAILILDEATAHIDTETEAVIQKAL-DVVKQGRTtfVI--AHRLSTI-RNADQILVLDKGEIVEKGNHEEL 651
Cdd:COG4152 148 PELLILDEPFSGLDPVNVELLKDVIrELAAKGTT--VIfsSHQMELVeELCDRIVIINKGRKVLSGSVDEI 216
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
447-651 |
3.33e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 77.44 E-value: 3.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 447 KHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMS---RQELRSHMGIVLQDPYlfsgtigsn 523
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKddeWRAVRSDIQMIFQDPL--------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 524 VSLdDERMTEEEIKnalrqvgAEPLLKKLPKGINEPVIEKGSTL------------------SSGERQLISFARALAFDP 585
Cdd:PRK15079 109 ASL-NPRMTIGEII-------AEPLRTYHPKLSRQEVKDRVKAMmlkvgllpnlinryphefSGGQCQRIGIARALILEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1718055426 586 AILILDEATAHIDTETEAVIQKALDVVKQ--GRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKGNHEEL 651
Cdd:PRK15079 181 KLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
446-661 |
4.00e-15 |
|
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: 75.19 E-value: 4.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 446 LKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIynmsrQELRSHMGIVLQDPYLFSG-TIGSNV 524
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI-----TEPGPDRMVVFQNYSLLPWlTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 525 SLDDERMTEEEIKNALRQVGAEPLLKklpKGINEPVIEKGSTLSSGERQLISFARALAFDPAILILDEATAHIDTETEAV 604
Cdd:TIGR01184 76 ALAVDRVLPDLSKSERRAIVEEHIAL---VGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 605 IQ-KALDVVKQGRTTFV-IAHRL-STIRNADQILVLDK------GEIVE----KGNHEELMALEGQYYQM 661
Cdd:TIGR01184 153 LQeELMQIWEEHRVTVLmVTHDVdEALLLSDRVVMLTNgpaaniGQILEvpfpRPRDRLEVVEDPSYYDL 222
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
430-646 |
4.81e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 75.30 E-value: 4.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEgEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYN-MSRQELRSHMGI 508
Cdd:PRK11614 6 LSFDKVSAHYGK-IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 509 VLQDPYLFSgtigsnvslddeRMTEEE--------IKNALRQVGAEPLLKKLPKgINEPVIEKGSTLSSGERQLISFARA 580
Cdd:PRK11614 85 VPEGRRVFS------------RMTVEEnlamggffAERDQFQERIKWVYELFPR-LHERRIQRAGTMSGGEQQMLAIGRA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1718055426 581 LAFDPAILILDEATAHIdteTEAVIQKALDVVKQ----GRTTFVIAhrlstiRNADQILVL-DKGEIVEKG 646
Cdd:PRK11614 152 LMSQPRLLLLDEPSLGL---APIIIQQIFDTIEQlreqGMTIFLVE------QNANQALKLaDRGYVLENG 213
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
444-651 |
6.58e-15 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 74.33 E-value: 6.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 444 EVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRqELRSHMGIVLQDPylfsgtigsn 523
Cdd:cd03265 14 EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPR-EVRRRIGIVFQDL---------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 524 vSLDDErMTEEE----------IKNALRQVGAEPLLKKLpkGINEPVIEKGSTLSSGERQLISFARALAFDPAILILDEA 593
Cdd:cd03265 83 -SVDDE-LTGWEnlyiharlygVPGAERRERIDELLDFV--GLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1718055426 594 TAHIDTETEA----VIQKALDvvKQGRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKGNHEEL 651
Cdd:cd03265 159 TIGLDPQTRAhvweYIEKLKE--EFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
421-650 |
6.96e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.80 E-value: 6.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 421 PAKERaLGR--VEFRDVSFAYqEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLL----------FRF-------YD 481
Cdd:COG0488 306 PPPER-LGKkvLELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLagelepdsgtVKLgetvkigYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 482 AQKGDVLIDGKSIY--------NMSRQELRSHMGIvlqdpYLFSGtigsnvslDDermteeeiknALRQVGaepllkklp 553
Cdd:COG0488 384 DQHQEELDPDKTVLdelrdgapGGTEQEVRGYLGR-----FLFSG--------DD----------AFKPVG--------- 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 554 kginepviekgsTLSSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQKALDVVKqGrTTFVIAH-R--LSTIrn 630
Cdd:COG0488 432 ------------VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFP-G-TVLLVSHdRyfLDRV-- 495
|
250 260
....*....|....*....|.
gi 1718055426 631 ADQILVLDKGEIVEK-GNHEE 650
Cdd:COG0488 496 ATRILEFEDGGVREYpGGYDD 516
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
151-406 |
2.05e-14 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 74.17 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 151 LLICLYGGLLVFSVF---FQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARItNDTEAIRDLYV-T 226
Cdd:cd18782 40 TLYVIGVVMLVAALLeavLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLTgT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 227 VLSTFVTSgIYMFGIFTALFLLDVKLAFVCLAIVPIIWLWS-----VIYRRYASYYNQKIRSinsdiNAKMNESIQGMTI 301
Cdd:cd18782 119 ALTTLLDV-LFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTflfgpILRRQIRRRAEASAKT-----QSYLVESLTGIQT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 302 IQAFRHQKETMREFEE-----LNEShfyFQNRMLnlnSLMSHNLVNVIRNLAFVCLIWHfgGASLNAAGIVSIGVLYAFV 376
Cdd:cd18782 193 VKAQNAELKARWRWQNryarsLGEG---FKLTVL---GTTSGSLSQFLNKLSSLLVLWV--GAYLVLRGELTLGQLIAFR 264
|
250 260 270
....*....|....*....|....*....|
gi 1718055426 377 DYLNRLFQPITGIVNQFSKLELARVSAGRV 406
Cdd:cd18782 265 ILSGYVTGPILRLSTLWQQFQELRVSLERL 294
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
446-641 |
2.15e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.12 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 446 LKHISFTAQKGETVALVGHTGSGKSSILNLLFRFY--DAQKGDVLIDGKSI--YNMSRQElrsHMGIVL--QD----PYL 515
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYphGTYEGEIIFEGEELqaSNIRDTE---RAGIAIihQElalvKEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 516 fsgTIGSNVSL----------DDERMTEEeiknalrqvgAEPLLKKLPKGINepVIEKGSTLSSGERQLISFARALAFDP 585
Cdd:PRK13549 98 ---SVLENIFLgneitpggimDYDAMYLR----------AQKLLAQLKLDIN--PATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1718055426 586 AILILDEATAHIdteTEAVIQKALDVVK----QGRTTFVIAHRLSTIRN-ADQILVLDKGE 641
Cdd:PRK13549 163 RLLILDEPTASL---TESETAVLLDIIRdlkaHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
446-646 |
3.31e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.59 E-value: 3.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 446 LKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSiYNMSRQELRSHMGIvlqdpylfsGTIGSNVS 525
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIN-YNKLDHKLAAQLGI---------GIIYQELS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 526 LDDERMTEEEIK-----------------NALRQVGAEPLLKklpKGINEPVIEKGSTLSSGERQLISFARALAFDPAIL 588
Cdd:PRK09700 91 VIDELTVLENLYigrhltkkvcgvniidwREMRVRAAMMLLR---VGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 589 ILDEATAHI-DTETEAVIQKALDVVKQGRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKG 646
Cdd:PRK09700 168 IMDEPTSSLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
432-601 |
4.62e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 75.10 E-value: 4.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 432 FRDVSFAYqEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIdgksiynmsRQELRshMGIVLQ 511
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGLR--IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 512 DPYLFSG-TIGSNV-SLDDERMTEEEIKNALRQVGAEP----------------------------LLKKLpkGINE--- 558
Cdd:COG0488 69 EPPLDDDlTVLDTVlDGDAELRALEAELEELEAKLAEPdedlerlaelqeefealggweaearaeeILSGL--GFPEedl 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1718055426 559 --PViekgSTLSSGERQLISFARALAFDPAILILDEATAHIDTET 601
Cdd:COG0488 147 drPV----SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
449-653 |
5.03e-14 |
|
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: 73.98 E-value: 5.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 449 ISFTAQKGETVALVGHTGSGKSSILNL---LFRFYDAQ---KGDVLIDGKSIYNMSRqELRsHMGIVLQDPYLF------ 516
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAiagLERPDSGRirlGGEVLQDSARGIFLPP-HRR-RIGYVFQEARLFphlsvr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 517 ---------SGTIGSNVSLDDermteeeiknALRQVGAEPLLKKLPkginepviekgSTLSSGERQLISFARALAFDPAI 587
Cdd:COG4148 96 gnllygrkrAPRAERRISFDE----------VVELLGIGHLLDRRP-----------ATLSGGERQRVAIGRALLSSPRL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1718055426 588 LILDEATAHIDTETEAVIqkaLDVVKQGRTTFVI-----AHRLSTI-RNADQILVLDKGEIVEKGNHEELMA 653
Cdd:COG4148 155 LLMDEPLAALDLARKAEI---LPYLERLRDELDIpilyvSHSLDEVaRLADHVVLLEQGRVVASGPLAEVLS 223
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
430-653 |
5.40e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 72.49 E-value: 5.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEgEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQEL---RSHM 506
Cdd:PRK11831 8 VDMRGVSFTRGN-RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 507 GIVLQDPYLFSG-TIGSNVSL---DDERMTEEEIKNA----LRQVGAEPLLKKLPkginepviekgSTLSSGERQLISFA 578
Cdd:PRK11831 87 SMLFQSGALFTDmNVFDNVAYplrEHTQLPAPLLHSTvmmkLEAVGLRGAAKLMP-----------SELSGGMARRAALA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718055426 579 RALAFDPAILILDEATAHIDTETEAVIQKALDVVKQ--GRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKGNHEELMA 653
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQALQA 233
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
446-644 |
6.05e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 74.83 E-value: 6.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 446 LKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDA--QKGDVLIDGKsiynmsRQELRS-----HMGIVL--QD---- 512
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHgsYEGEILFDGE------VCRFKDirdseALGIVIihQElali 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 513 PYLfsgTIGSNVSLDDERMTEEEIKNALRQVGAEPLLKKLpkGINEPVIEKGSTLSSGERQLISFARALAFDPAILILDE 592
Cdd:NF040905 91 PYL---SIAENIFLGNERAKRGVIDWNETNRRARELLAKV--GLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1718055426 593 ATAHI-DTETEAVIQKALDVVKQGRTTFVIAHRLSTIRN-ADQILVLDKGEIVE 644
Cdd:NF040905 166 PTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
446-625 |
7.01e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 72.12 E-value: 7.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 446 LKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYD-----AQKGDVLIDGKSIY--NMSRQELRSHMGIVLQDPYLFSG 518
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYapDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 519 TIGSNVSLDdERMT------EEEIKNALRQVGaepllkkLPKGINEPVIEKGSTLSSGERQLISFARALAFDPAILILDE 592
Cdd:PRK14243 106 SIYDNIAYG-ARINgykgdmDELVERSLRQAA-------LWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190
....*....|....*....|....*....|...
gi 1718055426 593 ATAHIDTETEAVIQKALDVVKQGRTTFVIAHRL 625
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
456-658 |
7.63e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 74.27 E-value: 7.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 456 GETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSI-YNMSRQELRSHMGIVLQDPYLFSG-TIGSNVSLDDE---- 529
Cdd:PRK10762 30 GRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtFNGPKSSQEAGIGIIHQELNLIPQlTIAENIFLGREfvnr 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 530 -------RMTEEeiknalrqvgAEPLLKKLpkGINEPVIEKGSTLSSGERQLISFARALAFDPAILILDEAT-AHIDTET 601
Cdd:PRK10762 110 fgridwkKMYAE----------ADKLLARL--NLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTdALTDTET 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1718055426 602 EAVIQKALDVVKQGRTTFVIAHRLSTIRN-ADQILVLDKGE-IVEKGNHE-------ELMA---LEGQY 658
Cdd:PRK10762 178 ESLFRVIRELKSQGRGIVYISHRLKEIFEiCDDVTVFRDGQfIAEREVADltedsliEMMVgrkLEDQY 246
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
433-662 |
8.59e-14 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 74.54 E-value: 8.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 433 RDVSFAYQEGE--EVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHM-GIv 509
Cdd:PRK13545 25 KDLFFRSKDGEyhYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLtGI- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 510 lqdpylfsgtigSNVSLDDERM--TEEEIKNALRQVGAeplLKKLPKGINEPViekgSTLSSGERQLISFARALAFDPAI 587
Cdd:PRK13545 104 ------------ENIELKGLMMglTKEKIKEIIPEIIE---FADIGKFIYQPV----KTYSSGMKSRLGFAISVHINPDI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1718055426 588 LILDEATAHID-TETEAVIQKALDVVKQGRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKGNHEELMALEGQYYQMY 662
Cdd:PRK13545 165 LVIDEALSVGDqTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDHYDEFLKKY 241
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
153-408 |
9.66e-14 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 72.12 E-value: 9.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 153 ICLYGGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVTVLSTFV 232
Cdd:cd18606 38 IGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 233 TSGIYMFGIFTalfLLDVKLAFVCLAIVPIIwlwsVIYRRYASYYNQKIRSIN-------SDINAKMNESIQGMTIIQAF 305
Cdd:cd18606 118 YTLSSIIGTFI---LIIIYLPWFAIALPPLL----VLYYFIANYYRASSRELKrlesilrSFVYANFSESLSGLSTIRAY 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 306 RHQKETMREFEEL----NESHFYFQ--NRMLNLN-SLMSHNLVNVIrnlAFVCLIWHFggaSLNAAgivSIGVLyafVDY 378
Cdd:cd18606 191 GAQDRFIKKNEKLidnmNRAYFLTIanQRWLAIRlDLLGSLLVLIV---ALLCVTRRF---SISPS---STGLV---LSY 258
|
250 260 270
....*....|....*....|....*....|
gi 1718055426 379 LNRLFQPITGIVNQFSKLELARVSAGRVFE 408
Cdd:cd18606 259 VLQITQVLSWLVRQFAEVENNMNSVERLLH 288
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
417-646 |
1.00e-13 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 71.21 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 417 EAGQPAKERALGRVEFRDVsfayqegeEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYN 496
Cdd:cd03267 16 EPGLIGSLKSLFKRKYREV--------EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 497 mSRQELRSHMGIVL------------QDPYLFSGTIgsnVSLDDERMTE--EEIKNALRqvgAEPLLKKlpkginePVIE 562
Cdd:cd03267 88 -RRKKFLRRIGVVFgqktqlwwdlpvIDSFYLLAAI---YDLPPARFKKrlDELSELLD---LEELLDT-------PVRQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 563 kgstLSSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQKALDVVKQGRTTFVI--AHRLSTI-RNADQILVLDK 639
Cdd:cd03267 154 ----LSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLltSHYMKDIeALARRVLVIDK 229
|
....*..
gi 1718055426 640 GEIVEKG 646
Cdd:cd03267 230 GRLLYDG 236
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
149-406 |
1.06e-13 |
|
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: 72.23 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 149 MVLLICLyGGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARItNDTEAIRDLY---- 224
Cdd:cd18566 42 QVLVIGV-VIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERL-NSLEQIREFLtgqa 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 225 VTVLSTFVTSGIYmfgiFTALFLLDVKLAFVCLAIVPIIWLWSVIY-----RRYASYYNQKIRSINSdinakMNESIQGM 299
Cdd:cd18566 120 LLALLDLPFVLIF----LGLIWYLGGKLVLVPLVLLGLFVLVAILLgpilrRALKERSRADERRQNF-----LIETLTGI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 300 TIIQAFRHQKETMREFEELNESHFY--FQNRMLNlNSLMshNLVNVIRNLAFVCLIWhfGGASLNAAGIVSIGVLYAFVD 377
Cdd:cd18566 191 HTIKAMAMEPQMLRRYERLQANAAYagFKVAKIN-AVAQ--TLGQLFSQVSMVAVVA--FGALLVINGDLTVGALIACTM 265
|
250 260
....*....|....*....|....*....
gi 1718055426 378 YLNRLFQPITGIVNQFSKLELARVSAGRV 406
Cdd:cd18566 266 LSGRVLQPLQRAFGLWTRFQQVRVAVRRL 294
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
445-644 |
1.08e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 70.76 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 445 VLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDgksiynmsrqelrshmgivlqdpyLFSGTIGSNV 524
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD------------------------VPDNQFGREA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 525 SLDDERMTEEEIKNALRQVGAepllkklpKGINEPV--IEKGSTLSSGERQLISFARALAFDPAILILDEATAHIDTETE 602
Cdd:COG2401 101 SLIDAIGRKGDFKDAVELLNA--------VGLSDAVlwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1718055426 603 AVIQKAL-DVVKQGRTTFVIA-HRlSTIRNA---DQILVLDKGEIVE 644
Cdd:COG2401 173 KRVARNLqKLARRAGITLVVAtHH-YDVIDDlqpDLLIFVGYGGVPE 218
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
430-649 |
1.22e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 72.56 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQeGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQElRSHMGIV 509
Cdd:PRK13536 42 IDLAGVSKSYG-DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA-RARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 510 LQ-DPYLFSGTIGSNVSLDDE--RMTEEEIKNALrqvgaEPLLK--KLPKGINEPViekgSTLSSGERQLISFARALAFD 584
Cdd:PRK13536 120 PQfDNLDLEFTVRENLLVFGRyfGMSTREIEAVI-----PSLLEfaRLESKADARV----SDLSGGMKRRLTLARALIND 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718055426 585 PAILILDEATAHIDTETEAVIQKAL-DVVKQGRTTFVIAHRLSTI-RNADQILVLDKG-EIVEKGNHE 649
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLrSLLARGKTILLTTHFMEEAeRLCDRLCVLEAGrKIAEGRPHA 258
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
434-664 |
1.53e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 71.58 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 434 DVSFAYQEGE----EVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLI-DGKSIYNMSR----QELRS 504
Cdd:PRK13645 11 NVSYTYAKKTpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgDYAIPANLKKikevKRLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 505 HMGIVLQDP--YLFSGTIGSNVSLDDERMTEEEiKNALRQVgaePLLKKLPKGINEPVIEKGSTLSSGERQLISFARALA 582
Cdd:PRK13645 91 EIGLVFQFPeyQLFQETIEKDIAFGPVNLGENK-QEAYKKV---PELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 583 FDPAILILDEATAHIDTETEAVIQKALDVV--KQGRTTFVIAHRLSTI-RNADQILVLDKGEIVEKG-------NHEELM 652
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFERLnkEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGspfeifsNQELLT 246
|
250
....*....|..
gi 1718055426 653 ALEGQYYQMYEL 664
Cdd:PRK13645 247 KIEIDPPKLYQL 258
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
445-655 |
1.57e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 71.17 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 445 VLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHMGIVLQDPYLfSGTIGSNV 524
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATT-PGDITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 525 SLDDERMTEEEIKNALRQVGAEPLLKKL-PKGINEPVIEKGSTLSSGERQLISFARALAFDPAILILDEATAHIDTETEA 603
Cdd:PRK10253 101 LVARGRYPHQPLFTRWRKEDEEAVTKAMqATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1718055426 604 VIQKALDVV--KQGRTTFVIAHRLS-TIRNADQILVLDKGEIVEKGNHEELMALE 655
Cdd:PRK10253 181 DLLELLSELnrEKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVTAE 235
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
151-406 |
1.91e-13 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 71.44 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 151 LLICLYGGLLVFSVF---FQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARItNDTEAIRDLY--- 224
Cdd:cd18568 40 LLNLILIGLLIVGIFqilLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRF-QENQKIRRFLtrs 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 225 -VTVLSTFVTSGIYmfgiFTALFLLDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTIIQ 303
Cdd:cd18568 119 aLTTILDLLMVFIY----LGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 304 AFRHQKETMREFEELneshfyfQNRMLNLN------SLMSHNLVNVIRNLAFVCLIWhfGGASLNAAGIVSIGVLYAFVD 377
Cdd:cd18568 195 ALAAERPIRWRWENK-------FAKALNTRfrgqklSIVLQLISSLINHLGTIAVLW--YGAYLVISGQLTIGQLVAFNM 265
|
250 260
....*....|....*....|....*....
gi 1718055426 378 YLNRLFQPITGIVNQFSKLELARVSAGRV 406
Cdd:cd18568 266 LFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
437-640 |
1.92e-13 |
|
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: 70.05 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 437 FAYQEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGK----SIYNMSRQELRSHMGIVLQD 512
Cdd:cd03290 8 FSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKnesePSFEATRSRNRYSVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 513 PYLFSGTIGSNVSLDDErMTEEEIKNALRQVGAEPLLKKLPKGINEPVIEKGSTLSSGERQLISFARALAFDPAILILDE 592
Cdd:cd03290 88 PWLLNATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1718055426 593 ATAHIDTE-TEAVIQKALDVVKQG--RTTFVIAHRLSTIRNADQILVLDKG 640
Cdd:cd03290 167 PFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
442-623 |
2.90e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 70.11 E-value: 2.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 442 GEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQElrshmGIVLQDPYLFS-GTI 520
Cdd:PRK11248 13 GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVFQNEGLLPwRNV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 521 GSNVSLD------DERMTEEEIKNALRQVGAEPLLKKLPkginepviekgSTLSSGERQLISFARALAFDPAILILDEAT 594
Cdd:PRK11248 88 QDNVAFGlqlagvEKMQRLEIAHQMLKKVGLEGAEKRYI-----------WQLSGGQRQRVGIARALAANPQLLLLDEPF 156
|
170 180 190
....*....|....*....|....*....|.
gi 1718055426 595 AHIDTETEAVIQKALDVV--KQGRTTFVIAH 623
Cdd:PRK11248 157 GALDAFTREQMQTLLLKLwqETGKQVLLITH 187
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
434-649 |
3.91e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 70.30 E-value: 3.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 434 DVSFAYQEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSHM------- 506
Cdd:PRK15056 11 DVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVpqseevd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 507 --------GIVLQDPYLFSGTIGSNVSLDDERMTEeeiknALRQVGaepLLKKLPKGINEpviekgstLSSGERQLISFA 578
Cdd:PRK15056 91 wsfpvlveDVVMMGRYGHMGWLRRAKKRDRQIVTA-----ALARVD---MVEFRHRQIGE--------LSGGQKKRVFLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1718055426 579 RALAFDPAILILDEATAHIDTETEAVIQKAL-DVVKQGRTTFVIAHRLSTIRNADQILVLDKGEIVEKGNHE 649
Cdd:PRK15056 155 RAIAQQGQVILLDEPFTGVDVKTEARIISLLrELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
158-378 |
4.10e-13 |
|
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: 70.36 E-value: 4.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 158 GLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVTVLSTFVTSGIY 237
Cdd:cd18780 50 GVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 238 MFGIFTALFLLDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTIIQAF-RHQKETMREFE 316
Cdd:cd18780 130 IIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFaKETKEVSRYSE 209
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1718055426 317 ELNESHFYfqNRMLNLNSLMSHNLVNVIRNLAFVCLIWHfgGASLNAAGIVSIGVLYAFVDY 378
Cdd:cd18780 210 KINESYLL--GKKLARASGGFNGFMGAAAQLAIVLVLWY--GGRLVIDGELTTGLLTSFLLY 267
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
430-655 |
6.96e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 69.83 E-value: 6.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEgEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQElRSHMGIV 509
Cdd:PRK13537 8 IDFRNVEKRYGD-KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 510 LQ----DPYLfsgTIGSNVSLDDER--MTEEEIKNALrqvgaEPLLK--KLPKGINEPVIEkgstLSSGERQLISFARAL 581
Cdd:PRK13537 86 PQfdnlDPDF---TVRENLLVFGRYfgLSAAAARALV-----PPLLEfaKLENKADAKVGE----LSGGMKRRLTLARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1718055426 582 AFDPAILILDEATAHIDTETEAVIQKAL-DVVKQGRTTFVIAHRLSTI-RNADQILVLDKGEIVEKGNHEELMALE 655
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLrSLLARGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
438-655 |
7.84e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 68.77 E-value: 7.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 438 AYQeGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQE-LRSHMGIVLQDPYLF 516
Cdd:PRK10895 12 AYK-GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 517 SgtigsNVSLDDERMTEEEIKNAL----RQVGAEPLLKKLpkGINEPVIEKGSTLSSGERQLISFARALAFDPAILILDE 592
Cdd:PRK10895 91 R-----RLSVYDNLMAVLQIRDDLsaeqREDRANELMEEF--HIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1718055426 593 ATAHIDTETEAVIQKALDVVK-QGRTTFVIAHRL-STIRNADQILVLDKGEIVEKGNHEELMALE 655
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
430-646 |
8.03e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 70.36 E-value: 8.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYqEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQelRSHMGIV 509
Cdd:PRK09452 15 VELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 510 LQDPYLFSG-TIGSNVS--LDDERMTEEEIK----NALRQVGAEPLLKKLPKginepviekgsTLSSGERQLISFARALA 582
Cdd:PRK09452 92 FQSYALFPHmTVFENVAfgLRMQKTPAAEITprvmEALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1718055426 583 FDPAILILDEATAHIDTETEAVIQ---KALDvvKQGRTTFV-IAH-RLSTIRNADQILVLDKGEIVEKG 646
Cdd:PRK09452 161 NKPKVLLLDESLSALDYKLRKQMQnelKALQ--RKLGITFVfVTHdQEEALTMSDRIVVMRDGRIEQDG 227
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
449-652 |
1.00e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.42 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 449 ISFTAQKGETVALVGHTGSGKSSIL----NLLfrfydAQKGDVLIDGKSIYNMSRQELRSHMG-IVLQDPYLFSGTI--- 520
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLarmaGLL-----PGSGSIQFAGQPLEAWSAAELARHRAyLSQQQTPPFAMPVfqy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 521 -----GSNVSLDDERMTEEEIKNALRqvgaepLLKKLPKGINepviekgsTLSSGERQLISFARA-LAFDPAI------L 588
Cdd:PRK03695 90 ltlhqPDKTRTEAVASALNEVAEALG------LDDKLGRSVN--------QLSGGEWQRVRLAAVvLQVWPDInpagqlL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1718055426 589 ILDEATAHIDTETEAVIQKALD-VVKQGRTTFVIAHRLS-TIRNADQILVLDKGEIVEKGNHEELM 652
Cdd:PRK03695 156 LLDEPMNSLDVAQQAALDRLLSeLCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
387-643 |
4.42e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 68.90 E-value: 4.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 387 TGIVNQFSKLELARVSAGRVFELLEEKNTEEAGQPakeralgRVEFRDVSFAYQEGEEVLKHISFTAQKGETVALVGHTG 466
Cdd:COG3845 222 TVDTAETSEEELAELMVGREVLLRVEKAPAEPGEV-------VLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAG 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 467 SGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRSH-MGIVLQDPyLFSGTIGSnvsldderMTEEEikNA-LRQVG 544
Cdd:COG3845 295 NGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPEDR-LGRGLVPD--------MSVAE--NLiLGRYR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 545 AEPLLKKL---------------------PKGINEPViekgSTLSSGERQLISFARALAFDPAILILDEATAHIDTE-TE 602
Cdd:COG3845 364 RPPFSRGGfldrkairafaeelieefdvrTPGPDTPA----RSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGaIE 439
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1718055426 603 AVIQKALDVVKQGRTTFVIAHRLSTIRN-ADQILVLDKGEIV 643
Cdd:COG3845 440 FIHQRLLELRDAGAAVLLISEDLDEILAlSDRIAVMYEGRIV 481
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
156-408 |
4.57e-12 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350047 [Multi-domain] Cd Length: 296 Bit Score: 67.12 E-value: 4.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 156 YGGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVTVLSTFVTSg 235
Cdd:cd18603 47 YGALGLGQAIFVFLGSLALALGCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNC- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 236 iyMFGIFTALFLLDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQ--KIRSIN-SDINAKMNESIQGMTIIQAFRHQKETM 312
Cdd:cd18603 126 --LFQVISTLVVISISTPIFLVVIIPLAILYFFIQRFYVATSRQlkRLESVSrSPIYSHFSETLQGASTIRAYGVQERFI 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 313 REFEEL-NESH-FYFQNRMLN---------LNSLMshnlvnvirnLAFVCLIWHFGGASLNaAGIVSIGVLYAF--VDYL 379
Cdd:cd18603 204 RESDRRvDENQrAYYPSIVSNrwlavrlefLGNLI----------VLFAALFAVLSRDSLS-PGLVGLSISYALqiTQTL 272
|
250 260
....*....|....*....|....*....
gi 1718055426 380 NRLfqpitgiVNQFSKLELARVSAGRVFE 408
Cdd:cd18603 273 NWL-------VRMTSELETNIVSVERIKE 294
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
444-651 |
4.59e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 67.80 E-value: 4.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 444 EVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQElrSHMGIVLQDPYLFSG-TIGS 522
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALFRHmTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 523 NVSLD------DERMTEEEIKNALRQ----VGAEPLLKKLPkginepviekgSTLSSGERQLISFARALAFDPAILILDE 592
Cdd:PRK10851 94 NIAFGltvlprRERPNAAAIKAKVTQllemVQLAHLADRYP-----------AQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1718055426 593 ATAHIDTETEAVIQKALDVVKQG---RTTFVIAHRLSTIRNADQILVLDKGEIVEKGNHEEL 651
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQLHEElkfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
430-628 |
6.00e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 66.60 E-value: 6.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYqEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQkGDVLIDGK------SIY----NMSR 499
Cdd:PRK14258 8 IKVNNLSFYY-DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGRveffnqNIYerrvNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 500 qeLRSHMGIVLQDPYLFSGTIGSNVS-----------LDDERMTEEEIKNAlrqvgaePLLKKLPKGINEPVIEkgstLS 568
Cdd:PRK14258 86 --LRRQVSMVHPKPNLFPMSVYDNVAygvkivgwrpkLEIDDIVESALKDA-------DLWDEIKHKIHKSALD----LS 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1718055426 569 SGERQLISFARALAFDPAILILDEATAHID----TETEAVIQKALdvVKQGRTTFVIAHRLSTI 628
Cdd:PRK14258 153 GGQQQRLCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSLR--LRSELTMVIVSHNLHQV 214
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
449-646 |
7.84e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 66.10 E-value: 7.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 449 ISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKS-----IYNMSRQE----LRSHMGIVLQDPY--LFS 517
Cdd:PRK11701 25 VSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdLYALSEAErrrlLRTEWGFVHQHPRdgLRM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 518 G-TIGSNVSlddERMTEEEIKN--ALRQVGAEPL---------LKKLPkginepviekgSTLSSGERQLISFARALAFDP 585
Cdd:PRK11701 105 QvSAGGNIG---ERLMAVGARHygDIRATAGDWLerveidaarIDDLP-----------TTFSGGMQQRLQIARNLVTHP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1718055426 586 AILILDEATAHIDTETEAviqKALD-----VVKQGRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKG 646
Cdd:PRK11701 171 RLVFMDEPTGGLDVSVQA---RLLDllrglVRELGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESG 234
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
429-605 |
8.20e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 64.90 E-value: 8.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 429 RVEFRDVSfAYQEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQElRSHmgi 508
Cdd:PRK13539 2 MLEGEDLA-CVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAE-ACH--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 509 vlqdpYLfsG---------TIGSNVSL------DDERMTEEeiknALRQVGAEPLLkKLPKGinepviekgsTLSSGERQ 573
Cdd:PRK13539 77 -----YL--GhrnamkpalTVAENLEFwaaflgGEELDIAA----ALEAVGLAPLA-HLPFG----------YLSAGQKR 134
|
170 180 190
....*....|....*....|....*....|..
gi 1718055426 574 LISFARALAFDPAILILDEATAHIDTETEAVI 605
Cdd:PRK13539 135 RVALARLLVSNRPIWILDEPTAALDAAAVALF 166
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
430-651 |
9.15e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 67.36 E-value: 9.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYqeGEEVL-KHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQElRShMGI 508
Cdd:PRK11000 4 VTLRNVTKAY--GDVVIsKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE-RG-VGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 509 VLQD----PYLfsgTIGSNVS--LDDERMTEEEIKNALRQVGA----EPLLKKLPKginepviekgsTLSSGERQLISFA 578
Cdd:PRK11000 80 VFQSyalyPHL---SVAENMSfgLKLAGAKKEEINQRVNQVAEvlqlAHLLDRKPK-----------ALSGGQRQRVAIG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 579 RALAFDPAILILDEATAHIDTeteaviqkALDVV----------KQGRTTFVIAH-RLSTIRNADQILVLDKGEIVEKGN 647
Cdd:PRK11000 146 RTLVAEPSVFLLDEPLSNLDA--------ALRVQmrieisrlhkRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGK 217
|
....
gi 1718055426 648 HEEL 651
Cdd:PRK11000 218 PLEL 221
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
445-651 |
1.12e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 66.67 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 445 VLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQElrSHMGIVLQDPYLFSG-TIGSN 523
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--RDICMVFQSYALFPHmSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 524 VS--LDDERMTEEEI----KNALRQVGAEpllkklpkGINEPVIEKgstLSSGERQLISFARALAFDPAILILDEATAHI 597
Cdd:PRK11432 99 VGygLKMLGVPKEERkqrvKEALELVDLA--------GFEDRYVDQ---ISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1718055426 598 DT-------ETEAVIQKALDVvkqgrTTFVIAHRLS-TIRNADQILVLDKGEIVEKGNHEEL 651
Cdd:PRK11432 168 DAnlrrsmrEKIRELQQQFNI-----TSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
446-649 |
1.21e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.67 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 446 LKHISFTAQKGETVALVGHTGSGKSSILNLLfrfydaqKGDVLID-GKSIYN----MSRQElrshmgivlQDP-YLFSGT 519
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDdGRIIYEqdliVARLQ---------QDPpRNVEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 520 IGSNVSLDDERMTE--EEIKNALRQVGAEP---LLKKLPK---------------GINEpVIE--------KGSTLSSGE 571
Cdd:PRK11147 83 VYDFVAEGIEEQAEylKRYHDISHLVETDPsekNLNELAKlqeqldhhnlwqlenRINE-VLAqlgldpdaALSSLSGGW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 572 RQLISFARALAFDPAILILDEATAHIDTETeavIQKALDVVK--QGRTTFvIAHRLSTIRN-ADQILVLDKGEIVE-KGN 647
Cdd:PRK11147 162 LRKAALGRALVSNPDVLLLDEPTNHLDIET---IEWLEGFLKtfQGSIIF-ISHDRSFIRNmATRIVDLDRGKLVSyPGN 237
|
..
gi 1718055426 648 HE 649
Cdd:PRK11147 238 YD 239
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
433-642 |
1.48e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 65.08 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 433 RDVSFAYQEgEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIdGKSIYNMSRQELRshmgIVLQD 512
Cdd:PRK11247 16 NAVSKRYGE-RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLA-GTAPLAEAREDTR----LMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 513 PYLFS-GTIGSNVSLDDERMTEEEIKNALRQVGAEPLLKKLPkginepviekgSTLSSGERQLISFARALAFDPAILILD 591
Cdd:PRK11247 90 ARLLPwKKVIDNVGLGLKGQWRDAALQALAAVGLADRANEWP-----------AALSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1718055426 592 EATAHIDTETEAVIQKALDVV--KQGRTTFVIAHRLS-TIRNADQILVLDKGEI 642
Cdd:PRK11247 159 EPLGALDALTRIEMQDLIESLwqQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
155-410 |
1.61e-11 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 65.57 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 155 LYGGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVTVLSTFVTS 234
Cdd:cd18604 48 IYALISLLSVLLGTLRYLLFFFGSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLES 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 235 GIYMFGIFTALFLldVKLAFVCLAIVPiiwlwSVIYRRYASYYNQKIRSIN-------SDINAKMNESIQGMTIIQAFRH 307
Cdd:cd18604 128 TLSLLVILIAIVV--VSPAFLLPAVVL-----AALYVYIGRLYLRASRELKrlesvarSPILSHFGETLAGLVTIRAFGA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 308 QKETMREFEELNESH---FYFQ---NRMLNLN-SLMShNLVNVIrnLAFVCLIWHFGGASLnaAGIvSIGVLYAFVDYln 380
Cdd:cd18604 201 EERFIEEMLRRIDRYsraFRYLwnlNRWLSVRiDLLG-ALFSFA--TAALLVYGPGIDAGL--AGF-SLSFALGFSSA-- 272
|
250 260 270
....*....|....*....|....*....|
gi 1718055426 381 rlfqpITGIVNQFSKLELARVSAGRVFELL 410
Cdd:cd18604 273 -----ILWLVRSYNELELDMNSVERIQEYL 297
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
431-644 |
2.76e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.47 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 431 EFRDVSFAYqEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSI-YNMSRQELRSHMGIV 509
Cdd:PRK11288 6 SFDGIGKTF-PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrFASTTAALAAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 510 LQD----PYLfsgTIGSNVSLD---------DERmteEEIKNALRQvgaeplLKKLPKGI--NEPViekgSTLSSGERQL 574
Cdd:PRK11288 85 YQElhlvPEM---TVAENLYLGqlphkggivNRR---LLNYEAREQ------LEHLGVDIdpDTPL----KYLSIGQRQM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1718055426 575 ISFARALAFDPAILILDEATAHIDT-ETEAVIQKALDVVKQGRTTFVIAHRLSTI-RNADQILVLDKGEIVE 644
Cdd:PRK11288 149 VEIAKALARNARVIAFDEPTSSLSArEIEQLFRVIRELRAEGRVILYVSHRMEEIfALCDAITVFKDGRYVA 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
449-642 |
5.35e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 65.62 E-value: 5.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 449 ISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQ-KGDVLIDGKSIYNMS-RQELRSHMGIVLQD-------PYLfsgT 519
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNpAQAIRAGIAMVPEDrkrhgivPIL---G 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 520 IGSNVSLD--DERMTEEEIKNALRQVGAEPLLKKLPKGINEPVIEKGStLSSGERQLISFARALAFDPAILILDEATAHI 597
Cdd:TIGR02633 356 VGKNITLSvlKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGR-LSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1718055426 598 DTETEAVIQKALD-VVKQGRTTFVIAHRLSTIRN-ADQILVLDKGEI 642
Cdd:TIGR02633 435 DVGAKYEIYKLINqLAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
155-327 |
5.42e-11 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 64.16 E-value: 5.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 155 LYGGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVTVLSTF--- 231
Cdd:cd18602 55 VYAGLSLGAVILSLVTNLAGELAGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLlrf 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 232 ---VTSGIYMFGIFTALFLldvklafvcLAIVPIIWLWSVIYRRY--ASYYNQKIRSI-NSDINAKMNESIQGMTIIQAF 305
Cdd:cd18602 135 lllCLSAIIVNAIVTPYFL---------IALIPIIIVYYFLQKFYraSSRELQRLDNItKSPVFSHFSETLGGLTTIRAF 205
|
170 180
....*....|....*....|....*
gi 1718055426 306 RHQKETMREFEELNESH---FYFQN 327
Cdd:cd18602 206 RQQARFTQQMLELIDRNntaFLFLN 230
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
447-653 |
5.86e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 63.18 E-value: 5.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 447 KHISFTAQKGETVALVGHTGSGKS----SILNLLFRFYDAQKGDVLIDGKSIynmSRQELRS-HMGIVLQDP-YLFSG-- 518
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPV---APCALRGrKIATIMQNPrSAFNPlh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 519 TIGSNVS---------LDDERMTEeeiknALRQVG---AEPLLKKLPkginepviekgSTLSSGERQLISFARALAFDPA 586
Cdd:PRK10418 97 TMHTHARetclalgkpADDATLTA-----ALEAVGlenAARVLKLYP-----------FEMSGGMLQRMMIALALLCEAP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 587 ILILDEATAHIDTETEAVIQKALD--VVKQGRTTFVIAHRLSTI-RNADQILVLDKGEIVEKGNHEELMA 653
Cdd:PRK10418 161 FIIADEPTTDLDVVAQARILDLLEsiVQKRALGMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETLFN 230
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
460-650 |
1.15e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 63.74 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 460 ALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQ-----ELRsHMGIVLQDPYLFSG-TIGSNVSLDDERMTE 533
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGiclppEKR-RIGYVFQDARLFPHyKVRGNLRYGMAKSMV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 534 EEIKNALRQVGAEPLLKKLPkginepviekgSTLSSGERQLISFARALAFDPAILILDEATAHIDT----ETEAVIQKal 609
Cdd:PRK11144 107 AQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrELLPYLER-- 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1718055426 610 dVVKQGRTTFV-IAHRLSTI-RNADQILVLDKGEIVEKGNHEE 650
Cdd:PRK11144 174 -LAREINIPILyVSHSLDEIlRLADRVVVLEQGKVKAFGPLEE 215
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
444-598 |
1.27e-10 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 61.97 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 444 EVLKHISFTAQKGETVALVGHTGSGKSSIlnllfrFY------DAQKGDVLIDGKSIYN--MSRqelRSHMGI--VLQDP 513
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHlpMHK---RARLGIgyLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 514 YLFSG-TIGSNVS--LDDERMTEEEIKNALRQvgaepLLKKLpkGINEPVIEKGSTLSSGERQLISFARALAFDPAILIL 590
Cdd:COG1137 88 SIFRKlTVEDNILavLELRKLSKKEREERLEE-----LLEEF--GITHLRKSKAYSLSGGERRRVEIARALATNPKFILL 160
|
....*...
gi 1718055426 591 DEATAHID 598
Cdd:COG1137 161 DEPFAGVD 168
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
449-642 |
2.01e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.79 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 449 ISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQK-GDVLIDGKSI-YNMSRQELRSHMGIVLQD-------PYLfsgT 519
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPVkIRNPQQAIAQGIAMVPEDrkrdgivPVM---G 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 520 IGSNVSLD--DERMTEEEIKNALRQVGAEPLLKKLPKGINEPVIEKGStLSSGERQLISFARALAFDPAILILDEATAHI 597
Cdd:PRK13549 358 VGKNITLAalDRFTGGSRIDDAAELKTILESIQRLKVKTASPELAIAR-LSGGNQQKAVLAKCLLLNPKILILDEPTRGI 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1718055426 598 DTETEAVIQKAL-DVVKQGRTTFVIAHRLSTIRN-ADQILVLDKGEI 642
Cdd:PRK13549 437 DVGAKYEIYKLInQLVQQGVAIIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
387-644 |
2.13e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 63.65 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 387 TGIVNQFSKLELARVSAGRVFELLEEKNTEEAGQPAKERALgrvEFRDVSfAYQEGEevLKHISFTAQKGETVALVGHTG 466
Cdd:PRK09700 226 SGMVSDVSNDDIVRLMVGRELQNRFNAMKENVSNLAHETVF---EVRNVT-SRDRKK--VRDISFSVCRGEILGFAGLVG 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 467 SGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQE-LRSHMGIVLQD-------------------PYLFSGTIGSNVSL 526
Cdd:PRK09700 300 SGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDaVKKGMAYITESrrdngffpnfsiaqnmaisRSLKDGGYKGAMGL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 527 DDERMtEEEIKNALRQvgaepLLKKLPKGINEPVIEkgstLSSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQ 606
Cdd:PRK09700 380 FHEVD-EQRTAENQRE-----LLALKCHSVNQNITE----LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIY 449
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1718055426 607 KAL-DVVKQGRTTFVIAHRLSTIRNA-DQILVLDKGEIVE 644
Cdd:PRK09700 450 KVMrQLADDGKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
444-659 |
2.91e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 61.20 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 444 EVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRF--YDAQKGDVLIDGKSIYNMSrQELRSHMGIVL--QDPYLFSGT 519
Cdd:CHL00131 21 EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLE-PEERAHLGIFLafQYPIEIPGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 520 -------IGSNVSLDDERMTE-------EEIKNALRQVGAEPLLkkLPKGINEpviekgsTLSSGERQLISFARALAFDP 585
Cdd:CHL00131 100 snadflrLAYNSKRKFQGLPEldpleflEIINEKLKLVGMDPSF--LSRNVNE-------GFSGGEKKRNEILQMALLDS 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1718055426 586 AILILDEATAHIDTETEAVIQKALDVVK-QGRTTFVIAH--RLSTIRNADQILVLDKGEIVEKGNHEELMALEGQYY 659
Cdd:CHL00131 171 ELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGDAELAKELEKKGY 247
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
160-408 |
2.97e-10 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 61.78 E-value: 2.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 160 LVFSVFFQYGQhyllQMSANRIIQKMrqdvFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVTVLSTFVTSGIYMF 239
Cdd:cd18605 60 LLRAFLFAYGG----LRAARRLHNKL----LSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 240 GIFTALFLLdvkLAFVCLAIVPIIwlwsVIYRRYASYY---NQKIRSINSDINAKM----NESIQGMTIIQAFRHQKETM 312
Cdd:cd18605 132 GYLVVICYQ---LPWLLLLLLPLA----FIYYRIQRYYratSRELKRLNSVNLSPLythfSETLKGLVTIRAFRKQERFL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 313 REFEELNEShfyFQNRMLNLNSL---MSHNL----VNVIRNLAFVCLIWHFGGASLNaAGIVSIGVLYA--FVDYLNrlf 383
Cdd:cd18605 205 KEYLEKLEN---NQRAQLASQAAsqwLSIRLqllgVLIVTFVALTAVVQHFFGLSID-AGLIGLALSYAlpITGLLS--- 277
|
250 260
....*....|....*....|....*
gi 1718055426 384 qpitGIVNQFSKLELARVSAGRVFE 408
Cdd:cd18605 278 ----GLLNSFTETEKEMVSVERVRQ 298
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
177-369 |
3.07e-10 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 61.53 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 177 SANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVTVLSTFVTSGIYMFGIFTALFLLDVKLAFVC 256
Cdd:cd18561 63 AAQRVKQHLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALIL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 257 LAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTIIQAFRHQKETMREFEelNESHFYFQNRMLNLN-SL 335
Cdd:cd18561 143 LVFALLIPLSPALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELA--ARAEDLRQATMKVLAvSL 220
|
170 180 190
....*....|....*....|....*....|....*...
gi 1718055426 336 MSHNLVNVIRNLAFVCLI----WHFGGASLNAAGIVSI 369
Cdd:cd18561 221 LSSGIMGLATALGTALALgvgaLRVLGGQLTLSSLLLI 258
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
434-651 |
3.08e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 62.05 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 434 DVSFAYQEGE-EVLKHISFTAQKGETVALVGHTGSGKS----SILNLLfrfydAQ----KGDVLIDGKSIYNMSRQEL-- 502
Cdd:PRK09473 19 RVTFSTPDGDvTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLL-----AAngriGGSATFNGREILNLPEKELnk 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 503 -RS-HMGIVLQD------PYLFSGTIGSNVSLDDERMT-----EEEIK--NALRQVGAEPLLKKLPKginepviekgsTL 567
Cdd:PRK09473 94 lRAeQISMIFQDpmtslnPYMRVGEQLMEVLMLHKGMSkaeafEESVRmlDAVKMPEARKRMKMYPH-----------EF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 568 SSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQKALDVVKQGRTT--FVIAHRLSTIRN-ADQILVLDKGEIVE 644
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaiIMITHDLGVVAGiCDKVLVMYAGRTME 242
|
....*..
gi 1718055426 645 KGNHEEL 651
Cdd:PRK09473 243 YGNARDV 249
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
449-654 |
3.19e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 62.90 E-value: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 449 ISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDV-------LIDGKSIYNMSRQELRSHMGIVLQDPYLFS-GTI 520
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPDGRGRAKRYIGILHQEYDLYPhRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 521 GSNVS------LDDERMTEEEIkNALRQVG-----AEPLLKKLPkginepviekgSTLSSGERQLISFARALAFDPAILI 589
Cdd:TIGR03269 383 LDNLTeaigleLPDELARMKAV-ITLKMVGfdeekAEEILDKYP-----------DELSEGERHRVALAQVLIKEPRIVI 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718055426 590 LDEATAHIDTETE-AVIQKALDVVKQGRTTFVI-AHRLSTIRN-ADQILVLDKGEIVEKGNHEELMAL 654
Cdd:TIGR03269 451 LDEPTGTMDPITKvDVTHSILKAREEMEQTFIIvSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
430-641 |
3.54e-10 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 58.61 E-value: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYqEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLfrfydaqkgdvlidgksiynmsRQELRSHMGIV 509
Cdd:cd03221 1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLI----------------------AGELEPDEGIV 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 510 LQDPYLfsgTIGSnvslddermteeeiknaLRQvgaepllkklpkginepviekgstLSSGERQLISFARALAFDPAILI 589
Cdd:cd03221 58 TWGSTV---KIGY-----------------FEQ------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1718055426 590 LDEATAHIDTETEAVIQKALdvVKQGRTTFVIAHRLSTIRN-ADQILVLDKGE 641
Cdd:cd03221 94 LDEPTNHLDLESIEALEEAL--KEYPGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
180-376 |
4.51e-10 |
|
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: 61.34 E-value: 4.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 180 RIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVTVLSTFVTSGIYMFGIFTALFLLDVKLAFVCLAI 259
Cdd:cd18585 65 RLLSNLRVWFYRKLEPLAPARLQKYRSGDLLNRIVADIDTLDNLYLRVLSPPVVALLVILATILFLAFFSPALALILLAG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 260 VPI-IWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTIIQAFRHQKETMREFEELNESHFYFQNRMLNLNSLmSH 338
Cdd:cd18585 145 LLLaGVVIPLLFYRLGKKIGQQLVQLRAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGL-SQ 223
|
170 180 190
....*....|....*....|....*....|....*...
gi 1718055426 339 NLVNVIRNLAFVCLIWHfgGASLNAAGIVSiGVLYAFV 376
Cdd:cd18585 224 ALMILLSGLTVWLVLWL--GAPLVQNGALD-GALLAML 258
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
429-651 |
4.84e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 60.80 E-value: 4.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 429 RVEFRDVSFAYQEGeevLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQK---GDVLIDGKSIYNMSR-----Q 500
Cdd:PRK09984 6 RVEKLAKTFNQHQA---LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQREGRlardiR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 501 ELRSHMGIVLQDPYLFS----------GTIGSNVSLDD-----ERMTEEEIKNALRQVGAEPLLKklpkginepviEKGS 565
Cdd:PRK09984 83 KSRANTGYIFQQFNLVNrlsvlenvliGALGSTPFWRTcfswfTREQKQRALQALTRVGMVHFAH-----------QRVS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 566 TLSSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQKALDVVKQ--GRTTFVIAHRLS-TIRNADQILVLDKGEI 642
Cdd:PRK09984 152 TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGHV 231
|
....*....
gi 1718055426 643 VEKGNHEEL 651
Cdd:PRK09984 232 FYDGSSQQF 240
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
448-651 |
6.80e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 60.00 E-value: 6.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 448 HISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELrSHMGIV--LQDPYLF-SGTIGSNV 524
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI-ARMGVVrtFQHVRLFrEMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 525 SLDDERMTEEEIKNAL------RQVGAEPL------LKKLpkGINEPVIEKGSTLSSGERQLISFARALAFDPAILILDE 592
Cdd:PRK11300 102 LVAQHQQLKTGLFSGLlktpafRRAESEALdraatwLERV--GLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1718055426 593 ATAHIDTETEAVIQKALDVVKQ--GRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKGNHEEL 651
Cdd:PRK11300 180 PAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
442-643 |
7.49e-10 |
|
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: 61.76 E-value: 7.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 442 GEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFY--DAQKGDVLIDGKSIYNMS-RQELRSHMGIVLQDPYLFSG 518
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNiRDTERAGIVIIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 519 -TIGSNVSLDDE------RMTEEEI----KNALRQVgaepllkKLPkgiNEPVIEKGSTLSSGERQLISFARALAFDPAI 587
Cdd:TIGR02633 93 lSVAENIFLGNEitlpggRMAYNAMylraKNLLREL-------QLD---ADNVTRPVGDYGGGQQQLVEIAKALNKQARL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1718055426 588 LILDEATAHIdteTEAVIQKALDVVK----QGRTTFVIAHRLSTIRN-ADQILVLDKGEIV 643
Cdd:TIGR02633 163 LILDEPSSSL---TEKETEILLDIIRdlkaHGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
179-378 |
1.29e-09 |
|
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: 59.79 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 179 NRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVTVLSTF---VTSGIYMFGIftaLFLLDVKLAFV 255
Cdd:cd18589 65 SRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLmwyLARGLFLFIF---MLWLSPKLALL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 256 CLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTIIQAFRHQK-ETMREFEELNESHfyfqnrMLNLNS 334
Cdd:cd18589 142 TALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEgEAQRYRQRLQKTY------RLNKKE 215
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1718055426 335 LMSHNL---VNVIRNLAFVCLIWHFGGaSLNAAGIVSIGVLYAFVDY 378
Cdd:cd18589 216 AAAYAVsmwTSSFSGLALKVGILYYGG-QLVTAGTVSSGDLVTFVLY 261
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
444-642 |
1.46e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.83 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 444 EVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQElRSHMGIVL-----QDPYLF-S 517
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-RLARGLVYlpedrQSSGLYlD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 518 GTIGSNV-SLDDERM---TEEEIKNAL-----RQVGAepllkKLpKGINEPViekgSTLSSGERQLISFARALAFDPAIL 588
Cdd:PRK15439 356 APLAWNVcALTHNRRgfwIKPARENAVleryrRALNI-----KF-NHAEQAA----RTLSGGNQQKVLIAKCLEASPQLL 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1718055426 589 ILDEATAHIDTETEAVIQKAL-DVVKQGRTTFVIAHRLSTIRN-ADQILVLDKGEI 642
Cdd:PRK15439 426 IVDEPTRGVDVSARNDIYQLIrSIAAQNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
139-324 |
2.39e-09 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 59.11 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 139 FQFYQpeikgMVLLICLyGGLLVFSVFFQYGQHYLLQMSANRIIQKMrqdvFSHIQRMPIRYFDNLPAGKVVARITNDTE 218
Cdd:cd18599 57 LNFYQ-----LVYGGSI-LVILLLSLIRGFVFVKVTLRASSRLHNKL----FQKILRSPMSFFDTTPTGRILNRFSKDLD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 219 AIrDLYV-TVLSTFVtsgIYMFGIFTALFLLDVKLAFVCLAIVPIIWLWSVIYRryasYYNQKIRSIN-------SDINA 290
Cdd:cd18599 127 EV-DVRLpFTLENFL---QNVLLVVFSLIIIAIVFPWFLIALIPLAIIFVFLSK----IFRRAIRELKrlenisrSPLFS 198
|
170 180 190
....*....|....*....|....*....|....*..
gi 1718055426 291 KMNESIQGMTIIQAFRHQKETMREFEEL---NESHFY 324
Cdd:cd18599 199 HLTATIQGLSTIHAFNKEKEFLSKFKKLldqNSSAFF 235
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
442-651 |
2.54e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.13 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 442 GEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSI-YNMSRQELRSHMGIVLQDPYLF-SGT 519
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdFKSSKEALENGISMVHQELNLVlQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 520 IGSNVSL----------DDERMTEEEIKnalrqvgaepLLKKLpkGINEPVIEKGSTLSSGERQLISFARALAFDPAILI 589
Cdd:PRK10982 90 VMDNMWLgryptkgmfvDQDKMYRDTKA----------IFDEL--DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718055426 590 LDEATAHIdTETEA-----VIQKaldVVKQGRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKGNHEEL 651
Cdd:PRK10982 158 MDEPTSSL-TEKEVnhlftIIRK---LKERGCGIVYISHKMEEIFQlCDEITILRDGQWIATQPLAGL 221
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
430-653 |
2.55e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 59.43 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGEEVLK---HISFTAQKGETVALVGHTGSGKSSILNLL--------------FRFYDaqkgdvlIDGK 492
Cdd:PRK15093 4 LDIRNLTIEFKTSDGWVKavdRVSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtkdnwrvtadrMRFDD-------IDLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 493 SIYNMSRQELRSH-MGIVLQDPylfsgtigsNVSLDDERMTEEEIKNAL---------------RQVGAEPLLKKLpkGI 556
Cdd:PRK15093 77 RLSPRERRKLVGHnVSMIFQEP---------QSCLDPSERVGRQLMQNIpgwtykgrwwqrfgwRKRRAIELLHRV--GI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 557 NEPVIEKGS---TLSSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQKALDVVKQ--GRTTFVIAHRLSTIRN- 630
Cdd:PRK15093 146 KDHKDAMRSfpyELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLSQw 225
|
250 260
....*....|....*....|...
gi 1718055426 631 ADQILVLDKGEIVEKGNHEELMA 653
Cdd:PRK15093 226 ADKINVLYCGQTVETAPSKELVT 248
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
449-651 |
2.64e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 59.37 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 449 ISFTAQKGETVALVGHTGSGKS----SILNLLFRFYDAQKGDVLIDGKSIYNMSRQELR----SHMGIVLQDPYLF---S 517
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRnlvgAEVAMIFQDPMTSlnpC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 518 GTIGSNVsLDDERMTEEEIKNALRQVGAEpLLKKLpkGINEPVIEKG---STLSSGERQLISFARALAFDPAILILDEAT 594
Cdd:PRK11022 106 YTVGFQI-MEAIKVHQGGNKKTRRQRAID-LLNQV--GIPDPASRLDvypHQLSGGMSQRVMIAMAIACRPKLLIADEPT 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 595 AHIDTETEA-VIQKALDVVKQGRTTFV-IAHRLSTI-RNADQILVLDKGEIVEKGNHEEL 651
Cdd:PRK11022 182 TALDVTIQAqIIELLLELQQKENMALVlITHDLALVaEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
421-654 |
3.50e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.80 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 421 PAKERALGRVEFR----DVSFAYQEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLF-RFYDAQ-KGDVLIDGKSI 494
Cdd:NF040905 247 PERTPKIGEVVFEvknwTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgRSYGRNiSGTVFKDGKEV 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 495 --YNMSR---------QELRSHMGIVLQDpylfsgTIGSNVSL------------DD--ERMTEEEIKNALRqvgaepll 549
Cdd:NF040905 327 dvSTVSDaidaglayvTEDRKGYGLNLID------DIKRNITLanlgkvsrrgviDEneEIKVAEEYRKKMN-------- 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 550 kklpkgINEP-VIEKGSTLSSGERQLISFARALAFDPAILILDEATAHIDT----ETEAVIQkalDVVKQGRTTFVIAHR 624
Cdd:NF040905 393 ------IKTPsVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVgakyEIYTIIN---ELAAEGKGVIVISSE 463
|
250 260 270
....*....|....*....|....*....|....*.
gi 1718055426 625 L-STIRNADQILVLDKGEIV-----EKGNHEELMAL 654
Cdd:NF040905 464 LpELLGMCDRIYVMNEGRITgelprEEASQERIMRL 499
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
434-653 |
4.33e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.51 E-value: 4.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 434 DVSFAYQEgEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQ--KGDVLIDGKSIynmSRQELRsHMGIVLQ 511
Cdd:PLN03211 73 DETRQIQE-RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKP---TKQILK-RTGFVTQ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 512 D----PYLFSGTIGSNVSLD--DERMTEEEIKNALRQVGAEPLLKKLPKGINEPVIEKGstLSSGERQLISFARALAFDP 585
Cdd:PLN03211 148 DdilyPHLTVRETLVFCSLLrlPKSLTKQEKILVAESVISELGLTKCENTIIGNSFIRG--ISGGERKRVSIAHEMLINP 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1718055426 586 AILILDEATAHID-TETEAVIQKALDVVKQGRTTFVIAHRLST--IRNADQILVLDKGEIVEKGNHEELMA 653
Cdd:PLN03211 226 SLLILDEPTSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
441-659 |
4.71e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.49 E-value: 4.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 441 EGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLF--RFYDAQKGDVLIDGKSIYNMSRQElRSHMGIVL--QDPYLF 516
Cdd:PRK09580 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPED-RAGEGIFMafQYPVEI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 517 SGTigSNvslddeRMTEEEIKNALRQV-GAEPL--------------LKKLPKGINEPVIEKGstLSSGERQLISFARAL 581
Cdd:PRK09580 91 PGV--SN------QFFLQTALNAVRSYrGQEPLdrfdfqdlmeekiaLLKMPEDLLTRSVNVG--FSGGEKKRNDILQMA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 582 AFDPAILILDEATAHIDTETEAVIQKALDVVKQGRTTFVIAHRLSTIRN---ADQILVLDKGEIVEKGNHEELMALEGQY 658
Cdd:PRK09580 161 VLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDyikPDYVHVLYQGRIVKSGDFTLVKQLEEQG 240
|
.
gi 1718055426 659 Y 659
Cdd:PRK09580 241 Y 241
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
423-650 |
5.82e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.77 E-value: 5.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 423 KERALG--RVEFRDVSfayqeGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSI-YNMSR 499
Cdd:PRK11288 249 RPRPLGevRLRLDGLK-----GPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIdIRSPR 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 500 QELRShmGIVL--QDPYlFSGTIGS-------NVS-----------LDDERmteeEIKNALRQVGAepLLKKLPkGINEP 559
Cdd:PRK11288 324 DAIRA--GIMLcpEDRK-AEGIIPVhsvadniNISarrhhlragclINNRW----EAENADRFIRS--LNIKTP-SREQL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 560 VIekgsTLSSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQKAL-DVVKQGRTTFVIAHRLSTIRN-ADQILVL 637
Cdd:PRK11288 394 IM----NLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIyELAAQGVAVLFVSSDLPEVLGvADRIVVM 469
|
250
....*....|...
gi 1718055426 638 DKGEIVEKGNHEE 650
Cdd:PRK11288 470 REGRIAGELAREQ 482
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
455-639 |
6.05e-09 |
|
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: 55.07 E-value: 6.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 455 KGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIdgksiynmsrqelrshmgivlqdpylfsgtigsnvsLDDERMTEE 534
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY------------------------------------IDGEDILEE 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 535 EIKNALrqvgaepllkklpkgiNEPVIEKGSTLSSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQKALDV--- 611
Cdd:smart00382 45 VLDQLL----------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrll 108
|
170 180 190
....*....|....*....|....*....|..
gi 1718055426 612 ----VKQGRTTFVIAHRLSTIRNADQILVLDK 639
Cdd:smart00382 109 lllkSEKNLTVILTTNDEKDLGPALLRRRFDR 140
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
442-646 |
7.35e-09 |
|
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: 59.26 E-value: 7.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 442 GEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIyNMSRQELRSHMGIVLQDPYLFSGTIG 521
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHLTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 522 SNVSLDDERMTEEEIKNAlrQVGAEPLLKKlpKGINEPVIEKGSTLSSGERQLISFARALAFDPAILILDEATAHIDTET 601
Cdd:TIGR01257 1021 AEHILFYAQLKGRSWEEA--QLEMEAMLED--TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1718055426 602 EAVIQKALDVVKQGRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKG 646
Cdd:TIGR01257 1097 RRSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSG 1142
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
136-385 |
1.19e-08 |
|
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: 56.85 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 136 QELFQFYQPEIKGMVLLICLYGGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITN 215
Cdd:cd18560 24 NALTLAKVKDLESAVTLILLYALLRFSSKLLKELRSLLYRRVQQNAYRELSLKTFAHLHSLSLDWHLSKKTGEVVRIMDR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 216 DTEAIRDL--YV------TVLSTFVTSGI--YMFGIFTALFLLdvkLAFVCLAIVPI-IWLWSVIYRRYAsyyNQKirsi 284
Cdd:cd18560 104 GTESANTLlsYLvfylvpTLLELIVVSVVfaFHFGAWLALIVF---LSVLLYGVFTIkVTEWRTKFRRAA---NKK---- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 285 NSDINAKMNESIQGMTIIQAFRHQKETMREFEELNESHFYFQNRMLNLNSLMSHnLVNVIRNLA-FVCLIWhfgGASLNA 363
Cdd:cd18560 174 DNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNV-GQQLIIQLGlTLGLLL---AGYRVV 249
|
250 260
....*....|....*....|..
gi 1718055426 364 AGIVSIGVLYAFVDYLNRLFQP 385
Cdd:cd18560 250 DGGLSVGDFVAVNTYIFQLFQP 271
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
445-652 |
1.75e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 55.99 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 445 VLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQ--------KGDVLIDGKSIYNMSRQEL---RSHMGIVLQDP 513
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLarlRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 514 YLFSgtIGSNVSL----------DDERMTEEEIKNALRQVGAEPLLKKlpkginepvieKGSTLSSGERQLISFARALA- 582
Cdd:PRK13547 96 FAFS--AREIVLLgrypharragALTHRDGEIAWQALALAGATALVGR-----------DVTTLSGGELARVQFARVLAq 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 583 --------FDPAILILDEATAHIDTETEaviQKALDVVKQ-------GRTTFVIAHRLSTiRNADQILVLDKGEIVEKGN 647
Cdd:PRK13547 163 lwpphdaaQPPRYLLLDEPTAALDLAHQ---HRLLDTVRRlardwnlGVLAIVHDPNLAA-RHADRIAMLADGAIVAHGA 238
|
....*
gi 1718055426 648 HEELM 652
Cdd:PRK13547 239 PADVL 243
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
184-406 |
2.25e-08 |
|
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: 56.17 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 184 KMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVTVLSTFVTSGIYMFGIFTALFLLDVKLAFVCLAIVPII 263
Cdd:cd18784 70 RIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 264 WLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTIIQAFRHQKETMREFEELNeshfyfqNRMLNLN-----SLMSH 338
Cdd:cd18784 150 AIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKL-------KDTYKLKikealAYGGY 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1718055426 339 NLVNVIRNLAFVCLIWHFGGaSLNAAGIVSIGVLYAFVDYLNRLFQPITGIVNQFSKLELARVSAGRV 406
Cdd:cd18784 223 VWSNELTELALTVSTLYYGG-HLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
112-322 |
2.44e-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: 56.13 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 112 VSDGKLTITNGDKSRTYAAEKLTKQElfqfyqpeiKGMVLLICLYGGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFS 191
Cdd:cd18558 30 TNGGMTNITGNSSGLNSSAGPFEKLE---------EEMTLYAYYYLIIGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 192 HIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVTVLSTFVTSGIYMFGIFTALFLLDVKLAFVCLAIVPIIWLWSVIYR 271
Cdd:cd18558 101 AIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1718055426 272 RYASYYNQKIRSINSDINAKMNESIQGM-TIIQAFRHQKETMREFEELNESH 322
Cdd:cd18558 181 KILSGFTDKEKKAYAKAGAVAEEVLEAFrTVIAFGGQQKEETRYAQNLEIAK 232
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
156-408 |
2.78e-08 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 55.79 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 156 YGGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVTVLSTFVTSG 235
Cdd:cd18601 65 YAGLTAATFVFGFLRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 236 IYMFGIftaLFLLDVKLAFVCLAIVPIIWLWSVIyRRY---ASYYNQKIRSIN-SDINAKMNESIQGMTIIQAFRHQKET 311
Cdd:cd18601 145 LQVVGV---VLLAVVVNPWVLIPVIPLVILFLFL-RRYylkTSREVKRIEGTTrSPVFSHLSSTLQGLWTIRAYSAQERF 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 312 MREFEELNESH----FYF--QNRMLNLN-SLMSHNLVNVIrnlAFVCLiwhFGGASLNaAGIVSIGVLYAFvdYLNRLFQ 384
Cdd:cd18601 221 QEEFDAHQDLHseawFLFlaTSRWLAVRlDALCALFVTVV---AFGSL---FLAESLD-AGLVGLSLSYAL--TLMGTFQ 291
|
250 260
....*....|....*....|....
gi 1718055426 385 pitGIVNQFSKLELARVSAGRVFE 408
Cdd:cd18601 292 ---WCVRQSAEVENLMTSVERVLE 312
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
150-322 |
3.97e-08 |
|
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: 55.11 E-value: 3.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 150 VLLICLYGGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVTVLS 229
Cdd:cd18584 37 LPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARLLALGPALLRRQSSGELATLLTEGVDALDGYFARYLP 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 230 TFVTSGIYMFGIFTALFLLDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQK-IRSINSdINAKMNESIQGMTIIQAFRHQ 308
Cdd:cd18584 117 QLVLAAIVPLLILVAVFPLDWVSALILLVTAPLIPLFMILIGKAAQAASRRqWAALSR-LSGHFLDRLRGLPTLKLFGRA 195
|
170
....*....|....
gi 1718055426 309 KETMREFEELNESH 322
Cdd:cd18584 196 RAQAARIARASEDY 209
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
455-638 |
6.73e-08 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 53.95 E-value: 6.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 455 KGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSI----------YNMS-RQELRSHMGIVLQDPYLfsgtigsn 523
Cdd:cd03237 24 ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsykpqyikadYEGTvRDLLSSITKDFYTHPYF-------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 524 vslddermtEEEIKNALrqvGAEPLL-KKLPkginepviekgsTLSSGERQLISFARALAFDPAILILDEATAHIDTETE 602
Cdd:cd03237 96 ---------KTEIAKPL---QIEQILdREVP------------ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 1718055426 603 AVIQKALD--VVKQGRTTFVIAHRLSTIRN-ADQILVLD 638
Cdd:cd03237 152 LMASKVIRrfAENNEKTAFVVEHDIIMIDYlADRLIVFE 190
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
149-405 |
1.53e-07 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). 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. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 53.38 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 149 MVLLICLYGGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPiryFDNLPAGkvvaritNDTEAIRDLyvTVL 228
Cdd:cd18586 41 LLGLTLGMVVLLAFDGLLRQVRSRILQRVGLRLDVELGRRVFRAVLELP---LESRPSG-------YWQQLLRDL--DTL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 229 STFVTSGIYM-------FGIFTA-LFLLDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMT 300
Cdd:cd18586 109 RNFLTGPSLFaffdlpwAPLFLAvIFLIHPPLGWVALVGAPVLVGLAWLNHRATRKPLGEANEAQAARDALAAETLRNAE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 301 IIQAFRHQKETMREFEELNESHFYFQNRMLNLNSLMShNLVNVIRNLAFVCLIwhFGGASLNAAGIVSIGVLYAFVDYLN 380
Cdd:cd18586 189 TIKALGMLGNLRRRWEARHAETLELQIRASDLAGAIS-AIGKTLRMALQSLIL--GVGAYLVIDGELTIGALIAASILSG 265
|
250 260
....*....|....*....|....*
gi 1718055426 381 RLFQPITGIVNQFSKLELARVSAGR 405
Cdd:cd18586 266 RALAPIDQLVGAWKQLSAARQAYER 290
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
442-610 |
1.68e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 52.11 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 442 GEEVL-KHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIyNMSRQELRSHM-------GIvlqDP 513
Cdd:PRK13538 12 DERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI-RRQRDEYHQDLlylghqpGI---KT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 514 YL-------FSGTIGSNVSlddermtEEEIKNALRQVGA---EPLlkklpkginePViekgSTLSSGERQLISFARALAF 583
Cdd:PRK13538 88 ELtalenlrFYQRLHGPGD-------DEALWEALAQVGLagfEDV----------PV----RQLSAGQQRRVALARLWLT 146
|
170 180
....*....|....*....|....*...
gi 1718055426 584 DPAILILDEA-TAhIDTETEAVIQKALD 610
Cdd:PRK13538 147 RAPLWILDEPfTA-IDKQGVARLEALLA 173
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
444-651 |
2.20e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 53.17 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 444 EVLKHISFTAQKGETVALVGHTGSGKSSILNLLfrfydA-----QKGDVLIDGKSIYNmSRQELRSHMGIV--------- 509
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKML-----TgilvpTSGEVRVLGYVPFK-RRKEFARRIGVVfgqrsqlww 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 510 ---LQDPYLFSGTIgsnvslddERMTEEEIKNALRQV----GAEPLLKKlpkginePViekgSTLSSGERQLISFARALA 582
Cdd:COG4586 110 dlpAIDSFRLLKAI--------YRIPDAEYKKRLDELvellDLGELLDT-------PV----RQLSLGQRMRCELAAALL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1718055426 583 FDPAILILDEATAHIDTETEAVIQKAL-DVVKQGRTTFVIA-HRLSTIRN-ADQILVLDKGEIVEKGNHEEL 651
Cdd:COG4586 171 HRPKILFLDEPTIGLDVVSKEAIREFLkEYNRERGTTILLTsHDMDDIEAlCDRVIVIDHGRIIYDGSLEEL 242
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
566-651 |
2.63e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 54.25 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 566 TLSSGERQLISFARAL---AFDPAILILDEATA--HIDTeteavIQKALDV----VKQGRTTFVIAHRLSTIRNADQILV 636
Cdd:TIGR00630 829 TLSGGEAQRIKLAKELskrSTGRTLYILDEPTTglHFDD-----IKKLLEVlqrlVDKGNTVVVIEHNLDVIKTADYIID 903
|
90 100
....*....|....*....|.
gi 1718055426 637 L-----DK-GEIVEKGNHEEL 651
Cdd:TIGR00630 904 LgpeggDGgGTVVASGTPEEV 924
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
430-592 |
4.32e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 52.54 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 430 VEFRDVSFAYQEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQE-------- 501
Cdd:PRK11650 4 LKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADrdiamvfq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 502 ---LRSHMgivlqdpylfsgTIGSNVS--LDDERMTEEEI----KNALRQVGAEPLLKKLPKginepviekgsTLSSGER 572
Cdd:PRK11650 84 nyaLYPHM------------SVRENMAygLKIRGMPKAEIeervAEAARILELEPLLDRKPR-----------ELSGGQR 140
|
170 180
....*....|....*....|
gi 1718055426 573 QLISFARALAFDPAILILDE 592
Cdd:PRK11650 141 QRVAMGRAIVREPAVFLFDE 160
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
429-638 |
4.45e-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: 53.21 E-value: 4.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 429 RVEFRDVSFAYQEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLI--DGKSIYnmsrqelrshm 506
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKpaKGKLFY----------- 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 507 giVLQDPYLFSGTIGSNV----SLDDER---MTEEEIKNALRQVGAEPLLKKlpKGINEPVIEKGSTLSSGERQLISFAR 579
Cdd:TIGR00954 520 --VPQRPYMTLGTLRDQIiypdSSEDMKrrgLSDKDLEQILDNVQLTHILER--EGGWSAVQDWMDVLSGGEKQRIAMAR 595
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1718055426 580 ALAFDPAILILDEATAHIDTETEAVIQKALDvvKQGRTTFVIAHRLSTIRNADQILVLD 638
Cdd:TIGR00954 596 LFYHKPQFAILDECTSAVSVDVEGYMYRLCR--EFGITLFSVSHRKSLWKYHEYLLYMD 652
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
158-320 |
4.81e-07 |
|
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: 51.78 E-value: 4.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 158 GLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDLYVTVLSTFVTSGIY 237
Cdd:cd18574 50 GLYLLQSLLTFAYISLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 238 MFGIFTALFLLDVKLAFVCLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTIIQAFRHQKETMREFEE 317
Cdd:cd18574 130 TVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEE 209
|
...
gi 1718055426 318 LNE 320
Cdd:cd18574 210 EVE 212
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
172-402 |
6.82e-07 |
|
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.
Pssm-ID: 350031 Cd Length: 293 Bit Score: 51.28 E-value: 6.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 172 YLLQMSANRIIQKMRQDVFSHIQRMPiryFDNLPA--GKVVARItNDTEAIRDlyvtvlstFVTSGIyMFGI----FTAL 245
Cdd:cd18587 64 YFIDVAGKRADVILSSRLFERVLGLR---LEARPAsvGSFANNL-REFESVRD--------FFTSAT-LTALidlpFVLL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 246 FLLDV-----KLAFVCLAIVPIIWLWSVIYRRYASYYNQKIRSINSDINAKMNESIQGMTIIQAFRHQKETMREFEELNE 320
Cdd:cd18587 131 FLAVIaliggPLALVPLVAIPLVLLYGLLLQKPLRRLVEESMRESAQKNALLVESLSGLETIKALGAEGRMQRRWEEAVA 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 321 SHFYFQNRMLNLNSLMShNLVNVIRNLAFVCLIwhFGGASLNAAGIVSIGVLYAFVDYLNRLFQPITGIVNQFSKLELAR 400
Cdd:cd18587 211 ALARSSLKSRLLSSSAT-NFAQFVQQLVTVAIV--IVGVYLISDGELTMGGLIACVILSGRALAPLGQIAGLLTRYQQAR 287
|
..
gi 1718055426 401 VS 402
Cdd:cd18587 288 TA 289
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
434-632 |
9.04e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.95 E-value: 9.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 434 DVSFAYQEgEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSI------YNMSRQELRSHMG 507
Cdd:PRK13540 6 ELDFDYHD-QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkkdlctYQKQLCFVGHRSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 508 IvlqDPYLfsgTIGSNVSLD-DERMTEEEIKNALRQVGAEPLLkKLPKGInepviekgstLSSGERQLISFARALAFDPA 586
Cdd:PRK13540 85 I---NPYL---TLRENCLYDiHFSPGAVGITELCRLFSLEHLI-DYPCGL----------LSSGQKRQVALLRLWMSKAK 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1718055426 587 ILILDEATAHIDTET-EAVIQKALDVVKQGRTTFVIAHRLSTIRNAD 632
Cdd:PRK13540 148 LWLLDEPLVALDELSlLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
446-652 |
1.11e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.58 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 446 LKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSiynmsrqelrshmgivlqdpylfsGTIGSNVS 525
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEV------------------------SVIAISAG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 526 LDDERMTEEEIKNALRQVGAEPL-LKKL-PKGIN-----EPVIEKGSTLSSGERQLISFARALAFDPAILILDEATAHID 598
Cdd:PRK13546 96 LSGQLTGIENIEFKMLCMGFKRKeIKAMtPKIIEfselgEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1718055426 599 -TETEAVIQKALDVVKQGRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKGNHEELM 652
Cdd:PRK13546 176 qTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVL 231
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
450-653 |
1.37e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.17 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 450 SFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQELRShmgiVLQDPYLFSGTIGSNVSLDDE 529
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQK----LVSDEWQRNNTDMLSPGEDDT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 530 RMTEEEI------KNAL-----RQVGAEPLLKKLPKginepviekgsTLSSGERQLISFARALAFDPAILILDEATAHID 598
Cdd:PRK10938 99 GRTTAEIiqdevkDPARceqlaQQFGITALLDRRFK-----------YLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1718055426 599 TETEAVIQKAL-DVVKQGRTTFVIAHRLSTIRN-ADQILVLDKGEIVEKGNHEELMA 653
Cdd:PRK10938 168 VASRQQLAELLaSLHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQ 224
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
446-653 |
1.73e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.16 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 446 LKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQ-----------ELRSHMGIVLqdpy 514
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdglangivyisEDRKRDGLVL---- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 515 lfSGTIGSNVSL---------------DDERMTEEEIKNALRqvgaepllkklpkgINEPVIEKG-STLSSGERQLISFA 578
Cdd:PRK10762 344 --GMSVKENMSLtalryfsraggslkhADEQQAVSDFIRLFN--------------IKTPSMEQAiGLLSGGNQQKVAIA 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 579 RALAFDPAILILDEATAHIDTETEAVIQKALDVVKQ-GRTTFVIAHRLSTIRN-ADQILVLDKGEI-----VEKGNHEEL 651
Cdd:PRK10762 408 RGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAeGLSIILVSSEMPEVLGmSDRILVMHEGRIsgeftREQATQEKL 487
|
..
gi 1718055426 652 MA 653
Cdd:PRK10762 488 MA 489
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
446-658 |
2.08e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.88 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 446 LKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNMSRQEL-----------RSHMGIVLQDPY 514
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAinhgfalvteeRRSTGIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 515 LFSGTIgSNVS--------LDDERMTEEE--IKNALRQvgaepllkKLPKgiNEPVIekgSTLSSGERQLISFARALAFD 584
Cdd:PRK10982 344 GFNSLI-SNIRnyknkvglLDNSRMKSDTqwVIDSMRV--------KTPG--HRTQI---GSLSGGNQQKVIIGRWLLTQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 585 PAILILDEATAHIDTETEAVI-QKALDVVKQGRTTFVIAHRLSTIRN-ADQILVLDKGE---IVE--KGNHEELMALEGQ 657
Cdd:PRK10982 410 PEILMLDEPTRGIDVGAKFEIyQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLvagIVDtkTTTQNEILRLASL 489
|
.
gi 1718055426 658 Y 658
Cdd:PRK10982 490 H 490
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
431-601 |
3.19e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.33 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 431 EFRDVSFAYqEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGK---SIYNMSRQELrshmg 507
Cdd:PRK11147 321 EMENVNYQI-DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlevAYFDQHRAEL----- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 508 ivlqDPylfSGTIGSNVSlddERMTEEEIKNALRQVgaeplLKKL------PKGINEPViekgSTLSSGERQLISFARaL 581
Cdd:PRK11147 395 ----DP---EKTVMDNLA---EGKQEVMVNGRPRHV-----LGYLqdflfhPKRAMTPV----KALSGGERNRLLLAR-L 454
|
170 180
....*....|....*....|.
gi 1718055426 582 AFDPA-ILILDEATAHIDTET 601
Cdd:PRK11147 455 FLKPSnLLILDEPTNDLDVET 475
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
359-633 |
4.34e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.63 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 359 ASLNAAGIvsigvlyAFVDYLNRlFQPITGIVNQFSKL-ELARVSAGRVFELLEE------KNTE--------EAGQPAK 423
Cdd:PRK10938 179 ASLHQSGI-------TLVLVLNR-FDEIPDFVQFAGVLaDCTLAETGEREEILQQalvaqlAHSEqlegvqlpEPDEPSA 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 424 ERALG----RVEFRDVSFAYQEgEEVLKHISFTAQKGETVALVGHTGSGKSSILNLL-----------FRFYDAQKGDvl 488
Cdd:PRK10938 251 RHALPanepRIVLNNGVVSYND-RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysndLTLFGRRRGS-- 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 489 idGKSIYnmsrqELRSHMGIV---LQDPYLFSGTIgSNVSLD---DERMTEEEIKNALRQVgAEPLLKKLpkGINEPVIE 562
Cdd:PRK10938 328 --GETIW-----DIKKHIGYVsssLHLDYRVSTSV-RNVILSgffDSIGIYQAVSDRQQKL-AQQWLDIL--GIDKRTAD 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 563 KG-STLSSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQKALDV-VKQGRTT--FV----------IAHRLSTI 628
Cdd:PRK10938 397 APfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQllFVshhaedapacITHRLEFV 476
|
....*
gi 1718055426 629 RNADQ 633
Cdd:PRK10938 477 PDGDI 481
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
435-657 |
5.00e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 49.55 E-value: 5.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 435 VSFAYQEGEEVLKHISFTAQKGETVALVGHTGSGKSSILNLLfrfydaqKGdvlIDgKSIYNMSRQELRSHMGIVLQDPY 514
Cdd:TIGR03719 10 VSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AG---VD-KDFNGEARPQPGIKVGYLPQEPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 515 L-FSGTIGSNV---------------------SLDDERMTE-----EEIKNALRQVGAEPLLKKL---------PKGiNE 558
Cdd:TIGR03719 79 LdPTKTVRENVeegvaeikdaldrfneisakyAEPDADFDKlaaeqAELQEIIDAADAWDLDSQLeiamdalrcPPW-DA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 559 PViekgSTLSSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQKALDVVKQgrTTFVIAHRLSTIRNADQ-ILVL 637
Cdd:TIGR03719 158 DV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG--TVVAVTHDRYFLDNVAGwILEL 231
|
250 260
....*....|....*....|....*...
gi 1718055426 638 DKGE-IVEKGNH-------EELMALEGQ 657
Cdd:TIGR03719 232 DRGRgIPWEGNYsswleqkQKRLEQEEK 259
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
173-406 |
5.34e-06 |
|
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and similar proteins; This group includes the 6-TMD of an uncharacterized peptidase-containing ABC transporter of T1SS (type 1 secretion systems), similar to heterocyst differentiation protein HetC. HetC is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350015 [Multi-domain] Cd Length: 294 Bit Score: 48.59 E-value: 5.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 173 LLQMSaNRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARItNDTEAIRD-LYVTVLSTFVTsgIYMFGIFTA-LFLLDV 250
Cdd:cd18571 66 LLHIS-SRINISIISDFLIKLMRLPISFFDTKMTGDILQRI-NDHSRIESfLTSSSLSILFS--LLNLIVFSIvLAYYNL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 251 K--LAFVCLAIVPIIWLWSVIYRRyaSYYNQKIRSINSDINAKMNESIQGMTIIQAFRHQKETMREFEELNESHFYFQNR 328
Cdd:cd18571 142 TifLIFLIGSVLYILWILLFLKKR--KKLDYKRFDLSSENQSKLIELINGMQEIKLNNSERQKRWEWERIQAKLFKINIK 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 329 MLNLNSLMS--HNLVNVIRNLA--FVCliwhfggASLNAAGIVSIGVLYAfVDY-LNRLFQPITGIVNQFSKLELARVSA 403
Cdd:cd18571 220 SLKLDQYQQigALFINQLKNILitFLA-------AKLVIDGEITLGMMLA-IQYiIGQLNSPIEQLIGFIQSLQDAKISL 291
|
...
gi 1718055426 404 GRV 406
Cdd:cd18571 292 ERL 294
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
445-657 |
9.24e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 47.80 E-value: 9.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 445 VLKHISFTAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKsiynmsrqeLRshMGIVLQDPYLfsgtiGSNV 524
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IGYVPQKLYL-----DTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 525 SLDDER-------MTEEEIKNALRQVGAEPLLkklpkgiNEPViekgSTLSSGERQLISFARALAFDPAILILDEATAHI 597
Cdd:PRK09544 83 PLTVNRflrlrpgTKKEDILPALKRVQAGHLI-------DAPM----QKLSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1718055426 598 DTETeaviQKAL-DVVKQGRTT-----FVIAHRLSTIR-NADQILVLDKG-------EIVEKgnHEELMALEGQ 657
Cdd:PRK09544 152 DVNG----QVALyDLIDQLRREldcavLMVSHDLHLVMaKTDEVLCLNHHiccsgtpEVVSL--HPEFISMFGP 219
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
566-658 |
1.56e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 48.15 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 566 TLSSGERQLISFARALAFDP---AILILDEATA--HIDTeteavIQKALDV----VKQGRTTFVIAHRLSTIRNADQILV 636
Cdd:PRK00349 830 TLSGGEAQRVKLAKELSKRStgkTLYILDEPTTglHFED-----IRKLLEVlhrlVDKGNTVVVIEHNLDVIKTADWIID 904
|
90 100
....*....|....*....|....*...
gi 1718055426 637 L-----DK-GEIVEKGNHEELMALEGQY 658
Cdd:PRK00349 905 LgpeggDGgGEIVATGTPEEVAKVEASY 932
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
452-641 |
2.16e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.47 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 452 TAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNmsRQELRSHMGIVLQDpyLFSGTIGSNVsldDERM 531
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYK--PQYISPDYDGTVEE--FLRSANTDDF---GSSY 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 532 TEEEIknaLRQVGAEPLLKKlpkginePViekgSTLSSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQKALD- 610
Cdd:COG1245 435 YKTEI---IKPLGLEKLLDK-------NV----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRr 500
|
170 180 190
....*....|....*....|....*....|...
gi 1718055426 611 -VVKQGRTTFVIAHRLSTIRN-ADQILVLDkGE 641
Cdd:COG1245 501 fAENRGKTAMVVDHDIYLIDYiSDRLMVFE-GE 532
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
446-646 |
2.23e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 45.39 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 446 LKHISFTAQKGETVALVGHTGSGKSSILNLLFRfydAQKGDVLIDGKSIYNmsrqelrshmgivlQDPYLFsgtIGSNVS 525
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLY---ASGKARLISFLPKFS--------------RNKLIF---IDQLQF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 526 LddermteeeIKNALrqvGAEPLLKKLpkginepviekgSTLSSGERQLISFARALA--FDPAILILDEATAHIDTETea 603
Cdd:cd03238 71 L---------IDVGL---GYLTLGQKL------------STLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQD-- 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1718055426 604 vIQKALDVVK----QGRTTFVIAHRLSTIRNADQILVLDK------GEIVEKG 646
Cdd:cd03238 125 -INQLLEVIKglidLGNTVILIEHNLDVLSSADWIIDFGPgsgksgGKVVFSG 176
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
143-406 |
2.57e-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: 46.71 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 143 QPEIKGMVLLICLYGGLLVFSVFFQYGQHYLLQMSAnriiqKMR----QDVFSHIQRMPIRYFDNLPAGKVVARITNDTE 218
Cdd:cd18579 33 EPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGM-----RVRsalsSLIYRKALRLSSSARQETSTGEIVNLMSVDVQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 219 AIRDLYVTVLstFVTSGIYMFGIftALFLLDVKL---AFVCLAI----VPIIwlwSVIYRRYASYYNQKIRSINSDINAk 291
Cdd:cd18579 108 RIEDFFLFLH--YLWSAPLQIIV--ALYLLYRLLgwaALAGLGVllllIPLQ---AFLAKLISKLRKKLMKATDERVKL- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 292 MNESIQGMTII------QAFRHQKETMREfEELNESHFYfqNRMLNLNSLMShNLVNVIrnLAFVCLIWH-FGGASLNAA 364
Cdd:cd18579 180 TNEILSGIKVIklyaweKPFLKRIEELRK-KELKALRKF--GYLRALNSFLF-FSTPVL--VSLATFATYvLLGNPLTAA 253
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1718055426 365 givsigVLYAFVDYLNRLFQPITGIVNQFSKLELARVSAGRV 406
Cdd:cd18579 254 ------KVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
565-658 |
1.13e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.40 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 565 STLSSGERQLISFARALA---FDPAILILDEATA--HIDTeteavIQKALDV----VKQGRTTFVIAHRLSTIRNADQIL 635
Cdd:COG0178 825 TTLSGGEAQRVKLASELSkrsTGKTLYILDEPTTglHFHD-----IRKLLEVlhrlVDKGNTVVVIEHNLDVIKTADWII 899
|
90 100 110
....*....|....*....|....*....|...
gi 1718055426 636 VL-----DK-GEIVEKGNHEELMALE----GQY 658
Cdd:COG0178 900 DLgpeggDGgGEIVAEGTPEEVAKVKasytGRY 932
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
456-625 |
1.15e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 45.77 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 456 GETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNmSRQELRSHMGIVLQdpylFSGTigsnvsldDERMTEEE 535
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQ----FDAI--------DDLLTGRE 2031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 536 ---IKNALRQVGAEPLLKKLPKGINEPVIEK-----GSTLSSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQK 607
Cdd:TIGR01257 2032 hlyLYARLRGVPAEEIEKVANWSIQSLGLSLyadrlAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWN 2111
|
170
....*....|....*....
gi 1718055426 608 AL-DVVKQGRTTFVIAHRL 625
Cdd:TIGR01257 2112 TIvSIIREGRAVVLTSHSM 2130
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
463-638 |
1.26e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 43.71 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 463 GHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNmsrqelrshmgivLQDPYLfsGTIGSNVSLDDERMTEE------EI 536
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINN-------------IAKPYC--TYIGHNLGLKLEMTVFEnlkfwsEI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 537 KNALRQVGAEPLLKKLPKGINEpvieKGSTLSSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQKaLDVVK--Q 614
Cdd:PRK13541 98 YNSAETLYAAIHYFKLHDLLDE----KCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNN-LIVMKanS 172
|
170 180
....*....|....*....|....
gi 1718055426 615 GRTTFVIAHRLSTIRNAdQILVLD 638
Cdd:PRK13541 173 GGIVLLSSHLESSIKSA-QILQLD 195
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
150-248 |
2.21e-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: 43.64 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 150 VLLICLYGGLLVFSVFFQYGQHYLLQMSANRIIQKMRQDVFSHIQRMPIRYFDNLPAGKVVARITNDTEAIRDL------ 223
Cdd:cd18582 38 LLLLLAYGLARILSSLFNELRDALFARVSQRAVRRLALRVFRHLHSLSLRFHLSRKTGALSRAIERGTRGIEFLlrfllf 117
|
90 100
....*....|....*....|....*....
gi 1718055426 224 YV--TVLSTFVTSGI--YMFGIFTALFLL 248
Cdd:cd18582 118 NIlpTILELLLVCGIlwYLYGWSYALITL 146
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
452-641 |
2.26e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.41 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 452 TAQKGETVALVGHTGSGKSSILNLLFRFYDAQKGDVLIDGKSIYNmsRQELRSHMGIVLQDpYLFSgtIGSNVsldDERM 531
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYK--PQYIKPDYDGTVED-LLRS--ITDDL---GSSY 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 532 TEEEIKNALrqvGAEPLLKKlpkginePViekgSTLSSGERQLISFARALAFDPAILILDEATAHIDTETEAVIQKALD- 610
Cdd:PRK13409 433 YKSEIIKPL---QLERLLDK-------NV----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRr 498
|
170 180 190
....*....|....*....|....*....|...
gi 1718055426 611 -VVKQGRTTFVIAHRLSTIRN-ADQILVLDkGE 641
Cdd:PRK13409 499 iAEEREATALVVDHDIYMIDYiSDRLMVFE-GE 530
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
565-637 |
2.48e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 2.48e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1718055426 565 STLSSGERQLISFARALAF---DPAILILDEATAHIDT-ETEAVIQKALDVVKQGRTTFVIAHRLSTIRNADQILVL 637
Cdd:PRK00635 808 SSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHThDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLEL 884
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
566-623 |
7.93e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 7.93e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1718055426 566 TLSSGERQLISFARALAFDPAILILDEATAHIDteTEAVIQKALDVVKQGRTTFVIAH 623
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD--LHAVLWLETYLLKWPKTFIVVSH 399
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
435-476 |
1.09e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 40.84 E-value: 1.09e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1718055426 435 VSFAYQEGEEVLKHISftaqKGETVALVGHTGSGKSSILNLL 476
Cdd:cd01854 68 VSAKTGEGLDELRELL----KGKTSVLVGQSGVGKSTLLNAL 105
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
545-651 |
1.17e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 41.64 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 545 AEPLLKKLpkGINEPVIEKGSTLSSGERQLISFARALAFDPAILILDEATAHIDTETE-AVIQKALDVVKQGRTTFVIAH 623
Cdd:NF000106 125 ADELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRnEVWDEVRSMVRDGATVLLTTQ 202
|
90 100
....*....|....*....|....*....
gi 1718055426 624 RLSTIRN-ADQILVLDKGEIVEKGNHEEL 651
Cdd:NF000106 203 YMEEAEQlAHELTVIDRGRVIADGKVDEL 231
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
565-658 |
1.47e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.92 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 565 STLSSGERQLISFARAL--AFDPAILILDEATA--HiDTETEAVIQKALDVVKQGRTTFVIAHRLSTIRNADQILVLDK- 639
Cdd:TIGR00630 487 GTLSGGEAQRIRLATQIgsGLTGVLYVLDEPSIglH-QRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVIDIGPg 565
|
90 100
....*....|....*....|....*...
gi 1718055426 640 -----GEIVEKGNHEELMA----LEGQY 658
Cdd:TIGR00630 566 agehgGEVVASGTPEEILAnpdsLTGQY 593
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
237-406 |
2.04e-03 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 40.59 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 237 YMFGIFTALFLLDVKLAFVCLAIVPIIWlwSVIYRRYasyYNQKIRSINSdinaKMNESIQGMTIIQAF---RHQKETMR 313
Cdd:cd18583 133 YLFDPYMGLIVAVVMVLYVWSTIKLTSW--RTKLRRD---MIDADREERS----ILTESLLNWETVKYFnrePYEKERYR 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 314 E-FEELNESHFyfqnrmlnlNSLMSHNLVNVIRNLAFVCLIwhFGGASLNAAGIV----SIGVLYAFVDYLNRLFQPITG 388
Cdd:cd18583 204 EaVKNYQKAER---------KYLFSLNLLNAVQSLILTLGL--LAGCFLAAYQVSqgqaTVGDFVTLLTYWAQLSGPLNF 272
|
170
....*....|....*...
gi 1718055426 389 IVNQFSKLELARVSAGRV 406
Cdd:cd18583 273 FATLYRSIQSDLIDAERL 290
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
456-626 |
6.46e-03 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 38.89 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 456 GETVALVGHTGSGKSSILNLLF--------RFYDAQKGDVLID---GKSIYNMSRQELRSHMGIVLQDPYL------FSG 518
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFTKLLEGDVKVIVKPQYVdlipkaVKG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1718055426 519 TIGSNVSLDDERMTEEEIknaLRQVGAEPLLKKlpkginepvieKGSTLSSGERQLISFARALAFDPAILILDEATAHID 598
Cdd:cd03236 106 KVGELLKKKDERGKLDEL---VDQLELRHVLDR-----------NIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
170 180 190
....*....|....*....|....*....|.
gi 1718055426 599 TE---TEAVIQKALdvVKQGRTTFVIAHRLS 626
Cdd:cd03236 172 IKqrlNAARLIREL--AEDDNYVLVVEHDLA 200
|
|
| |
