|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
25-620 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 736.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 25 PKNFWKTVKRLFRYMSKRMLSIIAVLVLAIAAVVFQIQTPKVLGQATTEIFKGvmkgaaemkqglkitsfpIDFDKIGQI 104
Cdd:COG1132 2 SKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAG------------------GDLSALLLL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 105 LLIVIAMYLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQQNLTQLI 184
Cdd:COG1132 64 LLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 185 TSIVTFVGVLWMMLTISWQLTLIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKSFNHEESDQ 264
Cdd:COG1132 144 RSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREEREL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 265 EVFEKENEKLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPITQIANLMNT 344
Cdd:COG1132 224 ERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 345 IQATVASAERVFEVLDEEEMVDEPSGIPVETDSPYRVSFEHVAFGYSPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLI 424
Cdd:COG1132 304 LQRALASAERIFELLDEPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 425 NLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMVLQDTWLFTGSIYDNIHYGNEQASEEEVIRAAKAAHVDDFVRKLP 504
Cdd:COG1132 384 NLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 505 EGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLLENRTSFVVAHRLSTIRDADT 584
Cdd:COG1132 464 DGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADR 543
|
570 580 590
....*....|....*....|....*....|....*.
gi 488288408 585 IIVMAEGSIVETGTHDELMAKNGFYADLYNSQFSEE 620
Cdd:COG1132 544 ILVLDDGRIVEQGTHEELLARGGLYARLYRLQFGEE 579
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
33-616 |
2.05e-170 |
|
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: 502.06 E-value: 2.05e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 33 KRLFRYMSKRMLSIIAVLVLAIAAVVFQIQTP--------KVLGQAtteifkgvmkgaaemkqglkitsfpiDFDKIGQI 104
Cdd:COG2274 145 RWFLRLLRRYRRLLLQVLLASLLINLLALATPlftqvvidRVLPNQ--------------------------DLSTLWVL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 105 LLIVIAMYLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRaINDMDNIASTLQQNLTQLI 184
Cdd:COG2274 199 AIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASR-FRDVESIREFLTGSLLTAL 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 185 TSIVTFVGVLWMMLTISWQLTLIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKSFNHEESDQ 264
Cdd:COG2274 278 LDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFR 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 265 EVFEKENEKLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPITQIANLMNT 344
Cdd:COG2274 358 RRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQR 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 345 IQATVASAERVFEVLDEE-EMVDEPSGIPVETDSPyRVSFEHVAFGYSP-EKLLMKDFNLNVKPGEMVAIVGPTGAGKTT 422
Cdd:COG2274 438 FQDAKIALERLDDILDLPpEREEGRSKLSLPRLKG-DIELENVSFRYPGdSPPVLDNISLTIKPGERVAIVGRSGSGKST 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 423 LINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMVLQDTWLFTGSIYDNIHYGNEQASEEEVIRAAKAAHVDDFVRK 502
Cdd:COG2274 517 LLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEA 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 503 LPEGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLLENRTSFVVAHRLSTIRDA 582
Cdd:COG2274 597 LPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLA 676
|
570 580 590
....*....|....*....|....*....|....
gi 488288408 583 DTIIVMAEGSIVETGTHDELMAKNGFYADLYNSQ 616
Cdd:COG2274 677 DRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQ 710
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
46-355 |
4.97e-149 |
|
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: 432.21 E-value: 4.97e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 46 IIAVLVLAIAAVVFQIQTPKVLGQATTEIFKGVmkgaaemkqglkITSFPIDFDKIGQILLIVIAMYLISAVFNFLQQVI 125
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGL------------GGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 126 MTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQQNLTQLITSIVTFVGVLWMMLTISWQLT 205
Cdd:cd18547 69 MARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 206 LIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKSFNHEESDQEVFEKENEKLYHAGRKAQFIS 285
Cdd:cd18547 149 LIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYS 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 286 AIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPITQIANLMNTIQATVASAERV 355
Cdd:cd18547 229 GLLMPIMNFINNLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
31-619 |
2.76e-144 |
|
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: 430.29 E-value: 2.76e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 31 TVKRLFRYMSKRMLSIIAVLVLAIAAVVFQIQTPKVLGQATTEIFKGVmkgaaemkqglkitsfpiDFDKIGQILLIVIA 110
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGR------------------DRSVLWWVPLVVIG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 111 MYLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQQNLTQLITSIVTF 190
Cdd:TIGR02203 63 LAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 191 VGVLWMMLTISWQLTLIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKSFNHEESDQEVFEKE 270
Cdd:TIGR02203 143 IGLFIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 271 NEKLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPITQIANLMNTIQATVA 350
Cdd:TIGR02203 223 SNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 351 SAERVFEVLDEEEMVDEPSGIPVETDSpyRVSFEHVAFGYSP-EKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLER 429
Cdd:TIGR02203 303 AAESLFTLLDSPPEKDTGTRAIERARG--DVEFRNVTFRYPGrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 430 FYDISSGSIKYDGVDTRDLSREELRAHFSMVLQDTWLFTGSIYDNIHYGN-EQASEEEVIRAAKAAHVDDFVRKLPEGYQ 508
Cdd:TIGR02203 381 FYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 509 TILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLLENRTSFVVAHRLSTIRDADTIIVM 588
Cdd:TIGR02203 461 TPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVM 540
|
570 580 590
....*....|....*....|....*....|.
gi 488288408 589 AEGSIVETGTHDELMAKNGFYADLYNSQFSE 619
Cdd:TIGR02203 541 DDGRIVERGTHNELLARNGLYAQLHNMQFRE 571
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
101-617 |
6.46e-135 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 406.39 E-value: 6.46e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 101 IGQILLIVIAMYLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQQNL 180
Cdd:TIGR02204 57 LNRYFAFLLVVALVLALGTAARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 181 TQLITSIVTFVGVLWMMLTISWQLTLIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKSFNHE 260
Cdd:TIGR02204 137 SMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 261 ESDQEVFEKENEKLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPITQIAN 340
Cdd:TIGR02204 217 DAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 341 LMNTIQATVASAERVFEVLDEEEMVDEPSgIPVETDSPYR--VSFEHVAFGY--SPEKLLMKDFNLNVKPGEMVAIVGPT 416
Cdd:TIGR02204 297 VWGELQRAAGAAERLIELLQAEPDIKAPA-HPKTLPVPLRgeIEFEQVNFAYpaRPDQPALDGLNLTVRPGETVALVGPS 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 417 GAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMVLQDTWLFTGSIYDNIHYGNEQASEEEVIRAAKAAHV 496
Cdd:TIGR02204 376 GAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHA 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 497 DDFVRKLPEGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLLENRTSFVVAHRL 576
Cdd:TIGR02204 456 HEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRL 535
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 488288408 577 STIRDADTIIVMAEGSIVETGTHDELMAKNGFYADLYNSQF 617
Cdd:TIGR02204 536 ATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQF 576
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
33-607 |
9.98e-127 |
|
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: 384.88 E-value: 9.98e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 33 KRLFRYM--SKRMLSIIAVL-VLAIAAVVFQIqtpKVLGQATTEIFKGvmkgaaemkqglkitsfPIDFDKIGQILLIVI 109
Cdd:COG4988 6 KRLKRLArgARRWLALAVLLgLLSGLLIIAQA---WLLASLLAGLIIG-----------------GAPLSALLPLLGLLL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 110 AMYLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQQNLTQLITSIVT 189
Cdd:COG4988 66 AVLLLRALLAWLRERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 190 FVGVLWMMLTISWQLTLIALATVPLsLIVVMVV-----APRSQKHFAAqqksLGLLNNQVEETYGGHVVVKSFNHEESDQ 264
Cdd:COG4988 146 PLLILVAVFPLDWLSGLILLVTAPL-IPLFMILvgkgaAKASRRQWRA----LARLSGHFLDRLRGLTTLKLFGRAKAEA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 265 EVFEKENEKLyhagRKA-------QFISAIIMplmNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPITQ 337
Cdd:COG4988 221 ERIAEASEDF----RKRtmkvlrvAFLSSAVL---EFFASLSIALVAVYIGFRLLGGSLTLFAALFVLLLAPEFFLPLRD 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 338 IANLMNTIQATVASAERVFEVLDEEEMVDEPSGIPVETDSPYRVSFEHVAFGYSPEKLLMKDFNLNVKPGEMVAIVGPTG 417
Cdd:COG4988 294 LGSFYHARANGIAAAEKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 418 AGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMVLQDTWLFTGSIYDNIHYGNEQASEEEVIRAAKAAHVD 497
Cdd:COG4988 374 AGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLD 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 498 DFVRKLPEGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLLENRTSFVVAHRLS 577
Cdd:COG4988 454 EFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLA 533
|
570 580 590
....*....|....*....|....*....|
gi 488288408 578 TIRDADTIIVMAEGSIVETGTHDELMAKNG 607
Cdd:COG4988 534 LLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
20-622 |
4.93e-126 |
|
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: 384.56 E-value: 4.93e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 20 AKGPKPKNFWKTVKRLFRYMSKRMLSIIAVLVLAIAAVVFQIQTPKVLGQATteifkgVMKGAAEMkqglkITSFPIdfd 99
Cdd:COG5265 13 PPRLDLLLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAID------ALLSGAAA-----LLVVPV--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 100 kigqiLLIVI--AMYLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDiMSRAINDMDNIASTLq 177
Cdd:COG5265 79 -----GLLLAygLLRLLSVLFGELRDALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGG-LSRDIERGTKGIEFL- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 178 qnLTQLITSIV-TFV------GVLWMMLtiSWQLTLIALATVPLSLIVVMVVAPRSQKHF--------AAQQKSL-GLLN 241
Cdd:COG5265 152 --LRFLLFNILpTLLeialvaGILLVKY--DWWFALITLVTVVLYIAFTVVVTEWRTKFRremneadsEANTRAVdSLLN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 242 nqvEETygghvvVKSFNHEESDQEVFEKENEKLYHAGRKAQfisaIIMPLMNF----IKNLGYVFVAVLGGVKVANGMMD 317
Cdd:COG5265 228 ---YET------VKYFGNEAREARRYDEALARYERAAVKSQ----TSLALLNFgqalIIALGLTAMMLMAAQGVVAGTMT 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 318 LGD---VQAFLQytnQFSQPItqiaNLMNTI-----QAtVASAERVFEVLDEE-EMVDEPSGIPVETDSPyRVSFEHVAF 388
Cdd:COG5265 295 VGDfvlVNAYLI---QLYIPL----NFLGFVyreirQA-LADMERMFDLLDQPpEVADAPDAPPLVVGGG-EVRFENVSF 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 389 GYSPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMVLQDTWLFT 468
Cdd:COG5265 366 GYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFN 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 469 GSIYDNIHYGNEQASEEEVIRAAKAAHVDDFVRKLPEGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSV 548
Cdd:COG5265 446 DTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSAL 525
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488288408 549 DTRTEILIQAAMNRLLENRTSFVVAHRLSTIRDADTIIVMAEGSIVETGTHDELMAKNGFYADLYNSQFSEEVA 622
Cdd:COG5265 526 DSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEA 599
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
380-607 |
1.68e-119 |
|
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: 354.22 E-value: 1.68e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 380 RVSFEHVAFGYSPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSM 459
Cdd:cd03254 2 EIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 460 VLQDTWLFTGSIYDNIHYGNEQASEEEVIRAAKAAHVDDFVRKLPEGYQTILNEEASNISQGQRQLITIARAFLANPDVL 539
Cdd:cd03254 82 VLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488288408 540 ILDEATSSVDTRTEILIQAAMNRLLENRTSFVVAHRLSTIRDADTIIVMAEGSIVETGTHDELMAKNG 607
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
381-613 |
3.33e-117 |
|
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: 348.45 E-value: 3.33e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYSP-EKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSM 459
Cdd:cd03251 1 VEFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 460 VLQDTWLFTGSIYDNIHYGNEQASEEEVIRAAKAAHVDDFVRKLPEGYQTILNEEASNISQGQRQLITIARAFLANPDVL 539
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488288408 540 ILDEATSSVDTRTEILIQAAMNRLLENRTSFVVAHRLSTIRDADTIIVMAEGSIVETGTHDELMAKNGFYADLY 613
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
29-619 |
1.60e-114 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 353.94 E-value: 1.60e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 29 WKTVKRLFRYMS--KRMLsIIAVLVLAIAAVV--FQIQTPKVL-----GQATTEIFKgvmkgaaemkqglkitsfpidfd 99
Cdd:PRK11176 10 WQTFRRLWPTIApfKAGL-IVAGVALILNAASdtFMLSLLKPLlddgfGKADRSVLK----------------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 100 kigQILLIVIAMYLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQQN 179
Cdd:PRK11176 66 ---WMPLVVIGLMILRGITSFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 180 LTQLITSIVTFVGVLWMMLTISWQLTLIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKSFNH 259
Cdd:PRK11176 143 LITVVREGASIIGLFIMMFYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 260 EESDQEVFEKENEKLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGdvqaflQYTNQFS------Q 333
Cdd:PRK11176 223 QEVETKRFDKVSNRMRQQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAG------TITVVFSsmialmR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 334 PITQIANLMNTIQATVASAERVFEVLDEEEMVDEpsGIPVETDSPYRVSFEHVAFGY-SPEKLLMKDFNLNVKPGEMVAI 412
Cdd:PRK11176 297 PLKSLTNVNAQFQRGMAACQTLFAILDLEQEKDE--GKRVIERAKGDIEFRNVTFTYpGKEVPALRNINFKIPAGKTVAL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 413 VGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMVLQDTWLFTGSIYDNIHYG-NEQASEEEVIRAA 491
Cdd:PRK11176 375 VGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYArTEQYSREQIEEAA 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 492 KAAHVDDFVRKLPEGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLLENRTSFV 571
Cdd:PRK11176 455 RMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLV 534
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 488288408 572 VAHRLSTIRDADTIIVMAEGSIVETGTHDELMAKNGFYADLYNSQFSE 619
Cdd:PRK11176 535 IAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQFGQ 582
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
32-612 |
3.72e-114 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 357.11 E-value: 3.72e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 32 VKRLFRYMSKRMLSIIAVLVLAIAAVVFQIQTPKVLGQATTEIFkgvmkgaaemkqglkiTSFpiDFDKIGQILLIVIAM 111
Cdd:TIGR00958 149 LFRLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLG----------------GDK--GPPALASAIFFMCLL 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 112 YLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQQNLTQLITSIVTFV 191
Cdd:TIGR00958 211 SIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 192 GVLWMMLTISWQLTLIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKSFNHEESDQEVFEKEN 271
Cdd:TIGR00958 291 GLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEAL 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 272 EKLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPITQIANLMNTIQATVAS 351
Cdd:TIGR00958 371 EETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGA 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 352 AERVFEVLDEEEMVdEPSGIPVETDSPYRVSFEHVAFGY--SPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLER 429
Cdd:TIGR00958 451 SEKVFEYLDRKPNI-PLTGTLAPLNLEGLIEFQDVSFSYpnRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQN 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 430 FYDISSGSIKYDGVDTRDLSREELRAHFSMVLQDTWLFTGSIYDNIHYGNEQASEEEVIRAAKAAHVDDFVRKLPEGYQT 509
Cdd:TIGR00958 530 LYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDT 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 510 ILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRllENRTSFVVAHRLSTIRDADTIIVMA 589
Cdd:TIGR00958 610 EVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSR--ASRTVLLIAHRLSTVERADQILVLK 687
|
570 580
....*....|....*....|...
gi 488288408 590 EGSIVETGTHDELMAKNGFYADL 612
Cdd:TIGR00958 688 KGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
381-616 |
3.77e-109 |
|
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: 327.65 E-value: 3.77e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYSPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMV 460
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 461 LQDTWLFTGSIYDNIHYGNEQASEEEVIRAAKAAHVDDFVRKLPEGYQTILNEEASNISQGQRQLITIARAFLANPDVLI 540
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488288408 541 LDEATSSVDTRTEILIQAAMNRLLENRTSFVVAHRLSTIRDADTIIVMAEGSIVETGTHDELMAKNGFYADLYNSQ 616
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
156-614 |
9.06e-109 |
|
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: 338.66 E-value: 9.06e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 156 HSNGDIMSRAINDMDNIastlqQNL-----TQLITSIVTFVGVLWMMLTISWQLTLIALATVPLSLIVVMVVAPRSQKHF 230
Cdd:COG4987 109 LRSGDLLNRLVADVDAL-----DNLylrvlLPLLVALLVILAAVAFLAFFSPALALVLALGLLLAGLLLPLLAARLGRRA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 231 AAQQKSL-GLLNNQVEETYGGHVVVKSFNHEESDQEVFEKENEKLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGV 309
Cdd:COG4987 184 GRRLAAArAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAP 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 310 KVANGMMDLGDVQAFLqytnqFS-----QPITQIANLMNTIQATVASAERVFEVLDEEEMVDEPSGiPVETDSPYRVSFE 384
Cdd:COG4987 264 LVAAGALSGPLLALLV-----LAalalfEALAPLPAAAQHLGRVRAAARRLNELLDAPPAVTEPAE-PAPAPGGPSLELE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 385 HVAFGYSPE-KLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMVLQD 463
Cdd:COG4987 338 DVSFRYPGAgRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQR 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 464 TWLFTGSIYDNIHYGNEQASEEEVIRAAKAAHVDDFVRKLPEGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDE 543
Cdd:COG4987 418 PHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDE 497
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488288408 544 ATSSVDTRTEILIQAAMNRLLENRTSFVVAHRLSTIRDADTIIVMAEGSIVETGTHDELMAKNGFYADLYN 614
Cdd:COG4987 498 PTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
381-616 |
2.09e-102 |
|
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: 310.63 E-value: 2.09e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGY--SPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFS 458
Cdd:cd03249 1 IEFKNVSFRYpsRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 459 MVLQDTWLFTGSIYDNIHYGNEQASEEEVIRAAKAAHVDDFVRKLPEGYQTILNEEASNISQGQRQLITIARAFLANPDV 538
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488288408 539 LILDEATSSVDTRTEILIQAAMNRLLENRTSFVVAHRLSTIRDADTIIVMAEGSIVETGTHDELMAKNGFYADLYNSQ 616
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
105-612 |
2.38e-101 |
|
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: 323.43 E-value: 2.38e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 105 LLIVIAMYLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRA-INDmdNIASTLQQNLTQL 183
Cdd:TIGR03796 197 LLGMGLTALLQGVLTWLQLYYLRRLEIKLAVGMSARFLWHILRLPVRFFAQRHAGDIASRVqLND--QVAEFLSGQLATT 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 184 ITSIVTFVGVLWMMLTISWQLTLIALATVPLSLIVVMVVApRSQKHFAAQ-QKSLGLLNNQveeTYGGHVVVKSFNHEES 262
Cdd:TIGR03796 275 ALDAVMLVFYALLMLLYDPVLTLIGIAFAAINVLALQLVS-RRRVDANRRlQQDAGKLTGV---AISGLQSIETLKASGL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 263 DQEVFEK---ENEKLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPITQIA 339
Cdd:TIGR03796 351 ESDFFSRwagYQAKLLNAQQELGVLTQILGVLPTLLTSLNSALILVVGGLRVMEGQLTIGMLVAFQSLMSSFLEPVNNLV 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 340 NLMNTIQATVASAERVFEVLD--EEEMVDEPSGIPVETDSPYR----VSFEHVAFGYSP-EKLLMKDFNLNVKPGEMVAI 412
Cdd:TIGR03796 431 GFGGTLQELEGDLNRLDDVLRnpVDPLLEEPEGSAATSEPPRRlsgyVELRNITFGYSPlEPPLIENFSLTLQPGQRVAL 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 413 VGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMVLQDTWLFTGSIYDNIHYGNEQASEEEVIRAAK 492
Cdd:TIGR03796 511 VGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACK 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 493 AAHVDDFVRKLPEGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRllENRTSFVV 572
Cdd:TIGR03796 591 DAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRR--RGCTCIIV 668
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 488288408 573 AHRLSTIRDADTIIVMAEGSIVETGTHDELMAKNGFYADL 612
Cdd:TIGR03796 669 AHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARL 708
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
95-617 |
4.82e-101 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 319.21 E-value: 4.82e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 95 PIDFDKI------GQILLIVIAMYLISAVFNFLQQVIMTRVSQRTVYELRQELEA----KMNKVPISYYDTHSNGDIMSR 164
Cdd:PRK13657 39 PILFGRIidaisgKGDIFPLLAAWAGFGLFNIIAGVLVARHADRLAHRRRLAVLTeyfeRIIQLPLAWHSQRGSGRALHT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 165 AINDMDNIASTLQQNLTQLITSIVTFVGVLWMMLTISWQLT--LIALATVpLSLIVVMVVaprsQKHFAAQqkslgllnN 242
Cdd:PRK13657 119 LLRGTDALFGLWLEFMREHLATLVALVVLLPLALFMNWRLSlvLVVLGIV-YTLITTLVM----RKTKDGQ--------A 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 243 QVEETYGG---HV--------VVKSFNHEESDQEVFEKENEKLYhagrKAQfisaiiMPLMNF----------IKNLGYV 301
Cdd:PRK13657 186 AVEEHYHDlfaHVsdaignvsVVQSYNRIEAETQALRDIADNLL----AAQ------MPVLSWwalasvlnraASTITML 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 302 FVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPITQIANLMNTIQATVASAERVFEVLDEEEMVDEPSGIPVETDSPYRV 381
Cdd:PRK13657 256 AILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQVFMAAPKLEEFFEVEDAVPDVRDPPGAIDLGRVKGAV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 382 SFEHVAFGYSPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMVL 461
Cdd:PRK13657 336 EFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVF 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 462 QDTWLFTGSIYDNIHYGNEQASEEEVIRAAKAAHVDDFVRKLPEGYQTILNEEASNISQGQRQLITIARAFLANPDVLIL 541
Cdd:PRK13657 416 QDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILIL 495
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488288408 542 DEATSSVDTRTEILIQAAMNRLLENRTSFVVAHRLSTIRDADTIIVMAEGSIVETGTHDELMAKNGFYADLYNSQF 617
Cdd:PRK13657 496 DEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQG 571
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
49-616 |
3.06e-91 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 293.16 E-value: 3.06e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 49 VLVLAIAAVVfQIQTPKVLGQatteIFKGVMKGAAEMKQGLKItsfpidfdkIGQILLIVIAMYLISAVFnflqQVIMTR 128
Cdd:PRK10789 1 VALLIIIAML-QLIPPKVVGI----IVDGVTEQHMTTGQILMW---------IGTMVLIAVVVYLLRYVW----RVLLFG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 129 VSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQQNLTQLITSIVTFVGVLWMMLT-ISWQLTLI 207
Cdd:PRK10789 63 ASYQLAVELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMSTqISWQLTLL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 208 ALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKSFNHEESDQEVFEKENEKlyhAGRK------- 280
Cdd:PRK10789 143 ALLPMPVMAIMIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAED---TGKKnmrvari 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 281 -AQFISAIIMPLMnfIKNLgyvfVAVLGGV-KVANGMMDLGDVQAFLQYTNQFSQPITQIANLMNTIQATVASAERVFEV 358
Cdd:PRK10789 220 dARFDPTIYIAIG--MANL----LAIGGGSwMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 359 LDEEEMVDEPSGIPVETDSPYRVSFEhvAFGY-SPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGS 437
Cdd:PRK10789 294 LAEAPVVKDGSEPVPEGRGELDVNIR--QFTYpQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGD 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 438 IKYDGVDTRDLSREELRAHFSMVLQDTWLFTGSIYDNIHYGNEQASEEEVIRAAKAAHVDDFVRKLPEGYQTILNEEASN 517
Cdd:PRK10789 372 IRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVM 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 518 ISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLLENRTSFVVAHRLSTIRDADTIIVMAEGSIVETG 597
Cdd:PRK10789 452 LSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRG 531
|
570
....*....|....*....
gi 488288408 598 THDELMAKNGFYADLYNSQ 616
Cdd:PRK10789 532 NHDQLAQQSGWYRDMYRYQ 550
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
23-622 |
6.52e-89 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 287.77 E-value: 6.52e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 23 PKPKNFWKTVKRLFRYMSK-RMLSIIAVLVLAIAAVVfqiqtpKVLGQATTEIFKGVMKGAAEMKQGLkitsfpidfdkI 101
Cdd:PRK10790 2 RSFSQLWPTLKRLLAYGSPwRKPLGLAVLMLWVAAAA------EVSGPLLISYFIDNMVAKGNLPLGL-----------V 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 102 GQILLIVIAMYLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQQNLT 181
Cdd:PRK10790 65 AGLAAAYVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 182 QLITSIVTFVGVLWMMLTISWQLTLIALATVPlSLIVVMVVAPRSQKHFAAQQKS-LGLLNNQVEETYGGHVVVKSFNHE 260
Cdd:PRK10790 145 TVLRSAALIGAMLVAMFSLDWRMALVAIMIFP-AVLVVMVIYQRYSTPIVRRVRAyLADINDGFNEVINGMSVIQQFRQQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 261 ESDQEVFEKENEKLYHAGRKAQFISAIIM-PLMNFIKNLGYVFVAVLGGVKvANGMMDLGDVQAFLQYTNQFSQPITQIA 339
Cdd:PRK10790 224 ARFGERMGEASRSHYMARMQTLRLDGFLLrPLLSLFSALILCGLLMLFGFS-ASGTIEVGVLYAFISYLGRLNEPLIELT 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 340 NLMNTIQATVASAERVFEVLDEEEmvdEPSGIPVETDSPYRVSFEHVAFGYSPEKLLMKDFNLNVKPGEMVAIVGPTGAG 419
Cdd:PRK10790 303 TQQSMLQQAVVAGERVFELMDGPR---QQYGNDDRPLQSGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 420 KTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMVLQDTWLFTGSIYDNIHYGNEqASEEEVIRAAKAAHVDDF 499
Cdd:PRK10790 380 KSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD-ISEEQVWQALETVQLAEL 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 500 VRKLPEGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLLENRTSFVVAHRLSTI 579
Cdd:PRK10790 459 ARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTI 538
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 488288408 580 RDADTIIVMAEGSIVETGTHDELMAKNGFYADLYNSQF-SEEVA 622
Cdd:PRK10790 539 VEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLaGEELA 582
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
105-588 |
2.57e-83 |
|
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: 271.08 E-value: 2.57e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 105 LLIVIAMYLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQQNLTQLI 184
Cdd:TIGR02857 47 LGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 185 TSIVTFVGVLWMMLTISWQLTLIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKSFNHEESDQ 264
Cdd:TIGR02857 127 LAVIVPLAILAAVFPQDWISGLILLLTAPLIPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 265 EVFEKENEKLYHAG----RKAqFISAIIMplmNFIKNLGYVFVAVLGGVKVANGMMDLgdVQAF--LQYTNQFSQPITQI 338
Cdd:TIGR02857 207 AAIRRSSEEYRERTmrvlRIA-FLSSAVL---ELFATLSVALVAVYIGFRLLAGDLDL--ATGLfvLLLAPEFYLPLRQL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 339 ANLMNTIQATVASAERVFEVLDEEEMVdEPSGIPVETDSPYRVSFEHVAFGYSPEKLLMKDFNLNVKPGEMVAIVGPTGA 418
Cdd:TIGR02857 281 GAQYHARADGVAAAEALFAVLDAAPRP-LAGKAPVTAAPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGA 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 419 GKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMVLQDTWLFTGSIYDNIHYGNEQASEEEVIRAAKAAHVDD 498
Cdd:TIGR02857 360 GKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDE 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 499 FVRKLPEGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLLENRTSFVVAHRLST 578
Cdd:TIGR02857 440 FVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLAL 519
|
490
....*....|
gi 488288408 579 IRDADTIIVM 588
Cdd:TIGR02857 520 AALADRIVVL 529
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
31-616 |
2.89e-83 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 275.30 E-value: 2.89e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 31 TVKRLFRY-MSKRMLSIIAVLVLAIAAVVFQIQTPkvlgQATTEIFKGVMKGAaemkqglkitsfpiDFDKIGQILLIVI 109
Cdd:TIGR03797 122 GLRDLLRFaLRGARRDLLAILAMGLLGTLLGMLVP----IATGILIGTAIPDA--------------DRSLLVQIALALL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 110 AMYLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRA--INDMDNIASTlqQNLTQLITSI 187
Cdd:TIGR03797 184 AAAVGAAAFQLAQSLAVLRLETRMDASLQAAVWDRLLRLPVSFFRQYSTGDLASRAmgISQIRRILSG--STLTTLLSGI 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 188 VTFVGvLWMMLTISWQLTLIALAtVPLSLIVVMVVAPRSQKHFAAQQKSL-GLLNNQVEETYGGhvVVKsfnheesdQEV 266
Cdd:TIGR03797 262 FALLN-LGLMFYYSWKLALVAVA-LALVAIAVTLVLGLLQVRKERRLLELsGKISGLTVQLING--ISK--------LRV 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 267 FEKENE------KLYHAGRKAQFISAIIMPLMN-FIKNLGYVFVAVLGGVKV---ANGMMDLGDVQAFLQYTNQFSQPIT 336
Cdd:TIGR03797 330 AGAENRafarwaKLFSRQRKLELSAQRIENLLTvFNAVLPVLTSAALFAAAIsllGGAGLSLGSFLAFNTAFGSFSGAVT 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 337 QIANLMNTIQATVASAERVFEVLDEEEMVDEPSGIPVETDSpyRVSFEHVAFGYSPE-KLLMKDFNLNVKPGEMVAIVGP 415
Cdd:TIGR03797 410 QLSNTLISILAVIPLWERAKPILEALPEVDEAKTDPGKLSG--AIEVDRVTFRYRPDgPLILDDVSLQIEPGEFVAIVGP 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 416 TGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMVLQDTWLFTGSIYDNIhYGNEQASEEEVIRAAKAAH 495
Cdd:TIGR03797 488 SGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAG 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 496 VDDFVRKLPEGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLleNRTSFVVAHR 575
Cdd:TIGR03797 567 LAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL--KVTRIVIAHR 644
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 488288408 576 LSTIRDADTIIVMAEGSIVETGTHDELMAKNGFYADLYNSQ 616
Cdd:TIGR03797 645 LSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLARRQ 685
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
381-616 |
1.15e-82 |
|
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: 259.73 E-value: 1.15e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYSP-EKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSM 459
Cdd:cd03252 1 ITFEHVRFRYKPdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 460 VLQDTWLFTGSIYDNIHYGNEQASEEEVIRAAKAAHVDDFVRKLPEGYQTILNEEASNISQGQRQLITIARAFLANPDVL 539
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488288408 540 ILDEATSSVDTRTEILIQAAMNRLLENRTSFVVAHRLSTIRDADTIIVMAEGSIVETGTHDELMAKNGFYADLYNSQ 616
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
99-614 |
1.43e-78 |
|
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: 263.14 E-value: 1.43e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 99 DKIGQILLIVIAMYLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSR---AINDMDNIAST 175
Cdd:TIGR01193 193 GTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRftdASSIIDALAST 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 176 lqqnltqlitsIVTFVGVLWMMLTISW-------QLTLIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETY 248
Cdd:TIGR01193 273 -----------ILSLFLDMWILVIVGLflvrqnmLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 249 GGHVVVKSFNHEESDQEVFEKENEKLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYT 328
Cdd:TIGR01193 342 NGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQGQQAIKAVTKLILNVVILWTGAYLVMRGKLTLGQLITFNALL 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 329 NQFSQPITQIANLMNTIQATVASAERVFEVLDEEEMVDEPSGIPVETDSPYRVSFEHVAFGYSPEKLLMKDFNLNVKPGE 408
Cdd:TIGR01193 422 SYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTELNNLNGDIVINDVSYSYGYGSNILSDISLTIKMNS 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 409 MVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMVLQDTWLFTGSIYDNIHYGN-EQASEEEV 487
Cdd:TIGR01193 502 KTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAkENVSQDEI 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 488 IRAAKAAHVDDFVRKLPEGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEiliQAAMNRL--LE 565
Cdd:TIGR01193 582 WAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITE---KKIVNNLlnLQ 658
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 488288408 566 NRTSFVVAHRLSTIRDADTIIVMAEGSIVETGTHDELMAKNGFYADLYN 614
Cdd:TIGR01193 659 DKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIH 707
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
381-591 |
2.04e-75 |
|
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: 238.05 E-value: 2.04e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYSP-EKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSM 459
Cdd:cd03228 1 IEFKNVSFSYPGrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 460 VLQDTWLFTGSIYDNIhygneqaseeeviraakaahvddfvrklpegyqtilneeasnISQGQRQLITIARAFLANPDVL 539
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488288408 540 ILDEATSSVDTRTEILIQAAMNRLLENRTSFVVAHRLSTIRDADTIIVMAEG 591
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
46-355 |
3.06e-73 |
|
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: 237.06 E-value: 3.06e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 46 IIAVLVLAIAAVVFQIQTPKVLGQATTEIFKGvmkgaaemkqglkitsfpIDFDKIGQILLIVIAMYLISAVFNFLQQVI 125
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPA------------------GDLSLLLWIALLLLLLALLRALLSYLRRYL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 126 MTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQQNLTQLITSIVTFVGVLWMMLTISWQLT 205
Cdd:cd07346 63 AARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 206 LIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKSFNHEESDQEVFEKENEKLYHAGRKAQFIS 285
Cdd:cd07346 143 LVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLS 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 286 AIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPITQIANLMNTIQATVASAERV 355
Cdd:cd07346 223 ALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
380-598 |
3.23e-73 |
|
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: 234.31 E-value: 3.23e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 380 RVSFEHVAFGYSPE-KLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFS 458
Cdd:cd03244 2 DIEFKNVSLRYRPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 459 MVLQDTWLFTGSIYDNIHyGNEQASEEEVIRAAKAAHVDDFVRKLPEGYQTILNEEASNISQGQRQLITIARAFLANPDV 538
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLD-PFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 539 LILDEATSSVDTRTEILIQAAMNRLLENRTSFVVAHRLSTIRDADTIIVMAEGSIVETGT 598
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
380-597 |
3.30e-68 |
|
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: 221.31 E-value: 3.30e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 380 RVSFEHVAFGYSP-EKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFS 458
Cdd:cd03245 2 RIEFRNVSFSYPNqEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 459 MVLQDTWLFTGSIYDNIHYGNEQASEEEVIRAAKAAHVDDFVRKLPEGYQTILNEEASNISQGQRQLITIARAFLANPDV 538
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488288408 539 LILDEATSSVDTRTEILIQAAMNRLLENRTSFVVAHRLSTIRDADTIIVMAEGSIVETG 597
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
46-355 |
1.53e-67 |
|
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: 221.96 E-value: 1.53e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 46 IIAVLVLAIAAVVFQIQTPKVLGQAtteIFKGVMKGaaemkqglkitsfpiDFDKIGQILLIVIAMYLISAVFNFLQQVI 125
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPYLIKIA---IDEYIPNG---------------DLSGLLIIALLFLALNLVNWVASRLRIYL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 126 MTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQQNLTQLITSIVTFVGVLWMMLTISWQLT 205
Cdd:cd18545 64 MAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 206 LIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKSFNHEESDQEVFEKENEKLYHAGRKAQFIS 285
Cdd:cd18545 144 LVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLN 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 286 AIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPITQIANLMNTIQATVASAERV 355
Cdd:cd18545 224 ALFWPLVELISALGTALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
46-355 |
1.15e-66 |
|
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: 219.57 E-value: 1.15e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 46 IIAVLVLAIAAVVFQIQTPKVLGQATTEIfkgvmkgaaemkqglkITSFPIDFDKIGQILLIVIAMYLISAVFNFLQQVI 125
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDY----------------IVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 126 MTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQQNLTQLITSIVTFVGVLWMMLTISWQLT 205
Cdd:cd18544 65 LQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 206 LIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKSFNHEESDQEVFEKENEKLYHAGRKAQFIS 285
Cdd:cd18544 145 LISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLF 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 286 AIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPITQIANLMNTIQATVASAERV 355
Cdd:cd18544 225 ALFRPLVELLSSLALALVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
47-355 |
8.93e-66 |
|
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: 217.30 E-value: 8.93e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 47 IAVLVLAIAAVVFQIQTPKVLGQATTEIFKGVmkgaaemkqglkitsfpiDFDKIGQILLIVIAMYLISAVFNFLQQVIM 126
Cdd:cd18542 2 LLAILALLLATALNLLIPLLIRRIIDSVIGGG------------------LRELLWLLALLILGVALLRGVFRYLQGYLA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 127 TRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQQNLTQLITSIVTFVGVLWMMLTISWQLTL 206
Cdd:cd18542 64 EKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 207 IALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKSFNHEESDQEVFEKENEKLYHAGRKAQFISA 286
Cdd:cd18542 144 ISLAIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLA 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488288408 287 IIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPITQIANLMNTIQATVASAERV 355
Cdd:cd18542 224 KYWPLMDFLSGLQIVLVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
46-355 |
5.26e-64 |
|
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: 212.68 E-value: 5.26e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 46 IIAVLVLAIAAVVFQIQTPKVLGQATTEIFKGVMkgaaemkqglkitsfpidfdkIGQILLIVIAMYLISAVFNFLQQVI 125
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGS---------------------SGGLLALLVALFLLQAVLSALSSYL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 126 MTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQQNLTQLITSIVTFVGVLWMMLTISWQLT 205
Cdd:cd18551 60 LGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 206 LIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKSFNHEESDQEVFEKENEKLYHAGRKAQFIS 285
Cdd:cd18551 140 LVTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIE 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 286 AIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPITQIANLMNTIQATVASAERV 355
Cdd:cd18551 220 ALIGPLMGLAVQLALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
46-355 |
1.39e-63 |
|
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: 211.63 E-value: 1.39e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 46 IIAVLVLAIAAVVFQIQTPKVLGQATTEIFKGvmkgaaemkqglkitsfPIDFDKIGQILLIVIAMYLISAVFNFLQQVI 125
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIG-----------------SKSLGLLLGLALLLLGAYLLRALLNFLRIYL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 126 MTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQQNLTQLITSIVTFVGVLWMMLTISWQLT 205
Cdd:cd18778 64 NHVAEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 206 LIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKSFNHEESDQEVFEKENEKLYHAGRKAQFIS 285
Cdd:cd18778 144 LLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLW 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 286 AIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPITQIANLMNTIQATVASAERV 355
Cdd:cd18778 224 AIFHPLMEFLTSLGTVLVLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
46-355 |
8.72e-63 |
|
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: 209.58 E-value: 8.72e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 46 IIAVLVLaIAAVVFQIQTPKVLGQATTEIFKGVmkgaaemkqglkitsfpIDFDKIGQILLIVIAMYLISAVFNFLQQVI 125
Cdd:cd18541 2 LLGILFL-ILVDLLQLLIPRIIGRAIDALTAGT-----------------LTASQLLRYALLILLLALLIGIFRFLWRYL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 126 MTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQQNLTQLITSIVTFVGVLWMMLTISWQLT 205
Cdd:cd18541 64 IFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 206 LIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKSFNHEESDQEVFEKENEKLYHAGRKAQFIS 285
Cdd:cd18541 144 LIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVD 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 286 AIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPITQIANLMNTIQATVASAERV 355
Cdd:cd18541 224 ALFFPLIGLLIGLSFLIVLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
380-593 |
1.36e-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: 206.55 E-value: 1.36e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 380 RVSFEHVAFGY--SPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHF 457
Cdd:cd03248 11 IVKFQNVTFAYptRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 458 SMVLQDTWLFTGSIYDNIHYGNEQASEEEVIRAAKAAHVDDFVRKLPEGYQTILNEEASNISQGQRQLITIARAFLANPD 537
Cdd:cd03248 91 SLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488288408 538 VLILDEATSSVDTRTEILIQAAMNRLLENRTSFVVAHRLSTIRDADTIIVMAEGSI 593
Cdd:cd03248 171 VLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
97-355 |
7.09e-61 |
|
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: 204.19 E-value: 7.09e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 97 DFDKIGQILLIVIAMYLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTL 176
Cdd:cd18552 34 DLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 177 QQNLTQLITSIVTFVGVLWMMLTISWQLTLIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKS 256
Cdd:cd18552 114 TSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 257 FNHEESDQEVFEKENEKLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPIT 336
Cdd:cd18552 194 FGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALVLWYGGYQVISGELTPGEFISFITALLLLYQPIK 273
|
250
....*....|....*....
gi 488288408 337 QIANLMNTIQATVASAERV 355
Cdd:cd18552 274 RLSNVNANLQRGLAAAERI 292
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
346-614 |
2.54e-59 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 208.55 E-value: 2.54e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 346 QAtVASAERVFEVLDEEEMVDEPSGIPVETDSPYRVSFEHVAFgYSPE-KLLMKDFNLNVKPGEMVAIVGPTGAGKTTLI 424
Cdd:PRK11174 316 QA-VGAAESLVTFLETPLAHPQQGEKELASNDPVTIEAEDLEI-LSPDgKTLAGPLNFTLPAGQRIALVGPSGAGKTSLL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 425 NLLERF--YdisSGSIKYDGVDTRDLSREELRAHFSMVLQDTWLFTGSIYDNIHYGNEQASEEEVIRAAKAAHVDDFVRK 502
Cdd:PRK11174 394 NALLGFlpY---QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 503 LPEGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLLENRTSFVVAHRLSTIRDA 582
Cdd:PRK11174 471 LPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQW 550
|
250 260 270
....*....|....*....|....*....|..
gi 488288408 583 DTIIVMAEGSIVETGTHDELMAKNGFYADLYN 614
Cdd:PRK11174 551 DQIWVMQDGQIVQQGDYAELSQAGGLFATLLA 582
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
46-355 |
8.37e-59 |
|
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: 198.89 E-value: 8.37e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 46 IIAVLVLAIAAVVFQIQTPKVLGQATTEIfkgvmkgaaemkqgLKITSFPIDFDKIGQILLIVIAMYLISAVFNFLQQVI 125
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDV--------------LIQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 126 MTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQQNLTQLITSIVTFVGVLWMMLTISWQLT 205
Cdd:cd18563 67 LARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 206 LIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKSFNHEESDQEVFEKENEKLYHAGRKAQFIS 285
Cdd:cd18563 147 LLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLW 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 286 AIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPITQIANLMNTIQATVASAERV 355
Cdd:cd18563 227 ATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
137-610 |
3.87e-56 |
|
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: 205.95 E-value: 3.87e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 137 LRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQQNLTQLITSIVTFVGVLWMMLTISwqlTLIALATVPLSL 216
Cdd:TIGR00957 1040 LHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLAT---PIAAVIIPPLGL 1116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 217 IVVMVvaprsQKHFAAQQKSLGLLNN--------QVEETYGGHVVVKSFNHEE-----SDQEVfeKENEKLYHAGRKAQF 283
Cdd:TIGR00957 1117 LYFFV-----QRFYVASSRQLKRLESvsrspvysHFNETLLGVSVIRAFEEQErfihqSDLKV--DENQKAYYPSIVANR 1189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 284 ISAIimpLMNFIKNLGYVFVA---VLGGVKVANGMMDLGdvqafLQYTNQFSQPITQIANLMNTIQATVASAERVFEVLD 360
Cdd:TIGR00957 1190 WLAV---RLECVGNCIVLFAAlfaVISRHSLSAGLVGLS-----VSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSE 1261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 361 EEE----MVDE---PSGIPVETdspyRVSFEHVAFGYSPE-KLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYD 432
Cdd:TIGR00957 1262 TEKeapwQIQEtapPSGWPPRG----RVEFRNYCLRYREDlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINE 1337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 433 ISSGSIKYDGVDTRDLSREELRAHFSMVLQDTWLFTGSIYDNIH-YGneQASEEEVIRAAKAAHVDDFVRKLPEGYQTIL 511
Cdd:TIGR00957 1338 SAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDpFS--QYSDEEVWWALELAHLKTFVSALPDKLDHEC 1415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 512 NEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLLENRTSFVVAHRLSTIRDADTIIVMAEG 591
Cdd:TIGR00957 1416 AEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKG 1495
|
490 500
....*....|....*....|
gi 488288408 592 SIVETGTHDELMAKNG-FYA 610
Cdd:TIGR00957 1496 EVAEFGAPSNLLQQRGiFYS 1515
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
159-576 |
4.93e-56 |
|
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: 198.35 E-value: 4.93e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 159 GDIMSRAINDMDNIASTLQQNLTQLITSIVTFVGVLWMMLTISWQLTLIALATVPLSLIVVMVVAPR-SQKHFAAQQKSL 237
Cdd:TIGR02868 110 GDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAAGLLLAGFVAPLVSLRaARAAEQALARLR 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 238 GLLNNQVEETYGGHVVVKSFNHEESDQEVFEKENEKLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMD 317
Cdd:TIGR02868 190 GELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLA 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 318 LGDVQAF----LQYTNQFSqPITQIANlmnTIQATVASAERVFEVLDEEEMVDEPSG---IPVETDSPYRVsFEHVAFGY 390
Cdd:TIGR02868 270 PVTLAVLvllpLAAFEAFA-ALPAAAQ---QLTRVRAAAERIVEVLDAAGPVAEGSApaaGAVGLGKPTLE-LRDLSAGY 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 391 SPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMVLQDTWLFTGS 470
Cdd:TIGR02868 345 PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTT 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 471 IYDNIHYGNEQASEEEVIRAAKAAHVDDFVRKLPEGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDT 550
Cdd:TIGR02868 425 VRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDA 504
|
410 420
....*....|....*....|....*.
gi 488288408 551 RTEILIQAAMNRLLENRTSFVVAHRL 576
Cdd:TIGR02868 505 ETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
46-355 |
3.05e-55 |
|
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: 189.24 E-value: 3.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 46 IIAVLVLAIAAVVFQIQTPKVLGQAtteIFKGVMKGaaemkqglkitsfpiDFDKIGQILLIVIAMYLISAVFNFLQQVI 125
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYG---IDSGVRAG---------------DLGVLLLAAAAYLAVVLAGWVAQRAQTRL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 126 MTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQQNLTQLITSIVTFVGVLWMMLTISWQLT 205
Cdd:cd18546 63 TGRTGERLLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 206 LIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKSFNHEESDQEVFEKENEKLYHAGRKAQFIS 285
Cdd:cd18546 143 LVALAALPPLALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLV 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 286 AIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPITQIANLMNTIQATVASAERV 355
Cdd:cd18546 223 AIYFPGVELLGNLATAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
348-616 |
5.28e-53 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 190.81 E-value: 5.28e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 348 TVASAERVFEVLDEEEMVDEPSGIPVETDSPyRVSFEHVAFGYSPEKL-LMKDFNLNVKPGEMVAIVGPTGAGKTTLINL 426
Cdd:PRK11160 307 VIASARRINEITEQKPEVTFPTTSTAAADQV-SLTLNNVSFTYPDQPQpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 427 LERFYDISSGSIKYDGVDTRDLSREELRAHFSMVLQDTWLFTGSIYDNIHYGNEQASEEEVIRAAK----AAHVDDfvrk 502
Cdd:PRK11160 386 LTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQqvglEKLLED---- 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 503 lPEGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLLENRTSFVVAHRLSTIRDA 582
Cdd:PRK11160 462 -DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQF 540
|
250 260 270
....*....|....*....|....*....|....
gi 488288408 583 DTIIVMAEGSIVETGTHDELMAKNGFYADLYNSQ 616
Cdd:PRK11160 541 DRICVMDNGQIIEQGTHQELLAQQGRYYQLKQRL 574
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
333-605 |
1.57e-52 |
|
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: 189.19 E-value: 1.57e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 333 QPITQIANLMNTIQATVASAERVFEVLDEEEMVDEPSGIPVETdspYRVSFEHVAFGYSP-EKLLMKDFNLNVKPGEMVA 411
Cdd:COG4618 286 APIEQAIGGWKQFVSARQAYRRLNELLAAVPAEPERMPLPRPK---GRLSVENLTVVPPGsKRPILRGVSFSLEPGEVLG 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 412 IVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMVLQDTWLFTGSIYDNI-HYGneQASEEEVIRA 490
Cdd:COG4618 363 VIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 491 AKAAHVDDFVRKLPEGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRL-LENRTS 569
Cdd:COG4618 441 AKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATV 520
|
250 260 270
....*....|....*....|....*....|....*.
gi 488288408 570 FVVAHRLSTIRDADTIIVMAEGSIVETGTHDELMAK 605
Cdd:COG4618 521 VVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
88-355 |
4.30e-52 |
|
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: 181.17 E-value: 4.30e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 88 GLKITSFPIDFDKIGQILLIVIAMYLI---SAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSR 164
Cdd:cd18564 37 GLLGLAPLLGPDPLALLLLAAAALVGIallRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 165 AINDMDNIASTLQQNLTQLITSIVTFVGVLWMMLTISWQLTLIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQV 244
Cdd:cd18564 117 LTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 245 EETYGGHVVVKSFNHEESDQEVFEKENEKLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAF 324
Cdd:cd18564 197 QESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVF 276
|
250 260 270
....*....|....*....|....*....|.
gi 488288408 325 LQYTNQFSQPITQIANLMNTIQATVASAERV 355
Cdd:cd18564 277 LAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
104-605 |
4.69e-52 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 187.56 E-value: 4.69e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 104 ILLIVIAMYLIsaVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDiMSRAINDMDNiastlqqnLTQL 183
Cdd:TIGR01842 46 LMLTVLALGLY--LFLGLLDALRSFVLVRIGEKLDGALNQPIFAASFSATLRRGSGD-GLQALRDLDQ--------LRQF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 184 ITS--IVTFVGVLWM--MLTISWQL-TLIALATVpLSLIVVMVVA---PR-SQKHFAAQQKSLGLLNNQVEETYGGHVVV 254
Cdd:TIGR01842 115 LTGpgLFAFFDAPWMpiYLLVCFLLhPWIGILAL-GGAVVLVGLAllnNRaTKKPLKEATEASIRANNLADSALRNAEVI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 255 KSFNHEESDQEVFEKENEKLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQP 334
Cdd:TIGR01842 194 EAMGMMGNLTKRWGRFHSKYLSAQSAASDRAGMLSNLSKYFRIVLQSLVLGLGAYLAIDGEITPGMMIAGSILVGRALAP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 335 ITQIANLMNTIQATVASAERVFEVLDEEEMVDEPSGIPvetDSPYRVSFEHVAFGYSPEKL-LMKDFNLNVKPGEMVAIV 413
Cdd:TIGR01842 274 IDGAIGGWKQFSGARQAYKRLNELLANYPSRDPAMPLP---EPEGHLSVENVTIVPPGGKKpTLRGISFSLQAGEALAII 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 414 GPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMVLQDTWLFTGSIYDNIHYGNEQASEEEVIRAAKA 493
Cdd:TIGR01842 351 GPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKL 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 494 AHVDDFVRKLPEGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRL-LENRTSFVV 572
Cdd:TIGR01842 431 AGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVI 510
|
490 500 510
....*....|....*....|....*....|...
gi 488288408 573 AHRLSTIRDADTIIVMAEGSIVETGTHDELMAK 605
Cdd:TIGR01842 511 THRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
97-354 |
3.30e-50 |
|
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: 175.72 E-value: 3.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 97 DFDKIGQILLIVIAMYLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTL 176
Cdd:cd18549 37 NLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISELA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 177 QQNLTQLITSIVTFVGVLWMMLTISWQLTLIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKS 256
Cdd:cd18549 117 HHGPEDLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 257 FNHEESDQEVFEKENEKLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPIT 336
Cdd:cd18549 197 FANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIR 276
|
250
....*....|....*...
gi 488288408 337 QIANLMNTIQATVASAER 354
Cdd:cd18549 277 RLVNFTEQYQKGMAGFER 294
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
97-355 |
6.67e-50 |
|
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: 174.98 E-value: 6.67e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 97 DFDKIGQILLIVIAMYLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTL 176
Cdd:cd18576 31 DTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 177 QQNLTQLITSIVTFVGVLWMMLTISWQLTLIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKS 256
Cdd:cd18576 111 TTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 257 FNHEESDQEVFEKENEKLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPIT 336
Cdd:cd18576 191 FTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIG 270
|
250
....*....|....*....
gi 488288408 337 QIANLMNTIQATVASAERV 355
Cdd:cd18576 271 SLADLYGQLQKALGASERV 289
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
46-355 |
1.09e-49 |
|
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: 174.51 E-value: 1.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 46 IIAVLVLAIAAVVFQIQTPKVLGQATTEifkGVMKGaaemkqglkitsfpiDFDKIGQILLIVIAMYLISAVFNFLQQVI 125
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDE---GIANG---------------DLSYILRTGLLMLLLALLGLIAGILAGYF 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 126 MTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQQNLTQLITSIVTFVGVLWMMLTISWQLT 205
Cdd:cd18548 63 AAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 206 LIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKSFNHEESDQEVFEKENEKLYHAGRKAQFIS 285
Cdd:cd18548 143 LILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLM 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 286 AIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPITQIANLMNTIQATVASAERV 355
Cdd:cd18548 223 ALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKRI 292
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
46-335 |
1.14e-49 |
|
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: 173.60 E-value: 1.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 46 IIAVLVLAIAAVVFQIQTPKVLGQATTEIFKGVMKgaaemkqglkitsfpiDFDKIGQILLIVIAMYLISAVFNFLQQVI 125
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDP----------------ETQALNVYSLALLLLGLAQFILSFLQSYL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 126 MTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQQNLTQLITSIVTFVGVLWMMLTISWQLT 205
Cdd:pfam00664 65 LNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 206 LIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKSFNHEESDQEVFEKENEKLYHAGRKAQFIS 285
Cdd:pfam00664 145 LVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVAN 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 488288408 286 AIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPI 335
Cdd:pfam00664 225 GLSFGITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
380-598 |
8.71e-47 |
|
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: 163.74 E-value: 8.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 380 RVSFEHVAFGYSPE-KLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFS 458
Cdd:cd03369 6 EIEVENLSVRYAPDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 459 MVLQDTWLFTGSIYDNIHYGNEQaSEEEVIRAAKAAhvddfvrklpegyqtilnEEASNISQGQRQLITIARAFLANPDV 538
Cdd:cd03369 86 IIPQDPTLFSGTIRSNLDPFDEY-SDEEIYGALRVS------------------EGGLNLSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 539 LILDEATSSVDTRTEILIQAAMNRLLENRTSFVVAHRLSTIRDADTIIVMAEGSIVETGT 598
Cdd:cd03369 147 LVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
99-616 |
2.49e-46 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 176.76 E-value: 2.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 99 DKIGQILLIVIAMYLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQQ 178
Cdd:PTZ00265 94 ENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 179 NLTQLITSIVTFVGVLWMMLTISWQLTLIALATVPLSLIVVMVVaprsQKHFAAQQKSLGLLNNQ----VEETYGGHVVV 254
Cdd:PTZ00265 174 KFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVIC----NKKVKINKKTSLLYNNNtmsiIEEALVGIRTV 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 255 KSFNHEESdqeVFEKEN--EKLYHA-GRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDL--------GDVQA 323
Cdd:PTZ00265 250 VSYCGEKT---ILKKFNlsEKLYSKyILKANFMESLHIGMINGFILASYAFGFWYGTRIIISDLSNQqpnndfhgGSVIS 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 324 FLQ--YTNQFSQPIT--QIANLMNTIQATvasaERVFEVLDEEEMVDEPSGIPVETDSPyRVSFEHVAFGYSPEK--LLM 397
Cdd:PTZ00265 327 ILLgvLISMFMLTIIlpNITEYMKSLEAT----NSLYEIINRKPLVENNDDGKKLKDIK-KIQFKNVRFHYDTRKdvEIY 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 398 KDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKY-DGVDTRDLSREELRAHFSMVLQDTWLFTGSIYDNIH 476
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIK 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 477 YG--------------NEQAS-------------------------------------------EEEVIRAAKAAHVDDF 499
Cdd:PTZ00265 482 YSlyslkdlealsnyyNEDGNdsqenknkrnscrakcagdlndmsnttdsneliemrknyqtikDSEVVDVSKKVLIHDF 561
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 500 VRKLPEGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLL--ENRTSFVVAHRLS 577
Cdd:PTZ00265 562 VSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLS 641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 578 TIRDADTIIVMA----------------------------------------------EGS-IVETGTHDELMA-KNGFY 609
Cdd:PTZ00265 642 TIRYANTIFVLSnrergstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnAGSyIIEQGTHDALMKnKNGIY 721
|
....*..
gi 488288408 610 ADLYNSQ 616
Cdd:PTZ00265 722 YTMINNQ 728
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
46-355 |
3.86e-46 |
|
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: 164.58 E-value: 3.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 46 IIAVLVLAIAAVVFQIQTPKVLGQatteIFKGVMKGAaemkqglkitsfpiDFDKIGQILLIVIAMYLISAVFNFLQQVI 125
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRR----AIDGPIAHG--------------DRSALWPLVLLLLALGVAEAVLSFLRRYL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 126 MTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMdniaSTLQQNLT---QLITSIVTFVGVLWMMLTISW 202
Cdd:cd18543 63 AGRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDL----SLVQRFLAfgpFLLGNLLTLVVGLVVMLVLSP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 203 QLTLIALATVPLslivVMVVAPRSQKHF-----AAQQKsLGLLNNQVEETYGGHVVVKSFNHEESDQEVFEKENEKLYHA 277
Cdd:cd18543 139 PLALVALASLPP----LVLVARRFRRRYfpasrRAQDQ-AGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRAT 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488288408 278 GRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPITQIANLMNTIQATVASAERV 355
Cdd:cd18543 214 RLRAARLRARFWPLLEALPELGLAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
16-609 |
4.83e-46 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 175.60 E-value: 4.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 16 RNIGAKGPK-PKNFWKTVKRLFRYmsKRMLSIIAVLVLAIAAV--VFQIQTPKVLGQatteIFKGVMKGAAEMKQGLkit 92
Cdd:PTZ00265 800 RNLFKRKPKaPNNLRIVYREIFSY--KKDVTIIALSILVAGGLypVFALLYAKYVST----LFDFANLEANSNKYSL--- 870
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 93 sfpidfdkigQILLIVIAMYLISAVFNFLQQVIMTRVSQ---RTVYE--LRQEleakmnkvpISYYDTHSNG-DIMSRAI 166
Cdd:PTZ00265 871 ----------YILVIAIAMFISETLKNYYNNVIGEKVEKtmkRRLFEniLYQE---------ISFFDQDKHApGLLSAHI 931
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 167 N-DMDNIASTLQQNLTQLITSIVTFVgvlwMMLTISWQLTLIALATVPLSLIVVM-VVAPRS--------QKHFAAQQKS 236
Cdd:PTZ00265 932 NrDVHLLKTGLVNNIVIFTHFIVLFL----VSMVMSFYFCPIVAAVLTGTYFIFMrVFAIRArltankdvEKKEINQPGT 1007
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 237 LGLLNNQVE------------------------ETYGGHVVVKSFNHEESDQEVFEKENEKLYHAGRKAQFisaiimplm 292
Cdd:PTZ00265 1008 VFAYNSDDEifkdpsfliqeafynmntviiyglEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQL--------- 1078
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 293 nFIKNLGYVFVAVL---GGVKVANGMMDLGdvqAFLqYTNQFSqpiTQIANLMNTIQATVASAERVFEVLDEEEMVD--E 367
Cdd:PTZ00265 1079 -FINSFAYWFGSFLirrGTILVDDFMKSLF---TFL-FTGSYA---GKLMSLKGDSENAKLSFEKYYPLIIRKSNIDvrD 1150
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 368 PSGIPVET--DSPYRVSFEHVAFGY--SPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDI---------- 433
Cdd:PTZ00265 1151 NGGIRIKNknDIKGKIEIMDVNFRYisRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkn 1230
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 434 --------------------------------------------SSGSIKYDGVDTRDLSREELRAHFSMVLQDTWLFTG 469
Cdd:PTZ00265 1231 ehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNM 1310
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 470 SIYDNIHYGNEQASEEEVIRAAKAAHVDDFVRKLPEGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVD 549
Cdd:PTZ00265 1311 SIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488288408 550 TRTEILIQAAMNRLLE--NRTSFVVAHRLSTIRDADTIIVMAE----GSIVET-GTHDELM-AKNGFY 609
Cdd:PTZ00265 1391 SNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQAhGTHEELLsVQDGVY 1458
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
96-355 |
6.64e-46 |
|
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: 163.89 E-value: 6.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 96 IDFDKIGQILLIVIAMYLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIAST 175
Cdd:cd18557 30 GDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 176 LQQNLTQLITSIVTFVGVLWMMLTISWQLTLIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVK 255
Cdd:cd18557 110 VTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 256 SFNHEESDQEVFEKENEKLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPI 335
Cdd:cd18557 190 SFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSV 269
|
250 260
....*....|....*....|
gi 488288408 336 TQIANLMNTIQATVASAERV 355
Cdd:cd18557 270 GGLSSLLADIMKALGASERV 289
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
46-355 |
9.01e-44 |
|
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: 158.88 E-value: 9.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 46 IIAVLVLAIAAVVFQIQTPKVLGQATTEIFKGVMKGAAEMKQGLKITsfpidfDKIGQILL---IVIAMYLISAVFNFLQ 122
Cdd:cd18565 1 LVLGLLASILNRLFDLAPPLLIGVAIDAVFNGEASFLPLVPASLGPA------DPRGQLWLlggLTVAAFLLESLFQYLS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 123 QVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQQNLTQLITSIVTFVGVLWMMLTISW 202
Cdd:cd18565 75 GVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 203 QLTLIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKSFNHEESDQEVFEKENEKLYHAGRKAQ 282
Cdd:cd18565 155 QLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAI 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488288408 283 FISAIIMPLMNFIKNLGYVFVAVLGGVKVANGM------MDLGDVQAFLQYTNQFSQPITQIANLMNTIQATVASAERV 355
Cdd:cd18565 235 RLRAAFFPVIRLVAGAGFVATFVVGGYWVLDGPplftgtLTVGTLVTFLFYTQRLLWPLTRLGDLIDQYQRAMASAKRV 313
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
381-605 |
9.34e-44 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 156.34 E-value: 9.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYSPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMV 460
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 461 LQ--DTWLFTGSIYDNIHYG--NEQASEEEVIRAAKAAhVDDFvrklpeGYQTILNEEASNISQGQRQLITIARAFLANP 536
Cdd:COG1122 81 FQnpDDQLFAPTVEEDVAFGpeNLGLPREEIRERVEEA-LELV------GLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488288408 537 DVLILDEATSSVDTRTEILIQAAMNRLLENRTSFVVA-HRLSTIRD-ADTIIVMAEGSIVETGTHDELMAK 605
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVAElADRVIVLDDGRIVADGTPREVFSD 224
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
394-612 |
1.41e-43 |
|
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: 156.61 E-value: 1.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 394 KLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMVLQDTWLFTGSIYD 473
Cdd:cd03288 34 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 474 NIHyGNEQASEEEVIRAAKAAHVDDFVRKLPEGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTE 553
Cdd:cd03288 114 NLD-PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 554 ILIQAAMNRLLENRTSFVVAHRLSTIRDADTIIVMAEGSIVETGTHDELMA-KNGFYADL 612
Cdd:cd03288 193 NILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAqEDGVFASL 252
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
304-607 |
4.08e-42 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 163.99 E-value: 4.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 304 AVLGGVKVANGMMDLGDVQAFLQYTNQFSQPITQIANLMNTIQATVASAERVFEVLD---EEEMVDE----PSGIPvetd 376
Cdd:PLN03232 1155 AVLRNGNAENQAGFASTMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDlpsEATAIIEnnrpVSGWP---- 1230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 377 SPYRVSFEHVAFGYSPE-KLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRA 455
Cdd:PLN03232 1231 SRGSIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRR 1310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 456 HFSMVLQDTWLFTGSIYDNIHYGNEQaSEEEVIRAAKAAHVDDFVRKLPEGYQTILNEEASNISQGQRQLITIARAFLAN 535
Cdd:PLN03232 1311 VLSIIPQSPVLFSGTVRFNIDPFSEH-NDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRR 1389
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488288408 536 PDVLILDEATSSVDTRTEILIQAAMNRLLENRTSFVVAHRLSTIRDADTIIVMAEGSIVETGTHDELMAKNG 607
Cdd:PLN03232 1390 SKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
338-621 |
1.98e-41 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 161.83 E-value: 1.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 338 IANLMNTI--QATVA-----SAERV---FEVLDEEEMVDE----PSGIPvetdSPYRVSFEHVAFGYSPE-KLLMKDFNL 402
Cdd:PLN03130 1185 ITSLLTAVlrLASLAenslnAVERVgtyIDLPSEAPLVIEnnrpPPGWP----SSGSIKFEDVVLRYRPElPPVLHGLSF 1260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 403 NVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMVLQDTWLFTGSIYDNIHYGNEQa 482
Cdd:PLN03130 1261 EISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEH- 1339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 483 SEEEVIRAAKAAHVDDFVRKLPEGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNR 562
Cdd:PLN03130 1340 NDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIRE 1419
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 488288408 563 LLENRTSFVVAHRLSTIRDADTIIVMAEGSIVETGTHDELMAKNGfyadlynSQFSEEV 621
Cdd:PLN03130 1420 EFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG-------SAFSKMV 1471
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
95-355 |
4.97e-41 |
|
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: 150.71 E-value: 4.97e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 95 PIDFDKIGQILLIVIAMYLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIAS 174
Cdd:cd18540 35 PGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 175 TLQQNLTQLITSIVTFVGVLWMMLTISWQLTLIALATVPLSLIVVMVVaprsQKHFAAQQKSLGLLNNQV----EETYGG 250
Cdd:cd18540 115 IISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSIYF----QKKILKAYRKVRKINSRItgafNEGITG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 251 HVVVKSFNHEESDQEVFEKENEKLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQ 330
Cdd:cd18540 191 AKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIATALVLWYGGILVLAGAITIGTLVAFISYATQ 270
|
250 260
....*....|....*....|....*
gi 488288408 331 FSQPITQIANLMNTIQATVASAERV 355
Cdd:cd18540 271 FFEPIQQLARVLAELQSAQASAERV 295
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
382-593 |
3.30e-40 |
|
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: 144.67 E-value: 3.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 382 SFEHVAFGYS-PEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMV 460
Cdd:cd03246 2 EVENVSFRYPgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 461 LQDTWLFTGSIYDNIhygneqaseeeviraakaahvddfvrklpegyqtilneeasnISQGQRQLITIARAFLANPDVLI 540
Cdd:cd03246 82 PQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488288408 541 LDEATSSVDTRTEILIQAAMNRL-LENRTSFVVAHRLSTIRDADTIIVMAEGSI 593
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
381-592 |
3.68e-40 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 145.30 E-value: 3.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYSPE----KLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLL--ErfYDISSGSIKYDGvdtrdlsreelr 454
Cdd:cd03250 1 ISVEDASFTWDSGeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSVSVPG------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 455 aHFSMVLQDTWLFTGSIYDNIHYGNEQASE--EEVIRAAkaAHVDDFvRKLPEGYQTILNEEASNISQGQRQLITIARAF 532
Cdd:cd03250 67 -SIAYVSQEPWIQNGTIRENILFGKPFDEEryEKVIKAC--ALEPDL-EILPDGDLTEIGEKGINLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488288408 533 LANPDVLILDEATSSVDTRTE--ILIQAAMNRLLENRTSFVVAHRLSTIRDADTIIVMAEGS 592
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVGrhIFENCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
381-604 |
1.28e-39 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 152.36 E-value: 1.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGY----SPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRA- 455
Cdd:COG1123 261 LEVRNLSKRYpvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREl 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 456 --HFSMVLQDTW--LFTG-SIYDNIHYG---NEQASEEEviRAAKAAHVDDFVRkLPEGYqtiLNEEASNISQGQRQLIT 527
Cdd:COG1123 341 rrRVQMVFQDPYssLNPRmTVGDIIAEPlrlHGLLSRAE--RRERVAELLERVG-LPPDL---ADRYPHELSGGQRQRVA 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 528 IARAFLANPDVLILDEATSSVDTRteilIQAA-MNRLLE-----NRTSFVVAHRLSTIRD-ADTIIVMAEGSIVETGTHD 600
Cdd:COG1123 415 IARALALEPKLLILDEPTSALDVS----VQAQiLNLLRDlqrelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTE 490
|
....
gi 488288408 601 ELMA 604
Cdd:COG1123 491 EVFA 494
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
97-355 |
3.06e-39 |
|
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: 145.70 E-value: 3.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 97 DFDKIGQILLIVIAMYLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTL 176
Cdd:cd18550 34 DLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 177 QQNLTQLITSIVTFVGVLWMMLTISWQLTLIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETY--GGHVVV 254
Cdd:cd18550 114 TGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLsvSGALLV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 255 KSFNHEESDQEVFEKENEKLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQP 334
Cdd:cd18550 194 KLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGP 273
|
250 260
....*....|....*....|.
gi 488288408 335 ITQIANLMNTIQATVASAERV 355
Cdd:cd18550 274 LTQLLNIQVDLMTSLALFERI 294
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
104-355 |
1.28e-38 |
|
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: 143.84 E-value: 1.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 104 ILLIVIAmyLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQQNLTQL 183
Cdd:cd18572 40 LLLLLLS--VLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 184 ITSIVTFVGVLWMMLTISWQLTLIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKSFNHEESD 263
Cdd:cd18572 118 LRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEERE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 264 QEVFEKENEKLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPITQIANLMN 343
Cdd:cd18572 198 ARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFS 277
|
250
....*....|..
gi 488288408 344 TIQATVASAERV 355
Cdd:cd18572 278 SLMQAVGAAEKV 289
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
398-546 |
1.73e-38 |
|
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: 138.93 E-value: 1.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 398 KDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMVLQDTWLFTG-SIYDNIH 476
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENLR 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488288408 477 YGneqASEEEVIRAAKAAHVDDFVRKLPEGYQ--TILNEEASNISQGQRQLITIARAFLANPDVLILDEATS 546
Cdd:pfam00005 82 LG---LLLKGLSKREKDARAEEALEKLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
382-591 |
3.24e-38 |
|
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: 138.53 E-value: 3.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 382 SFEHVAFGYsPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMVL 461
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 462 QdtwlftgsiydnihygneqaseeeviraakaahvddfvrklpegyqtilneeasnISQGQRQLITIARAFLANPDVLIL 541
Cdd:cd00267 80 Q-------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488288408 542 DEATSSVDTRTEILIQAAMNRLL-ENRTSFVVAHRLSTIRDA-DTIIVMAEG 591
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
398-605 |
1.77e-37 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 139.04 E-value: 1.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 398 KDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDlSREELRAHFSMVLQDTWLFTG-SIYDNIH 476
Cdd:COG1131 17 DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYVPQEPALYPDlTVRENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 477 -----YGNEQASEEEVI-RAAKAAHVDDFVRKLPEGYqtilneeasniSQGQRQLITIARAFLANPDVLILDEATSSVDT 550
Cdd:COG1131 96 ffarlYGLPRKEARERIdELLELFGLTDAADRKVGTL-----------SGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488288408 551 RTEILIQAAMNRLL-ENRTSFVVAHRLSTI-RDADTIIVMAEGSIVETGTHDELMAK 605
Cdd:COG1131 165 EARRELWELLRELAaEGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
381-602 |
2.29e-37 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 138.47 E-value: 2.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYSPEKLLmKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDI-----SSGSIKYDGVD--TRDLSREEL 453
Cdd:cd03260 1 IELRDLNVYYGDKHAL-KDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDiyDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 454 RAHFSMVLQDTWLFTGSIYDNIHYG-------NEQASEEEVIRAAKAAHVDDFV-RKLpegyqtilneEASNISQGQRQL 525
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAALWDEVkDRL----------HALGLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488288408 526 ITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLLENRTSFVVAHRLS-TIRDADTIIVMAEGSIVETGTHDEL 602
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQqAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
382-591 |
2.70e-37 |
|
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: 137.98 E-value: 2.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 382 SFEHVAFGY-SPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMV 460
Cdd:cd03225 1 ELKNLSFSYpDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 461 LQ--DTWLFTGSIYDNIHYG--NEQASEEEVIRAAKAAhVDDFvrklpeGYQTILNEEASNISQGQRQLITIARAFLANP 536
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVAFGleNLGLPEEEIEERVEEA-LELV------GLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488288408 537 DVLILDEATSSVDTRTEILIQAAMNRLLENRTSFVVA-HRLSTIRD-ADTIIVMAEG 591
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDG 210
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
380-597 |
4.84e-37 |
|
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: 137.64 E-value: 4.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 380 RVSFEHvafGYSPEKLLmKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREEL---RAH 456
Cdd:cd03257 8 SVSFPT---GGGSVKAL-DDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 457 FSMVLQD-------TWlftgSIYDNI------HYGNEQASEEEVIRAAKAAHV---DDFVRKLPegYQtilneeasnISQ 520
Cdd:cd03257 84 IQMVFQDpmsslnpRM----TIGEQIaeplriHGKLSKKEARKEAVLLLLVGVglpEEVLNRYP--HE---------LSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 521 GQRQLITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLLENR-TSFV-VAHRLSTIRD-ADTIIVMAEGSIVETG 597
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELgLTLLfITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
381-605 |
1.94e-36 |
|
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: 136.17 E-value: 1.94e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVA--FGYSPEKL-LMKDFNLNVKPGEMVAIVGPTGAGKTTL---INLLERFydiSSGSIKYDGVDTRDLSREELR 454
Cdd:cd03258 2 IELKNVSkvFGDTGGKVtALKDVSLSVPKGEIFGIIGRSGAGKSTLircINGLERP---TSGSVLVDGTDLTLLSGKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 455 A---HFSMVLQDTWLFTG-SIYDNIHYGNEQASEEEVIRAAKAAHVDDFVRklpegyqtiLNEEA----SNISQGQRQLI 526
Cdd:cd03258 79 KarrRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERVLELLELVG---------LEDKAdaypAQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 527 TIARAFLANPDVLILDEATSSVD--TRTEILiqaamNRLLE-NR----TSFVVAHRLSTIRD-ADTIIVMAEGSIVETGT 598
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDpeTTQSIL-----ALLRDiNRelglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGT 224
|
....*..
gi 488288408 599 HDELMAK 605
Cdd:cd03258 225 VEEVFAN 231
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
97-355 |
2.27e-36 |
|
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: 137.96 E-value: 2.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 97 DFDKIGQILLIVIAMYLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRaINDMDNIASTL 176
Cdd:cd18570 37 DINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISR-FNDANKIREAI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 177 QQNLTQLITSIVTFVGVLWMMLTISWQLTLIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKS 256
Cdd:cd18570 116 SSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 257 FNHEESDQEVFEKENEKLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPIT 336
Cdd:cd18570 196 LNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIE 275
|
250
....*....|....*....
gi 488288408 337 QIANLMNTIQATVASAERV 355
Cdd:cd18570 276 NLINLQPKIQEAKVAADRL 294
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
381-597 |
6.25e-36 |
|
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: 134.18 E-value: 6.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYSPEKLLMkDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREelRAHFSMV 460
Cdd:cd03259 1 LELKGLSKTYGSVRALD-DLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 461 LQDTWLFTG-SIYDNIHYG------NEQASEEEVIRAAKAAHVDDFVRKLPEGyqtilneeasnISQGQRQLITIARAFL 533
Cdd:cd03259 78 FQDYALFPHlTVAENIAFGlklrgvPKAEIRARVRELLELVGLEGLLNRYPHE-----------LSGGQQQRVALARALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488288408 534 ANPDVLILDEATSSVDTRTEILIQAAMNRLLENR--TSFVVAHRLS-TIRDADTIIVMAEGSIVETG 597
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
381-597 |
1.56e-34 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 128.97 E-value: 1.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYSP-EKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLsREELRAHFSM 459
Cdd:cd03247 1 LSINNVSFSYPEqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 460 VLQDTWLFTGSIYDNIhygneqaseeeviraakaahvddfvrklpeGYQtilneeasnISQGQRQLITIARAFLANPDVL 539
Cdd:cd03247 80 LNQRPYLFDTTLRNNL------------------------------GRR---------FSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488288408 540 ILDEATSSVDTRTEILIQAAMNRLLENRTSFVVAHRLSTIRDADTIIVMAEGSIVETG 597
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
48-355 |
1.93e-34 |
|
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: 132.64 E-value: 1.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 48 AVLVLAIAAVVfQIQTPKVLGQATTEIFKGVMkgaaemkqglkitSFPIDFDKIGQILLIVIAMYLISAVFNFLQQVIMT 127
Cdd:cd18573 1 ALALLLVSSAV-TMSVPFAIGKLIDVASKESG-------------DIEIFGLSLKTFALALLGVFVVGAAANFGRVYLLR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 128 RVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQQNLTQLITSIVTFVGVLWMMLTISWQLTLI 207
Cdd:cd18573 67 IAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 208 ALATVPLsLIVVMVVAPRSQKHFAAQ-QKSLGLLNNQVEETYGGHVVVKSFNHEESDQEVFEKENEKLYHAGRKAQFISA 286
Cdd:cd18573 147 MLLVVPP-IAVGAVFYGRYVRKLSKQvQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASG 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488288408 287 IIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPITQIANLMNTIQATVASAERV 355
Cdd:cd18573 226 LFFGSTGFSGNLSLLSVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
384-607 |
2.18e-34 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 130.75 E-value: 2.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 384 EHVAFGYSPEKLLmKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSReELRAHFSMVLQD 463
Cdd:COG4555 5 ENLSKKYGKVPAL-KDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR-EARRQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 464 TWLFTG-SIYDNIHYGNEQASEEeviRAAKAAHVDDFVRKLpeGYQTILNEEASNISQGQRQLITIARAFLANPDVLILD 542
Cdd:COG4555 83 RGLYDRlTVRENIRYFAELYGLF---DEELKKRIEELIELL--GLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488288408 543 EATSSVDTRTEILIQAAMNRLL-ENRTSFVVAHRLSTI-RDADTIIVMAEGSIVETGTHDELMAKNG 607
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVeALCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
150-602 |
3.44e-34 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 139.53 E-value: 3.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 150 ISYYDTHSNGDIMSRAINDMDNIASTLQQNLTQLITsivTFVGVLWMMLTISWQLTLIALATVPLSLIV--VMVV---AP 224
Cdd:PTZ00243 1046 MSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQ---CLFSICSSILVTSASQPFVLVALVPCGYLYyrLMQFynsAN 1122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 225 RSQKHFAAQQKSLglLNNQVEETYGGHVVVKSFNHEESD-QEVFEK----------ENEKLYHAGRKAQFISAIIMPLMN 293
Cdd:PTZ00243 1123 REIRRIKSVAKSP--VFTLLEEALQGSATITAYGKAHLVmQEALRRldvvyscsylENVANRWLGVRVEFLSNIVVTVIA 1200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 294 FIKnlgyVFVAVLGGVKVANGMMDLGDVQAfLQYTNQFSQPITQIAnlmnTIQATVASAERVFEVLDE---EEM------ 364
Cdd:PTZ00243 1201 LIG----VIGTMLRATSQEIGLVSLSLTMA-MQTTATLNWLVRQVA----TVEADMNSVERLLYYTDEvphEDMpeldee 1271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 365 ------------------VDEPSGIPVETDSPYR---VSFEHVAFGYS---PekLLMKDFNLNVKPGEMVAIVGPTGAGK 420
Cdd:PTZ00243 1272 vdalerrtgmaadvtgtvVIEPASPTSAAPHPVQagsLVFEGVQMRYReglP--LVLRGVSFRIAPREKVGIVGRTGSGK 1349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 421 TTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMVLQDTWLFTGSIYDNIHYGNEqASEEEVIRAAKAAHVDDFV 500
Cdd:PTZ00243 1350 STLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLE-ASSAEVWAALELVGLRERV 1428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 501 RKLPEGYQTILNEEASNISQGQRQLITIARAFLANPDVLIL-DEATSSVDTRTEILIQAAMNRLLENRTSFVVAHRLSTI 579
Cdd:PTZ00243 1429 ASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTV 1508
|
490 500
....*....|....*....|...
gi 488288408 580 RDADTIIVMAEGSIVETGTHDEL 602
Cdd:PTZ00243 1509 AQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
380-603 |
3.81e-34 |
|
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: 130.55 E-value: 3.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 380 RVSFEHVAFGYsPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSM 459
Cdd:COG1120 1 MLEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 460 VLQDT---WLFTgsIYDNIHYG---------NEQASEEEVIRAA-KAAHVDDFVRKLpegyqtilneeASNISQGQRQLI 526
Cdd:COG1120 80 VPQEPpapFGLT--VRELVALGryphlglfgRPSAEDREAVEEAlERTGLEHLADRP-----------VDELSGGERQRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 527 TIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRL--LENRTSFVVAHRLS-TIRDADTIIVMAEGSIVETGTHDELM 603
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
381-604 |
9.06e-34 |
|
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: 128.94 E-value: 9.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYSPEKLLmKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREEL---RAHF 457
Cdd:COG1127 6 IEVRNLTKSFGDRVVL-DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELyelRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 458 SMVLQDTWLFTG-SIYDNIHYG---NEQASEEEVIRAA----KAAHVDDFVRKLPegyqtilneeaSNISQGQRQLITIA 529
Cdd:COG1127 85 GMLFQGGALFDSlTVFENVAFPlreHTDLSEAEIRELVleklELVGLPGAADKMP-----------SELSGGMRKRVALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 530 RAFLANPDVLILDEATSSVD--TRTEI--LIQaAMNRLLeNRTSFVVAHRLSTIRD-ADTIIVMAEGSIVETGTHDELMA 604
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDpiTSAVIdeLIR-ELRDEL-GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
381-604 |
1.28e-33 |
|
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: 128.39 E-value: 1.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYSpEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREEL---RAHF 457
Cdd:cd03261 1 IELRGLTKSFG-GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 458 SMVLQDTWLFTG-SIYDNIHYG---NEQASEEEVIRAAK----AAHVDDFVRKLPegyqtilneeaSNISQGQRQLITIA 529
Cdd:cd03261 80 GMLFQSGALFDSlTVFENVAFPlreHTRLSEEEIREIVLekleAVGLRGAEDLYP-----------AELSGGMKKRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488288408 530 RAFLANPDVLILDEATSSVDTRTEILIQAAMNRLLE--NRTSFVVAHRLSTIRD-ADTIIVMAEGSIVETGTHDELMA 604
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
383-591 |
3.90e-33 |
|
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: 124.99 E-value: 3.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 383 FEHVAFGYsPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSRE--ELRAHFSMV 460
Cdd:cd03229 3 LKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRIGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 461 LQDTWLFTG-SIYDNIHYGneqaseeeviraakaahvddfvrklpegyqtilneeasnISQGQRQLITIARAFLANPDVL 539
Cdd:cd03229 82 FQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488288408 540 ILDEATSSVDTRTEILIQAAMNRLLEN--RTSFVVAHRLS-TIRDADTIIVMAEG 591
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDeAARLADRVVVLRDG 177
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
99-355 |
4.76e-33 |
|
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: 128.75 E-value: 4.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 99 DKIGQILLIVIAMYLISAVFNFLQQVIMTRVSQRTVYELRQE-LEAKMNKvPISYYDTHSNGDIMSRAINDMDNIASTLQ 177
Cdd:cd18577 44 DDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRyLKALLRQ-DIAWFDKNGAGELTSRLTSDTNLIQDGIG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 178 QNLTQLITSIVTFVGVLWMMLTISWQLTLIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKSF 257
Cdd:cd18577 123 EKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAF 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 258 NHEESDQEVFEKENEKLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDV-QAFLQYTNqFSQPIT 336
Cdd:cd18577 203 GGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDVlTVFFAVLI-GAFSLG 281
|
250
....*....|....*....
gi 488288408 337 QIANLMNTIQATVASAERV 355
Cdd:cd18577 282 QIAPNLQAFAKARAAAAKI 300
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
381-612 |
5.59e-33 |
|
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: 126.65 E-value: 5.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYSPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMV 460
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 461 LQDTWLFTG-SIYDNI-------HYGNEQaseeeviRAAKAAHVDDFVRKLPEGYqtiLNEEASNISQGQRQLITIARAF 532
Cdd:cd03295 81 IQQIGLFPHmTVEENIalvpkllKWPKEK-------IRERADELLALVGLDPAEF---ADRYPHELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 533 LANPDVLILDEATSSVDTRTEILIQAAMNRLLE--NRTSFVVAHRL-STIRDADTIIVMAEGSIVETGTHDELMAK--NG 607
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRSpaND 230
|
....*
gi 488288408 608 FYADL 612
Cdd:cd03295 231 FVAEF 235
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
381-596 |
4.21e-32 |
|
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: 123.74 E-value: 4.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGY---SPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVdtrdlSREELRAHF 457
Cdd:cd03293 1 LEVRNVSKTYgggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE-----PVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 458 SMVLQDT----WLftgSIYDNIHYGNEQA------SEEEVIRAAKAAHVDDFVRKLPegyqtilneeaSNISQGQRQLIT 527
Cdd:cd03293 76 GYVFQQDallpWL---TVLDNVALGLELQgvpkaeARERAEELLELVGLSGFENAYP-----------HQLSGGMRQRVA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488288408 528 IARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLLE--NRTSFVVAHRLS-TIRDADTIIVMAE--GSIVET 596
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVAE 215
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
385-604 |
4.61e-32 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 124.53 E-value: 4.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 385 HVAFGYSPEKL-LMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMVLQD 463
Cdd:COG1124 8 SVSYGQGGRRVpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 464 TwlfTGS------IYD------NIHYGNEQasEEEVIRAAKAAHVD-DFVRKLPegYQtilneeasnISQGQRQLITIAR 530
Cdd:COG1124 88 P---YASlhprhtVDRilaeplRIHGLPDR--EERIAELLEQVGLPpSFLDRYP--HQ---------LSGGQRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 531 AFLANPDVLILDEATSSVD--TRTEILiqaamnRLLE------NRTSFVVAHRLSTI-RDADTIIVMAEGSIVETGTHDE 601
Cdd:COG1124 152 ALILEPELLLLDEPTSALDvsVQAEIL------NLLKdlreerGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVAD 225
|
...
gi 488288408 602 LMA 604
Cdd:COG1124 226 LLA 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
385-604 |
5.32e-32 |
|
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: 130.02 E-value: 5.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 385 HVAFGYSPEKLLmKDFNLNVKPGEMVAIVGPTGAGKTTL---INLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMVL 461
Cdd:COG1123 11 SVRYPGGDVPAV-DGVSLTIAPGETVALVGESGSGKSTLalaLMGLLPHGGRISGEVLLDGRDLLELSEALRGRRIGMVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 462 QD--TWLFTGSIYDNIHYGNE------QASEEEVIRAAKAAHVDDFVRKLPegyqtilneeaSNISQGQRQLITIARAFL 533
Cdd:COG1123 90 QDpmTQLNPVTVGDQIAEALEnlglsrAEARARVLELLEAVGLERRLDRYP-----------HQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488288408 534 ANPDVLILDEATSSVDTRTEILIQAAMNRLLENR--TSFVVAHRLSTIRD-ADTIIVMAEGSIVETGTHDELMA 604
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILA 232
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
381-595 |
6.29e-32 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 123.24 E-value: 6.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYSPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREE---LRAHF 457
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 458 SMVLQDTWLFTG-SIYDNIHY-----GneqASEEEVIRAAKAA--HVD--DFVRKLPEgyqtilneeasNISQGQRQLIT 527
Cdd:COG2884 82 GVVFQDFRLLPDrTVYENVALplrvtG---KSRKEIRRRVREVldLVGlsDKAKALPH-----------ELSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488288408 528 IARAFLANPDVLILDEATSSVDTRT--EILiqaamnRLLE--NR--TSFVVA-HRLSTIRDADT-IIVMAEGSIVE 595
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETswEIM------ELLEeiNRrgTTVLIAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
398-595 |
1.91e-31 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 122.07 E-value: 1.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 398 KDFNLNVKPGEMVAIVGPTGAGKTTLINL---LERFydiSSGSIKYDGVDTRDLSREEL----RAHFSMVLQDTWLFTG- 469
Cdd:COG1136 25 RGVSLSIEAGEFVAIVGPSGSGKSTLLNIlggLDRP---TSGEVLIDGQDISSLSERELarlrRRHIGFVFQFFNLLPEl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 470 SIYDNI----HYGNEQASE--EEVIRAAKAAHVDDFVRKLPegyqtilneeaSNISQGQRQLITIARAFLANPDVLILDE 543
Cdd:COG1136 102 TALENValplLLAGVSRKErrERARELLERVGLGDRLDHRP-----------SQLSGGQQQRVAIARALVNRPKLILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488288408 544 ATSSVDTRTEILIQAAMNRL-LENRTSFVVA-HRLSTIRDADTIIVMAEGSIVE 595
Cdd:COG1136 171 PTGNLDSKTGEEVLELLRELnRELGTTIVMVtHDPELAARADRVIRLRDGRIVS 224
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
167-607 |
2.21e-31 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 131.01 E-value: 2.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 167 NDMDNIASTLQQNLTQLIT------SIVTFVGVLWMMLTISWQL-TLIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGL 239
Cdd:PLN03130 402 NLMTTDAEALQQICQQLHTlwsapfRIIIAMVLLYQQLGVASLIgSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGL 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 240 LNnqveETYGGHVVVKSFNHEESDQ-EVFEKENEKLYHAgRKAQFISAIIMPLMNFIKnlgyVFVAVlggvkVANGMM-- 316
Cdd:PLN03130 482 MN----EVLAAMDTVKCYAWENSFQsKVQTVRDDELSWF-RKAQLLSAFNSFILNSIP----VLVTV-----VSFGVFtl 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 317 ---DLGDVQAFLQYT---------NQFSQPITQIANlmntiqATVaSAERVFEVLDEEEMVDEPSgIPVETDSPyRVSFE 384
Cdd:PLN03130 548 lggDLTPARAFTSLSlfavlrfplFMLPNLITQAVN------ANV-SLKRLEELLLAEERVLLPN-PPLEPGLP-AISIK 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 385 HVAFGYSP--EKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLIN-LLERFYDISSGSIKydgvdtrdlsreeLRAHFSMVL 461
Cdd:PLN03130 619 NGYFSWDSkaERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVV-------------IRGTVAYVP 685
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 462 QDTWLFTGSIYDNIHYGN--EQASEEEVIRAAKAAHVDDFvrkLPEGYQTILNEEASNISQGQRQLITIARAFLANPDVL 539
Cdd:PLN03130 686 QVSWIFNATVRDNILFGSpfDPERYERAIDVTALQHDLDL---LPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVY 762
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488288408 540 ILDEATSSVDTRT-EILIQAAMNRLLENRTSFVVAHRLSTIRDADTIIVMAEGSIVETGTHDELMaKNG 607
Cdd:PLN03130 763 IFDDPLSALDAHVgRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELS-NNG 830
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
398-621 |
2.80e-31 |
|
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: 122.75 E-value: 2.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 398 KDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRA----HFSMVLQDTWLFTG-SIY 472
Cdd:cd03294 41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLPHrTVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 473 DNIHYGNEQASEEEVIRAAKAAHVDDFVRKlpEGYQTILNEEasnISQGQRQLITIARAFLANPDVLILDEATSSVDTrt 552
Cdd:cd03294 121 ENVAFGLEVQGVPRAEREERAAEALELVGL--EGWEHKYPDE---LSGGMQQRVGLARALAVDPDILLMDEAFSALDP-- 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488288408 553 eiLIQAAMNRLL------ENRTSFVVAHRLS-TIRDADTIIVMAEGSIVETGTHDELMAKNgfyADLYNSQFSEEV 621
Cdd:cd03294 194 --LIRREMQDELlrlqaeLQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTNP---ANDYVREFFRGV 264
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
384-597 |
4.05e-31 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 119.46 E-value: 4.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 384 EHVAFGYsPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMVLQd 463
Cdd:cd03214 3 ENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 464 twlftgsiydnihygneqaseeeVIRAAKAAHvddfvrklpegyqtILNEEASNISQGQRQLITIARAFLANPDVLILDE 543
Cdd:cd03214 81 -----------------------ALELLGLAH--------------LADRPFNELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488288408 544 ATSSVDTRTEILIQAAMNRL--LENRTSFVVAHRLS-TIRDADTIIVMAEGSIVETG 597
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLarERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
398-598 |
7.18e-31 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 123.65 E-value: 7.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 398 KDFNLNVKPGEMVAIVGPTGAGKTTL---INLLERFydiSSGSIKYDGVDTRDLSREELRA---HFSMVLQDTWLFTG-S 470
Cdd:COG1135 22 DDVSLTIEKGEIFGIIGYSGAGKSTLircINLLERP---TSGSVLVDGVDLTALSERELRAarrKIGMIFQHFNLLSSrT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 471 IYDNIHYGNEQA--SEEEviRAAKAAHVDDFVrklpeGyqtiLNEEA----SNISQGQRQLITIARAFLANPDVLILDEA 544
Cdd:COG1135 99 VAENVALPLEIAgvPKAE--IRKRVAELLELV-----G----LSDKAdaypSQLSGGQKQRVGIARALANNPKVLLCDEA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488288408 545 TSSVDTRT--EILiqaamnRLLE--NR----TSFVVAHRLSTIRD-ADTIIVMAEGSIVETGT 598
Cdd:COG1135 168 TSALDPETtrSIL------DLLKdiNRelglTIVLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
381-593 |
9.03e-31 |
|
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: 119.90 E-value: 9.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGY---SPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREEL---- 453
Cdd:cd03255 1 IELKNLSKTYgggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 454 RAHFSMVLQDTWLFTG-SIYDNIHYGNEQASEEEVIRAAKAAHVddfVRKLpeGYQTILNEEASNISQGQRQLITIARAF 532
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELPLLLAGVPKKERRERAEEL---LERV--GLGDRLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488288408 533 LANPDVLILDEATSSVDTRTEILIQAAMNRL--LENRTSFVVAHRLSTIRDADTIIVMAEGSI 593
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
398-604 |
1.13e-30 |
|
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: 120.23 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 398 KDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREEL-RAHFSMVLQDTWLFTG-SIYDNI 475
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIaRLGIGRTFQIPRLFPElTVLENV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 476 ----------HYGNEQASEEEVIRAAKAAHVDDFVrklpeGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEAT 545
Cdd:cd03219 97 mvaaqartgsGLLLARARREEREARERAEELLERV-----GLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488288408 546 SSVdTRTEilIQAAMNRLLE----NRTSFVVAHRLSTIRD-ADTIIVMAEGSIVETGTHDELMA 604
Cdd:cd03219 172 AGL-NPEE--TEELAELIRElrerGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
97-355 |
1.23e-30 |
|
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: 121.44 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 97 DFDKIGQILLIVIAMYLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTL 176
Cdd:cd18575 31 NTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 177 QQNLTQLITSIVTFVGVLWMMLTISWQLTLIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKS 256
Cdd:cd18575 111 GSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 257 FNHEESDQEVFEKENEKLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPIT 336
Cdd:cd18575 191 FTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVG 270
|
250
....*....|....*....
gi 488288408 337 QIANLMNTIQATVASAERV 355
Cdd:cd18575 271 ALSEVWGDLQRAAGAAERL 289
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
384-594 |
4.14e-30 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 117.36 E-value: 4.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 384 EHVAFGYSPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGvdtRDLSREELRAHFSMVLQD 463
Cdd:cd03226 3 ENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 464 T--WLFTGSIYDNIHYGNEQASEE-EVIRAA-KAAHVDDFVRKLPEgyqtilneeasNISQGQRQLITIARAFLANPDVL 539
Cdd:cd03226 80 VdyQLFTDSVREELLLGLKELDAGnEQAETVlKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488288408 540 ILDEATSSVDTRTEILIQAAMNRL-LENRTSFVVAHRLSTIRD-ADTIIVMAEGSIV 594
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELaAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
205-607 |
4.35e-30 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 127.01 E-value: 4.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 205 TLIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNnqveETYGGHVVVKSFNHEESDQEVFEK-ENEKLyHAGRKAQF 283
Cdd:PLN03232 447 SLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIIN----EILASMDTVKCYAWEKSFESRIQGiRNEEL-SWFRKAQL 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 284 ISAiimpLMNFIKNLGYVFVAVLG-GVKVANGMmDLGDVQAF--LQYTNQFSQPITQIANLMNTIQATVASAERVFEVLD 360
Cdd:PLN03232 522 LSA----FNSFILNSIPVVVTLVSfGVFVLLGG-DLTPARAFtsLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLL 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 361 EEEMVDEPSGiPVETDSPyRVSFEHVAFGYSP--EKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLIN-LLERFYDISSGS 437
Cdd:PLN03232 597 SEERILAQNP-PLQPGAP-AISIKNGYFSWDSktSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSS 674
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 438 IkydgvdtrdlsreELRAHFSMVLQDTWLFTGSIYDNIHYGNEQASEE--EVIRAAKAAHVDDFvrkLPEGYQTILNEEA 515
Cdd:PLN03232 675 V-------------VIRGSVAYVPQVSWIFNATVRENILFGSDFESERywRAIDVTALQHDLDL---LPGRDLTEIGERG 738
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 516 SNISQGQRQLITIARAFLANPDVLILDEATSSVDTR-TEILIQAAMNRLLENRTSFVVAHRLSTIRDADTIIVMAEGSIV 594
Cdd:PLN03232 739 VNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIK 818
|
410
....*....|...
gi 488288408 595 ETGTHDELmAKNG 607
Cdd:PLN03232 819 EEGTFAEL-SKSG 830
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
97-355 |
6.38e-30 |
|
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: 119.66 E-value: 6.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 97 DFDKIGQILLIVIAMYLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTL 176
Cdd:cd18780 37 ALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 177 QQNLTQLITSIVTFVGVLWMMLTISWQLTLIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKS 256
Cdd:cd18780 117 TVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 257 FNHEESDQEVFEKENEKLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPIT 336
Cdd:cd18780 197 FAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFA 276
|
250
....*....|....*....
gi 488288408 337 QIANLMNTIQATVASAERV 355
Cdd:cd18780 277 FLSSLYGDFMQAVGASVRV 295
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
398-593 |
9.94e-30 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 115.19 E-value: 9.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 398 KDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDlSREELRAHFSMVLQDTWLFTG-SIYDNIH 476
Cdd:cd03230 17 DDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPEEPSLYENlTVRENLK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 477 YgneqaseeeviraakaahvddfvrklpegyqtilneeasniSQGQRQLITIARAFLANPDVLILDEATSSVDTRTEILI 556
Cdd:cd03230 96 L-----------------------------------------SGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREF 134
|
170 180 190
....*....|....*....|....*....|....*....
gi 488288408 557 QAAMNRLL-ENRTSFVVAHRLSTIRD-ADTIIVMAEGSI 593
Cdd:cd03230 135 WELLRELKkEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
375-596 |
9.97e-30 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 118.27 E-value: 9.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 375 TDSPYRVSFEHVAFGYSPEK---LLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSRE 451
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 452 elrahFSMVLQDT----WLftgSIYDNIHYGNEQASEEEVIRAAKAAHV------DDFVRKLPegyqtilneeaSNISQG 521
Cdd:COG1116 82 -----RGVVFQEPallpWL---TVLDNVALGLELRGVPKAERRERARELlelvglAGFEDAYP-----------HQLSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 522 QRQLITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLLE--NRTSFVVAH------RLstirdADTIIVMAE--G 591
Cdd:COG1116 143 MRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTHdvdeavFL-----ADRVVVLSArpG 217
|
....*
gi 488288408 592 SIVET 596
Cdd:COG1116 218 RIVEE 222
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
397-611 |
3.18e-29 |
|
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: 115.90 E-value: 3.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 397 MKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRahFSMVLQDTWLFTG-SIYDNI 475
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRD--ISYVPQNYALFPHmTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 476 HYGNEQASEEeviRAAKAAHVDDFVRKLpeGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEIL 555
Cdd:cd03299 93 AYGLKKRKVD---KKEIERKVLEIAEML--GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488288408 556 IQAAMNRLL-ENRTSFV-VAHRLSTIRD-ADTIIVMAEGSIVETGTHDELM--AKNGFYAD 611
Cdd:cd03299 168 LREELKKIRkEFGVTVLhVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFkkPKNEFVAE 228
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
399-604 |
3.44e-29 |
|
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: 116.29 E-value: 3.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 399 DFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREElRAHFSMV--LQDTWLFTG-SIYDNI 475
Cdd:COG0411 22 DVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHR-IARLGIArtFQNPRLFPElTVLENV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 476 -----------------HYGNEQASEEEVirAAKAAHVDDFVrklpeGYQTILNEEASNISQGQRQLITIARAFLANPDV 538
Cdd:COG0411 101 lvaaharlgrgllaallRLPRARREEREA--RERAEELLERV-----GLADRADEPAGNLSYGQQRRLEIARALATEPKL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488288408 539 LILDEATSSVdTRTEIliqAAMNRLL------ENRTSFVVAHRLSTIRD-ADTIIVMAEGSIVETGTHDELMA 604
Cdd:COG0411 174 LLLDEPAAGL-NPEET---EELAELIrrlrdeRGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAEVRA 242
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
383-602 |
4.56e-29 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 115.74 E-value: 4.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 383 FEHVAFGYSPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREEL---RAHFSM 459
Cdd:cd03256 3 VENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 460 VLQDTWLFTG-SIYDNIHYGN-----------EQASEEEVIRAAKAahVDDFvrklpeGYQTILNEEASNISQGQRQLIT 527
Cdd:cd03256 83 IFQQFNLIERlSVLENVLSGRlgrrstwrslfGLFPKEEKQRALAA--LERV------GLLDKAYQRADQLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 528 IARAFLANPDVLILDEATSSVDTRT-----EILIQAAMNrllENRTSFVVAHRLSTIRD-ADTIIVMAEGSIVETGTHDE 601
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASsrqvmDLLKRINRE---EGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAE 231
|
.
gi 488288408 602 L 602
Cdd:cd03256 232 L 232
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
95-355 |
3.95e-28 |
|
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: 114.53 E-value: 3.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 95 PIDFDKIGQILLIVIAMYLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAiNDMDNIAS 174
Cdd:cd18555 35 PGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFENRSSGDLLFRA-NSNVYIRQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 175 TLQQNLTQLITSIVTFVGVLWMMLTISWQLTLIALATVPLSLIVVMVVAPR----SQKHFAAQQKSLGLLNnqveETYGG 250
Cdd:cd18555 114 ILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKikklNQEEIVAQTKVQSYLT----ETLYG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 251 HVVVKSFNHEEsdqEVFEKENE---KLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQY 327
Cdd:cd18555 190 IETIKSLGSEK---NIYKKWENlfkKQLKAFKKKERLSNILNSISSSIQFIAPLLILWIGAYLVINGELTLGELIAFSSL 266
|
250 260
....*....|....*....|....*...
gi 488288408 328 TNQFSQPITQIANLMNTIQATVASAERV 355
Cdd:cd18555 267 AGSFLTPIVSLINSYNQFILLKSYLERL 294
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
182-620 |
4.30e-28 |
|
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: 120.82 E-value: 4.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 182 QLITSIVTFVGVLW-------MMLTISWQ-LTLIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVE---ETYGG 250
Cdd:TIGR00957 426 QRFMDLATYINMIWsaplqviLALYFLWLnLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKlmnEILNG 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 251 HVVVKSFNHEESDQEVFEKENEKLYHAGRKAQFISA------IIMPLMNFIKNLgYVFVAVlggvkVANGMMDLGDVQAF 324
Cdd:TIGR00957 506 IKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAvgtftwVCTPFLVALITF-AVYVTV-----DENNILDAEKAFVS 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 325 LQYTNQFSQPITQIANLMNTI-QATVaSAERVFEVLDEEEMvdEPSGI---PVETDSPYRVSFEHVAFGYS---PEKLLM 397
Cdd:TIGR00957 580 LALFNILRFPLNILPMVISSIvQASV-SLKRLRIFLSHEEL--EPDSIerrTIKPGEGNSITVHNATFTWArdlPPTLNG 656
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 398 KDFNlnVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIkydgvdtrdlsreELRAHFSMVLQDTWLFTGSIYDNIHY 477
Cdd:TIGR00957 657 ITFS--IPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV-------------HMKGSVAYVPQQAWIQNDSLRENILF 721
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 478 GN--EQASEEEVIRAAkaAHVDDfVRKLPEGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEIL 555
Cdd:TIGR00957 722 GKalNEKYYQQVLEAC--ALLPD-LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKH 798
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488288408 556 IQAAM---NRLLENRTSFVVAHRLSTIRDADTIIVMAEGSIVETGTHDELMAKNGFYADLYNSQFSEE 620
Cdd:TIGR00957 799 IFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAPDE 866
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
381-603 |
6.25e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 113.16 E-value: 6.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYSP-EKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSM 459
Cdd:PRK13632 8 IKVENVSFSYPNsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 460 VLQ--DTWLFTGSIYDNIHYG--NEQASEEEViraakAAHVDDFVRKLpeGYQTILNEEASNISQGQRQLITIARAFLAN 535
Cdd:PRK13632 88 IFQnpDNQFIGATVEDDIAFGleNKKVPPKKM-----KDIIDDLAKKV--GMEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 536 PDVLILDEATSSVDTRTEILIQAAMNRLLENRTSFVVA--HRLSTIRDADTIIVMAEGSIVETGTHDELM 603
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISitHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
399-602 |
7.43e-28 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 114.38 E-value: 7.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 399 DFNLNVKPGEMVAIVGPTGAGKTTL----INLLERFYdISSGSIKYDGVDTRDLSREELRA----HFSMVLQD--TWL-- 466
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTLaraiLGLLPPPG-ITSGEILFDGEDLLKLSEKELRKirgrEIQMIFQDpmTSLnp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 467 -FTgsIYD------NIHYG-NEQASEEEVIRAAKA---AHVDDFVRKLPegYQtilneeasnISQGQRQLITIARAFLAN 535
Cdd:COG0444 102 vMT--VGDqiaeplRIHGGlSKAEARERAIELLERvglPDPERRLDRYP--HE---------LSGGMRQRVMIARALALE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488288408 536 PDVLILDEATSSVDtrteILIQAAMNRLL-----ENRTSFV-VAHRLSTIRD-ADTIIVMAEGSIVETGTHDEL 602
Cdd:COG0444 169 PKLLIADEPTTALD----VTIQAQILNLLkdlqrELGLAILfITHDLGVVAEiADRVAVMYAGRIVEEGPVEEL 238
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
380-602 |
9.37e-28 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 114.79 E-value: 9.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 380 RVSFEHVAFGYSPEKLLmKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREElRaHFSM 459
Cdd:COG3839 3 SLELENVSKSYGGVEAL-KDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-R-NIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 460 VLQDTWLF-TGSIYDNIHYG--NEQASEEE----VIRAAKAAHVDDFVRKLPegyqtilneeaSNISQGQRQLITIARAF 532
Cdd:COG3839 80 VFQSYALYpHMTVYENIAFPlkLRKVPKAEidrrVREAAELLGLEDLLDRKP-----------KQLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 533 LANPDVLILDEATSSVD------TRTEIliqAAMNRllENRTSFV-VAHrlstirD-------ADTIIVMAEGSIVETGT 598
Cdd:COG3839 149 VREPKVFLLDEPLSNLDaklrveMRAEI---KRLHR--RLGTTTIyVTH------DqveamtlADRIAVMNDGRIQQVGT 217
|
....
gi 488288408 599 HDEL 602
Cdd:COG3839 218 PEEL 221
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
104-595 |
1.45e-27 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 117.21 E-value: 1.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 104 ILLIVIAMylisaVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQqNLTQL 183
Cdd:COG4615 55 AGLLVLLL-----LSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFV-RLPEL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 184 ITSIVTFVGVLWMMLTISWQLTLIALATVPLSLIVVMVVAPRSQKHFAaqqkslgllnnQVEETYggHVVVKSFnheesd 263
Cdd:COG4615 129 LQSVALVLGCLAYLAWLSPPLFLLTLVLLGLGVAGYRLLVRRARRHLR-----------RAREAE--DRLFKHF------ 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 264 QEVFEKENE-KLyHAGRKAQFISAIIMP--------------LMNFIKNLG----YVFVAVLGGVKVANGMMDLGDVQA- 323
Cdd:COG4615 190 RALLEGFKElKL-NRRRRRAFFDEDLQPtaeryrdlriradtIFALANNWGnllfFALIGLILFLLPALGWADPAVLSGf 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 324 -----FLqytnqfSQPITQIANLMNTI-QATVASA--ERVFEVLDEEEMVDEPSGIPVETDSPYRVSFEHVAFGYSPEKl 395
Cdd:COG4615 269 vlvllFL------RGPLSQLVGALPTLsRANVALRkiEELELALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGED- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 396 lmkD--------FNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMVLQDTWLF 467
Cdd:COG4615 342 ---GdegftlgpIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 468 tgsiyDNIhYGNEQASEEEVIRA-AKAAHVDDFVRklpegyqtILNEEASNI--SQGQRQ---LITiarAFLANPDVLIL 541
Cdd:COG4615 419 -----DRL-LGLDGEADPARARElLERLELDHKVS--------VEDGRFSTTdlSQGQRKrlaLLV---ALLEDRPILVF 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488288408 542 DEATSSVDTR------TEIL--IQAamnrllENRTSFVVAHrlstirD------ADTIIVMAEGSIVE 595
Cdd:COG4615 482 DEWAADQDPEfrrvfyTELLpeLKA------RGKTVIAISH------DdryfdlADRVLKMDYGKLVE 537
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
402-605 |
2.21e-27 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 113.29 E-value: 2.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 402 LNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRA---HFSMVLQDTWlftGS------IY 472
Cdd:COG4608 39 FDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPlrrRMQMVFQDPY---ASlnprmtVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 473 DNIHYG---NEQASEEEviRAAKAAHVDDFVRklpegyqtiLNEEASN-----ISQGQRQLITIARAFLANPDVLILDEA 544
Cdd:COG4608 116 DIIAEPlriHGLASKAE--RRERVAELLELVG---------LRPEHADrypheFSGGQRQRIGIARALALNPKLIVCDEP 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488288408 545 TSSVDtrteILIQA-AMNrLLE------NRTSFVVAHRLSTIRD-ADTIIVMAEGSIVETGTHDELMAK 605
Cdd:COG4608 185 VSALD----VSIQAqVLN-LLEdlqdelGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
396-606 |
4.40e-27 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 109.84 E-value: 4.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 396 LMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREElRAhFSMVLQDTWLFTG-SIYDN 474
Cdd:COG3840 14 FPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-RP-VSMLFQENNLFPHlTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 475 I--------HYGNEQasEEEVIRAAKAAHVDDFVRKLPEgyqtilneeasNISQGQRQLITIARAFLANPDVLILDEATS 546
Cdd:COG3840 92 IglglrpglKLTAEQ--RAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488288408 547 SVDT--RTEILI---QAAMNRlleNRTSFVVAHRLSTIRD-ADTIIVMAEGSIVETGTHDELMAKN 606
Cdd:COG3840 159 ALDPalRQEMLDlvdELCRER---GLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGE 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
398-602 |
6.08e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 114.73 E-value: 6.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 398 KDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLS-REELRAHFSMVLQDTWLFTG-SIYDNI 475
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIAIIHQELNLVPNlSVAENI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 476 HYGNEQAS-----EEEVIRAAKAA------HVDdfvrklpegyqtiLNEEASNISQGQRQLITIARAFLANPDVLILDEA 544
Cdd:COG1129 101 FLGREPRRgglidWRAMRRRARELlarlglDID-------------PDTPVGDLSVAQQQLVEIARALSRDARVLILDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488288408 545 TSSVDTR-TEILIqAAMNRLLENRTSFV-VAHRLSTIRD-ADTIIVMAEGSIVETG-----THDEL 602
Cdd:COG1129 168 TASLTEReVERLF-RIIRRLKAQGVAIIyISHRLDEVFEiADRVTVLRDGRLVGTGpvaelTEDEL 232
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
314-592 |
8.23e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 114.90 E-value: 8.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 314 GMMDLGDV----QAFLQYTNQFSQPITQIANLmntiqAT-VASAERV---FEVLDE-EEMVDEPSGIPVETDSpyRVSFE 384
Cdd:COG4178 294 GEITLGGLmqaaSAFGQVQGALSWFVDNYQSL-----AEwRATVDRLagfEEALEAaDALPEAASRIETSEDG--ALALE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 385 HVAFgYSPE-KLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKY-DGVDTrdlsreelrahfsMVL- 461
Cdd:COG4178 367 DLTL-RTPDgRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV-------------LFLp 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 462 QDTWLFTGSIYDNIHY--GNEQASEEEVIRAAKAAHVDDFVRKLpegyqtilNEEA--SNI-SQGQRQLITIARAFLANP 536
Cdd:COG4178 433 QRPYLPLGTLREALLYpaTAEAFSDAELREALEAVGLGHLAERL--------DEEAdwDQVlSLGEQQRLAFARLLLHKP 504
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 488288408 537 DVLILDEATSSVDTRTEILIQAAMNRLLENRTSFVVAHRLSTIRDADTIIVMAEGS 592
Cdd:COG4178 505 DWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
372-602 |
9.15e-27 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 109.36 E-value: 9.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 372 PVETDSPYRVSFEHVAFGYSpEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDI-----SSGSIKYDGVD-- 444
Cdd:COG1117 3 APASTLEPKIEVRNLNVYYG-DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLipgarVEGEILLDGEDiy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 445 TRDLSREELRAHFSMVLQDTWLFTGSIYDNIHYG-------NEQASEEEVIRAAKAA----HVDDfvrklpegyqtILNE 513
Cdd:COG1117 82 DPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgikSKSELDEIVEESLRKAalwdEVKD-----------RLKK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 514 EASNISQGQRQLITIARAfLA-NPDVLILDEATSSVDTRTEILIQAAMNRLLENRTSFVVAHRLS-TIRDADTIIVMAEG 591
Cdd:COG1117 151 SALGLSGGQQQRLCIARA-LAvEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQqAARVSDYTAFFYLG 229
|
250
....*....|.
gi 488288408 592 SIVETGTHDEL 602
Cdd:COG1117 230 ELVEFGPTEQI 240
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
385-593 |
9.20e-27 |
|
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: 108.39 E-value: 9.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 385 HVAFGyspEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTL---INLLERfydISSGSIKYDGVDTRDLSRE--ELRAHFSM 459
Cdd:cd03262 7 HKSFG---DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTIIIDGLKLTDDKKNinELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 460 VLQDTWLFTG-SIYDNIHYG-------NEQASEEEVIRAAKAAHVDDFVRKLPegyqtilneeaSNISQGQRQLITIARA 531
Cdd:cd03262 81 VFQQFNLFPHlTVLENITLApikvkgmSKAEAEERALELLEKVGLADKADAYP-----------AQLSGGQQQRVAIARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488288408 532 FLANPDVLILDEATSSVD--TRTEILiqAAMNRLL-ENRTSFVVAHRLSTIRD-ADTIIVMAEGSI 593
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDpeLVGEVL--DVMKDLAeEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
381-606 |
1.06e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 110.10 E-value: 1.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGY-SPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGvdtRDLSRE---ELRAH 456
Cdd:PRK13635 6 IRVEHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG---MVLSEEtvwDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 457 FSMVLQ--DTWLFTGSIYDNIHYG--NEQASEEEVIRaakaaHVDDFVRKLpeGYQTILNEEASNISQGQRQLITIARAF 532
Cdd:PRK13635 83 VGMVFQnpDNQFVGATVQDDVAFGleNIGVPREEMVE-----RVDQALRQV--GMEDFLNREPHRLSGGQKQRVAIAGVL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488288408 533 LANPDVLILDEATSSVDTRTEILIQAAMNRLLENRTSFVVA--HRLSTIRDADTIIVMAEGSIVETGTHDELMAKN 606
Cdd:PRK13635 156 ALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSitHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSG 231
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
381-597 |
1.18e-26 |
|
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: 108.11 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYsPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREElrAHFSMV 460
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 461 LQDTWLFTG-SIYDNIHYG------NEQASEEEVIRAAKAAHVDdfvrklpegyqTILNEEASNISQGQRQLITIARAFL 533
Cdd:cd03301 78 FQNYALYPHmTVYDNIAFGlklrkvPKDEIDERVREVAELLQIE-----------HLLDRKPKQLSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488288408 534 ANPDVLILDEATSSVDTRTEILIQAAMNRLLEN--RTSFVVAH-RLSTIRDADTIIVMAEGSIVETG 597
Cdd:cd03301 147 REPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlgTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
357-602 |
1.28e-26 |
|
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: 109.95 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 357 EVLDEEEMVDEPSGIPVETDSpyrVSFEHVAFGYSPeklLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSG 436
Cdd:cd03291 19 ELLEKAKQENNDRKHSSDDNN---LFFSNLCLVGAP---VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 437 SIKYDGvdtrdlsreelRAHFSMvlQDTWLFTGSIYDNIHYG--NEQASEEEVIraaKAAHVDDFVRKLPEGYQTILNEE 514
Cdd:cd03291 93 KIKHSG-----------RISFSS--QFSWIMPGTIKENIIFGvsYDEYRYKSVV---KACQLEEDITKFPEKDNTVLGEG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 515 ASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEILI-QAAMNRLLENRTSFVVAHRLSTIRDADTIIVMAEGSI 593
Cdd:cd03291 157 GITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSS 236
|
....*....
gi 488288408 594 VETGTHDEL 602
Cdd:cd03291 237 YFYGTFSEL 245
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
381-603 |
1.32e-26 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 108.64 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYSPEKLLmKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLS--------REE 452
Cdd:COG1121 7 IELENLTVSYGGRPVL-EDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARrrigyvpqRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 453 LRAHFSMVLQDT----------WLFTGSiydnihygneQASEEEVIRAAKAAHVDDFVRKLpegyqtIlneeaSNISQGQ 522
Cdd:COG1121 86 VDWDFPITVRDVvlmgrygrrgLFRRPS----------RADREAVDEALERVGLEDLADRP------I-----GELSGGQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 523 RQLITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLL-ENRTSFVVAHRLSTIRD-ADTIIVMAEGSIVEtGTHD 600
Cdd:COG1121 145 QQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRrEGKTILVVTHDLGAVREyFDRVLLLNRGLVAH-GPPE 223
|
...
gi 488288408 601 ELM 603
Cdd:COG1121 224 EVL 226
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
398-604 |
5.24e-26 |
|
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: 106.36 E-value: 5.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 398 KDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREE-LRAHFSMVLQDTWLFTG-SIYDNI 475
Cdd:cd03224 17 FGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVEENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 476 HYGnEQASEEEVIRAAKAAHVDDFVRkLPEgyqtILNEEASNISQGQRQLITIARAFLANPDVLILDEAT-----SSVDT 550
Cdd:cd03224 97 LLG-AYARRRAKRKARLERVYELFPR-LKE----RRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSeglapKIVEE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488288408 551 RTEILIQaaMNRllENRTSFVVAHRLSTIRD-ADTIIVMAEGSIVETGTHDELMA 604
Cdd:cd03224 171 IFEAIRE--LRD--EGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
382-589 |
6.68e-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: 105.69 E-value: 6.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 382 SFEHVAFGYSpEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTrdlsrEELRAHFSMVL 461
Cdd:cd03235 1 EVEDLTVSYG-GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-----EKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 462 QDT---WLFTGSIYD----------NIHYGNEQASEEEVIRAAKAAHVDDFV-RKLpegyqtilneeaSNISQGQRQLIT 527
Cdd:cd03235 75 QRRsidRDFPISVRDvvlmglyghkGLFRRLSKADKAKVDEALERVGLSELAdRQI------------GELSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488288408 528 IARAFLANPDVLILDEATSSVDTRTEILIQAAMNRL-LENRTSFVVAHRLSTIRD-ADTIIVMA 589
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEyFDRVLLLN 206
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
381-611 |
7.65e-26 |
|
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: 106.17 E-value: 7.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYSPEKLLmKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREelRAHFSMV 460
Cdd:cd03300 1 IELENVSKFYGGFVAL-DGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 461 LQDTWLFTG-SIYDNIHYG------NEQASEEEVIRAAKAAHVDDFVRKLPegyqtilneeaSNISQGQRQLITIARAFL 533
Cdd:cd03300 78 FQNYALFPHlTVFENIAFGlrlkklPKAEIKERVAEALDLVQLEGYANRKP-----------SQLSGGQQQRVAIARALV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 534 ANPDVLILDEATSSVDTRTEILIQAAMNRLLEN-RTSFV-VAHRLS-TIRDADTIIVMAEGSIVETGTHDEL--MAKNGF 608
Cdd:cd03300 147 NEPKVLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVfVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEIyeEPANRF 226
|
...
gi 488288408 609 YAD 611
Cdd:cd03300 227 VAD 229
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
381-594 |
3.12e-25 |
|
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: 103.40 E-value: 3.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYSPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLL--ERFYDISSGSIKYDGvdtRDLSREELRAHFS 458
Cdd:cd03213 9 LTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLING---RPLDKRSFRKIIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 459 MVLQDTWLF-TGSIYDNIHYgneqaseeeviraakAAHVddfvrklpegyqtilneeaSNISQGQRQLITIARAFLANPD 537
Cdd:cd03213 86 YVPQDDILHpTLTVRETLMF---------------AAKL-------------------RGLSGGERKRVSIALELVSNPS 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 538 VLILDEATSSVDTRTEILIQAAMNRL-LENRTSFVVAHRLST--IRDADTIIVMAEGSIV 594
Cdd:cd03213 132 LLFLDEPTSGLDSSSALQVMSLLRRLaDTGRTIICSIHQPSSeiFELFDKLLLLSQGRVI 191
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
384-601 |
3.89e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 105.51 E-value: 3.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 384 EHVAFGYSP----EKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRD--LSREELRAHF 457
Cdd:PRK13637 6 ENLTHIYMEgtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIRKKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 458 SMVLQ--DTWLFTGSIYDNIHYG--NEQASEEE----VIRAAKAAHVDdfvrklpegYQTILNEEASNISQGQRQLITIA 529
Cdd:PRK13637 86 GLVFQypEYQLFEETIEKDIAFGpiNLGLSEEEienrVKRAMNIVGLD---------YEDYKDKSPFELSGGQKRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488288408 530 RAFLANPDVLILDEATSSVD--TRTEILIQAAMNRLLENRTSFVVAHRLSTI-RDADTIIVMAEGSIVETGTHDE 601
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDpkGRDEILNKIKELHKEYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE 231
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
381-602 |
4.63e-25 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 106.72 E-value: 4.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYSPEKLLmKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREElRaHFSMV 460
Cdd:COG3842 6 LELENVSKRYGDVTAL-DDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK-R-NVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 461 LQDTWLF---TgsIYDNIHYG--NEQASEEEviRAAKAAHV------DDFVRKLPegyqtilneeaSNISQGQRQLITIA 529
Cdd:COG3842 83 FQDYALFphlT--VAENVAFGlrMRGVPKAE--IRARVAELlelvglEGLADRYP-----------HQLSGGQQQRVALA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 530 RAFLANPDVLILDEATSSVD------TRTEIL-IQAAMNrllenrTSFV-VAHRLS---TIrdADTIIVMAEGSIVETGT 598
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALDaklreeMREELRrLQRELG------ITFIyVTHDQEealAL--ADRIAVMNDGRIEQVGT 219
|
....
gi 488288408 599 HDEL 602
Cdd:COG3842 220 PEEI 223
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
380-585 |
1.42e-24 |
|
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: 101.79 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 380 RVSFEHVAFGYSpEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDlSREELRAHFSM 459
Cdd:COG4133 2 MLEAENLSCRRG-ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 460 VLQDTWLFTG-SIYDNIHY----GNEQASEEEVIRAAKAAHVDDFvrklpegyqtiLNEEASNISQGQRQLITIARAFLA 534
Cdd:COG4133 80 LGHADGLKPElTVRENLRFwaalYGLRADREAIDEALEAVGLAGL-----------ADLPVRQLSAGQKRRVALARLLLS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488288408 535 NPDVLILDEATSSVDTRTEILIQAAMNRLLENRTSFVVA-HRLSTIRDADTI 585
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVL 200
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
381-603 |
1.80e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 102.48 E-value: 1.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVA--FGYSPeklLMKDFNLNVKPGEMVAIVGPTGAGKTTL---INLLErfyDISSGSIKYDGVDTRDLSREE--L 453
Cdd:PRK09493 2 IEFKNVSkhFGPTQ---VLHNIDLNIDQGEVVVIIGPSGSGKSTLlrcINKLE---EITSGDLIVDGLKVNDPKVDErlI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 454 RAHFSMVLQDTWLFTG-SIYDNIHYGNEQaseeevIRAAKAAHVDDFVRKLPE--GYQTILNEEASNISQGQRQLITIAR 530
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHlTALENVMFGPLR------VRGASKEEAEKQARELLAkvGLAERAHHYPSELSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488288408 531 AFLANPDVLILDEATSSVDT--RTEILiqAAMNRLL-ENRTSFVVAHRLSTIRDADT-IIVMAEGSIVETGTHDELM 603
Cdd:PRK09493 150 ALAVKPKLMLFDEPTSALDPelRHEVL--KVMQDLAeEGMTMVIVTHEIGFAEKVASrLIFIDKGRIAEDGDPQVLI 224
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
104-362 |
2.01e-24 |
|
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: 104.07 E-value: 2.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 104 ILLIVIAmyLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYD--THSNGDIMSRAINDMDNIASTLQQNLT 181
Cdd:cd18578 56 LMFLVLA--IVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDdpENSTGALTSRLSTDASDVRGLVGDRLG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 182 QLITSIVTFVGVLWMMLTISWQLTLIALATVPLSLIVVMVVApRSQKHFAAQ-QKSLGLLNNQVEETYGGHVVVKSFNHE 260
Cdd:cd18578 134 LILQAIVTLVAGLIIAFVYGWKLALVGLATVPLLLLAGYLRM-RLLSGFEEKnKKAYEESSKIASEAVSNIRTVASLTLE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 261 ESDQEVFEKENEKLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDV-QAF--LQYTnqfSQPITQ 337
Cdd:cd18578 213 DYFLEKYEEALEEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFfIVFmaLIFG---AQSAGQ 289
|
250 260
....*....|....*....|....*
gi 488288408 338 IANLMNTIQATVASAERVFEVLDEE 362
Cdd:cd18578 290 AFSFAPDIAKAKAAAARIFRLLDRK 314
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
393-597 |
3.37e-24 |
|
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: 101.19 E-value: 3.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 393 EKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLE---RFYDISSGSIKYDGvdtRDLSREELRAHFSMVLQ-DTWLFT 468
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNG---QPRKPDQFQKCVAYVRQdDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 469 GSIYDNIHYGNEQASEEEVIRAAKAAHVDDFVRKLPeGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSV 548
Cdd:cd03234 96 LTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDL-ALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488288408 549 DTRTEILIQAAMNRLL-ENRTSFVVAH--RLSTIRDADTIIVMAEGSIVETG 597
Cdd:cd03234 175 DSFTALNLVSTLSQLArRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
376-603 |
3.41e-24 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 105.12 E-value: 3.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 376 DSPYRvSFEHVAFGYSPEKLL--------MKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRD 447
Cdd:PRK10070 16 EHPQR-AFKYIEQGLSKEQILektglslgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 448 LSREEL----RAHFSMVLQDTWLFTG-SIYDNIHYGNEQASEEEVIRAAKAAhvdDFVRKLpeGYQTILNEEASNISQGQ 522
Cdd:PRK10070 95 ISDAELrevrRKKIAMVFQSFALMPHmTVLDNTAFGMELAGINAEERREKAL---DALRQV--GLENYAHSYPDELSGGM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 523 RQLITIARAFLANPDVLILDEATSSVD--TRTEILIQAAMNRLLENRTSFVVAHRL-STIRDADTIIVMAEGSIVETGTH 599
Cdd:PRK10070 170 RQRVGLARALAINPDILLMDEAFSALDplIRTEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTP 249
|
....
gi 488288408 600 DELM 603
Cdd:PRK10070 250 DEIL 253
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
396-604 |
5.12e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 101.37 E-value: 5.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 396 LMKDFNLNVKPGEMVAIVGPTGAGKTTL---INLLERFYD--ISSGSIKYDGvdTRDLSRE-----ELRAHFSMVLQDTW 465
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLlrcINLLEQPEAgtIRVGDITIDT--ARSLSQQkglirQLRQHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 466 LFTG-SIYDNIHYG----NEQASEEEVIRA----AK---AAHVDDFVRKLpegyqtilneeasniSQGQRQLITIARAFL 533
Cdd:PRK11264 96 LFPHrTVLENIIEGpvivKGEPKEEATARArellAKvglAGKETSYPRRL---------------SGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488288408 534 ANPDVLILDEATSSVDTRteiLIQAAMN--RLL--ENRTSFVVAHRLSTIRD-ADTIIVMAEGSIVETGTHDELMA 604
Cdd:PRK11264 161 MRPEVILFDEPTSALDPE---LVGEVLNtiRQLaqEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
381-607 |
7.92e-24 |
|
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: 99.79 E-value: 7.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYSPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREE---LRAHF 457
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 458 SMVLQDT-WLFTGSIYDNIHYGNE--QASEEEVIRAAKAAHvdDFVrklpeGYQTILNEEASNISQGQRQLITIARAFLA 534
Cdd:cd03292 81 GVVFQDFrLLPDRNVYENVAFALEvtGVPPREIRKRVPAAL--ELV-----GLSHKHRALPAELSGGEQQRVAIARAIVN 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488288408 535 NPDVLILDEATSSVDTrteiliqaamnrllenRTSFVVAHRLSTIRDADTIIVMA--EGSIVETGTHDELMAKNG 607
Cdd:cd03292 154 SPTILIADEPTGNLDP----------------DTTWEIMNLLKKINKAGTTVVVAthAKELVDTTRHRVIALERG 212
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
104-355 |
9.67e-24 |
|
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: 101.90 E-value: 9.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 104 ILLIVIAMYLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRaINDMDNIASTLQQNLTQL 183
Cdd:cd18782 44 IGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTR-ISELDTIRGFLTGTALTT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 184 ITSIVTFVGVLWMMLTISWQLTLIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKSFNHEESD 263
Cdd:cd18782 123 LLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 264 QEVFEKENEKLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPITQIANLMN 343
Cdd:cd18782 203 RWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQ 282
|
250
....*....|..
gi 488288408 344 TIQATVASAERV 355
Cdd:cd18782 283 QFQELRVSLERL 294
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
398-597 |
1.57e-23 |
|
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: 98.91 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 398 KDFNLNVK---PGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGV---DTR---DLSREelRAHFSMVLQDTWLFT 468
Cdd:cd03297 11 PDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRkkiNLPPQ--QRKIGLVFQQYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 469 G-SIYDNIHYGNEQASEEEvIRaakaahvdDFVRKLPE--GYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEAT 545
Cdd:cd03297 89 HlNVRENLAFGLKRKRNRE-DR--------ISVDELLDllGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488288408 546 SSVDTRTEILIQAAMNRLLE--NRTSFVVAHRLSTI-RDADTIIVMAEGSIVETG 597
Cdd:cd03297 160 SALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
398-604 |
2.61e-23 |
|
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: 98.90 E-value: 2.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 398 KDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREEL-RAHFSMVLQDTWLFTG-SIYDNI 475
Cdd:COG0410 20 HGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSlTVEENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 476 HYGNEQASEEEVIRAAKAAHVDDFVRkLPEgyqtILNEEASNISQGQRQLITIARAFLANPDVLILDEAT-----SSVDT 550
Cdd:COG0410 100 LLGAYARRDRAEVRADLERVYELFPR-LKE----RRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSlglapLIVEE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488288408 551 RTEILiqAAMNRllENRTSFVVAHRLSTIRD-ADTIIVMAEGSIVETGTHDELMA 604
Cdd:COG0410 175 IFEII--RRLNR--EGVTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELLA 225
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
390-603 |
3.17e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 99.08 E-value: 3.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 390 YSPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDIS-----SGSIKYDG-------VDTRDLSREelrahF 457
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGhniysprTDTVDLRKE-----I 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 458 SMVLQDTWLFTGSIYDNIHYG-------NEQASEEEVIRAAKAAHVDDFVRKlpegyqtILNEEASNISQGQRQLITIAR 530
Cdd:PRK14239 89 GMVFQQPNPFPMSIYENVVYGlrlkgikDKQVLDEAVEKSLKGASIWDEVKD-------RLHDSALGLSGGQQQRVCIAR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488288408 531 AFLANPDVLILDEATSSVDTRTEILIQAAMNRLLENRTSFVVAHRLSTI-RDADTIIVMAEGSIVETG-THDELM 603
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNdTKQMFM 236
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
147-593 |
3.97e-23 |
|
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: 104.99 E-value: 3.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 147 KVPISYYDTHSNGDIMSRAINDMDNIASTLQQNLTQLITSIVTFVGVLwmmLTISWQLTLIALATVPLSLIVVMVVAprs 226
Cdd:TIGR01271 970 QAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAI---FVVSVLQPYIFIAAIPVAVIFIMLRA--- 1043
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 227 qkHFAAQQKSLGLLNNQVEETYGGHVV--------VKSFNHEESDQEVFEKE------NEKLYHAG-RKAQFISAIIMPL 291
Cdd:TIGR01271 1044 --YFLRTSQQLKQLESEARSPIFSHLItslkglwtIRAFGRQSYFETLFHKAlnlhtaNWFLYLSTlRWFQMRIDIIFVF 1121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 292 MnFIknlGYVFVAVLG--------GVKVANGMMDLGDVQAFLqytnqfsqpITQIanlmnTIQATVASAERVFEVLD--- 360
Cdd:TIGR01271 1122 F-FI---AVTFIAIGTnqdgegevGIILTLAMNILSTLQWAV---------NSSI-----DVDGLMRSVSRVFKFIDlpq 1183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 361 --------------EEEMVDEPSGIPVETDSPYRVSFEHVAFGYSPE-KLLMKDFNLNVKPGEMVAIVGPTGAGKTTLIN 425
Cdd:TIGR01271 1184 eeprpsggggkyqlSTVLVIENPHAQKCWPSGGQMDVQGLTAKYTEAgRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLS 1263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 426 LLERFYDiSSGSIKYDGVDTRDLSREELRAHFSMVLQDTWLFTGSIYDNIHyGNEQASEEEVIRAAKAAHVDDFVRKLPE 505
Cdd:TIGR01271 1264 ALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD-PYEQWSDEEIWKVAEEVGLKSVIEQFPD 1341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 506 GYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLLENRTSFVVAHRLSTIRDADTI 585
Cdd:TIGR01271 1342 KLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQF 1421
|
....*...
gi 488288408 586 IVMAEGSI 593
Cdd:TIGR01271 1422 LVIEGSSV 1429
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
108-355 |
4.71e-23 |
|
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: 99.47 E-value: 4.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 108 VIAMYLI---SAVFNFLQQVI----MTRVS---QRTVYE--LRQELEakmnkvpisYYDTHSNGDIMSRAINDMDNIAST 175
Cdd:cd18589 39 ITVMSLLtiaSAVSEFVCDLIynitMSRIHsrlQGLVFAavLRQEIA---------FFDSNQTGDIVSRVTTDTEDMSES 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 176 LQQNLTQLITSIVTFVGVLWMMLTISWQLTLIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVK 255
Cdd:cd18589 110 LSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 256 SFNHEESDQEVFEKENEKLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPI 335
Cdd:cd18589 190 SFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGGQLVTAGTVSSGDLVTFVLYELQFTSAV 269
|
250 260
....*....|....*....|
gi 488288408 336 TQIANLMNTIQATVASAERV 355
Cdd:cd18589 270 EVLLSYYPSVMKAVGSSEKI 289
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
396-605 |
4.90e-23 |
|
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: 104.61 E-value: 4.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 396 LMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGvdtrdlsreelRAHFSMvlQDTWLFTGSIYDNI 475
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-----------RISFSP--QTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 476 HYGnEQASEEEVIRAAKAAHVDDFVRKLPEGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEIL 555
Cdd:TIGR01271 508 IFG-LSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKE 586
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488288408 556 I-QAAMNRLLENRTSFVVAHRLSTIRDADTIIVMAEGSIVETGTHDELMAK 605
Cdd:TIGR01271 587 IfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAK 637
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
99-355 |
4.99e-23 |
|
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: 99.80 E-value: 4.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 99 DKIGQILLIVIAMYLISAVF----NFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIAS 174
Cdd:cd18554 39 EKVYKLFTIIGIMFFIFLILrppvEYYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 175 TLQQNLTQLITSIVTFVGVLWMMLTISWQLTLIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVV 254
Cdd:cd18554 119 FITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 255 KSFNHEESDQEVFEKENEKLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQP 334
Cdd:cd18554 199 KSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSP 278
|
250 260
....*....|....*....|.
gi 488288408 335 ITQIANLMNTIQATVASAERV 355
Cdd:cd18554 279 LRRLVNSFTTLTQSFASMDRV 299
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
384-606 |
6.48e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 97.73 E-value: 6.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 384 EHVAFGYspEKLLMKdFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREelRAHFSMVLQD 463
Cdd:PRK10771 5 TDITWLY--HHLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 464 TWLFTG-SIYDNIHYG-------NEQaSEEEVIRAAKAAHVDDFVRKLPegyqtilneeaSNISQGQRQLITIARAFLAN 535
Cdd:PRK10771 80 NNLFSHlTVAQNIGLGlnpglklNAA-QREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVRE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 536 PDVLILDEATSSVDT--RTEILiqaamnRLLE------NRTSFVVAHRLS-TIRDADTIIVMAEGSIVETGTHDELMAKN 606
Cdd:PRK10771 148 QPILLLDEPFSALDPalRQEML------TLVSqvcqerQLTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
381-603 |
6.61e-23 |
|
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: 98.23 E-value: 6.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYSpEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGS------IKYDGVDTRdlsreELR 454
Cdd:COG1119 4 LELRNVTVRRG-GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrlfgERRGGEDVW-----ELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 455 AH---FSMVLQDTWL------------FTGSIYDNIHYGNEQASE-EEVIRAAKAAHVDDfvRKLPEgyqtilneeasnI 518
Cdd:COG1119 78 KRiglVSPALQLRFPrdetvldvvlsgFFDSIGLYREPTDEQRERaRELLELLGLAHLAD--RPFGT------------L 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 519 SQGQRQLITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLLENR-TSFV-VAHRLSTIRDADT-IIVMAEGSIVE 595
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVlVTHHVEEIPPGIThVLLLKDGRVVA 223
|
....*...
gi 488288408 596 TGTHDELM 603
Cdd:COG1119 224 AGPKEEVL 231
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
379-605 |
2.41e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 97.61 E-value: 2.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 379 YRVSFEHVAFGYSPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGvDTRDLSRE---ELRA 455
Cdd:PRK13636 4 YILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDG-KPIDYSRKglmKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 456 HFSMVLQ--DTWLFTGSIYDNIHYG--NEQASEEEVIRaakaaHVDDFVRKlpEGYQTILNEEASNISQGQRQLITIARA 531
Cdd:PRK13636 83 SVGMVFQdpDNQLFSASVYQDVSFGavNLKLPEDEVRK-----RVDNALKR--TGIEHLKDKPTHCLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488288408 532 FLANPDVLILDEATSSVDTRTEILIQAAMNRLLE--NRTSFVVAHRLSTIR-DADTIIVMAEGSIVETGTHDELMAK 605
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
107-355 |
4.38e-22 |
|
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: 96.80 E-value: 4.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 107 IVIAMYLIS---AVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRaINDMDNIASTLQQN-LTQ 182
Cdd:cd18588 44 LAIGLLVVAlfeAVLSGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFESRQVGDTVAR-VRELESIRQFLTGSaLTL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 183 LITSIVTFVgVLWMMLTISWQLTLIALATVPLSLIVVMVVAPRSQKhFAAQQKSLGLLNNQ-VEETYGGHVVVKSFNHEE 261
Cdd:cd18588 123 VLDLVFSVV-FLAVMFYYSPTLTLIVLASLPLYALLSLLVTPILRR-RLEEKFQRGAENQSfLVETVTGIETVKSLAVEP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 262 SDQEVFEKENEKLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPITQIANL 341
Cdd:cd18588 201 QFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQL 280
|
250
....*....|....
gi 488288408 342 MNTIQATVASAERV 355
Cdd:cd18588 281 WQDFQQAKVSVERL 294
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
398-596 |
4.83e-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: 93.26 E-value: 4.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 398 KDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLS-REELRAHFSMVLQdtwlftgsiydnih 476
Cdd:cd03216 17 DGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGIAMVYQ-------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 477 ygneqaseeeviraakaahvddfvrklpegyqtilneeasnISQGQRQLITIARAFLANPDVLILDEATSSVDTR-TEIL 555
Cdd:cd03216 83 -----------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAeVERL 121
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488288408 556 IqAAMNRLLENRTSFV-VAHRLSTIRD-ADTIIVMAEGSIVET 596
Cdd:cd03216 122 F-KVIRRLRAQGVAVIfISHRLDEVFEiADRVTVLRDGRVVGT 163
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
394-598 |
1.29e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 94.45 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 394 KLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMVLQDTWL---FT-- 468
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsfpFTve 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 469 -----GSIydnIHYGNEQASEEEVIRAAKAAHVDDFVRKLpegYQTilneeasnISQGQRQLITIARAF--LANPD---- 537
Cdd:PRK13548 95 evvamGRA---PHGLSRAEDDALVAAALAQVDLAHLAGRD---YPQ--------LSGGEQQRVQLARVLaqLWEPDgppr 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488288408 538 VLILDEATSSVDTR-TEILIQAAMNRLLENRTS-FVVAHRLS-TIRDADTIIVMAEGSIVETGT 598
Cdd:PRK13548 161 WLLLDEPTSALDLAhQHHVLRLARQLAHERGLAvIVVLHDLNlAARYADRIVLLHQGRLVADGT 224
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
393-597 |
1.58e-21 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 93.05 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 393 EKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLsrEELRAHFSMVLQDTWLF---TG 469
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKN--IEALRRIGALIEAPGFYpnlTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 470 ----SIYDNIhYGNEQASEEEVIRAAKAAHVDDfvrklpegyqtilnEEASNISQGQRQLITIARAFLANPDVLILDEAT 545
Cdd:cd03268 90 renlRLLARL-LGIRKKRIDEVLDVVGLKDSAK--------------KKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488288408 546 SSVDTrteILIqAAMNRLL-----ENRTSFVVAHRLSTIRD-ADTIIVMAEGSIVETG 597
Cdd:cd03268 155 NGLDP---DGI-KELRELIlslrdQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
390-602 |
1.80e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 94.34 E-value: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 390 YSPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGV------DTRDLSREELRAHFSMVLQD 463
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 464 TWLFTG-SIYDNIHYGNEQASEEEVIRAAKAahVDDFVRK--LPEGYQTILNEEASNISQGQRQLITIARAFLANPDVLI 540
Cdd:PRK14246 99 PNPFPHlSIYDNIAYPLKSHGIKEKREIKKI--VEECLRKvgLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488288408 541 LDEATSSVDTRTEILIQAAMNRLLENRTSFVVAHRLSTI-RDADTIIVMAEGSIVETGTHDEL 602
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
398-604 |
1.82e-21 |
|
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: 98.22 E-value: 1.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 398 KDFNLNVKPGEMVAIVGPTGAGKTTL----INLLErfydiSSGSIKYDGVDTRDLSREE---LRAHFSMVLQDTWlftGS 470
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLglalLRLIP-----SEGEIRFDGQDLDGLSRRAlrpLRRRMQVVFQDPF---GS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 471 IydN--------------IHY--GNEQASEEEVIRAAKAAHVD-DFVRKLPegyqtilNEeasnISQGQRQLITIARAFL 533
Cdd:COG4172 375 L--SprmtvgqiiaeglrVHGpgLSAAERRARVAEALEEVGLDpAARHRYP-------HE----FSGGQRQRIAIARALI 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488288408 534 ANPDVLILDEATSSVDtRTeilIQAAMNRLL-----ENRTSFV-VAHRLSTIRD-ADTIIVMAEGSIVETGTHDELMA 604
Cdd:COG4172 442 LEPKLLVLDEPTSALD-VS---VQAQILDLLrdlqrEHGLAYLfISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
381-597 |
2.05e-21 |
|
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: 92.64 E-value: 2.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYsPEKLLMKDFNLNVKPGeMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDlSREELRAHFSMV 460
Cdd:cd03264 1 LQLENLTKRY-GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 461 LQDtwlFTgsIYDNIH-----------YGNEQA-SEEEVIRAAKAAHVDDFVRKLPEGYqtilneeasniSQGQRQLITI 528
Cdd:cd03264 78 PQE---FG--VYPNFTvrefldyiawlKGIPSKeVKARVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVGI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 529 ARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLLENRTSFVVAHRLSTIRD-ADTIIVMAEGSIVETG 597
Cdd:cd03264 142 AQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
381-605 |
2.12e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 94.70 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYSP----EKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKY------DGVDTRDLSR 450
Cdd:PRK13634 3 ITFQKVEHRYQYktpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 451 eeLRAHFSMVLQ--DTWLFTGSIYDNIHYG--NEQASEEEVIRaaKAAHVDDFVrKLPEgyqTILNEEASNISQGQRQLI 526
Cdd:PRK13634 83 --LRKKVGIVFQfpEHQLFEETVEKDICFGpmNFGVSEEDAKQ--KAREMIELV-GLPE---ELLARSPFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 527 TIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLLE--NRTSFVVAHRLSTI-RDADTIIVMAEGSIVETGTHDELM 603
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKekGLTTVLVTHSMEDAaRYADQIVVMHKGTVFLQGTPREIF 234
|
..
gi 488288408 604 AK 605
Cdd:PRK13634 235 AD 236
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
398-602 |
2.14e-21 |
|
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: 92.95 E-value: 2.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 398 KDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDlSREELRAHFSMVLQDTWLFTG-SIYDNIH 476
Cdd:cd03263 19 DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALFDElTVREHLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 477 Y-------GNEQASEEeviraakaahVDDFVRKLpeGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVD 549
Cdd:cd03263 98 FyarlkglPKSEIKEE----------VELLLRVL--GLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488288408 550 TRTEILIQAAMNRLLENRTSFVVAHRLSTI-RDADTIIVMAEGSIVETGTHDEL 602
Cdd:cd03263 166 PASRRAIWDLILEVRKGRSIILTTHSMDEAeALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
399-602 |
3.46e-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: 92.79 E-value: 3.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 399 DFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFsmVLQDTWLFTG-SIYDNIHY 477
Cdd:cd03296 20 DVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGF--VFQHYALFRHmTVFDNVAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 478 G----------NEQASEEEVIRAAKAAHVDDFVRKLPegyqtilneeaSNISQGQRQLITIARAFLANPDVLILDEATSS 547
Cdd:cd03296 98 GlrvkprserpPEAEIRAKVHELLKLVQLDWLADRYP-----------AQLSGGQRQRVALARALAVEPKVLLLDEPFGA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488288408 548 VDTRTEILIQAAMNRLLE--NRTSFVVAHRLSTIRD-ADTIIVMAEGSIVETGTHDEL 602
Cdd:cd03296 167 LDAKVRKELRRWLRRLHDelHVTTVFVTHDQEEALEvADRVVVMNKGRIEQVGTPDEV 224
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
394-598 |
3.71e-21 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 95.78 E-value: 3.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 394 KLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREelRAHFSMVLQDTWLFTG-SIY 472
Cdd:PRK09452 27 KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVFQSYALFPHmTVF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 473 DNIHYG------NEQASEEEVIRAAKAAHVDDFVRKLPegyqtilneeaSNISQGQRQLITIARAFLANPDVLILDEATS 546
Cdd:PRK09452 105 ENVAFGlrmqktPAAEITPRVMEALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPKVLLLDESLS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 547 SVDTRTEILIQAAMNRLleNRT---SFV-VAH----RLSTirdADTIIVMAEGSIVETGT 598
Cdd:PRK09452 174 ALDYKLRKQMQNELKAL--QRKlgiTFVfVTHdqeeALTM---SDRIVVMRDGRIEQDGT 228
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
388-592 |
4.04e-21 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 92.39 E-value: 4.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 388 FGYSPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAH----FSMVLQD 463
Cdd:cd03290 8 FSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 464 TWLFTGSIYDNIHYG---NEQaSEEEVIRAAKAAHVDDFvrkLPEGYQTILNEEASNISQGQRQLITIARAFLANPDVLI 540
Cdd:cd03290 88 PWLLNATVEENITFGspfNKQ-RYKAVTDACSLQPDIDL---LPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488288408 541 LDEATSSVDTR-TEILIQAAMNRLLEN--RTSFVVAHRLSTIRDADTIIVMAEGS 592
Cdd:cd03290 164 LDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
388-598 |
4.73e-21 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 93.21 E-value: 4.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 388 FGYSPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRA---HFSMVLQDT 464
Cdd:PRK10419 19 SGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAfrrDIQMVFQDS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 465 wlfTGSIydnihygNEQASEEEVIR-----------AAKAAHVDDFVR--KLPEgyqTILNEEASNISQGQRQLITIARA 531
Cdd:PRK10419 99 ---ISAV-------NPRKTVREIIReplrhllsldkAERLARASEMLRavDLDD---SVLDKRPPQLSGGQLQRVCLARA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488288408 532 FLANPDVLILDEATSSVDtrteILIQAAMNRLLENR-----TSFV-VAHRLSTI-RDADTIIVMAEGSIVETGT 598
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLD----LVLQAGVIRLLKKLqqqfgTACLfITHDLRLVeRFCQRVMVMDNGQIVETQP 235
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
381-602 |
5.26e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 93.28 E-value: 5.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGY-SPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSM 459
Cdd:PRK13648 8 IVFKNVSFQYqSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 460 VLQDTW-LFTGSI--YDnIHYGNEQaseeeviraaKAAHVDDFVRKLPEGYQTI-----LNEEASNISQGQRQLITIARA 531
Cdd:PRK13648 88 VFQNPDnQFVGSIvkYD-VAFGLEN----------HAVPYDEMHRRVSEALKQVdmlerADYEPNALSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488288408 532 FLANPDVLILDEATSSVDTRTEILIQAAMNRLLENR--TSFVVAHRLSTIRDADTIIVMAEGSIVETGTHDEL 602
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
397-597 |
6.23e-21 |
|
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: 91.66 E-value: 6.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 397 MKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTrdlSRE--ELRAHFSMVLQDTWLFTG-SIYD 473
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV---VKEpaEARRRLGFVSDSTGLYDRlTARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 474 NIHYgneQASEEEVIRAAKAAHVDDFVRKLpeGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVD-TRT 552
Cdd:cd03266 98 NLEY---FAGLYGLKGDELTARLEELADRL--GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDvMAT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488288408 553 EILIQAAMNRLLENRTSFVVAHRLSTI-RDADTIIVMAEGSIVETG 597
Cdd:cd03266 173 RALREFIRQLRALGKCILFSTHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
396-602 |
7.78e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 94.38 E-value: 7.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 396 LMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFsmVLQDTWLFTG-SIYDN 474
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGF--VFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 475 IHYGNEQASEEEviRAAKAAhVDDFVRKLPEGYQT--ILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRT 552
Cdd:PRK10851 95 IAFGLTVLPRRE--RPNAAA-IKAKVTQLLEMVQLahLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488288408 553 EILIQAAMNRLLENR--TSFVVAH-RLSTIRDADTIIVMAEGSIVETGTHDEL 602
Cdd:PRK10851 172 RKELRRWLRQLHEELkfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
399-597 |
9.01e-21 |
|
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: 91.02 E-value: 9.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 399 DFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVD--TRDLSREELrahfSMVLQDTWLFTG-SIYDNI 475
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDvtAAPPADRPV----SMLFQENNLFAHlTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 476 HYG-------NEQaSEEEVIRAAKAAHVDDFVRKLPEgyqtilneeasNISQGQRQLITIARAFLANPDVLILDEATSSV 548
Cdd:cd03298 92 GLGlspglklTAE-DRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488288408 549 DT--RTEILIQAAMNRLLENRTSFVVAHRLSTIRD-ADTIIVMAEGSIVETG 597
Cdd:cd03298 160 DPalRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
399-602 |
1.11e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 94.02 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 399 DFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREElrAHFSMVLQDTWLFTG-SIYDNIHY 477
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--RDICMVFQSYALFPHmSLGENVGY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 478 G---NEQASEEEVIRAAKAAHVDDFvrklpEGYQtilNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDT---- 550
Cdd:PRK11432 102 GlkmLGVPKEERKQRVKEALELVDL-----AGFE---DRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDAnlrr 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488288408 551 --RTEIliqaamnRLLENR---TSFVVAHRLS-TIRDADTIIVMAEGSIVETGTHDEL 602
Cdd:PRK11432 174 smREKI-------RELQQQfniTSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
104-355 |
1.15e-20 |
|
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: 92.62 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 104 ILLIVIAMYLIS---AVFNFLQQVIMTRVSQRtvyelrqeLEAKMN--------KVPISYYDTHSNGDIMSRaINDMDNI 172
Cdd:cd18568 41 LNLILIGLLIVGifqILLSAVRQYLLDYFANR--------IDLSLLsdfykhllSLPLSFFASRKVGDIITR-FQENQKI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 173 ASTLQQNLTQLITSIVTFVGVLWMMLTISWQLTLIALATVPLSLIVVMVVAPR----SQKHFAAQQKSlgllNNQVEETY 248
Cdd:cd18568 112 RRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKlkrnSREIFQANAEQ----QSFLVEAL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 249 GGHVVVKSFNHEESDQEVFEKENEKLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYT 328
Cdd:cd18568 188 TGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLGTIAVLWYGAYLVISGQLTIGQLVAFNMLF 267
|
250 260
....*....|....*....|....*..
gi 488288408 329 NQFSQPITQIANLMNTIQATVASAERV 355
Cdd:cd18568 268 GSVINPLLALVGLWDELQETRISVERL 294
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
385-602 |
1.23e-20 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 91.05 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 385 HVAFGYSPeklLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREElRAHFSM--VLQ 462
Cdd:TIGR03410 7 NVYYGQSH---ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE-RARAGIayVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 463 DTWLFTG-SIYDNIHYGNEqaseeevIRAAKAAHVDDFVRKLPEGYQTILNEEASNISQGQRQLITIARAFLANPDVLIL 541
Cdd:TIGR03410 83 GREIFPRlTVEENLLTGLA-------ALPRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488288408 542 DEATSSVDTRTEILIQAAMNRLLENR--TSFVVAHRLSTIRD-ADTIIVMAEGSIVETGTHDEL 602
Cdd:TIGR03410 156 DEPTEGIQPSIIKDIGRVIRRLRAEGgmAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
393-597 |
1.24e-20 |
|
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: 90.28 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 393 EKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERF--YDISSGSIKYDGVDTRDLSREElRAHFSMVLqdTWlftgs 470
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEE-RARLGIFL--AF----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 471 iydnihygneQASEEevIRAAKaahVDDFVRKLPEGYqtilneeasniSQGQRQLITIARAFLANPDVLILDEATSSVDT 550
Cdd:cd03217 84 ----------QYPPE--IPGVK---NADFLRYVNEGF-----------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488288408 551 RTEILIQAAMNRLLENRTSF-VVAH--RLSTIRDADTIIVMAEGSIVETG 597
Cdd:cd03217 138 DALRLVAEVINKLREEGKSVlIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
404-605 |
1.40e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 93.11 E-value: 1.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 404 VKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREE---LRAHFSMVLQDTWlftGSIydNIHYGNE 480
Cdd:PRK11308 38 LERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqklLRQKIQIVFQNPY---GSL--NPRKKVG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 481 QASEEEVI------RAAKAAHVDDFVRKL---PEGYQtilnEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDtr 551
Cdd:PRK11308 113 QILEEPLLintslsAAERREKALAMMAKVglrPEHYD----RYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD-- 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488288408 552 teILIQAAMNRLL-----ENRTSFV-VAHRLSTIRD-ADTIIVMAEGSIVETGTHDELMAK 605
Cdd:PRK11308 187 --VSVQAQVLNLMmdlqqELGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
396-593 |
1.87e-20 |
|
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: 91.84 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 396 LMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISsGSIKYDGVDTRDLSREELRAHFSMVLQDTWLFTGSIYDNI 475
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 476 HyGNEQASEEEVIRAAKAAHVDDFVRKLPEGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEIL 555
Cdd:cd03289 98 D-PYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQV 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 488288408 556 IQAAMNRLLENRTSFVVAHRLSTIRDADTIIVMAEGSI 593
Cdd:cd03289 177 IRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
393-594 |
3.06e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 90.92 E-value: 3.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 393 EKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSrEELRAHF-SMVLQDTWLFTG-- 469
Cdd:COG1101 18 EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP-EYKRAKYiGRVFQDPMMGTAps 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 470 -SIYDN------------IHYGneqaseeevIRAAKAAHVDDFVRKLPEGYQTILNEEASNISQGQRQLITIARAFLANP 536
Cdd:COG1101 97 mTIEENlalayrrgkrrgLRRG---------LTKKRRELFRELLATLGLGLENRLDTKVGLLSGGQRQALSLLMATLTKP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488288408 537 DVLILDEATSSVDTRTEILIQAAMNRLLE--NRTSFVVAHRLstiRDA----DTIIVMAEGSIV 594
Cdd:COG1101 168 KLLLLDEHTAALDPKTAALVLELTEKIVEenNLTTLMVTHNM---EQAldygNRLIMMHEGRII 228
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
105-345 |
3.50e-20 |
|
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: 91.37 E-value: 3.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 105 LLIVIA-----MYLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRaINDMDNIASTLQQN 179
Cdd:cd18567 40 LLTVLAigfglLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFEKRHLGDIVSR-FGSLDEIQQTLTTG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 180 LTQLITSIVTFVGVLWMMLTISWQLTLIALATVPLSLIVVMVVAPRSQK------HFAAQQKSLgLLnnqveETYGGHVV 253
Cdd:cd18567 119 FVEALLDGLMAILTLVMMFLYSPKLALIVLAAVALYALLRLALYPPLRRateeqiVASAKEQSH-FL-----ETIRGIQT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 254 VKSFNHEESDQEVFEKENEKLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQ 333
Cdd:cd18567 193 IKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLFGLENILVIYLGALLVLDGEFTVGMLFAFLAYKDQFSS 272
|
250
....*....|..
gi 488288408 334 pitQIANLMNTI 345
Cdd:cd18567 273 ---RASSLIDKL 281
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
384-602 |
3.63e-20 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 92.13 E-value: 3.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 384 EHVAFGYSPEKLLmKDFNLNVKPGEMVAIVGPTGAGKTTLINL---LERfydISSGSIKYDGVD-TRDLSREELRAHFsm 459
Cdd:COG1118 6 RNISKRFGSFTLL-DDVSLEIASGELVALLGPSGSGKTTLLRIiagLET---PDSGRIVLNGRDlFTNLPPRERRVGF-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 460 VLQDTWLF---TgsIYDNIHYG--NEQASEEEviRAAKAA------HVDDFVRKLPegyqtilneeaSNISQGQRQLITI 528
Cdd:COG1118 80 VFQHYALFphmT--VAENIAFGlrVRPPSKAE--IRARVEellelvQLEGLADRYP-----------SQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 529 ARAFLANPDVLILDEATSSVDT--RTEI---LIqaamnRLLE--NRTSFVVAH------RLstirdADTIIVMAEGSIVE 595
Cdd:COG1118 145 ARALAVEPEVLLLDEPFGALDAkvRKELrrwLR-----RLHDelGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQ 214
|
....*..
gi 488288408 596 TGTHDEL 602
Cdd:COG1118 215 VGTPDEV 221
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
381-605 |
3.77e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 91.01 E-value: 3.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGY-SPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTT---LINLLERFYDISSGSIKYDGVDTRDLSREELRAH 456
Cdd:PRK13640 6 VEFKHVSFTYpDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 457 FSMVLQ--DTWLFTGSIYDNIHYG--NEQASEEEVIRAakaahVDDFVRKLpeGYQTILNEEASNISQGQRQLITIARAF 532
Cdd:PRK13640 86 VGIVFQnpDNQFVGATVGDDVAFGleNRAVPRPEMIKI-----VRDVLADV--GMLDYIDSEPANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488288408 533 LANPDVLILDEATSSVDT--RTEIL--IQAAMNRllENRTSFVVAHRLSTIRDADTIIVMAEGSIVETGTHDELMAK 605
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPagKEQILklIRKLKKK--NNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
389-598 |
5.56e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 91.79 E-value: 5.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 389 GYSPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLI---NLLERfydISSGSIKYDGVDTRDLSREELRA---------- 455
Cdd:PRK11153 13 QGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIrciNLLER---PTSGRVLVDGQDLTALSEKELRKarrqigmifq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 456 HFSMVLQDTwlftgsIYDNIHYGNEQASEEeviRAAKAAHVD---------DFVRKLPegyqtilneeaSNISQGQRQLI 526
Cdd:PRK11153 90 HFNLLSSRT------VFDNVALPLELAGTP---KAEIKARVTellelvglsDKADRYP-----------AQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488288408 527 TIARAFLANPDVLILDEATSSVDTRT--EIL-IQAAMNRLLeNRTSFVVAHRLSTIRD-ADTIIVMAEGSIVETGT 598
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATtrSILeLLKDINREL-GLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
390-576 |
8.27e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 89.46 E-value: 8.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 390 YSPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDI-----SSGSIKYDGVD--TRDLSREELRAHFSMVLQ 462
Cdd:PRK14243 19 YYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNlyAPDVDPVEVRRRIGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 463 DTWLFTGSIYDNIHYGNE----QASEEEVI-RAAKAAHVDDFVRKLpegyqtiLNEEASNISQGQRQLITIARAFLANPD 537
Cdd:PRK14243 99 KPNPFPKSIYDNIAYGARingyKGDMDELVeRSLRQAALWDEVKDK-------LKQSGLSLSGGQQQRLCIARAIAVQPE 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 488288408 538 VLILDEATSSVDTRTEILIQAAMNRLLENRTSFVVAHRL 576
Cdd:PRK14243 172 VILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
125-355 |
1.73e-19 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 89.32 E-value: 1.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 125 IMTRVSQRTvyelRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQQNLTQLITSIVTFVGVLWMMLTISWQL 204
Cdd:cd18590 63 TLSRLNLRL----RHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 205 TLIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKSFNHEESDQEVFEKENEKLYHAGRKAQFI 284
Cdd:cd18590 139 TLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTV 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488288408 285 SAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPITQIANLMNTIQATVASAERV 355
Cdd:cd18590 219 RAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
384-603 |
2.49e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 87.76 E-value: 2.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 384 EHVAFGYSpEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMVLQD 463
Cdd:PRK11231 6 ENLTVGYG-TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 464 TWLFTG-SIYDNIHYGNE----------QASEEEVIRAAKAAHVDDFVRKLpegyqtilneeASNISQGQRQlitiaRAF 532
Cdd:PRK11231 85 HLTPEGiTVRELVAYGRSpwlslwgrlsAEDNARVNQAMEQTRINHLADRR-----------LTDLSGGQRQ-----RAF 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488288408 533 LA-----NPDVLILDEATSSVDTRTEILIQAAMNRL-LENRTSFVVAHRLS-TIRDADTIIVMAEGSIVETGTHDELM 603
Cdd:PRK11231 149 LAmvlaqDTPVVLLDEPTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
384-588 |
2.57e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 87.08 E-value: 2.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 384 EHVAFGYSPEKLLmKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMVLQD 463
Cdd:PRK10247 11 QNVGYLAGDAKIL-NNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 464 TWLFTGSIYDNIHYGNE---QASEEEVIRaakaahvDDFVR-KLPEgyqTILNEEASNISQGQRQLITIARAFLANPDVL 539
Cdd:PRK10247 90 PTLFGDTVYDNLIFPWQirnQQPDPAIFL-------DDLERfALPD---TILTKNIAELSGGEKQRISLIRNLQFMPKVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488288408 540 ILDEATSSVDTRTEILIQAAMNRLLENRTSFV--VAHRLSTIRDADTIIVM 588
Cdd:PRK10247 160 LLDEITSALDESNKHNVNEIIHRYVREQNIAVlwVTHDKDEINHADKVITL 210
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
386-602 |
3.48e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 87.28 E-value: 3.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 386 VAFGYSPeklLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDIS-----SGSIKYDGVDTRDLSREELRAHFSMV 460
Cdd:PRK14247 11 VSFGQVE---VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRRVQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 461 LQ-DTWLFTGSIYDNIHYG--------NEQASEEEVIRAAKAAHVDDFVRKLpegyqtiLNEEASNISQGQRQLITIARA 531
Cdd:PRK14247 88 FQiPNPIPNLSIFENVALGlklnrlvkSKKELQERVRWALEKAQLWDEVKDR-------LDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488288408 532 FLANPDVLILDEATSSVDTRTEILIQAAMNRLLENRTSFVVAH-RLSTIRDADTIIVMAEGSIVETGTHDEL 602
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
372-612 |
3.63e-19 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 92.53 E-value: 3.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 372 PVETDSPYRVSFEHVAFGYSPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSG------SIKYdgvdt 445
Cdd:PTZ00243 651 PTSERSAKTPKMKTDDFFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGrvwaerSIAY----- 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 446 rdlsreelrahfsmVLQDTWLFTGSIYDNIHYGNEqaseEEVIRAAKAAHVDDF---VRKLPEGYQTILNEEASNISQGQ 522
Cdd:PTZ00243 726 --------------VPQQAWIMNATVRGNILFFDE----EDAARLADAVRVSQLeadLAQLGGGLETEIGEKGVNLSGGQ 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 523 RQLITIARAFLANPDVLILDEATSSVDTRT-EILIQAAMNRLLENRTSFVVAHRLSTIRDADTIIVMAEGSIVETGTHDE 601
Cdd:PTZ00243 788 KARVSLARAVYANRDVYLLDDPLSALDAHVgERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSAD 867
|
250
....*....|.
gi 488288408 602 LMAKNgFYADL 612
Cdd:PTZ00243 868 FMRTS-LYATL 877
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
381-604 |
6.34e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 87.35 E-value: 6.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYSPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSR-EELRAHFSM 459
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 460 VLQ--DTWLFTGSIYDNIHYGNEQASEEEV-IRaakaAHVDdfvRKLPE-GYQTILNEEASNISQGQRQLITIARAFLAN 535
Cdd:PRK13644 82 VFQnpETQFVGRTVEEDLAFGPENLCLPPIeIR----KRVD---RALAEiGLEKYRHRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 536 PDVLILDEATSSVDTRTEILIQAAMNRLLEN-RTSFVVAHRLSTIRDADTIIVMAEGSIVETGTHDELMA 604
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
385-605 |
9.13e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 86.71 E-value: 9.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 385 HVAFGYSP--EKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMVLQ 462
Cdd:PRK13650 9 NLTFKYKEdqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 463 --DTWLFTGSIYDNIHYGNEQ---ASEEEVIRAAKAAhvdDFVrklpeGYQTILNEEASNISQGQRQLITIARAFLANPD 537
Cdd:PRK13650 89 npDNQFVGATVEDDVAFGLENkgiPHEEMKERVNEAL---ELV-----GMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488288408 538 VLILDEATSSVDT--RTEiLIQAAMN-RLLENRTSFVVAHRLSTIRDADTIIVMAEGSIVETGTHDELMAK 605
Cdd:PRK13650 161 IIILDEATSMLDPegRLE-LIKTIKGiRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
381-579 |
1.20e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 86.24 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYSPEKLLmKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISS-----GSIKYDG--VDTRDLSREEL 453
Cdd:PRK14258 8 IKVNNLSFYYDTQKIL-EGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNqnIYERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 454 RAHFSMVLQDTWLFTGSIYDNIHYG------NEQASEEEVIRAA-KAAHVDDFVRKLpegyqtiLNEEASNISQGQRQLI 526
Cdd:PRK14258 87 RRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIVESAlKDADLWDEIKHK-------IHKSALDLSGGQQQRL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488288408 527 TIARAFLANPDVLILDEATSSVD----TRTEILIQAAmnRLLENRTSFVVAHRLSTI 579
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSL--RLRSELTMVIVSHNLHQV 214
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
381-613 |
1.21e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 86.76 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGY---SP-EKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVD----TRDLSREE 452
Cdd:PRK13646 3 IRFDNVSYTYqkgTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithkTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 453 LRAHFSMVLQ--DTWLFTGSIYDNIHYG--NEQASEEEVIRAAKAAHVD-DFVRKlpegyqtILNEEASNISQGQRQLIT 527
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGpkNFKMNLDEVKNYAHRLLMDlGFSRD-------VMSQSPFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 528 IARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLL--ENRTSFVVAHRLSTI-RDADTIIVMAEGSIVETGTHDELMA 604
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFK 235
|
....*....
gi 488288408 605 KNGFYADLY 613
Cdd:PRK13646 236 DKKKLADWH 244
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
97-355 |
2.33e-18 |
|
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: 85.83 E-value: 2.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 97 DFDKIGQILLIVIAMYLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTL 176
Cdd:cd18784 31 SQDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 177 QQNLTQLITSIVTFVGVLWMMLTISWQLTLIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKS 256
Cdd:cd18784 111 SLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 257 FNHEESDQEVFEKENEKLYHAGRKAQFI------SAIIMPLMNFIKNLGYvfvavlGGVKVANGMMDLGDVQAFLQYTNQ 330
Cdd:cd18784 191 FANEDGEANRYSEKLKDTYKLKIKEALAyggyvwSNELTELALTVSTLYY------GGHLVITGQISGGNLISFILYQLE 264
|
250 260
....*....|....*....|....*
gi 488288408 331 FSQPITQIANLMNTIQATVASAERV 355
Cdd:cd18784 265 LGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
379-597 |
2.45e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 85.56 E-value: 2.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 379 YRVSFEHVAFGYSPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFS 458
Cdd:PRK13647 3 NIIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 459 MVLQ--DTWLFTGSIYDNIHYG--NEQASEEEVIR----AAKAAHVDDFVRKLPEgyqtilneeasNISQGQRQLITIAR 530
Cdd:PRK13647 83 LVFQdpDDQVFSSTVWDDVAFGpvNMGLDKDEVERrveeALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488288408 531 AFLANPDVLILDEATSSVDTRTEILIQAAMNRLLENRTSFVVA-HRLSTIRD-ADTIIVMAEGSIVETG 597
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEG 220
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
49-355 |
2.63e-18 |
|
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: 85.67 E-value: 2.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 49 VLVLAIAAVVFQIQTPKVLGQATTEIFKGVMKGAAEMKQGLKITSFPIdfdkigqillivIAMYLISAVFNFLQQVIMTR 128
Cdd:cd18574 1 AVLSALAAALVNIQIPLLLGDLVNVISRSLKETNGDFIEDLKKPALKL------------LGLYLLQSLLTFAYISLLSV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 129 VSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQQNLTQLITSIVTFVGVLWMMLTISWQLTLIA 208
Cdd:cd18574 69 VGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 209 LATVPLSLIVVMVVAP--RSQKHFAAQQ--KSLGLlnnqVEETYGGHVVVKSFNHEESDQEVFEKENEKLYHAGRKAQFI 284
Cdd:cd18574 149 LVIVPVVVLVGTLYGSflRKLSRRAQAQvaKATGV----ADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEKLGLG 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488288408 285 SAIIMPLMNFIKN---LGYVFVavlGGVKVANGMMDLGDVQAFLQYTNQFSQPITQIANLMNTIQATVASAERV 355
Cdd:cd18574 225 IGIFQGLSNLALNgivLGVLYY---GGSLVSRGELTAGDLMSFLVATQTIQRSLAQLSVLFGQYVKGKSAGARV 295
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
399-604 |
3.07e-18 |
|
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: 86.69 E-value: 3.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 399 DFNLNVK---PGEMV-AIVGPTGAGKTTLINL---LERFydiSSGSIKYDG---VDTR---DLSREelRAHFSMVLQDTW 465
Cdd:COG4148 13 GFTLDVDftlPGRGVtALFGPSGSGKTTLLRAiagLERP---DSGRIRLGGevlQDSArgiFLPPH--RRRIGYVFQEAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 466 LF-TGSIYDNIHYGNEQASeeeviRAAKAAHVDDFVRKLpeGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEA 544
Cdd:COG4148 88 LFpHLSVRGNLLYGRKRAP-----RAERRISFDEVVELL--GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488288408 545 TSSVD--TRTEILiqaamnRLLEN-RTSF-----VVAHRLSTI-RDADTIIVMAEGSIVETGTHDELMA 604
Cdd:COG4148 161 LAALDlaRKAEIL------PYLERlRDELdipilYVSHSLDEVaRLADHVVLLEQGRVVASGPLAEVLS 223
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
398-602 |
3.81e-18 |
|
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: 83.57 E-value: 3.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 398 KDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSReELRAHFSMVLQDTWL---FTGsiYDN 474
Cdd:cd03265 17 RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPR-EVRRRIGIVFQDLSVddeLTG--WEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 475 --IH---YGNEQAseeevIRAAKAAHVDDFVrklpeGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVD 549
Cdd:cd03265 94 lyIHarlYGVPGA-----ERRERIDELLDFV-----GLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488288408 550 TRTEILIQAAMNRLLE--NRTSFVVAHRLSTIRD-ADTIIVMAEGSIVETGTHDEL 602
Cdd:cd03265 164 PQTRAHVWEYIEKLKEefGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
386-597 |
4.26e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 86.82 E-value: 4.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 386 VAFGYSPeklLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMVLQDTW 465
Cdd:PRK09536 11 VEFGDTT---VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 466 L-FTGSIYDNIHYGN----------EQASEEEVIRAAKAAHVDDFVrklpegyqtilNEEASNISQGQRQLITIARAFLA 534
Cdd:PRK09536 88 LsFEFDVRQVVEMGRtphrsrfdtwTETDRAAVERAMERTGVAQFA-----------DRPVTSLSGGERQRVLLARALAQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488288408 535 NPDVLILDEATSSVDTRTEILIQAAMNRLLEN-RTSFVVAHRLS-TIRDADTIIVMAEGSIVETG 597
Cdd:PRK09536 157 ATPVLLLDEPTASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDlAARYCDELVLLADGRVRAAG 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
346-605 |
4.61e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.43 E-value: 4.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 346 QATvaSAERVFEVLDEEEMVDEPSGIPVETDSPYR-----VSFEHVAFGYsPEKLLMKDFNLNVKPGEMVAIVGPTGAGK 420
Cdd:COG0488 278 QAQ--SRIKALEKLEREEPPRRDKTVEIRFPPPERlgkkvLELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 421 TTLINLLERFYDISSGSIKYdGVDTR----DLSREELRAhfsmvlqdtwlfTGSIYDNIHYGNEQASEEEVIRAAKA--- 493
Cdd:COG0488 355 STLLKLLAGELEPDSGTVKL-GETVKigyfDQHQEELDP------------DKTVLDELRDGAPGGTEQEVRGYLGRflf 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 494 --AHVDDFVRKLpegyqtilneeasniSQGQR---QLitiARAFLANPDVLILDEATSSVDTRT-EILIQAamnrlLEN- 566
Cdd:COG0488 422 sgDDAFKPVGVL---------------SGGEKarlAL---AKLLLSPPNVLLLDEPTNHLDIETlEALEEA-----LDDf 478
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 488288408 567 -RTSFVVAH-R--LSTIrdADTIIVMAEGSIVE-TGTHDELMAK 605
Cdd:COG0488 479 pGTVLLVSHdRyfLDRV--ATRILEFEDGGVREyPGGYDDYLEK 520
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
398-602 |
1.88e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 84.31 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 398 KDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLsrEELRAHFSMVLQDTWLFTG-SIYDNIH 476
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDV--PPAERGVGMVFQSYALYPHlSVAENMS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 477 YGNEQASeeeviraAKAAHVDDFVRKLPEGYQT--ILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEI 554
Cdd:PRK11000 98 FGLKLAG-------AKKEEINQRVNQVAEVLQLahLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488288408 555 LIQAAMNRLLE--NRTSFVVAH-RLSTIRDADTIIVMAEGSIVETGTHDEL 602
Cdd:PRK11000 171 QMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
398-604 |
3.35e-17 |
|
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: 81.05 E-value: 3.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 398 KDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREElRAHFSMVL--QDTWLFTG-SIYDN 474
Cdd:cd03218 17 NGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLGIGYlpQEASIFRKlTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 475 IHYGNEQASEEEVIRAAKAAHV-DDFvrklpeGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTE 553
Cdd:cd03218 96 ILAVLEIRGLSKKEREEKLEELlEEF------HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488288408 554 ILIQAAMNRLLENRTSFVVA-HRLS-TIRDADTIIVMAEGSIVETGTHDELMA 604
Cdd:cd03218 170 QDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
384-552 |
3.84e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 81.67 E-value: 3.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 384 EHVAFGYsPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREElrahfSMVLQD 463
Cdd:PRK11248 5 SHLYADY-GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 464 TWLFT-GSIYDNIHYGNEQASEEEVIRAAKAAHVDDFVRKLPEGYQTILneeasNISQGQRQLITIARAFLANPDVLILD 542
Cdd:PRK11248 79 EGLLPwRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIW-----QLSGGQRQRVGIARALAANPQLLLLD 153
|
170
....*....|
gi 488288408 543 EATSSVDTRT 552
Cdd:PRK11248 154 EPFGALDAFT 163
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
388-604 |
3.95e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 82.05 E-value: 3.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 388 FGYSPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDG--VDTRDLSREELRAHFSMVLQ--D 463
Cdd:PRK13639 9 YSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTVGIVFQnpD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 464 TWLFTGSIYDNIHYG--NEQASEEEVIR----AAKAAHVDDFVRKLPEgyqtilneeasNISQGQRQLITIARAFLANPD 537
Cdd:PRK13639 89 DQLFAPTVEEDVAFGplNLGLSKEEVEKrvkeALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488288408 538 VLILDEATSSVDTRTEILIqaaMNRLLE-NR---TSFVVAHRLSTI-RDADTIIVMAEGSIVETGTHDELMA 604
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQI---MKLLYDlNKegiTIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
381-605 |
4.16e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 82.06 E-value: 4.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYSPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSRE-ELRAHFSM 459
Cdd:PRK13633 10 VSYKYESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDIRNKAGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 460 VLQ--DTWLFTGSIYDNIHYGNEQAS-EEEVIRaakaAHVDDFVRKLpeGYQTILNEEASNISQGQRQLITIARAFLANP 536
Cdd:PRK13633 90 VFQnpDNQIVATIVEEDVAFGPENLGiPPEEIR----ERVDESLKKV--GMYEYRRHAPHLLSGGQKQRVAIAGILAMRP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488288408 537 DVLILDEATSSVDT--RTEIliqaaMNRLLE-----NRTSFVVAHRLSTIRDADTIIVMAEGSIVETGTHDELMAK 605
Cdd:PRK13633 164 ECIIFDEPTAMLDPsgRREV-----VNTIKElnkkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
401-602 |
4.38e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 81.19 E-value: 4.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 401 NLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELrAHFSMV--LQDTWLFTG-SIYDNIHY 477
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI-ARMGVVrtFQHVRLFREmTVIENLLV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 478 GNEQ-----------------ASEEEVIraAKAAHVDDFVrklpeGYQTILNEEASNISQGQRQLITIARAFLANPDVLI 540
Cdd:PRK11300 104 AQHQqlktglfsgllktpafrRAESEAL--DRAATWLERV-----GLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILM 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488288408 541 LDEATSSVDTRTEILIQAAMNRLlenRTSFVVA-----HRLSTIRD-ADTIIVMAEGSIVETGTHDEL 602
Cdd:PRK11300 177 LDEPAAGLNPKETKELDELIAEL---RNEHNVTvllieHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
398-602 |
6.33e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 83.92 E-value: 6.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 398 KDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDG--VDTRDlSREELRAHFSMVLQDTWLF-TGSIYDN 474
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRS-PRDAIALGIGMVHQHFMLVpNLTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 475 IHYGNEQaSEEEVIRAAKAAHVddfVRKLPEGYQTILNEEA--SNISQGQRQLITIARAFLANPDVLILDEATsSVDTRT 552
Cdd:COG3845 101 IVLGLEP-TKGGRLDRKAARAR---IRELSERYGLDVDPDAkvEDLSVGEQQRVEILKALYRGARILILDEPT-AVLTPQ 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488288408 553 EI--LIqAAMNRLLENRTSFV-VAHRLSTIRD-ADTIIVMAEGSIVETG-----THDEL 602
Cdd:COG3845 176 EAdeLF-EILRRLAAEGKSIIfITHKLREVMAiADRVTVLRRGKVVGTVdtaetSEEEL 233
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
378-597 |
6.34e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.07 E-value: 6.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 378 PYrVSFEHVAFGYSPEKLLmKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSrEELRAHf 457
Cdd:PRK09700 4 PY-ISMAGIGKSFGPVHAL-KSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD-HKLAAQ- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 458 smvlqdtwLFTGSIYDNIHYGNEQASEEEV------IRAAKAAHVDD--FVRKLPE------GYQTILNEEASNISQGQR 523
Cdd:PRK09700 80 --------LGIGIIYQELSVIDELTVLENLyigrhlTKKVCGVNIIDwrEMRVRAAmmllrvGLKVDLDEKVANLSISHK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488288408 524 QLITIARAFLANPDVLILDEATSSV-DTRTEILIqAAMNRLLENRTSFV-VAHRLSTIRD-ADTIIVMAEGSIVETG 597
Cdd:PRK09700 152 QMLEIAKTLMLDAKVIIMDEPTSSLtNKEVDYLF-LIMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
385-604 |
8.49e-17 |
|
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: 83.58 E-value: 8.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 385 HVAFG-YSPEKLLMKDFNLNVKPGEMVAIVGPTGAGKT----TLINLLERFYDISSGSIKYDGVDTRDLSREELRA---- 455
Cdd:COG4172 13 SVAFGqGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 456 HFSMVLQD--TWL---FTgsIYDNI------HYG-NEQASEEEVIRAAKAAHVDDfvrklPEgyqTILNEEASNISQGQR 523
Cdd:COG4172 93 RIAMIFQEpmTSLnplHT--IGKQIaevlrlHRGlSGAAARARALELLERVGIPD-----PE---RRLDAYPHQLSGGQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 524 QLITIARAfLAN-PDVLILDEATSSVD--TRTEIL-----IQAAMNR--LLenrtsfvVAHRLSTIRD-ADTIIVMAEGS 592
Cdd:COG4172 163 QRVMIAMA-LANePDLLIADEPTTALDvtVQAQILdllkdLQRELGMalLL-------ITHDLGVVRRfADRVAVMRQGE 234
|
250
....*....|..
gi 488288408 593 IVETGTHDELMA 604
Cdd:COG4172 235 IVEQGPTAELFA 246
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
394-604 |
8.92e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 80.91 E-value: 8.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 394 KLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGsIKYDG---------VDTRDLSreELRAHFSMVLQDT 464
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGdvllggrsiFNYRDVL--EFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 465 WLFTGSIYDNIHYG--NEQASEEEVIRAAKAAHVDDFvrKLPEGYQTILNEEASNISQGQRQLITIARAFLANPDVLILD 542
Cdd:PRK14271 111 NPFPMSIMDNVLAGvrAHKLVPRKEFRGVAQARLTEV--GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488288408 543 EATSSVDTRTEILIQAAMNRLLENRTSFVVAHRLS-TIRDADTIIVMAEGSIVETGTHDELMA 604
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
397-594 |
1.49e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 83.23 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 397 MKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREEL----RAHFSMVLQDTWLFTgsiy 472
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLS---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 473 dniHYGNEQASEEEVI-----RAAKAAHVDDFVRKLpeGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSS 547
Cdd:PRK10535 100 ---HLTAAQNVEVPAVyagleRKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488288408 548 VDTRTEILIQAAMNRLLEN-RTSFVVAHRLSTIRDADTIIVMAEGSIV 594
Cdd:PRK10535 175 LDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
367-597 |
2.21e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 82.45 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 367 EPSGIPVETDSP----YRVSFEHVAFGYSP--------EKLLMKDFNLNVKPGEMVAIVGPTGAGKTT----LINLLErf 430
Cdd:PRK15134 260 EPSGDPVPLPEPasplLDVEQLQVAFPIRKgilkrtvdHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 431 ydiSSGSIKYDGVDTRDLSREEL---RAHFSMVLQDTW------LFTGSIYDN---IHYG--NEQASEEEVIRAAKAAHV 496
Cdd:PRK15134 338 ---SQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPNsslnprLNVLQIIEEglrVHQPtlSAAQREQQVIAVMEEVGL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 497 DDFVR-KLPegyqtilneeaSNISQGQRQLITIARAFLANPDVLILDEATSSVDtRTeilIQAAMNRLL-----ENRTSF 570
Cdd:PRK15134 415 DPETRhRYP-----------AEFSGGQRQRIAIARALILKPSLIILDEPTSSLD-KT---VQAQILALLkslqqKHQLAY 479
|
250 260
....*....|....*....|....*....
gi 488288408 571 V-VAHRLSTIRD-ADTIIVMAEGSIVETG 597
Cdd:PRK15134 480 LfISHDLHVVRAlCHQVIVLRQGEVVEQG 508
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
381-575 |
2.52e-16 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 76.81 E-value: 2.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYSPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIkydgvdtrdlSREELRAHFsMV 460
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI----------GMPEGEDLL-FL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 461 LQDTWLFTGSIYDNIHYgneqaseeeviraakaahvddfvrklPegYQTILneeasniSQGQRQLITIARAFLANPDVLI 540
Cdd:cd03223 70 PQRPYLPLGTLREQLIY--------------------------P--WDDVL-------SGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190
....*....|....*....|....*....|....*.
gi 488288408 541 LDEATSSVDTRTEiliQAAMNRLLENRTSFV-VAHR 575
Cdd:cd03223 115 LDEATSALDEESE---DRLYQLLKELGITVIsVGHR 147
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
390-597 |
4.89e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 78.35 E-value: 4.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 390 YSPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDIS-----SGSIKYDGVD--TRDLSREELRAHFSMVLQ 462
Cdd:PRK14267 13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNiySPDVDPIEVRREVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 463 DTWLFTG-SIYDNIHYG--------NEQASEEEVIRAAKAAHVDDFVRKLpegyqtiLNEEASNISQGQRQLITIARAFL 533
Cdd:PRK14267 93 YPNPFPHlTIYDNVAIGvklnglvkSKKELDERVEWALKKAALWDEVKDR-------LNDYPSNLSGGQRQRLVIARALA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488288408 534 ANPDVLILDEATSSVDTRTEILIQAAMNRLLENRTSFVVAHR-LSTIRDADTIIVMAEGSIVETG 597
Cdd:PRK14267 166 MKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
384-604 |
1.02e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 77.83 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 384 EHVAFGYSPEKLL--MKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMVL 461
Cdd:PRK13642 8 ENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 462 Q--DTWLFTGSIYDNIHYG--NEQASEEEVIR----AAKAAHVDDFVRKLPegyqtilneeaSNISQGQRQLITIARAFL 533
Cdd:PRK13642 88 QnpDNQFVGATVEDDVAFGmeNQGIPREEMIKrvdeALLAVNMLDFKTREP-----------ARLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488288408 534 ANPDVLILDEATSSVDT--RTEILIQAAMNRLLENRTSFVVAHRLSTIRDADTIIVMAEGSIVETGTHDELMA 604
Cdd:PRK13642 157 LRPEIIILDESTSMLDPtgRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
371-597 |
1.42e-15 |
|
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: 76.03 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 371 IPVETDSPYRVSFEHVAFGYSPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGvdtrdlsr 450
Cdd:cd03220 12 TYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 451 eelrahfsmvlQDTWLF----------TGsiYDNIH-----YGNEQASEEEVIRAAKA-AHVDDFvrklpegyqtiLNEE 514
Cdd:cd03220 84 -----------RVSSLLglgggfnpelTG--RENIYlngrlLGLSRKEIDEKIDEIIEfSELGDF-----------IDLP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 515 ASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLLEN-RTSFVVAHRLSTIRD-ADTIIVMAEGS 592
Cdd:cd03220 140 VKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQgKTVILVSHDPSSIKRlCDRALVLEKGK 219
|
....*
gi 488288408 593 IVETG 597
Cdd:cd03220 220 IRFDG 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
381-597 |
1.46e-15 |
|
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: 75.78 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVA--FGyspEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDG--VDTRDLSR-----E 451
Cdd:cd03269 1 LEVENVTkrFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpLDIAARNRigylpE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 452 ELRAHFSMVLQDTWLFTGSIYDnihYGNEQAseeeviraakAAHVDDFVRKLP-EGYQTILNEEasnISQGQRQLITIAR 530
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKG---LKKEEA----------RRRIDEWLERLElSEYANKRVEE---LSKGNQQKVQFIA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488288408 531 AFLANPDVLILDEATSSVDTRTEILIQAAMNRLLENRTSFV-VAHRLSTIRD-ADTIIVMAEGSIVETG 597
Cdd:cd03269 142 AVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVIlSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
399-596 |
2.85e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 78.68 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 399 DFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISS--GSIKYDG--VDTRDLSREELRA----HfsmvlQDTWLFTG- 469
Cdd:NF040905 19 DVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGevCRFKDIRDSEALGiviiH-----QELALIPYl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 470 SIYDNIHYGNEQASE-----EEVIRAAKaahvdDFVRK--LPEGYQTILneeaSNISQGQRQLITIARAFLANPDVLILD 542
Cdd:NF040905 94 SIAENIFLGNERAKRgvidwNETNRRAR-----ELLAKvgLDESPDTLV----TDIGVGKQQLVEIAKALSKDVKLLILD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 543 EATSSV-DTRTEILiqaaMNRLLENR----TSFVVAHRLSTIRD-ADTIIVMAEGSIVET 596
Cdd:NF040905 165 EPTAALnEEDSAAL----LDLLLELKaqgiTSIIISHKLNEIRRvADSITVLRDGRTIET 220
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
380-606 |
2.86e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 78.86 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 380 RVSFEHVAFGYSPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSM 459
Cdd:PRK10522 322 TLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 460 VLQDTWLFTGSIydnihyGNEQaseeeviRAAKAAHVDDFVRKLPEGYQ-TILNEEASNI--SQGQRQLITIARAFLANP 536
Cdd:PRK10522 402 VFTDFHLFDQLL------GPEG-------KPANPALVEKWLERLKMAHKlELEDGRISNLklSKGQKKRLALLLALAEER 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488288408 537 DVLILDEATSSVDTR-TEILIQAAMNRLLE-NRTSFVVAHRLSTIRDADTIIVMAEGSIVE-TGTHDELMAKN 606
Cdd:PRK10522 469 DILLLDEWAADQDPHfRREFYQVLLPLLQEmGKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERDAASRD 541
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
381-549 |
3.23e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 75.30 E-value: 3.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYSPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREE---LRAHF 457
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 458 SMVLQDTWLFTG-SIYDNIHYG--NEQASEEEVIRAAKAAhVDdfvrklpegyQTILNEEASN----ISQGQRQLITIAR 530
Cdd:PRK10908 82 GMIFQDHHLLMDrTVYDNVAIPliIAGASGDDIRRRVSAA-LD----------KVGLLDKAKNfpiqLSGGEQQRVGIAR 150
|
170
....*....|....*....
gi 488288408 531 AFLANPDVLILDEATSSVD 549
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLD 169
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
381-604 |
3.46e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 76.41 E-value: 3.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYSP----EKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDG----VDTRDLSREE 452
Cdd:PRK13641 3 IKFENVDYIYSPgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 453 LRAHFSMVLQ--DTWLFTGSIYDNIHYG--NEQASEEEVIRAAKaahvdDFVRK--LPEgyqTILNEEASNISQGQRQLI 526
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGpkNFGFSEDEAKEKAL-----KWLKKvgLSE---DLISKSPFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 527 TIARAFLANPDVLILDEATSSVDTRT-EILIQAAMNRLLENRTSFVVAHRLSTIRD-ADTIIVMAEGSIVETGTHDELMA 604
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFS 234
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
391-602 |
3.67e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.94 E-value: 3.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 391 SPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLErFYdiSSGSIKYDG---VDTRDLSREELRAHFSMVLQDTwLF 467
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FR--SPKGVKGSGsvlLNGMPIDAKEMRAISAYVQQDD-LF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 468 TGSI--YDNIHYGNEQASEEEVIRAAKAAHVDDFVRK--LPEGYQTILNEEA--SNISQGQRQLITIARAFLANPDVLIL 541
Cdd:TIGR00955 111 IPTLtvREHLMFQAHLRMPRRVTKKEKRERVDEVLQAlgLRKCANTRIGVPGrvKGLSGGERKRLAFASELLTDPPLLFC 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488288408 542 DEATSSVDTRTEILIQAAMNRLLEN-RTSFVVAHRLST--IRDADTIIVMAEGSIVETGTHDEL 602
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQVLKGLAQKgKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
398-593 |
3.81e-15 |
|
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: 74.01 E-value: 3.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 398 KDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLS-REELRAHFSMVLQD---TWLFTG-SIY 472
Cdd:cd03215 17 RDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIAYVPEDrkrEGLVLDlSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 473 DNIhygneqaseeeVIRAakaahvddfvrklpegyqtILneeasniSQGQRQLITIARAFLANPDVLILDEATSSVDTRT 552
Cdd:cd03215 97 ENI-----------ALSS-------------------LL-------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488288408 553 EILIQAAMNRLLENRTSFVVahrLST-----IRDADTIIVMAEGSI 593
Cdd:cd03215 140 KAEIYRLIRELADAGKAVLL---ISSeldelLGLCDRILVMYEGRI 182
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
399-600 |
4.29e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 75.35 E-value: 4.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 399 DFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDG-----VDTRDLSREELRahfsMVLQDTWLF------ 467
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAERR----RLLRTEWGFvhqhpr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 468 -----TGSIYDNI----------HYGN--EQASE--EEV-IRAAKaahVDDfvrkLPEGYqtilneeasniSQGQRQLIT 527
Cdd:PRK11701 100 dglrmQVSAGGNIgerlmavgarHYGDirATAGDwlERVeIDAAR---IDD----LPTTF-----------SGGMQQRLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 528 IARAFLANPDVLILDEATSSVDtrteILIQAAMNRLLENRTS------FVVAHRLSTIRD-ADTIIVMAEGSIVETGTHD 600
Cdd:PRK11701 162 IARNLVTHPRLVFMDEPTGGLD----VSVQARLLDLLRGLVRelglavVIVTHDLAVARLlAHRLLVMKQGRVVESGLTD 237
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
104-353 |
5.61e-15 |
|
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: 75.78 E-value: 5.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 104 ILLIVIAMYLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQQNLTQL 183
Cdd:cd18561 38 PLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 184 ITSIVTFVGVLWMMLTISWQLTLIALATVPLSLIVVMVV----APRSQKHFAAqqksLGLLNNQVEETYGGHVVVKSFNH 259
Cdd:cd18561 118 LVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWdrlaKDTGRRHWAA----YGRLSAQFLDSLQGMTTLKAFGA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 260 EESDQEVFEKENEKLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPITQIA 339
Cdd:cd18561 194 SKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGVGALRVLGGQLTLSSLLLILFLSREFFRPLRDLG 273
|
250
....*....|....
gi 488288408 340 NLMNTIQATVASAE 353
Cdd:cd18561 274 AYWHAGYQGISAAD 287
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
400-603 |
5.86e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 74.88 E-value: 5.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 400 FNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDiSSGSIKYDGVDTRDLSREEL---RAHFSMvlQDTWLFTGSIYdniH 476
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAELarhRAYLSQ--QQSPPFAMPVF---Q 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 477 Y----GNEQASEEEVIRAakaahVDDFVRKLpeGYQTILNEEASNISQGQRQLITIARAFL-----ANPD--VLILDEAT 545
Cdd:COG4138 89 YlalhQPAGASSEAVEQL-----LAQLAEAL--GLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptINPEgqLLLLDEPM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488288408 546 SSVDtrteILIQAAMNRLLEN-----RTSFVVAHRLS-TIRDADTIIVMAEGSIVETGTHDELM 603
Cdd:COG4138 162 NSLD----VAQQAALDRLLRElcqqgITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
381-608 |
6.63e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 75.54 E-value: 6.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYSPEKLL----MKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREE---- 452
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFasraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 453 LRAHFSMVLQ--DTWLFTGSIYDNIHYGNEQ----ASEEEVIRAAKAAHV---DDFVRKLPegyqtilneeaSNISQGQR 523
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGPQNfgipKEKAEKIAAEKLEMVglaDEFWEKSP-----------FELSGGQM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 524 QLITIARAFLANPDVLILDEATSSVDTRTEIliqaAMNRLLEN-----RTSFVVAHRLSTIRD-ADTIIVMAEGSIVETG 597
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARI----EMMQLFESihqsgQTVVLVTHLMDDVADyADYVYLLEKGHIISCG 226
|
250
....*....|.
gi 488288408 598 THDELMAKNGF 608
Cdd:PRK13643 227 TPSDVFQEVDF 237
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
390-602 |
6.73e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 76.28 E-value: 6.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 390 YSPEKLL--MKDFNLNVKPGEMVAIVGPTGAGKTTL----INLLErfydISSGSIKYDGVDTRDLSREELRAHFS---MV 460
Cdd:PRK15079 28 WQPPKTLkaVDGVTLRLYEGETLGVVGESGCGKSTFaraiIGLVK----ATDGEVAWLGKDLLGMKDDEWRAVRSdiqMI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 461 LQDTW------LFTGSIYDN---IHYgnEQASEEEVIRAAKAAHVDdfVRKLPEgyqtILNEEASNISQGQRQLITIARA 531
Cdd:PRK15079 104 FQDPLaslnprMTIGEIIAEplrTYH--PKLSRQEVKDRVKAMMLK--VGLLPN----LINRYPHEFSGGQCQRIGIARA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488288408 532 FLANPDVLILDEATSSVDtrteILIQAAMNRLL-----ENRTSFV-VAHRLSTIRD-ADTIIVMAEGSIVETGTHDEL 602
Cdd:PRK15079 176 LILEPKLIICDEPVSALD----VSIQAQVVNLLqqlqrEMGLSLIfIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
397-597 |
1.02e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 73.91 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 397 MKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDlSREELRAHFSMVL------------QDT 464
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWK-RRKKFLRRIGVVFgqktqlwwdlpvIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 465 WLFTGSIYDnIHYGNEQASEEEVIRAAKAAHvddfvrklpegyqtILNEEASNISQGQRQLITIARAFLANPDVLILDEA 544
Cdd:cd03267 116 FYLLAAIYD-LPPARFKKRLDELSELLDLEE--------------LLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488288408 545 TSSVDTRTEILIQAAMNRLLENR--TSFVVAHRLSTI-RDADTIIVMAEGSIVETG 597
Cdd:cd03267 181 TIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIeALARRVLVIDKGRLLYDG 236
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
399-600 |
1.28e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 73.90 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 399 DFNLNVKPGEMVAIVGPTGAGKTTLI---NLLERfydISSGSIKYDGvDTRDLSRE-------ELRAHFSMVLQDTWLFT 468
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLrvlNLLEM---PRSGTLNIAG-NHFDFSKTpsdkairELRRNVGMVFQQYNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 469 G-SIYDNIHYG-------NEQASEEEVIRAAKAAHVDDFVRKLPEgyqtilneeasNISQGQRQLITIARAFLANPDVLI 540
Cdd:PRK11124 96 HlTVQQNLIEApcrvlglSKDQALARAEKLLERLRLKPYADRFPL-----------HLSGGQQQRVAIARALMMEPQVLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488288408 541 LDEATSSVDtrTEILIQAA--MNRLLENR-TSFVVAHRLSTIRDADTIIV-MAEGSIVETGTHD 600
Cdd:PRK11124 165 FDEPTAALD--PEITAQIVsiIRELAETGiTQVIVTHEVEVARKTASRVVyMENGHIVEQGDAS 226
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
397-602 |
1.32e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 76.03 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 397 MKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSreELRAHFSMVLQDTWLFTG-SIYDNI 475
Cdd:PRK11607 35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP--PYQRPINMMFQSYALFPHmTVEQNI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 476 HYGNEQ---ASEEEVIRAAKA---AHVDDFVRKLPEgyqtilneeasNISQGQRQLITIARAFLANPDVLILDEATSSVD 549
Cdd:PRK11607 113 AFGLKQdklPKAEIASRVNEMlglVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488288408 550 TRTEILIQAAMNRLLE--NRTSFVVAH-RLSTIRDADTIIVMAEGSIVETGTHDEL 602
Cdd:PRK11607 182 KKLRDRMQLEVVDILErvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
394-601 |
1.47e-14 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 72.90 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 394 KLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYD---ISSGSIKYDGVDTRDLSREelRAHFSMVLQDTWLFTG- 469
Cdd:COG4136 14 RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRLTALPAE--QRRIGILFQDDLLFPHl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 470 SIYDNIHYG-----NEQASEEEVIRAAKAAHVDDFVRKLPegyqtilneeaSNISQGQRQLITIARAFLANPDVLILDEA 544
Cdd:COG4136 92 SVGENLAFAlpptiGRAQRRARVEQALEEAGLAGFADRDP-----------ATLSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488288408 545 TSSVDT--RTEILiqaamnrllenrtSFVVAHrlstIRDADTIIVMAegsivetgTHDE 601
Cdd:COG4136 161 FSKLDAalRAQFR-------------EFVFEQ----IRQRGIPALLV--------THDE 194
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
398-604 |
1.72e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 76.21 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 398 KDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLS-REELRAHFSMVLQD---TWLFTG-SIY 472
Cdd:COG1129 269 RDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSpRDAIRAGIAYVPEDrkgEGLVLDlSIR 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 473 DNI---------HYGneqaseeeVI-RAAKAAHVDDFVRKL----PEGYQTIlneeaSNISQGQRQLITIARAFLANPDV 538
Cdd:COG1129 349 ENItlasldrlsRGG--------LLdRRRERALAEEYIKRLriktPSPEQPV-----GNLSGGNQQKVVLAKWLATDPKV 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488288408 539 LILDEATSSVD--TRTEilIQAAMNRLLENRTSFVVAhrlST-----IRDADTIIVMAEGSIV-----ETGTHDELMA 604
Cdd:COG1129 416 LILDEPTRGIDvgAKAE--IYRLIRELAAEGKAVIVI---SSelpelLGLSDRILVMREGRIVgeldrEEATEEAIMA 488
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
393-604 |
2.36e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 73.46 E-value: 2.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 393 EKLLMKDFNLNVKPGEMVAIVGPTGAGKTTL---INLLERfydISSGSIKYDGVDTRdLSREE--------------LRA 455
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFlrcINFLEK---PSEGSIVVNGQTIN-LVRDKdgqlkvadknqlrlLRT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 456 HFSMVLQ--DTWLFTgSIYDNIHYG-------NEQASEEEVIRAAKAAHVDDFVR-KLPegyqtilneeaSNISQGQRQL 525
Cdd:PRK10619 93 RLTMVFQhfNLWSHM-TVLENVMEApiqvlglSKQEARERAVKYLAKVGIDERAQgKYP-----------VHLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 526 ITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLLEN-RTSFVVAHRLSTIRDADT-IIVMAEGSIVETGTHDELM 603
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSShVIFLHQGKIEEEGAPEQLF 240
|
.
gi 488288408 604 A 604
Cdd:PRK10619 241 G 241
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
375-603 |
2.48e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 73.48 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 375 TDSPYRVSFEHVAFGYSpEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELR 454
Cdd:PRK10253 2 TESVARLRGEQLTLGYG-KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 455 AHFSMVLQDTwLFTGSIydnihygneqaSEEEVIRAAKAAHVDDFVRKLPE------------GYQTILNEEASNISQGQ 522
Cdd:PRK10253 81 RRIGLLAQNA-TTPGDI-----------TVQELVARGRYPHQPLFTRWRKEdeeavtkamqatGITHLADQSVDTLSGGQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 523 RQLITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLleNR----TSFVVAHRLS-TIRDADTIIVMAEGSIVETG 597
Cdd:PRK10253 149 RQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSEL--NRekgyTLAAVLHDLNqACRYASHLIALREGKIVAQG 226
|
....*.
gi 488288408 598 THDELM 603
Cdd:PRK10253 227 APKEIV 232
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
400-603 |
3.07e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 72.66 E-value: 3.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 400 FNLNVKPGEMVAIVGPTGAGKTTLI----NLLErfydiSSGSIKYDGVDTRDLSREEL---RAHFSMvlQDTWLFTGSIY 472
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLarmaGLLP-----GSGSIQFAGQPLEAWSAAELarhRAYLSQ--QQTPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 473 dniHY----GNEQASEeevirAAKAAHVDDFVRKLpeGYQTILNEEASNISQGQRQLITIARAFL-----ANPD--VLIL 541
Cdd:PRK03695 88 ---QYltlhQPDKTRT-----EAVASALNEVAEAL--GLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPAgqLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488288408 542 DEATSSVDtrteILIQAAMNRLLE-----NRTSFVVAHRLS-TIRDADTIIVMAEGSIVETGTHDELM 603
Cdd:PRK03695 158 DEPMNSLD----VAQQAALDRLLSelcqqGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
397-602 |
4.05e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 75.66 E-value: 4.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 397 MKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDG----------VDTRDLSREELR----AHFSMVLQ 462
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRhvrgADMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 463 DTW-----LFT--GSIYDNI--HYGneqASEEEVIRAAKaaHVDDFVRkLPEGyQTILNEEASNISQGQRQLITIARAFL 533
Cdd:PRK10261 112 EPMtslnpVFTvgEQIAESIrlHQG---ASREEAMVEAK--RMLDQVR-IPEA-QTILSRYPHQLSGGMRQRVMIAMALS 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488288408 534 ANPDVLILDEATSSVDtrteILIQAAMNRL---LENRTSFVV---AHRLSTIRD-ADTIIVMAEGSIVETGTHDEL 602
Cdd:PRK10261 185 CRPAVLIADEPTTALD----VTIQAQILQLikvLQKEMSMGVifiTHDMGVVAEiADRVLVMYQGEAVETGSVEQI 256
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
398-605 |
5.22e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 72.04 E-value: 5.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 398 KDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGvdtrdlsRE----ELRAHFSMVLqdtwlfTGsiYD 473
Cdd:COG1134 43 KDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-------RVsallELGAGFHPEL------TG--RE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 474 NIH-----YGneqASEEEVirAAKAAHVDDF----------VRklpegyqtilneeasNISQGQRqlitiAR-AF-LA-- 534
Cdd:COG1134 108 NIYlngrlLG---LSRKEI--DEKFDEIVEFaelgdfidqpVK---------------TYSSGMR-----ARlAFaVAta 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488288408 535 -NPDVLILDEATSSVDTRTEILIQAAMNRLLEN-RTSFVVAHRLSTIRD-ADTIIVMAEGSIVETGTHDELMAK 605
Cdd:COG1134 163 vDPDILLVDEVLAVGDAAFQKKCLARIRELRESgRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
393-604 |
5.57e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 72.49 E-value: 5.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 393 EKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREEL---RAHFSMVLQDTWLFTG 469
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLFQSGALFTD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 470 -SIYDNIHYGNEQASE--EEVIRAAkaahvddFVRKLPE-GYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEAT 545
Cdd:PRK11831 99 mNVFDNVAYPLREHTQlpAPLLHST-------VMMKLEAvGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPF 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488288408 546 SSVDTRTE-ILIQ--AAMNRLLeNRTSFVVAHRLSTIRD-ADTIIVMAEGSIVETGTHDELMA 604
Cdd:PRK11831 172 VGQDPITMgVLVKliSELNSAL-GVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQALQA 233
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
399-610 |
5.79e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 73.35 E-value: 5.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 399 DFNLNVKPGEMVAIVGPTGAGKTTLIN-----LLERFYDISSGSIK------YDGVDTRDLSRE-----ELRAHFSMVLQ 462
Cdd:PRK13631 44 NISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVGDIYigdkknNHELITNPYSKKiknfkELRRRVSMVFQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 463 --DTWLFTGSIYDNIHYG--NEQASEEEVIRAAKAahvddFVRKLPEGYqTILNEEASNISQGQRQLITIARAFLANPDV 538
Cdd:PRK13631 124 fpEYQLFKDTIEKDIMFGpvALGVKKSEAKKLAKF-----YLNKMGLDD-SYLERSPFGLSGGQKRRVAIAGILAIQPEI 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488288408 539 LILDEATSSVDTRTE-ILIQAAMNRLLENRTSFVVAHRLSTIRD-ADTIIVMAEGSIVETGTHDELMAKNGFYA 610
Cdd:PRK13631 198 LIFDEPTAGLDPKGEhEMMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIFTDQHIIN 271
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
390-574 |
7.81e-14 |
|
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: 71.67 E-value: 7.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 390 YSPEKLLMKDFNLNVKPG-----EMVAIVGPTGAGKTTLINLLerfydisSGSIKYDGVDT----RDLSR--EELRAHFS 458
Cdd:cd03237 3 YPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKML-------AGVLKPDEGDIeielDTVSYkpQYIKADYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 459 MVLQDtwlFTGSIYDNihYGNEQASEEEVIRaakaahvddfvrklPEGYQTILNEEASNISQGQRQLITIARAFLANPDV 538
Cdd:cd03237 76 GTVRD---LLSSITKD--FYTHPYFKTEIAK--------------PLQIEQILDREVPELSGGELQRVAIAACLSKDADI 136
|
170 180 190
....*....|....*....|....*....|....*...
gi 488288408 539 LILDEATSSVDTRTEILIQAAMNRLLEN--RTSFVVAH 574
Cdd:cd03237 137 YLLDEPSAYLDVEQRLMASKVIRRFAENneKTAFVVEH 174
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
105-355 |
1.21e-13 |
|
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they 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: 350013 [Multi-domain] Cd Length: 294 Bit Score: 71.74 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 105 LLIVIAMYLISAVFNFLQQVIMTRvsqrtvyelrqeLEAKMN------------KVPISYYDTHSNGDIMSR-AINDMdn 171
Cdd:cd18569 45 LLGMALTALLQGLLTWLQQYYLLR------------LETKLAlssssrffwhvlRLPVEFFSQRYAGDIASRvQSNDR-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 172 IASTLQQNLTQLITSIVTFVGVLWMMLTISWQLTLIALATVPLSLIVVMVVAPR----SQKHFAAQQKSLGLLNN--QVE 245
Cdd:cd18569 111 VANLLSGQLATTVLNLVMAVFYALLMLQYDVPLTLIGIAIALLNLLVLRLVSRKrvdlNRRLLQDSGKLTGTTMSglQMI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 246 ETygghvvVKSfNHEESDqeVFEK---ENEKLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQ 322
Cdd:cd18569 191 ET------LKA-SGAESD--FFSRwagYQAKVLNAQQELGRTNQLLGALPTLLSALTNAAILGLGGLLVMDGALTIGMLV 261
|
250 260 270
....*....|....*....|....*....|...
gi 488288408 323 AFLQYTNQFSQPITQIANLMNTIQATVASAERV 355
Cdd:cd18569 262 AFQSLMASFLAPVNSLVGLGGTLQEMRGDMERL 294
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
50-335 |
1.46e-13 |
|
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: 71.76 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 50 LVLAIAAVVFQIQTPKVLGQAtteifkgvmkgaaemkqglkITSFPIDFDKIGQILLIVIAMY----LISAVFNFLQQVI 125
Cdd:cd18582 2 LLLLVLAKLLNVAVPFLLKYA--------------------VDALSAPASALLAVPLLLLLAYglarILSSLFNELRDAL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 126 MTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGD---IMSRAINDMDNIASTLqqnLTQLITSIVTFVGVLWMMLTI-S 201
Cdd:cd18582 62 FARVSQRAVRRLALRVFRHLHSLSLRFHLSRKTGAlsrAIERGTRGIEFLLRFL---LFNILPTILELLLVCGILWYLyG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 202 WQLTLIALATVPLSLIVVMVVAPRSQKHFAAQqkslgllnNQVEETYGGHVV--------VKSFNHEESDQEVFEKENEK 273
Cdd:cd18582 139 WSYALITLVTVALYVAFTIKVTEWRTKFRREM--------NEADNEANAKAVdsllnyetVKYFNNEEYEAERYDKALAK 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488288408 274 LYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGD---VQAFLQytnQFSQPI 335
Cdd:cd18582 211 YEKAAVKSQTSLALLNIGQALIISLGLTAIMLLAAQGVVAGTLTVGDfvlVNTYLL---QLYQPL 272
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
374-595 |
1.63e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.99 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 374 ETDSPYRVSFEHVAFGYS---PEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDgVDTRDLSR 450
Cdd:COG2401 20 VLDLSERVAIVLEAFGVElrvVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD-VPDNQFGR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 451 EElrahfsmvlqdtwlftgSIYDNIHYGNEQASEEEVIRAAKAAHVDDFVRKLPEgyqtilneeasnISQGQRQLITIAR 530
Cdd:COG2401 99 EA-----------------SLIDAIGRKGDFKDAVELLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLAL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488288408 531 AFLANPDVLILDEATSSVDTRTEILIQAAMNRLL-ENRTSFVVA-HRLSTIRD--ADTIIVMAEGSIVE 595
Cdd:COG2401 150 LLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLArRAGITLVVAtHHYDVIDDlqPDLLIFVGYGGVPE 218
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
398-605 |
1.77e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 71.66 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 398 KDFNLNVKPGEMVAIVGPTGAGKTTLINLLErfyDI---SSGSIKYDGVD-TRDlsREELRAHFSMV------------L 461
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLT---GIlvpTSGEVRVLGYVpFKR--RKEFARRIGVVfgqrsqlwwdlpA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 462 QDTWLFTGSIYDnIhygNEQASEEEVIRAAKAAHVDDF----VRKLpegyqtilneeasniSQGQRQLITIARAFLANPD 537
Cdd:COG4586 114 IDSFRLLKAIYR-I---PDAEYKKRLDELVELLDLGELldtpVRQL---------------SLGQRMRCELAAALLHRPK 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488288408 538 VLILDEATSSVDtrteILIQAAMNRLL-----ENRTSFVVA-HRLSTIRD-ADTIIVMAEGSIVETGTHDELMAK 605
Cdd:COG4586 175 ILFLDEPTIGLD----VVSKEAIREFLkeynrERGTTILLTsHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
397-591 |
1.89e-13 |
|
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: 70.19 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 397 MKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDG--VDTRDLSREELRAHFSMVlqdTWLftgSIYDN 474
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGkqITEPGPDRMVVFQNYSLL---PWL---TVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 475 IHYG----NEQASEEEviraaKAAHVDDFVRKLpeGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDT 550
Cdd:TIGR01184 75 IALAvdrvLPDLSKSE-----RRAIVEEHIALV--GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488288408 551 RT-EILIQAAMNRLLENR-TSFVVAHRL-STIRDADTIIVMAEG 591
Cdd:TIGR01184 148 LTrGNLQEELMQIWEEHRvTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
396-591 |
2.31e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 69.84 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 396 LMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLS---REELRAH-------FSMVLQDtw 465
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaaKAELRNQklgfiyqFHHLLPD-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 466 lFTGSiydnihygnEQASEEEVIRAAKAAHVDDFVRKLPE--GYQTILNEEASNISQGQRQLITIARAFLANPDVLILDE 543
Cdd:PRK11629 102 -FTAL---------ENVAMPLLIGKKKPAEINSRALEMLAavGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488288408 544 ATSSVDTRTEILIQAAMNRLleNR---TSF-VVAHRLSTIRDADTIIVMAEG 591
Cdd:PRK11629 172 PTGNLDARNADSIFQLLGEL--NRlqgTAFlVVTHDLQLAKRMSRQLEMRDG 221
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
392-594 |
3.10e-13 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 68.83 E-value: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 392 PEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLI----NLLERFYDIsSGSIKYDGVDTrDLSREELRAHFSMVLQdtwlf 467
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLkalaNRTEGNVSV-EGDIHYNGIPY-KEFAEKYPGEIIYVSE----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 468 tgsiyDNIHygNEQASEEEVIRAAKAAHVDDFVRKlpegyqtilneeasnISQGQRQLITIARAFLANPDVLILDEATSS 547
Cdd:cd03233 91 -----EDVH--FPTLTVRETLDFALRCKGNEFVRG---------------ISGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488288408 548 VDTRTEILIQAAMnRLL---ENRTSFVVAHRLS-TIRDA-DTIIVMAEGSIV 594
Cdd:cd03233 149 LDSSTALEILKCI-RTMadvLKTTTFVSLYQASdEIYDLfDKVLVLYEGRQI 199
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
390-604 |
3.55e-13 |
|
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: 72.14 E-value: 3.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 390 YSPEKLLMK---DFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKY-------DGVDTRDLSREELRAHFSM 459
Cdd:TIGR03269 290 ISVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvDMTKPGPDGRGRAKRYIGI 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 460 VLQDTWLFT-GSIYDNI--HYGNEQASEEEVIRAA---KAAHVDDfvrklpEGYQTILNEEASNISQGQRQLITIARAFL 533
Cdd:TIGR03269 370 LHQEYDLYPhRTVLDNLteAIGLELPDELARMKAVitlKMVGFDE------EKAEEILDKYPDELSEGERHRVALAQVLI 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488288408 534 ANPDVLILDEATSSVDTRTEILIQAAMNRLLE--NRTSFVVAHRLSTIRD-ADTIIVMAEGSIVETGTHDELMA 604
Cdd:TIGR03269 444 KEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
393-565 |
4.79e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 68.36 E-value: 4.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 393 EKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREElRAHF---------SMVLQD 463
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAE-ACHYlghrnamkpALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 464 TWLFTGSIydnihYGNEQASEEEVIRAAKAAHVDDfvrkLPEGYqtilneeasnISQGQRQLITIARAFLANPDVLILDE 543
Cdd:PRK13539 93 NLEFWAAF-----LGGEELDIAAALEAVGLAPLAH----LPFGY----------LSAGQKRRVALARLLVSNRPIWILDE 153
|
170 180
....*....|....*....|..
gi 488288408 544 ATSSVDTRTEILIQAAMNRLLE 565
Cdd:PRK13539 154 PTAALDAAAVALFAELIRAHLA 175
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
381-591 |
4.89e-13 |
|
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: 66.70 E-value: 4.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYSpEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLerfydisSGSIKYDgvdtrdlsreelrahfsmv 460
Cdd:cd03221 1 IELENLSKTYG-GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLI-------AGELEPD------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 461 lqdtwlfTGSIydnihygneqaseeEVIRAAKAAHVDDFvrklpegyqtilneeasniSQGQRQLITIARAFLANPDVLI 540
Cdd:cd03221 54 -------EGIV--------------TWGSTVKIGYFEQL-------------------SGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488288408 541 LDEATSSVDTRT-EILIQAamnrLLE-NRTSFVVAH-R--LSTIrdADTIIVMAEG 591
Cdd:cd03221 94 LDEPTNHLDLESiEALEEA----LKEyPGTVILVSHdRyfLDQV--ATKIIELEDG 143
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
381-598 |
6.36e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 69.39 E-value: 6.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGY---SP-EKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSR----EE 452
Cdd:PRK13649 3 INLQNVSYTYqagTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 453 LRAHFSMVLQ--DTWLFTGSIYDNIHYG--NEQASEEEVIRAA--KAAHV---DDFVRKLPegyqtilneeaSNISQGQR 523
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGpqNFGVSQEEAEALAreKLALVgisESLFEKNP-----------FELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 524 QLITIARAFLANPDVLILDEATSSVDT--RTEI------LIQAAMnrllenrTSFVVAHRLSTIRD-ADTIIVMAEGSIV 594
Cdd:PRK13649 152 RRVAIAGILAMEPKILVLDEPTAGLDPkgRKELmtlfkkLHQSGM-------TIVLVTHLMDDVANyADFVYVLEKGKLV 224
|
....
gi 488288408 595 ETGT 598
Cdd:PRK13649 225 LSGK 228
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
397-597 |
9.73e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 68.76 E-value: 9.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 397 MKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMVLQDTWLFTGSIYDNIH 476
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVDWSFPVLVEDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 477 YGneQASEEEVIRAAKA---AHVDDFVRKLpeGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTE 553
Cdd:PRK15056 103 MG--RYGHMGWLRRAKKrdrQIVTAALARV--DMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488288408 554 ILIQAAMNRLL-ENRTSFVVAHRLSTIRDADTIIVMAEGSIVETG 597
Cdd:PRK15056 179 ARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
390-602 |
1.02e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 68.68 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 390 YSPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMVLQ--DTWLF 467
Cdd:PRK13652 13 YSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQnpDDQIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 468 TGSIYDNIHYG--NEQASEEEViraakAAHVDDFVRKLpeGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEAT 545
Cdd:PRK13652 93 SPTVEQDIAFGpiNLGLDEETV-----AHRVSSALHML--GLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 546 SSVDTRTEILIQAAMNRLLENRTSFVV--AHRLSTIRD-ADTIIVMAEGSIVETGTHDEL 602
Cdd:PRK13652 166 AGLDPQGVKELIDFLNDLPETYGMTVIfsTHQLDLVPEmADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
96-355 |
1.10e-12 |
|
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: 69.01 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 96 IDFDKIGQILLIVIAM---YLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRaINDMDNI 172
Cdd:cd18571 33 INNKDLNFIYLILIAQlvlFLGSTSIEFIRSWILLHISSRINISIISDFLIKLMRLPISFFDTKMTGDILQR-INDHSRI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 173 ASTLQQNLTQLITSIVTFVGVLWMMLTISWQLTLIALATVPLSLIVVMVVAPR----SQKHFAAQQKSlgllNNQVEETY 248
Cdd:cd18571 112 ESFLTSSSLSILFSLLNLIVFSIVLAYYNLTIFLIFLIGSVLYILWILLFLKKrkklDYKRFDLSSEN----QSKLIELI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 249 GGHVVVKSFNHEESDQEVFEKENEKLYHAGRKA----QFISAIIMpLMNFIKNLGYVFVAVLGgvkVANGMMDLGDVQAf 324
Cdd:cd18571 188 NGMQEIKLNNSERQKRWEWERIQAKLFKINIKSlkldQYQQIGAL-FINQLKNILITFLAAKL---VIDGEITLGMMLA- 262
|
250 260 270
....*....|....*....|....*....|..
gi 488288408 325 LQY-TNQFSQPITQIANLMNTIQATVASAERV 355
Cdd:cd18571 263 IQYiIGQLNSPIEQLIGFIQSLQDAKISLERL 294
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
378-601 |
1.28e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 71.29 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 378 PYRVSFEHV-AFGYSPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLL----ERFYDISSGSIKYDGVDTRDLSRE- 451
Cdd:TIGR00956 57 ILTRGFRKLkKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEIKKHy 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 452 --------ELRAHF-SMVLQDTWLFT------GSIYDNIhygneqaSEEEviRAAKAAHVDDFVRKLPEGYQTIL-NEEA 515
Cdd:TIGR00956 137 rgdvvynaETDVHFpHLTVGETLDFAarcktpQNRPDGV-------SREE--YAKHIADVYMATYGLSHTRNTKVgNDFV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 516 SNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEI-LIQA--AMNRLLENrTSFVVAHRLStiRDA----DTIIVM 588
Cdd:TIGR00956 208 RGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALeFIRAlkTSANILDT-TPLVAIYQCS--QDAyelfDKVIVL 284
|
250
....*....|...
gi 488288408 589 AEGSIVETGTHDE 601
Cdd:TIGR00956 285 YEGYQIYFGPADK 297
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
399-588 |
1.49e-12 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 66.49 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 399 DFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIkydgvdtrdlsREELRAHFSMVLQDT---WLFTGSIYDNI 475
Cdd:NF040873 10 GVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQRSevpDSLPLTVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 476 HYG--NEQASEEEVIRAAKAAhVDDFVRKLpeGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTE 553
Cdd:NF040873 79 AMGrwARRGLWRRLTRDDRAA-VDDALERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESR 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 488288408 554 ILIQAAMNRLL-ENRTSFVVAHRLSTIRDADTIIVM 588
Cdd:NF040873 156 ERIIALLAEEHaRGATVVVVTHDLELVRRADPCVLL 191
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
397-592 |
1.92e-12 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 67.07 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 397 MKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTR-DLSreelrahfsmvlqdtwlftgsiydni 475
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWvDLA-------------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 476 hygneQASEEEVI--RAAKAAHVDDFVRKLPEgyQTILN-------------EEAS----------NI------------ 518
Cdd:COG4778 81 -----QASPREILalRRRTIGYVSQFLRVIPR--VSALDvvaepllergvdrEEARararellarlNLperlwdlppatf 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488288408 519 SQGQRQLITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLLENRTSFV-VAHRLSTiRD--ADTIIVMAEGS 592
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEV-REavADRVVDVTPFS 229
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
393-593 |
1.99e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 67.78 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 393 EKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIkYDGVDTRDLSREELRahfsMVLQDTWLFT-GSI 471
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEAREDTR----LMFQDARLLPwKKV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 472 YDNIHYGNEQASEEEVIRAAKAAHVDDfvRKlpegyqtilNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTR 551
Cdd:PRK11247 99 IDNVGLGLKGQWRDAALQALAAVGLAD--RA---------NEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488288408 552 TEILIQAAMNRLLENR--TSFVVAHRLS-TIRDADTIIVMAEGSI 593
Cdd:PRK11247 168 TRIEMQDLIESLWQQHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
397-602 |
3.06e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.31 E-value: 3.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 397 MKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSreELRAH---FSMVLQDTWLFTG-SIY 472
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT--PAKAHqlgIYLVPQEPLLFPNlSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 473 DNIHYG--NEQASEEEVirAAKAAHVddfvrklpeGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVD- 549
Cdd:PRK15439 105 ENILFGlpKRQASMQKM--KQLLAAL---------GCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTp 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488288408 550 TRTEILIQaAMNRLLENRTSFV-VAHRLSTIRD-ADTIIVMAEGSIVETGTHDEL 602
Cdd:PRK15439 174 AETERLFS-RIRELLAQGVGIVfISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
398-607 |
3.76e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 67.44 E-value: 3.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 398 KDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDG--VDTRDLSR-----EE--LRAhfSMVLQDTWLFT 468
Cdd:COG4152 18 DDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGepLDPEDRRRigylpEErgLYP--KMKVGEQLVYL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 469 GSIYDnihygneqASEEEVIRAAK--------AAHVDDFVRKLpegyqtilneeasniSQGQRQLITIARAFLANPDVLI 540
Cdd:COG4152 96 ARLKG--------LSKAEAKRRADewlerlglGDRANKKVEEL---------------SKGNQQKVQLIAALLHDPELLI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488288408 541 LDEATS-----SVDT-RTEILIQAAmnrllENRTSFVVAHRLSTI-RDADTIIVMAEGSIVETGTHDELMAKNG 607
Cdd:COG4152 153 LDEPFSgldpvNVELlKDVIRELAA-----KGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEIRRQFG 221
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
384-604 |
5.61e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.07 E-value: 5.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 384 EHVAFGYSPEKLLmKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLS-REELRAHFSMVLQ 462
Cdd:PRK10895 7 KNLAKAYKGRRVV-EDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 463 DTWLFTG-SIYDNIhygneqASEEEVIRAAKAAHVDDFVRKLPEGYQT--ILNEEASNISQGQRQLITIARAFLANPDVL 539
Cdd:PRK10895 86 EASIFRRlSVYDNL------MAVLQIRDDLSAEQREDRANELMEEFHIehLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488288408 540 ILDEATSSVDTRTEILIQAAMNRLLENRTSFVVA-HRL-STIRDADTIIVMAEGSIVETGTHDELMA 604
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVrETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
400-605 |
5.86e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 67.24 E-value: 5.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 400 FNLNVKPGEMVAIVGPTGAGKT----TLINLLERFYDISSGSIKYDGVDTRDLSREELRA----HFSMVLQD-------- 463
Cdd:COG4170 26 VSLTLNEGEIRGLVGESGSGKSliakAICGITKDNWHVTADRFRWNGIDLLKLSPRERRKiigrEIAMIFQEpsscldps 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 464 ------------TWLFTGSIYDNIHYGNEQASEE--EV-IRaakaahvddfvrklpeGYQTILNEEASNISQGQRQLITI 528
Cdd:COG4170 106 akigdqlieaipSWTFKGKWWQRFKWRKKRAIELlhRVgIK----------------DHKDIMNSYPHELTEGECQKVMI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 529 ARAFLANPDVLILDEATSSVD--TRTEIL-IQAAMNRLlENRTSFVVAHRLSTI-RDADTIIVMAEGSIVETGTHDELMA 604
Cdd:COG4170 170 AMAIANQPRLLIADEPTNAMEstTQAQIFrLLARLNQL-QGTSILLISHDLESIsQWADTITVLYCGQTVESGPTEQILK 248
|
.
gi 488288408 605 K 605
Cdd:COG4170 249 S 249
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
399-609 |
5.94e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 67.06 E-value: 5.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 399 DFNLNVKPGEMVAIVGPTGAGKT----TLINLLERFYDIsSGSIKYDGVDTRDLSREEL---RA-HFSMVLQD--TWLft 468
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRI-GGSATFNGREILNLPEKELnklRAeQISMIFQDpmTSL-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 469 gSIYDNI------------HYGNEQASEEEViRAAKAAhvddfvrKLPEGYQTIlNEEASNISQGQRQLITIARAFLANP 536
Cdd:PRK09473 111 -NPYMRVgeqlmevlmlhkGMSKAEAFEESV-RMLDAV-------KMPEARKRM-KMYPHEFSGGMRQRVMIAMALLCRP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488288408 537 DVLILDEATSSVDTRTEILIQAAMNRLLE--NRTSFVVAHRLSTIRD-ADTIIVMAEGSIVETGThdelmAKNGFY 609
Cdd:PRK09473 181 KLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGN-----ARDVFY 251
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
385-545 |
6.09e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.17 E-value: 6.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 385 HVAFGyspEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGvdtrdlsreelRAHFSMVLQDT 464
Cdd:COG0488 5 SKSFG---GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 465 WLFTG-SIYDNIHYGNEQASE-EEVIRAA--KAAHVDDFVRKLPE---------GYQ------TIL----------NEEA 515
Cdd:COG0488 71 PLDDDlTVLDTVLDGDAELRAlEAELEELeaKLAEPDEDLERLAElqeefealgGWEaearaeEILsglgfpeedlDRPV 150
|
170 180 190
....*....|....*....|....*....|
gi 488288408 516 SNISQGQRQLITIARAFLANPDVLILDEAT 545
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPT 180
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
398-605 |
6.85e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 67.18 E-value: 6.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 398 KDFNLNVKPGEMVAIVGPTGAGKTTLINL---LERfydISSGSIKYDG--VDT-----RDLsreelrahfSMVLQDTWLF 467
Cdd:PRK11650 21 KGIDLDVADGEFIVLVGPSGCGKSTLLRMvagLER---ITSGEIWIGGrvVNElepadRDI---------AMVFQNYALY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 468 TG-SIYDNIHYG--NEQASEEE----VIRAAKAAHVDDFVRKLPegyqtilneeaSNISQGQRQLITIARAFLANPDVLI 540
Cdd:PRK11650 89 PHmSVRENMAYGlkIRGMPKAEieerVAEAARILELEPLLDRKP-----------RELSGGQRQRVAMGRAIVREPAVFL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488288408 541 LDEATSSVDT------RTEilIQAAMNRLleNRTSFVVAH-RLSTIRDADTIIVMAEGSIVETGTHDELMAK 605
Cdd:PRK11650 158 FDEPLSNLDAklrvqmRLE--IQRLHRRL--KTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVEVYEK 225
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
104-355 |
1.01e-11 |
|
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: 66.07 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 104 ILLIVIAmYLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRaINDMDniasTLQQNLT-Q 182
Cdd:cd18566 45 VIGVVIA-ILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLER-LNSLE----QIREFLTgQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 183 LITSI------VTFVGVLWMmltISWQLTLIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKS 256
Cdd:cd18566 119 ALLALldlpfvLIFLGLIWY---LGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 257 FNHEESDQEVFEKENEKLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPIT 336
Cdd:cd18566 196 MAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLVINGDLTVGALIACTMLSGRVLQPLQ 275
|
250
....*....|....*....
gi 488288408 337 QIANLMNTIQATVASAERV 355
Cdd:cd18566 276 RAFGLWTRFQQVRVAVRRL 294
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
384-603 |
1.17e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 65.10 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 384 EHVAFGYSPEKLLmKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVD-----TRDLSREE--LRA- 455
Cdd:COG4604 5 KNVSKRYGGKVVL-DDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDvattpSRELAKRLaiLRQe 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 456 -HFSMVLqdtwlftgSIYDNI-------HYGNEQASEEEVIRAAKAA-HVDDFVRKLpegyqtiLNEeasnISQGQRQli 526
Cdd:COG4604 84 nHINSRL--------TVRELVafgrfpySKGRLTAEDREIIDEAIAYlDLEDLADRY-------LDE----LSGGQRQ-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 527 tiaRAFLA-----NPDVLILDEATSSVDTRTEILIQAAMNRLLE--NRTSFVVAHrlstirD-------ADTIIVMAEGS 592
Cdd:COG4604 143 ---RAFIAmvlaqDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADelGKTVVIVLH------DinfascyADHIVAMKDGR 213
|
250
....*....|.
gi 488288408 593 IVETGTHDELM 603
Cdd:COG4604 214 VVAQGTPEEII 224
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
383-604 |
1.40e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 65.80 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 383 FEHVAFGYSP----EKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSG-SIKYDGVDTRDLSR----EEL 453
Cdd:PRK13645 9 LDNVSYTYAKktpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqTIVGDYAIPANLKKikevKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 454 RAHFSMVLQ--DTWLFTGSIYDNIHYG--NEQASEEEVIRaaKAAHVDDFVrKLPEGYqtiLNEEASNISQGQRQLITIA 529
Cdd:PRK13645 89 RKEIGLVFQfpEYQLFQETIEKDIAFGpvNLGENKQEAYK--KVPELLKLV-QLPEDY---VKRSPFELSGGQKRRVALA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488288408 530 RAFLANPDVLILDEATSSVDTRTEILIQAAMNRLLEN--RTSFVVAHRLSTI-RDADTIIVMAEGSIVETGTHDELMA 604
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
406-594 |
1.53e-11 |
|
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: 62.78 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 406 PGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKY-DGVDTRDLSREELRahfsmvlqdtwlftgsiydnihygneqase 484
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYiDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 485 eeviraakaahvddfvrklpegyQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEILIQAA----- 559
Cdd:smart00382 51 -----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrl 107
|
170 180 190
....*....|....*....|....*....|....*.
gi 488288408 560 -MNRLLENRTSFVVAHRLSTIRDADTIIVMAEGSIV 594
Cdd:smart00382 108 lLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIV 143
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
397-608 |
1.62e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 65.49 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 397 MKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSR------------------------EE 452
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKtkekekvleklviqktrfkkikkiKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 453 LRAHFSMVLQ--DTWLFTGSIYDNIHYG-------NEQASEeeviRAAKAAHVDDfvrkLPEGYqtiLNEEASNISQGQR 523
Cdd:PRK13651 103 IRRRVGVVFQfaEYQLFEQTIEKDIIFGpvsmgvsKEEAKK----RAAKYIELVG----LDESY---LQRSPFELSGGQK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 524 QLITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRL-LENRTSFVVAHRL-STIRDADTIIVMAEGSIVETGTHDE 601
Cdd:PRK13651 172 RRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLdNVLEWTKRTIFFKDGKIIKDGDTYD 251
|
....*..
gi 488288408 602 LMAKNGF 608
Cdd:PRK13651 252 ILSDNKF 258
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
394-605 |
2.77e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 66.36 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 394 KLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERF--YDISSGSIKY----------------DG------------- 442
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYhvalcekcgyverpskVGepcpvcggtlepe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 443 -VDTRDLS---REELRAHFSMVLQDTWLFTG--SIYDNIHYGNEQASEEEVIRAAKAAHVDDFVrKLPEGYQTIlneeAS 516
Cdd:TIGR03269 93 eVDFWNLSdklRRRIRKRIAIMLQRTFALYGddTVLDNVLEALEEIGYEGKEAVGRAVDLIEMV-QLSHRITHI----AR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 517 NISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLL--ENRTSFVVAHRLSTIRD-ADTIIVMAEGSI 593
Cdd:TIGR03269 168 DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWPEVIEDlSDKAIWLENGEI 247
|
250
....*....|..
gi 488288408 594 VETGTHDELMAK 605
Cdd:TIGR03269 248 KEEGTPDEVVAV 259
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
381-604 |
2.93e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 64.83 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYSpEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREElRAHFSMV 460
Cdd:PRK13537 8 IDFRNVEKRYG-DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 461 LQdtwlftgsiYDNIhygNEQASEEEVIR------AAKAAHVDDFVRKLPEGYQTILNEEA--SNISQGQRQLITIARAF 532
Cdd:PRK13537 86 PQ---------FDNL---DPDFTVRENLLvfgryfGLSAAAARALVPPLLEFAKLENKADAkvGELSGGMKRRLTLARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488288408 533 LANPDVLILDEATSSVDTRTEILIQAAMNRLL-ENRTSFVVAHRLSTI-RDADTIIVMAEGSIVETGTHDELMA 604
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
392-594 |
3.36e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 65.97 E-value: 3.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 392 PEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTL-INLLERFY--DISsGSIKYDG--VDTRDLSR---------EELRAHF 457
Cdd:NF040905 271 PERKVVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYgrNIS-GTVFKDGkeVDVSTVSDaidaglayvTEDRKGY 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 458 SMVLQDTwlftgsIYDNIHYGNEQaseeeviRAAKAAHVDDFV-RKLPEGYQTILN-------EEASNISQGQRQLITIA 529
Cdd:NF040905 350 GLNLIDD------IKRNITLANLG-------KVSRRGVIDENEeIKVAEEYRKKMNiktpsvfQKVGNLSGGNQQKVVLS 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 530 RAFLANPDVLILDEATSSVDTRTEILIQAAMNRLLENRTSFVVahrLST-----IRDADTIIVMAEGSIV 594
Cdd:NF040905 417 KWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIV---ISSelpelLGMCDRIYVMNEGRIT 483
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
359-587 |
3.81e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.99 E-value: 3.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 359 LDEEEMVDEPSGIPVETDSPYRVSFEHVAFGYSPEKLLMKDFNLNVKPG-----EMVAIVGPTGAGKTTLINLLerfydi 433
Cdd:PRK13409 312 LPEENMRIRPEPIEFEERPPRDESERETLVEYPDLTKKLGDFSLEVEGGeiyegEVIGIVGPNGIGKTTFAKLL------ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 434 sSGSIKYDG--VDTR-DLSR--EELRAHFSMVLQDTWLFTGSIYDNIHYgneqasEEEVIRaakaahvddfvrklPEGYQ 508
Cdd:PRK13409 386 -AGVLKPDEgeVDPElKISYkpQYIKPDYDGTVEDLLRSITDDLGSSYY------KSEIIK--------------PLQLE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 509 TILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLLENR--TSFVVAHRLSTIrD--ADT 584
Cdd:PRK13409 445 RLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEReaTALVVDHDIYMI-DyiSDR 523
|
...
gi 488288408 585 IIV 587
Cdd:PRK13409 524 LMV 526
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
400-613 |
4.62e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 66.19 E-value: 4.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 400 FNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTrDLSREELRAHFSMVLQDTWLFTG-SIYDNI-HY 477
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAEHIlFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 478 GNEQASEEEVIRAAKAAHVDDfvrklpEGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEILIQ 557
Cdd:TIGR01257 1028 AQLKGRSWEEAQLEMEAMLED------TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488288408 558 AAMNRLLENRTSFVVAHRLSTIRD-ADTIIVMAEGSIVETGThdELMAKNGFYADLY 613
Cdd:TIGR01257 1102 DLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGT--PLFLKNCFGTGFY 1156
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
401-596 |
4.74e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 65.34 E-value: 4.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 401 NLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISS--GSIKYDGVDTRDLS-REELRAHFSMVLQDTWLFTG-SIYDNIH 476
Cdd:PRK13549 25 SLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNiRDTERAGIAIIHQELALVKElSVLENIF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 477 YGNEqaseeevIRAAKAAHVDDFVRKlpegYQTILNE---------EASNISQGQRQLITIARAFLANPDVLILDEATSS 547
Cdd:PRK13549 105 LGNE-------ITPGGIMDYDAMYLR----AQKLLAQlkldinpatPVGNLGLGQQQLVEIAKALNKQARLLILDEPTAS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488288408 548 VdTRTEILIQAAMNRLLENR--TSFVVAHRLSTIRD-ADTIIVMAEGSIVET 596
Cdd:PRK13549 174 L-TESETAVLLDIIRDLKAHgiACIYISHKLNEVKAiSDTICVIRDGRHIGT 224
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
404-602 |
4.92e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 64.38 E-value: 4.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 404 VKPGEMVAIVGPTGAGKT----TLINLLERFYDISSGSIKYDGVDTRDLSREELR----AHFSMVLQDTWLFTGSIYD-- 473
Cdd:PRK11022 30 VKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRnlvgAEVAMIFQDPMTSLNPCYTvg 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 474 -------NIHYG-NEQASEEEVIRAAKAAHVDDfvrklPEgyqTILNEEASNISQGQRQLITIARAFLANPDVLILDEAT 545
Cdd:PRK11022 110 fqimeaiKVHQGgNKKTRRQRAIDLLNQVGIPD-----PA---SRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPT 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488288408 546 SSVDtrteILIQAAMNRLL------ENRTSFVVAHRLSTIRD-ADTIIVMAEGSIVETGTHDEL 602
Cdd:PRK11022 182 TALD----VTIQAQIIELLlelqqkENMALVLITHDLALVAEaAHKIIVMYAGQVVETGKAHDI 241
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
106-357 |
5.09e-11 |
|
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: 64.06 E-value: 5.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 106 LIVIAMYLI--SAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQQNLTQL 183
Cdd:cd18580 41 LGVYAALLVlaSVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 184 ITSIVTFVGVLWMMLTISWQLtliALATVPLSLIVVMVvaprsQKHF--AAQQ-KSLGL-----LNNQVEETYGGHVVVK 255
Cdd:cd18580 121 LQSLFSVLGSLIVIAIVSPYF---LIVLPPLLVVYYLL-----QRYYlrTSRQlRRLESesrspLYSHFSETLSGLSTIR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 256 SFNHeesdQEVFEKENEKLYHAGRKAQFIS-------AIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAfLQYT 328
Cdd:cd18580 193 AFGW----QERFIEENLRLLDASQRAFYLLlavqrwlGLRLDLLGALLALVVALLAVLLRSSISAGLVGLALTYA-LSLT 267
|
250 260
....*....|....*....|....*....
gi 488288408 329 NQFSQPITQIANLMNTIqatvASAERVFE 357
Cdd:cd18580 268 GSLQWLVRQWTELETSM----VSVERILE 292
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
381-604 |
5.60e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 62.97 E-value: 5.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYSPEKLLmKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREE-LRAHFSM 459
Cdd:PRK11614 6 LSFDKVSAHYGKIQAL-HEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 460 VLQDTWLFTG-SIYDNIHYGNEQASEEEVIRaaKAAHVDDFVRKLPEGYQtilnEEASNISQGQRQLITIARAFLANPDV 538
Cdd:PRK11614 85 VPEGRRVFSRmTVEENLAMGGFFAERDQFQE--RIKWVYELFPRLHERRI----QRAGTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488288408 539 LILDEATSSVdtrTEILIQAAMNRLLENR----TSFVVAHRLS-TIRDADTIIVMAEGSIVETGTHDELMA 604
Cdd:PRK11614 159 LLLDEPSLGL---APIIIQQIFDTIEQLReqgmTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLA 226
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
106-355 |
5.73e-11 |
|
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: 63.69 E-value: 5.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 106 LIVIAMYLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRaINDMDNIASTLQQNL--TQL 183
Cdd:cd18783 46 IGVVIALLFEGILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAGVLTKH-MQQIERIRQFLTGQLfgTLL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 184 -ITSIVTFVGVLWMMltiSWQLTLIALA-TVPLSLIVVMVVAP---RSQKHFAAQQKSLGLLnnqvEETYGGHVVVKSFN 258
Cdd:cd18783 125 dATSLLVFLPVLFFY---SPTLALVVLAfSALIALIILAFLPPfrrRLQALYRAEGERQAFL----VETVHGIRTVKSLA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 259 HE-----ESDQEVFEKENEKLyHAGRKAQFISAIIMPLMNFIkNLGYVFVAVLGgvkVANGMMDLGDVQAFLQYTNQFSQ 333
Cdd:cd18783 198 LEprqrrEWDERVARAIRARF-AVGRLSNWPQTLTGPLEKLM-TVGVIWVGAYL---VFAGSLTVGALIAFNMLAGRVAG 272
|
250 260
....*....|....*....|..
gi 488288408 334 PITQIANLMNTIQATVASAERV 355
Cdd:cd18783 273 PLVQLAGLVQEYQEARLSVRML 294
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
399-604 |
5.75e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.32 E-value: 5.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 399 DFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLS-REELRAHFSMVLQDTWLFTG-SIYDNIH 476
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAStTAALAAGVAIIYQELHLVPEmTVAENLY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 477 YGNEQASEEEVIRAAKAAHVDDFVRKLpeGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTR-TEIL 555
Cdd:PRK11288 102 LGQLPHKGGIVNRRLLNYEAREQLEHL--GVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAReIEQL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488288408 556 IqAAMNRL-LENRTSFVVAHRLSTI-RDADTIIVMAEGSIVETG------THDELMA 604
Cdd:PRK11288 180 F-RVIRELrAEGRVILYVSHRMEEIfALCDAITVFKDGRYVATFddmaqvDRDQLVQ 235
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
402-591 |
7.19e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.02 E-value: 7.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 402 LNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTR-DLSREELRAHFSMVLQDTWLFTG-SIYDNIHYGN 479
Cdd:PRK10762 25 LNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEAGIGIIHQELNLIPQlTIAENIFLGR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 480 EQASEEEVIRAAKA-AHVDDFVRKL--PEGYQTILNEeasnISQGQRQLITIARAFLANPDVLILDEATSSV-DTRTEIL 555
Cdd:PRK10762 105 EFVNRFGRIDWKKMyAEADKLLARLnlRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESL 180
|
170 180 190
....*....|....*....|....*....|....*...
gi 488288408 556 IQaAMNRLLENRTSFV-VAHRLSTIRD-ADTIIVMAEG 591
Cdd:PRK10762 181 FR-VIRELKSQGRGIVyISHRLKEIFEiCDDVTVFRDG 217
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
401-596 |
7.54e-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: 64.85 E-value: 7.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 401 NLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISS--GSIKYDGVDTRDLS-REELRAHFSMVLQDTWLFTG-SIYDNIH 476
Cdd:TIGR02633 21 DLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNiRDTERAGIVIIHQELTLVPElSVAENIF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 477 YGNeqaseeEVIRAAKAAHVDDFVRKLPEGYQTiLNEEASNISQ-------GQRQLITIARAFLANPDVLILDEATSSV- 548
Cdd:TIGR02633 101 LGN------EITLPGGRMAYNAMYLRAKNLLRE-LQLDADNVTRpvgdyggGQQQLVEIAKALNKQARLLILDEPSSSLt 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488288408 549 DTRTEILIQAAMNRLLENRTSFVVAHRLSTIRD-ADTIIVMAEGSIVET 596
Cdd:TIGR02633 174 EKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQHVAT 222
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
406-597 |
7.69e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 64.88 E-value: 7.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 406 PGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDG--VDTRDLSR-EELRAHFSMVLQDTW------LFTG-SIYDNI 475
Cdd:PRK10261 349 PGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqrIDTLSPGKlQALRRDIQFIFQDPYasldprQTVGdSIMEPL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 476 HYGNEQASEEEvirAAKAAHVDDFVRKLPEGYQTILNEeasnISQGQRQLITIARAFLANPDVLILDEATSSVDT--RTE 553
Cdd:PRK10261 429 RVHGLLPGKAA---AARVAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEAVSALDVsiRGQ 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488288408 554 ILiqaamNRLLENRTSFVVA-----HRLSTI-RDADTIIVMAEGSIVETG 597
Cdd:PRK10261 502 II-----NLLLDLQRDFGIAylfisHDMAVVeRISHRVAVMYLGQIVEIG 546
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
393-550 |
1.23e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 61.36 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 393 EKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLsREELRahfsmvlQDTwLFTG--- 469
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQ-RDEYH-------QDL-LYLGhqp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 470 ------SIYDNIHY---GNEQASEEEVIRAAKAAHVDDFVRkLPegyqtilneeASNISQGQRQLITIARAFLANPDVLI 540
Cdd:PRK13538 84 giktelTALENLRFyqrLHGPGDDEALWEALAQVGLAGFED-VP----------VRQLSAGQQRRVALARLWLTRAPLWI 152
|
170
....*....|
gi 488288408 541 LDEATSSVDT 550
Cdd:PRK13538 153 LDEPFTAIDK 162
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
401-596 |
1.60e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.60 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 401 NLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTR-DLSREELRAHFSMVLQDTWLFTG-SIYDNIHYG 478
Cdd:PRK10982 18 NLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELNLVLQrSVMDNMWLG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 479 NeqaseeeviRAAKAAHVDDfvRKLPEGYQTILNE---------EASNISQGQRQLITIARAFLANPDVLILDEATSSVd 549
Cdd:PRK10982 98 R---------YPTKGMFVDQ--DKMYRDTKAIFDEldididpraKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL- 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488288408 550 TRTEILIQAAMNRLLENRTSFVV--AHRLSTIRD-ADTIIVMAEGSIVET 596
Cdd:PRK10982 166 TEKEVNHLFTIIRKLKERGCGIVyiSHKMEEIFQlCDEITILRDGQWIAT 215
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
359-587 |
1.83e-10 |
|
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: 63.65 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 359 LDEEEMVDEPSGIPVETDSPYRVSFEHVAFGYSPEKLLMKDFNLNVKPGEM-----VAIVGPTGAGKTTLINLLERFYDI 433
Cdd:COG1245 313 LPEENVRIRDEPIEFEVHAPRREKEEETLVEYPDLTKSYGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 434 SSGSIK----------YDGVDTRDLSREELRAHFSMVLQDTWLftgsiydnihygneqasEEEVIRaakaahvddfvrkl 503
Cdd:COG1245 393 DEGEVDedlkisykpqYISPDYDGTVEEFLRSANTDDFGSSYY-----------------KTEIIK-------------- 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 504 PEGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLLENR--TSFVVAHRLSTIrD 581
Cdd:COG1245 442 PLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDHDIYLI-D 520
|
....*...
gi 488288408 582 --ADTIIV 587
Cdd:COG1245 521 yiSDRLMV 528
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
388-605 |
1.88e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 61.95 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 388 FGYSPEKLLmKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGvDTRDLSRE---ELRAHFSMVLQD- 463
Cdd:PRK13638 9 FRYQDEPVL-KGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQG-KPLDYSKRgllALRQQVATVFQDp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 464 -TWLFTGSIYDNIHYG--NEQASEEEVIRaakaaHVDDFVRKLPEgyQTILNEEASNISQGQRQLITIARAFLANPDVLI 540
Cdd:PRK13638 87 eQQIFYTDIDSDIAFSlrNLGVPEAEITR-----RVDEALTLVDA--QHFRHQPIQCLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488288408 541 LDEATSSVDTRTEILIQAAMNRLLENRTSFVV-AHRLSTIRD-ADTIIVMAEGSIVETGTHDELMAK 605
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFAC 226
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
399-597 |
2.04e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 62.58 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 399 DFNLNVK---PGEMV-AIVGPTGAGKTTLINLLERFYDISSGSIKYDG---VDTRD---LSREELRAHFsmVLQDTWLFT 468
Cdd:PRK11144 12 DLCLTVNltlPAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKgicLPPEKRRIGY--VFQDARLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 469 G-SIYDNIHYGneqaseeevIRAAKAAHVDDFVRKLpeGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSS 547
Cdd:PRK11144 90 HyKVRGNLRYG---------MAKSMVAQFDKIVALL--GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLAS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488288408 548 VDT--RTEILiqAAMNRLLE--NRTSFVVAHRLSTI-RDADTIIVMAEGSIVETG 597
Cdd:PRK11144 159 LDLprKRELL--PYLERLAReiNIPILYVSHSLDEIlRLADRVVVLEQGKVKAFG 211
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
402-552 |
2.62e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 60.95 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 402 LNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSRE---ELRA-HFSMVLQDTWLF-TGSIYDNIH 476
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRAkHVGFVFQSFMLIpTLNALENVE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 477 Y------GNEQASEEEVIRAAKAAHVDDFVRKLPegyqtilneeaSNISQGQRQLITIARAFLANPDVLILDEATSSVDT 550
Cdd:PRK10584 111 LpallrgESSRQSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
|
..
gi 488288408 551 RT 552
Cdd:PRK10584 180 QT 181
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
393-599 |
3.00e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.96 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 393 EKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLL--ERFYDISSGSIKYDGVDTRDLSREElRAHFSMVLQDTW----- 465
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPED-RAGEGIFMAFQYpveip 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 466 -----LFTGSIYDNIHYGNEQaseEEVIRAAKAAHVDDFVR--KLPEGYQTilneEASNI--SQGQRQLITIARAFLANP 536
Cdd:PRK09580 92 gvsnqFFLQTALNAVRSYRGQ---EPLDRFDFQDLMEEKIAllKMPEDLLT----RSVNVgfSGGEKKRNDILQMAVLEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488288408 537 DVLILDEATSSVDTRTEILIQAAMNRLLENRTSFVVAHRLSTIRD---ADTIIVMAEGSIVETGTH 599
Cdd:PRK09580 165 ELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDyikPDYVHVLYQGRIVKSGDF 230
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
381-563 |
3.16e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.90 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYSPEKLLmKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDgvdtrdlsrEELRAHF--- 457
Cdd:PRK09544 5 VSLENVSVSFGQRRVL-SDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN---------GKLRIGYvpq 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 458 SMVLQDTWLFTGSIYDNIHYGNEQASEEEVIRAAKAAHvddfvrklpegyqtILNEEASNISQGQRQLITIARAFLANPD 537
Cdd:PRK09544 75 KLYLDTTLPLTVNRFLRLRPGTKKEDILPALKRVQAGH--------------LIDAPMQKLSGGETQRVLLARALLNRPQ 140
|
170 180
....*....|....*....|....*.
gi 488288408 538 VLILDEATSSVDTRTEILIQAAMNRL 563
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALYDLIDQL 166
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
105-243 |
3.17e-10 |
|
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: 61.66 E-value: 3.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 105 LLIVIAMYLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQQNLTQLI 184
Cdd:cd18584 40 LLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARLLALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLV 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488288408 185 TSIVTFVGVLWMMLTISWQLTLIALATVPLsLIVVMVV-----APRSQKHFAAqqksLGLLNNQ 243
Cdd:cd18584 120 LAAIVPLLILVAVFPLDWVSALILLVTAPL-IPLFMILigkaaQAASRRQWAA----LSRLSGH 178
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
155-317 |
3.19e-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: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 155 THSNGDIMSRAINDMDNIastlqQNL-----TQLITSIVTFVGVLWMMLTISWQLTLIALATVPLSLIVVMVVAPRSQKH 229
Cdd:cd18585 88 KYRSGDLLNRIVADIDTL-----DNLylrvlSPPVVALLVILATILFLAFFSPALALILLAGLLLAGVVIPLLFYRLGKK 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 230 FAAQQKSL-GLLNNQVEETYGGHVVVKSFNHEESDQEVFEKENEKLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGG 308
Cdd:cd18585 163 IGQQLVQLrAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGLSQALMILLSGLTVWLVLWLGA 242
|
....*....
gi 488288408 309 VKVANGMMD 317
Cdd:cd18585 243 PLVQNGALD 251
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
398-543 |
3.28e-10 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 60.81 E-value: 3.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 398 KDFNLNVKPGEMVAIVGPTGAGKTTLinllerFYDI------SSGSIKYDGVDTRDLSREElRAHFSM--VLQDTWLFTG 469
Cdd:COG1137 20 KDVSLEVNQGEIVGLLGPNGAGKTTT------FYMIvglvkpDSGRIFLDGEDITHLPMHK-RARLGIgyLPQEASIFRK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 470 -SIYDNI------HYGNEQASEEEViraakAAHVDDF----VRKLPegyqtilneeASNISQGQRQLITIARAFLANPDV 538
Cdd:COG1137 93 lTVEDNIlavlelRKLSKKEREERL-----EELLEEFgithLRKSK----------AYSLSGGERRRVEIARALATNPKF 157
|
....*
gi 488288408 539 LILDE 543
Cdd:COG1137 158 ILLDE 162
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
401-615 |
4.27e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 60.80 E-value: 4.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 401 NLNVKPGEMVAIVGPTGAGKTTLINLLERFY--DISSGS--------IKYDGVDTRDLSREelRAHFSMVLQDTWLFTG- 469
Cdd:PRK09984 24 DLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGShiellgrtVQREGRLARDIRKS--RANTGYIFQQFNLVNRl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 470 SIYDNIHYGNEQASE--EEVIRAAKAAHVDDFVRKLPE-GYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATS 546
Cdd:PRK09984 102 SVLENVLIGALGSTPfwRTCFSWFTREQKQRALQALTRvGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488288408 547 SVDTRTEILIQAAMNRLLENR--TSFVVAHRLS-TIRDADTIIVMAEGSIVETGTHDELmaKNGFYADLYNS 615
Cdd:PRK09984 182 SLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF--DNERFDHLYRS 251
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
399-549 |
6.05e-10 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 59.29 E-value: 6.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 399 DFNLNvkPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVD---TRDLSREELR--AHFSMVLQDTwlftgSIYD 473
Cdd:TIGR01189 20 SFTLN--AGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPlaeQRDEPHENILylGHLPGLKPEL-----SALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 474 NIHY-----GNEQASEEEVIRAAKAAHVDDfvrkLPEGYqtilneeasnISQGQRQLITIARAFLANPDVLILDEATSSV 548
Cdd:TIGR01189 93 NLHFwaaihGGAQRTIEDALAAVGLTGFED----LPAAQ----------LSAGQQRRLALARLWLSRRPLWILDEPTTAL 158
|
.
gi 488288408 549 D 549
Cdd:TIGR01189 159 D 159
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
187-351 |
6.57e-10 |
|
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: 60.53 E-value: 6.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 187 IVTFVGVLWMmltISWQLTLIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKSFNHEESDQEV 266
Cdd:cd18587 128 VLLFLAVIAL---IGGPLALVPLVAIPLVLLYGLLLQKPLRRLVEESMRESAQKNALLVESLSGLETIKALGAEGRMQRR 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 267 FEKENEKLYHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPITQIANLMNTIQ 346
Cdd:cd18587 205 WEEAVAALARSSLKSRLLSSSATNFAQFVQQLVTVAIVIVGVYLISDGELTMGGLIACVILSGRALAPLGQIAGLLTRYQ 284
|
....*
gi 488288408 347 ATVAS 351
Cdd:cd18587 285 QARTA 289
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
398-593 |
9.11e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.22 E-value: 9.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 398 KDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLS-REELRAHFSMVLQD------------T 464
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStAQRLARGLVYLPEDrqssglyldaplA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 465 WLFTGSIYDN----IHYGNEQASEEEVIRA--AKAAHVDDFVRKLpegyqtilneeasniSQGQRQLITIARAFLANPDV 538
Cdd:PRK15439 360 WNVCALTHNRrgfwIKPARENAVLERYRRAlnIKFNHAEQAARTL---------------SGGNQQKVLIAKCLEASPQL 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488288408 539 LILDEATSSVD--TRTEI--LIQ--AAmnrllENRTSFVVAHRLSTIRD-ADTIIVMAEGSI 593
Cdd:PRK15439 425 LIVDEPTRGVDvsARNDIyqLIRsiAA-----QNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
43-321 |
1.71e-09 |
|
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: 59.60 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 43 MLSIIAVLVLAIAAVVFQIQTPKVLGQATTEIFKGVMKGAAEM----KQGLKITSFPIDFDKIGQILLIVIamylisavf 118
Cdd:cd18558 6 LCAIIHGGLLPAFMVIFGDMTDSFTNGGMTNITGNSSGLNSSAgpfeKLEEEMTLYAYYYLIIGAIVLITA--------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 119 nFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQQNLTQLITSIVTFVGVLWMML 198
Cdd:cd18558 77 -YIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 199 TISWQLTLIALATVPLSLIVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKSFNHEESDQEVFEKENEKLYHAG 278
Cdd:cd18558 156 IRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNG 235
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 488288408 279 RKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDV 321
Cdd:cd18558 236 IKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEV 278
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
393-598 |
1.82e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.88 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 393 EKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERF--YDISSGSIKYDGVDTRDLSREElRAHFSMVLQdtwlftgs 470
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPEE-RAHLGIFLA-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 471 iydnIHYGNEQA--SEEEVIRAA-KAAHVddfVRKLPE----GYQTILNEEASNI---------------SQGQRQLITI 528
Cdd:CHL00131 90 ----FQYPIEIPgvSNADFLRLAyNSKRK---FQGLPEldplEFLEIINEKLKLVgmdpsflsrnvnegfSGGEKKRNEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488288408 529 ARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLLENRTSFV-VAH--RLSTIRDADTIIVMAEGSIVETGT 598
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
394-563 |
2.59e-09 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 57.25 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 394 KLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDIS--SGSIKYDGvdtrdlsrEELRAHFSMVlqdtwlfTGSI 471
Cdd:cd03232 20 RQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILING--------RPLDKNFQRS-------TGYV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 472 YDN-IHYGNeqASEEEVIRaakaahvddFVRKLPEgyqtilneeasnISQGQRQLITIARAFLANPDVLILDEATSSVDT 550
Cdd:cd03232 85 EQQdVHSPN--LTVREALR---------FSALLRG------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170
....*....|...
gi 488288408 551 RTEILIQAAMNRL 563
Cdd:cd03232 142 QAAYNIVRFLKKL 154
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
372-600 |
3.18e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 59.07 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 372 PVETDSPYRVSFEHVAFGYSpEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSRE 451
Cdd:PRK13536 33 IPGSMSTVAIDLAGVSKSYG-DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 452 ElRAHFSMVLQ-DTWLFTGSIYDNI-----HYGNEQASEEEVIRAakaahVDDFVRklpegYQTILNEEASNISQGQRQL 525
Cdd:PRK13536 112 A-RARIGVVPQfDNLDLEFTVRENLlvfgrYFGMSTREIEAVIPS-----LLEFAR-----LESKADARVSDLSGGMKRR 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488288408 526 ITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLL-ENRTSFVVAHRLSTI-RDADTIIVMAEG-SIVETGTHD 600
Cdd:PRK13536 181 LTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHFMEEAeRLCDRLCVLEAGrKIAEGRPHA 258
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
399-604 |
7.42e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.56 E-value: 7.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 399 DFNLNVKPGEMVAIVGPTGAGKT----TLINLLER---FYdiSSGSIKYDGVDTRDLSREELRA----HFSMVLQDTWLF 467
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppvVY--PSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEPMVS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 468 TGSIYD---------NIHYG-NEQASEEEVIRAAKAAHVDDFVRKLpegyqtilNEEASNISQGQRQLITIARAFLANPD 537
Cdd:PRK15134 105 LNPLHTlekqlyevlSLHRGmRREAARGEILNCLDRVGIRQAAKRL--------TDYPHQLSGGERQRVMIAMALLTRPE 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488288408 538 VLILDEATSSVDtrteILIQAAMNRLLE------NRTSFVVAHRLSTIRD-ADTIIVMAEGSIVETGTHDELMA 604
Cdd:PRK15134 177 LLIADEPTTALD----VSVQAQILQLLRelqqelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFS 246
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
398-604 |
1.18e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 57.73 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 398 KDFNLNVKPGEMVAIVGPTGAGKTTLINLL--ERfyDISSGSIKYDGVDTRDLSREELRA-----------HFSMVLqdt 464
Cdd:COG3845 275 KDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPRERRRlgvayipedrlGRGLVP--- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 465 wlfTGSIYDNI---HYGNEQASEEEVIRAAKAAhvdDFVRKLPEGYQtI----LNEEASNISQGQRQLITIARAFLANPD 537
Cdd:COG3845 350 ---DMSVAENLilgRYRRPPFSRGGFLDRKAIR---AFAEELIEEFD-VrtpgPDTPARSLSGGNQQKVILARELSRDPK 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 538 VLILDEATSSVDtrteilIQAAM---NRLLENRTS----FVVAHRLSTIRD-ADTIIVMAEGSIVETGTHDE-------- 601
Cdd:COG3845 423 LLIAAQPTRGLD------VGAIEfihQRLLELRDAgaavLLISEDLDEILAlSDRIAVMYEGRIVGEVPAAEatreeigl 496
|
...
gi 488288408 602 LMA 604
Cdd:COG3845 497 LMA 499
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
103-355 |
1.26e-08 |
|
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: 56.77 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 103 QILLIVIAMYLIS-AVFNFLQQVIMTRVSQRTvyelRQELEAKM-NKVPISYYDTHSN---GDIMsRAINDMDNIASTLQ 177
Cdd:cd18583 37 EIGLYVLLRFLQSgGGLGLLRSWLWIPVEQYS----YRALSTAAfNHVMNLSMDFHDSkksGEVL-KAIEQGSSINDLLE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 178 QNLTQLI-TSIVTFVGVLWMMLTISWQLTLIALATVPLSLIVVMVVAPRSQKhfaaQQKSLglLNNQVEETYGGHVV--- 253
Cdd:cd18583 112 QILFQIVpMIIDLVIAIVYLYYLFDPYMGLIVAVVMVLYVWSTIKLTSWRTK----LRRDM--IDADREERSILTESlln 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 254 ---VKSFNheesdQEVFEKE------NEKLyHAGRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAF 324
Cdd:cd18583 186 wetVKYFN-----REPYEKEryreavKNYQ-KAERKYLFSLNLLNAVQSLILTLGLLAGCFLAAYQVSQGQATVGDFVTL 259
|
250 260 270
....*....|....*....|....*....|.
gi 488288408 325 LQYTNQFSQPITQIANLMNTIQATVASAERV 355
Cdd:cd18583 260 LTYWAQLSGPLNFFATLYRSIQSDLIDAERL 290
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
404-563 |
1.27e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.20 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 404 VKPGEMVAIVGPTGAGKTTLINLL-ERfydISSGSIKYdgvDTRDLSREELRAHFSMVL-----QDTWLFTGSIYDNIHY 477
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLaER---VTTGVITG---GDRLVNGRPLDSSFQRSIgyvqqQDLHLPTSTVRESLRF 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 478 GNEQASEEEVIRAAKAAHVDDFVRKLP-EGY-QTILNEEASNISQGQRQLITIARAFLANPDVLI-LDEATSSVDTRTEI 554
Cdd:TIGR00956 860 SAYLRQPKSVSKSEKMEYVEEVIKLLEmESYaDAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAW 939
|
....*....
gi 488288408 555 LIQAAMNRL 563
Cdd:TIGR00956 940 SICKLMRKL 948
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
376-604 |
1.44e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 57.97 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 376 DSPYRVSFEHVA---------FGYSP----------EKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLerfydisSG 436
Cdd:PLN03211 44 DVCYRVKFENMKnkgsnikriLGHKPkisdetrqiqERTILNGVTGMASPGEILAVLGPSGSGKSTLLNAL-------AG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 437 SIKYDG------VDTRDLSREELRaHFSMVLQDTWLF------TGSIYDNIHYGNEQASEEEVIRAAKAAHVDDFVRKLp 504
Cdd:PLN03211 117 RIQGNNftgtilANNRKPTKQILK-RTGFVTQDDILYphltvrETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKC- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 505 eGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVD-TRTEILIQAAMNRLLENRTSFVVAHRLST--IRD 581
Cdd:PLN03211 195 -ENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSSrvYQM 273
|
250 260
....*....|....*....|...
gi 488288408 582 ADTIIVMAEGSIVETGTHDELMA 604
Cdd:PLN03211 274 FDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
387-587 |
1.64e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.65 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 387 AFGYSPeklLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKY--DGVDTR---DLSREElrahfsmvl 461
Cdd:PRK11147 12 SFSDAP---LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeqDLIVARlqqDPPRNV--------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 462 qdtwlfTGSIYDNIHYG---------------------------NEQASEEEVIRAAKAAHVDDFVRKLPEgyQTILNEE 514
Cdd:PRK11147 80 ------EGTVYDFVAEGieeqaeylkryhdishlvetdpseknlNELAKLQEQLDHHNLWQLENRINEVLA--QLGLDPD 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488288408 515 A--SNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTeilIQAAMNRLLENRTSFV-VAHRLSTIRDADTIIV 587
Cdd:PRK11147 152 AalSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET---IEWLEGFLKTFQGSIIfISHDRSFIRNMATRIV 224
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
398-604 |
1.86e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.32 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 398 KDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDG--VDTRDlSREELRAHFSMVLQD---TWLFTG-SI 471
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGheVVTRS-PQDGLANGIVYISEDrkrDGLVLGmSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 472 YDNI---------HYGNEQASEEEVIRaakaahVDDFVR----KLPEGYQTIlneeaSNISQGQRQLITIARAFLANPDV 538
Cdd:PRK10762 348 KENMsltalryfsRAGGSLKHADEQQA------VSDFIRlfniKTPSMEQAI-----GLLSGGNQQKVAIARGLMTRPKV 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488288408 539 LILDEATSSVDTRTEILIQAAMNRLLENRTSFV-VAHRLSTIRD-ADTIIVMAEGSI-----VETGTHDELMA 604
Cdd:PRK10762 417 LILDEPTRGVDVGAKKEIYQLINQFKAEGLSIIlVSSEMPEVLGmSDRILVMHEGRIsgeftREQATQEKLMA 489
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
50-354 |
2.06e-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: 56.08 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 50 LVLAIAAVVFQIQTPKVLGQATTEIFKGVMKgaaemkqglkitsfpiDFDKIGQILLIVIAMYLISAVFNFLQQVIMTRV 129
Cdd:cd18560 2 LLLLILGKACNVLAPLFLGRAVNALTLAKVK----------------DLESAVTLILLYALLRFSSKLLKELRSLLYRRV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 130 SQRTVYELRQELEAKMNKVPISYYDTHSNGD---IMSRAINDMDNIASTLQQNLTQLITSIVTFVGVLWMMLtiSWQLTL 206
Cdd:cd18560 66 QQNAYRELSLKTFAHLHSLSLDWHLSKKTGEvvrIMDRGTESANTLLSYLVFYLVPTLLELIVVSVVFAFHF--GAWLAL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 207 IALATVpLSLIVVMVVAPRSQKHF---------AAQQKSLGLLNNQveETygghvvVKSFNHEESDQEVFEKENEKLYHA 277
Cdd:cd18560 144 IVFLSV-LLYGVFTIKVTEWRTKFrraankkdnEAHDIAVDSLLNF--ET------VKYFTNEKYEVDRYGEAVKEYQKS 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488288408 278 GRKAQFISAIIMPLMNFIKNLGYVFVAVLGGVKVANGMMDLGDVQAFLQYTNQFSQPITQIANLMNTIQATVASAER 354
Cdd:cd18560 215 SVKVQASLSLLNVGQQLIIQLGLTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSLTDMEN 291
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
381-607 |
2.14e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.21 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYsPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYD-----GVDTRDlsreelra 455
Cdd:PRK15064 320 LEVENLTKGF-DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSenaniGYYAQD-------- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 456 HFSMVLQDTWLFtgsiyDNIHYGNEQASEEEVIRAAKAAHV---DDFVRKlpegyqtilneeASNISQGQRQLITIARAF 532
Cdd:PRK15064 391 HAYDFENDLTLF-----DWMSQWRQEGDDEQAVRGTLGRLLfsqDDIKKS------------VKVLSGGEKGRMLFGKLM 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 533 LANPDVLILDEATSSVDTRTeilIQaAMNRLLENR--TSFVVAH-R--LSTIrdADTIIVMAEGSIVE-TGTHDELMAKN 606
Cdd:PRK15064 454 MQKPNVLVMDEPTNHMDMES---IE-SLNMALEKYegTLIFVSHdRefVSSL--ATRIIEITPDGVVDfSGTYEEYLRSQ 527
|
.
gi 488288408 607 G 607
Cdd:PRK15064 528 G 528
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
397-604 |
2.53e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.57 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 397 MKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDG--VDTRDLSREELRahFSMVLQD--TWL----FT 468
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhpLHFGDYSYRSQR--IRMIFQDpsTSLnprqRI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 469 GSIYDNIHYGNEQASEEEviraaKAAHVDDFVRKLpegyqTILNEEAS----NISQGQRQLITIARAFLANPDVLILDEA 544
Cdd:PRK15112 107 SQILDFPLRLNTDLEPEQ-----REKQIIETLRQV-----GLLPDHASyyphMLAPGQKQRLGLARALILRPKVIIADEA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488288408 545 TSSVD--TRTEILiqaamNRLLENRTS------FVVAHRLSTIRDADTIIVMAEGSIVETGTHDELMA 604
Cdd:PRK15112 177 LASLDmsMRSQLI-----NLMLELQEKqgisyiYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLA 239
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
401-604 |
3.65e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 55.58 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 401 NLNVKPGEMVAIVGPTGAGKT----TLINLLERFYDISSGSIKYDGVDTRDLS---REELRAH-FSMVLQDT-------- 464
Cdd:PRK15093 27 SMTLTEGEIRGLVGESGSGKSliakAICGVTKDNWRVTADRMRFDDIDLLRLSpreRRKLVGHnVSMIFQEPqscldpse 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 465 ------------WLFTGSIYDNIHYGNEQASEEeVIRAAKAAHvDDFVRKLPegYQtilneeasnISQGQRQLITIARAF 532
Cdd:PRK15093 107 rvgrqlmqnipgWTYKGRWWQRFGWRKRRAIEL-LHRVGIKDH-KDAMRSFP--YE---------LTEGECQKVMIAIAL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488288408 533 LANPDVLILDEATSSVDTRTeiliQAAMNRLL------ENRTSFVVAHRLSTIRD-ADTIIVMAEGSIVETGTHDELMA 604
Cdd:PRK15093 174 ANQPRLLIADEPTNAMEPTT----QAQIFRLLtrlnqnNNTTILLISHDLQMLSQwADKINVLYCGQTVETAPSKELVT 248
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
95-580 |
4.49e-08 |
|
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: 56.30 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 95 PIDFDKI-GQILLIVIAMYLISAVFNFLQQVIMTRVSQR-TVYELRQELEAkmnkvpISYYDThSNGDIMSRAINDM--- 169
Cdd:TIGR00954 131 PRNFAWIlFKWFLIAPPASFINSAIKYLLKELKLRFRVRlTRYLYSKYLSG------FTFYKV-SNLDSRIQNPDQLltq 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 170 ------DNIAStLQQNLTQLITSIVTFVGVLWMMLTisWQLTLIALATVPLSLIVVMVVAPRSQKHFAAQQKSLG----- 238
Cdd:TIGR00954 204 dvekfcDSVVE-LYSNLTKPILDVILYSFKLLTALG--SVGPAGLFAYLFATGVVLTKLRPPIGKLTVEEQALEGeyryv 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 239 ---LLNNQvEET--YGGHVVVKsfnheESDQEVFEKENEKLyhagRKAQFISAIIMPLMNFIKN-----LGYVFVAV--L 306
Cdd:TIGR00954 281 hsrLIMNS-EEIafYQGNKVEK-----ETVMSSFYRLVEHL----NLIIKFRFSYGFLDNIVAKytwsaVGLVAVSIpiF 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 307 GGVKVANGMMDLGD-VQAFlqYTN-----QFSQPITQIANLMNTIQATVASAERVFEVLD----------EEEMVDEP-- 368
Cdd:TIGR00954 351 DKTHPAFLEMSEEElMQEF--YNNgrlllKAADALGRLMLAGRDMTRLAGFTARVDTLLQvlddvksgnfKRPRVEEIes 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 369 -------------SGIPVETDSpyRVSFEHVAFGYSPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDIss 435
Cdd:TIGR00954 429 greggrnsnlvpgRGIVEYQDN--GIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPV-- 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 436 gsikYDGVDTRDlSREEL-----RAHFSM-VLQDTWLFTGSIYDNIHYGneqASEEEVIRAAKAAHVDDFVRKlpEGYQT 509
Cdd:TIGR00954 505 ----YGGRLTKP-AKGKLfyvpqRPYMTLgTLRDQIIYPDSSEDMKRRG---LSDKDLEQILDNVQLTHILER--EGGWS 574
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488288408 510 ILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEiliqAAMNRLLENR--TSFVVAHRLSTIR 580
Cdd:TIGR00954 575 AVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVE----GYMYRLCREFgiTLFSVSHRKSLWK 643
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
393-560 |
5.00e-08 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 53.65 E-value: 5.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 393 EKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRAHFSMVLQDTWLFTGSIY 472
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 473 DNIHYGNEQASEEEVIRAAKAAHVDDFvRKLPEGYqtilneeasnISQGQRQLITIARAFLANPDVLILDEATSSVDTRT 552
Cdd:cd03231 92 ENLRFWHADHSDEQVEEALARVGLNGF-EDRPVAQ----------LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
....*...
gi 488288408 553 EILIQAAM 560
Cdd:cd03231 161 VARFAEAM 168
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
399-604 |
5.68e-08 |
|
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: 55.60 E-value: 5.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 399 DFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDIS-SGSIKYDG--VDTRDlSREELRAHFSMVLQD------------ 463
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDIRN-PAQAIRAGIAMVPEDrkrhgivpilgv 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 464 ---TWLFTGSIYDNIHYGNEQASEEEVIRAAKAAHVDDFVRKLPEGyqtilneeasNISQGQRQLITIARAFLANPDVLI 540
Cdd:TIGR02633 357 gknITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIG----------RLSGGNQQKAVLAKMLLTNPRVLI 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488288408 541 LDEATSSVDTRTEILIQAAMNRLLENRTSF-VVAHRLSTIRD-ADTIIVMAEG----SIVETG-THDELMA 604
Cdd:TIGR02633 427 LDEPTRGVDVGAKYEIYKLINQLAQEGVAIiVVSSELAEVLGlSDRVLVIGEGklkgDFVNHAlTQEQVLA 497
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
391-604 |
8.93e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 53.55 E-value: 8.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 391 SPEKLLMKDFNLNVKPGEMVAIVGPTGAGKT----TLINLLERFYDISSGSIKYDGVdtrDLSREELRA-HFSMVLQDtw 465
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGK---PVAPCALRGrKIATIMQN-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 466 lfTGSIYDNIHygNEQASEEEVIRAAKAAHVDDFVRKLPEGY-----QTILNEEASNISQGQRQLITIARAFLANPDVLI 540
Cdd:PRK10418 88 --PRSAFNPLH--TMHTHARETCLALGKPADDATLTAALEAVglenaARVLKLYPFEMSGGMLQRMMIALALLCEAPFII 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488288408 541 LDEATSSVDtrteILIQAAMNRLLENRTS------FVVAHRLSTI-RDADTIIVMAEGSIVETGTHDELMA 604
Cdd:PRK10418 164 ADEPTTDLD----VVAQARILDLLESIVQkralgmLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETLFN 230
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
399-549 |
1.21e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.54 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 399 DFNLNvkPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSREELRA---HFSMVLQDTwlftgSIYDNI 475
Cdd:PRK13543 31 DFHVD--AGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAylgHLPGLKADL-----STLENL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 476 HYGN-------EQASEEEVIRAAKAAHVDDFVRKLpegyqtilneeasniSQGQRQLITIARAFLANPDVLILDEATSSV 548
Cdd:PRK13543 104 HFLCglhgrraKQMPGSALAIVGLAGYEDTLVRQL---------------SAGQKKRLALARLWLSPAPLWLLDEPYANL 168
|
.
gi 488288408 549 D 549
Cdd:PRK13543 169 D 169
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
392-555 |
1.38e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.57 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 392 PEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKydgVDTR------DLSREELRAHfsmvlqdtw 465
Cdd:PRK11147 330 DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH---CGTKlevayfDQHRAELDPE--------- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 466 lftGSIYDNIHYGneqasEEEVIRAAKAAHV----DDF----------VRKLpegyqtilneeasniSQGQRQLITIARA 531
Cdd:PRK11147 398 ---KTVMDNLAEG-----KQEVMVNGRPRHVlgylQDFlfhpkramtpVKAL---------------SGGERNRLLLARL 454
|
170 180
....*....|....*....|....*
gi 488288408 532 FLANPDVLILDEATSSVDTRT-EIL 555
Cdd:PRK11147 455 FLKPSNLLILDEPTNDLDVETlELL 479
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
388-567 |
1.59e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 52.26 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 388 FGYSpEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDT-RDLSREELR----AHFSMVLQ 462
Cdd:PRK13540 9 FDYH-DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkKDLCTYQKQlcfvGHRSGINP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 463 DTWLFTGSIYDnIHYGNEQASEEEVIRAAKAAHVDDFvrklPEGYqtilneeasnISQGQRQLITIARAFLANPDVLILD 542
Cdd:PRK13540 88 YLTLRENCLYD-IHFSPGAVGITELCRLFSLEHLIDY----PCGL----------LSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180
....*....|....*....|....*
gi 488288408 543 EATSSVDTRTeilIQAAMNRLLENR 567
Cdd:PRK13540 153 EPLVALDELS---LLTIITKIQEHR 174
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
381-552 |
2.23e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 53.79 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 381 VSFEHVAFGYSpEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKY-DGVDTR--DLSREELRAhf 457
Cdd:TIGR03719 323 IEAENLTKAFG-DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKLAyvDQSRDALDP-- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 458 smvlqdtwlfTGSIYDNIHYGNeqaseeEVIRAAKA-----AHVDDFVRKLPEGYQTIlneeaSNISQGQRQLITIARAF 532
Cdd:TIGR03719 400 ----------NKTVWEEISGGL------DIIKLGKReipsrAYVGRFNFKGSDQQKKV-----GQLSGGERNRVHLAKTL 458
|
170 180
....*....|....*....|
gi 488288408 533 LANPDVLILDEATSSVDTRT 552
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLDVET 478
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
392-593 |
3.05e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.39 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 392 PEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYD-ISSGSIKYDG--VDTRDlSREELRAHFSMVLQDT---- 464
Cdd:PRK13549 273 PHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGkpVKIRN-PQQAIAQGIAMVPEDRkrdg 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 465 WLFTGSIYDNIHYGN-EQASEEEVIR-AAKAAHVDDFVRKL----PEGYQTIlneeaSNISQGQRQLITIARAFLANPDV 538
Cdd:PRK13549 352 IVPVMGVGKNITLAAlDRFTGGSRIDdAAELKTILESIQRLkvktASPELAI-----ARLSGGNQQKAVLAKCLLLNPKI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488288408 539 LILDEATSSVDTRTEILIQAAMNRLLENRTS-FVVAHRLSTIRD-ADTIIVMAEGSI 593
Cdd:PRK13549 427 LILDEPTRGIDVGAKYEIYKLINQLVQQGVAiIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
372-603 |
5.01e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 51.33 E-value: 5.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 372 PVETDSPYRVsfEHVAFGYsPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGV-----DTR 446
Cdd:PRK10575 5 TNHSDTTFAL--RNVSFRV-PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleswSSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 447 DLSRE------ELRAHFSMVLQD-----TWLFTGSIYdniHYGneQASEEEVIRAAKAAHVDDFVRKLpegyqtilneeA 515
Cdd:PRK10575 82 AFARKvaylpqQLPAAEGMTVRElvaigRYPWHGALG---RFG--AADREKVEEAISLVGLKPLAHRL-----------V 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 516 SNISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLLENR--TSFVVAHRLS-TIRDADTIIVMAEGS 592
Cdd:PRK10575 146 DSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINmAARYCDYLVALRGGE 225
|
250
....*....|.
gi 488288408 593 IVETGTHDELM 603
Cdd:PRK10575 226 MIAQGTPAELM 236
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
366-583 |
5.47e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 5.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 366 DEPSGIPVETDSPYRVSFEHVAFGYSpEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLL------------------ 427
Cdd:PRK10938 246 DEPSARHALPANEPRIVLNNGVVSYN-DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysndltlfgrr 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 428 ----ERFYDISSgSIKYdgVDtrdlSREELRAHFSMVLQDTWLftGSIYDNIhyGNEQAseeeviraakaahVDDFVRKL 503
Cdd:PRK10938 325 rgsgETIWDIKK-HIGY--VS----SSLHLDYRVSTSVRNVIL--SGFFDSI--GIYQA-------------VSDRQQKL 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 504 PEGYQTILNEEAS-------NISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLL-ENRTS--FV-- 571
Cdd:PRK10938 381 AQQWLDILGIDKRtadapfhSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIsEGETQllFVsh 460
|
250 260
....*....|....*....|
gi 488288408 572 --------VAHRLSTIRDAD 583
Cdd:PRK10938 461 haedapacITHRLEFVPDGD 480
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
398-604 |
8.42e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.09 E-value: 8.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 398 KDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTrdlsreELRAHFSMVLQDTWLFTGSIYDNIHY 477
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDI------SPRSPLDAVKKGMAYITESRRDNGFF 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 478 GNEQASEEEVI-RAAKAA----------HVDDfvRKLPEGYQTILNEEASNISQ-------GQRQLITIARAFLANPDVL 539
Cdd:PRK09700 354 PNFSIAQNMAIsRSLKDGgykgamglfhEVDE--QRTAENQRELLALKCHSVNQnitelsgGNQQKVLISKWLCCCPEVI 431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488288408 540 ILDEATSSVDTRTEILIQAAMNRLLEN-RTSFVVAHRLSTIRDA-DTIIVMAEGSIVE------TGTHDELMA 604
Cdd:PRK09700 432 IFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVcDRIAVFCEGRLTQiltnrdDMSEEEIMA 504
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
396-604 |
1.71e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.39 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 396 LMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDIS---SGSIKYDGVDTRDLSREELRAHFS--------MVLQDT 464
Cdd:PLN03140 180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFVPRKTSAYISqndvhvgvMTVKET 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 465 WLFT------GSIYDNIhygNEQASEEEVIRAAKAAHVDDFVRKLP-EGYQ-------------------TILNEEA-SN 517
Cdd:PLN03140 260 LDFSarcqgvGTRYDLL---SELARREKDAGIFPEAEVDLFMKATAmEGVKsslitdytlkilgldickdTIVGDEMiRG 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 518 ISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLLENRTSFVVAHRLS----TIRDADTIIVMAEGSI 593
Cdd:PLN03140 337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQpapeTFDLFDDIILLSEGQI 416
|
250
....*....|.
gi 488288408 594 VETGTHDELMA 604
Cdd:PLN03140 417 VYQGPRDHILE 427
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
390-549 |
2.18e-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: 50.70 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 390 YSPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINL---LERFYD----ISSG-SIKY------------------DGV 443
Cdd:TIGR03719 14 VPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRImagVDKDFNgearPQPGiKVGYlpqepqldptktvrenveEGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 444 -DTRD-LSR-EELRAHFSMVLQDtwlftgsiYDNIhyGNEQASEEEVIRAAKAAHVD-------DFVRkLPEGYQTIlne 513
Cdd:TIGR03719 94 aEIKDaLDRfNEISAKYAEPDAD--------FDKL--AAEQAELQEIIDAADAWDLDsqleiamDALR-CPPWDADV--- 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 488288408 514 eaSNISQGQRQLITIARAFLANPDVLILDEATSSVD 549
Cdd:TIGR03719 160 --TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
381-439 |
3.24e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.12 E-value: 3.24e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488288408 381 VSFEHV--AFGyspEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIK 439
Cdd:PRK11819 325 IEAENLskSFG---DRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK 382
|
|
| ABC_6TM_PglK_like |
cd18553 |
Six-transmembrane helical domain of the ABC transporter PglK and similar proteins; This group ... |
106-295 |
3.41e-06 |
|
Six-transmembrane helical domain of the ABC transporter PglK and similar proteins; This group represents the transmembrane (TM) domain of an active lipid-linked oligosaccharides flippase PglK (protein glycosylation K), which is a homodimeric ABC transporter that flips a lipid-linked oligosaccharide that serves as a glycan donor in N-linked protein glycosylation. Pglk mediates the ATP-dependent translocation of the undecaprenylpyrophosphate-linked heptasaccharide intermediate across the cell membrane; this is an essential step during the N-linked protein glycosylation pathway. This TM subunit exhibits 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. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.
Pssm-ID: 349997 Cd Length: 300 Bit Score: 49.08 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 106 LIVIAMYLISAVFNFLQQVIMTRVSQRTVYELRQELeaKMNKVPISYYD-THSNGDIMSRAINDMDNIASTLQQNLTQLI 184
Cdd:cd18553 58 IILIGFYIFRSLYNIFYTYLLNRFSFGRYHSIAYRL--FKNYLKLNYQDfTNKNSSDLSKSIINEASNLSQVIQSFLFIL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 185 TSIVTFVGVLWMMLTISWQLTLIalATVPLSL---IVVMVVAPRSQKHFAAQQKSLGLLNNQVEETYGGHVVVKSFNHEE 261
Cdd:cd18553 136 SEIFVILFIYSLLLYVNWKITLV--LTLFLGLnvfFITKIVSKKIKKQGKKREESQKKFYKILSETFGNFKIIKLKSNEK 213
|
170 180 190
....*....|....*....|....*....|....
gi 488288408 262 SDQEVFEKENEKLyhagRKAQFISAIIMPLMNFI 295
Cdd:cd18553 214 EILKNFSQASLKF----AKANIINQTLQTVPRLI 243
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
396-603 |
3.47e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.05 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 396 LMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDIS--------SGSIKYDG-----VDTRDLSReeLRAHFSMVLQ 462
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGeplaaIDAPRLAR--LRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 463 DTWLFtgSIYDNIHYGneqaSEEEVIRAAKAAHVDDFV--RKLP-EGYQTILNEEASNISQGQRQLITIARAF------- 532
Cdd:PRK13547 94 PAFAF--SAREIVLLG----RYPHARRAGALTHRDGEIawQALAlAGATALVGRDVTTLSGGELARVQFARVLaqlwpph 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 533 --LANPDVLILDEATSSVDTrteiliqAAMNRLLENRTSFVVAHRLSTI----------RDADTIIVMAEGSIVETGTHD 600
Cdd:PRK13547 168 daAQPPRYLLLDEPTAALDL-------AHQHRLLDTVRRLARDWNLGVLaivhdpnlaaRHADRIAMLADGAIVAHGAPA 240
|
...
gi 488288408 601 ELM 603
Cdd:PRK13547 241 DVL 243
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
105-357 |
3.87e-06 |
|
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: 49.00 E-value: 3.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 105 LLIVIAMYLISAVFNFLQQVIMTRVSQRTVYELRQELeakMNKV---PISYYDTHSNGDIMSRAINDMDNIASTLQQNLT 181
Cdd:cd18604 46 LGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHERL---LHSVlraPLRWLDTTPVGRILNRFSKDIETIDSELADSLS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 182 QLITSIVTFVGVLWMMLTISWQLTLIALATVPLSLIV--VMVVAPRSQKHFAAQQKS--LGLLNnqveETYGGHVVVKSF 257
Cdd:cd18604 123 SLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIgrLYLRASRELKRLESVARSpiLSHFG----ETLAGLVTIRAF 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 258 nheeSDQEVFEKENEKLYHAGRKAQFISAIIMPLMNF-IKNLGYVFVAVLGGVKVANGMMDLGDVqAF-LQYTNQFSQPI 335
Cdd:cd18604 199 ----GAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVrIDLLGALFSFATAALLVYGPGIDAGLA-GFsLSFALGFSSAI 273
|
250 260
....*....|....*....|..
gi 488288408 336 TQIANLMNTIQATVASAERVFE 357
Cdd:cd18604 274 LWLVRSYNELELDMNSVERIQE 295
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
105-357 |
6.74e-06 |
|
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: 48.29 E-value: 6.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 105 LLIVIAMYLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQQNLTQLI 184
Cdd:cd18605 45 LTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 185 TSIVTFVGVLWMMLTISWQLTLIalatvplsLIVVMVVAPRSQKHFAA--------QQKSLGLLNNQVEETYGGHVVVKS 256
Cdd:cd18605 125 AQLFGLLGYLVVICYQLPWLLLL--------LLPLAFIYYRIQRYYRAtsrelkrlNSVNLSPLYTHFSETLKGLVTIRA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 257 FNHEESdqevFEKENEKLYHAGRKAQFISAIIMPLMNF----IKNLGYVFVAVLGgvkVANGMMDLGDVQAFLQYTNQFS 332
Cdd:cd18605 197 FRKQER----FLKEYLEKLENNQRAQLASQAASQWLSIrlqlLGVLIVTFVALTA---VVQHFFGLSIDAGLIGLALSYA 269
|
250 260
....*....|....*....|....*....
gi 488288408 333 QPIT-QIANLMNTIQAT---VASAERVFE 357
Cdd:cd18605 270 LPITgLLSGLLNSFTETekeMVSVERVRQ 298
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
377-594 |
8.00e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.07 E-value: 8.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 377 SPYRVSFEHVAF-----------GYSPEKL-LMKDFNLNVKPGEMVAIVGPTGAGKTTLINLL--ERFYDISSGSIKYDG 442
Cdd:PLN03140 864 TPLAMSFDDVNYfvdmpaemkeqGVTEDRLqLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISG 943
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 443 VDTRD--LSR-----EELRAHFSMV-LQDTWLFTGSIYDNIHYGNEQASE--EEVIRAAKAAHVDDFVRKLPEgyqtiln 512
Cdd:PLN03140 944 FPKKQetFARisgycEQNDIHSPQVtVRESLIYSAFLRLPKEVSKEEKMMfvDEVMELVELDNLKDAIVGLPG------- 1016
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 513 eeASNISQGQRQLITIARAFLANPDVLILDEATSSVDTR-TEILIQAAMNRLLENRTSFVVAHRLST-IRDA-DTIIVMA 589
Cdd:PLN03140 1017 --VTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARaAAIVMRTVRNTVDTGRTVVCTIHQPSIdIFEAfDELLLMK 1094
|
....*
gi 488288408 590 EGSIV 594
Cdd:PLN03140 1095 RGGQV 1099
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
109-274 |
1.44e-05 |
|
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: 47.08 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 109 IAMY----LISAVFNFLQQVIMTRVSQRTVYELrqeLEAKMNKV---PISYYDTHSNGDIMSRAINDMDNIASTLQQNLT 181
Cdd:cd18606 38 IGIYaglgVLQAIFLFLFGLLLAYLGIRASKRL---HNKALKRVlraPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 182 QLITSIVTFVGVLWMML-TISWqltlIALATVPLSLIVVMVVA-----PRSQKHFAAQQKSlgLLNNQVEETYGGHVVVK 255
Cdd:cd18606 115 MFLYTLSSIIGTFILIIiYLPW----FAIALPPLLVLYYFIANyyrasSRELKRLESILRS--FVYANFSESLSGLSTIR 188
|
170
....*....|....*....
gi 488288408 256 SFNheesDQEVFEKENEKL 274
Cdd:cd18606 189 AYG----AQDRFIKKNEKL 203
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
346-427 |
2.22e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.47 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 346 QATVA-SAERVFEVLDEEEMVdepsgIPVETDSPYRVSF-------------EHVAFGYSpEKLLMKDFNLNVKPGEMVA 411
Cdd:PRK10636 269 KATKAkQAQSRIKMLERMELI-----APAHVDNPFHFSFrapeslpnpllkmEKVSAGYG-DRIILDSIKLNLVPGSRIG 342
|
90
....*....|....*.
gi 488288408 412 IVGPTGAGKTTLINLL 427
Cdd:PRK10636 343 LLGRNGAGKSTLIKLL 358
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
105-357 |
2.29e-05 |
|
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: 46.70 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 105 LLIVIAMYLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQQNLTQLI 184
Cdd:cd18603 44 LGVYGALGLGQAIFVFLGSLALALGCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 185 TSIVTFVGVLwmmLTISWQLTLIALATVPLSLIVVM-----VVAPRSQKHFAAQQKSlgLLNNQVEETYGGHVVVKSFNH 259
Cdd:cd18603 124 NCLFQVISTL---VVISISTPIFLVVIIPLAILYFFiqrfyVATSRQLKRLESVSRS--PIYSHFSETLQGASTIRAYGV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 260 eesdQEVFEKENEKLYHAGRKAQFISAIIMP----LMNFIKNLGyVFVAVLGGVkVANGMMDLGDVQAFLQYTNQfsqpI 335
Cdd:cd18603 199 ----QERFIRESDRRVDENQRAYYPSIVSNRwlavRLEFLGNLI-VLFAALFAV-LSRDSLSPGLVGLSISYALQ----I 268
|
250 260
....*....|....*....|....*.
gi 488288408 336 TQIANLM----NTIQATVASAERVFE 357
Cdd:cd18603 269 TQTLNWLvrmtSELETNIVSVERIKE 294
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
397-605 |
3.03e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.96 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 397 MKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGvdtrDLSREELRAHFSMVLqdtwlfTGsiYDNIH 476
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----EVSVIAISAGLSGQL------TG--IENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 477 Y-----GNEQASEEEVI-RAAKAAHVDDFVrklpegYQTIlneeaSNISQGQRQLITIARAFLANPDVLILDEATSSVDt 550
Cdd:PRK13546 108 FkmlcmGFKRKEIKAMTpKIIEFSELGEFI------YQPV-----KKYSSGMRAKLGFSINITVNPDILVIDEALSVGD- 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 551 rtEILIQAAMNRLLE----NRTSFVVAHRLSTIRDADTIIVMAE-GSIVETGTHDELMAK 605
Cdd:PRK13546 176 --QTFAQKCLDKIYEfkeqNKTIFFVSHNLGQVRQFCTKIAWIEgGKLKDYGELDDVLPK 233
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
345-557 |
5.50e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 5.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 345 IQATVASAERVFEVldeEEMVDEPS---GIPVETDSPYR--VSFEHVAFGYSPEKLLMKDFNLNVKPGEMVAIVGPTGAG 419
Cdd:PLN03073 471 VQSRIKALDRLGHV---DAVVNDPDykfEFPTPDDRPGPpiISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIG 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 420 KTTLINLLERFYDISSGSI-----------KYDGVDTRDLSREELrahfsmvlqdtwLFTGSIYDNIhygneqasEEEVI 488
Cdd:PLN03073 548 KSTILKLISGELQPSSGTVfrsakvrmavfSQHHVDGLDLSSNPL------------LYMMRCFPGV--------PEQKL 607
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488288408 489 RaakaAHVDDFvrklpeGYQTILNEEAS-NISQGQRQLITIARAFLANPDVLILDEATSSVD-TRTEILIQ 557
Cdd:PLN03073 608 R----AHLGSF------GVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDlDAVEALIQ 668
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
396-601 |
1.17e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.90 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 396 LMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDG--VDTRDlSREELRAhfSMVL------QDTWLF 467
Cdd:PRK11288 268 LREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRS-PRDAIRA--GIMLcpedrkAEGIIP 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 468 TGSIYDNI---------HYGNeqaseeeVIRAAK-AAHVDDFVRKL----PEGYQTILneeasNISQGQRQLITIARaFL 533
Cdd:PRK11288 345 VHSVADNInisarrhhlRAGC-------LINNRWeAENADRFIRSLniktPSREQLIM-----NLSGGNQQKAILGR-WL 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488288408 534 ANP-DVLILDEATSSVD--TRTEI--LIQAAMNRlleNRTSFVVAHRL-STIRDADTIIVMAEGSIVETGTHDE 601
Cdd:PRK11288 412 SEDmKVILLDEPTRGIDvgAKHEIynVIYELAAQ---GVAVLFVSSDLpEVLGVADRIVVMREGRIAGELAREQ 482
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
399-591 |
1.28e-04 |
|
ATP-binding cassette domain 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 more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.94 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 399 DFNLNVKP-----GEMVAIVGPTGAGKTTLINLLerfydisSGSIKYDGVDtrdlsreelrahfsmvlqDTWlftgsiyd 473
Cdd:cd03222 12 VFFLLVELgvvkeGEVIGIVGPNGTGKTTAVKIL-------AGQLIPNGDN------------------DEW-------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 474 nihygneqaseEEVIRAAKAAHVDdfvrklpegyqtilneeasnISQGQRQLITIARAFLANPDVLILDEATSSVDTRTE 553
Cdd:cd03222 59 -----------DGITPVYKPQYID--------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQR 107
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488288408 554 ILIQAAMNRLLEN--RTSFVVAHRLSTIRDADTIIVMAEG 591
Cdd:cd03222 108 LNAARAIRRLSEEgkKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
484-607 |
1.91e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 44.73 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 484 EEEVIRAAKAAHVDDFvrklpeGYQTILNEEASNISQGQRQLITIARAFLANPDVLILDEATSSVD--TRT---EILIQA 558
Cdd:NF033858 370 PAAEIAARVAEMLERF------DLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDpvARDmfwRLLIEL 443
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 488288408 559 AMNrllENRTSFVVAHRLSTIRDADTIIVMAEGSIVETGTHDELMAKNG 607
Cdd:NF033858 444 SRE---DGVTIFISTHFMNEAERCDRISLMHAGRVLASDTPAALVAARG 489
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
101-355 |
3.08e-04 |
|
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: 43.24 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 101 IGQILLIVIAMYLISAVFNFLQQVIMTRvSQRTVYELRQELEA----KMNKVPISYYDTHSNGDIMSRAINDMDNIASTL 176
Cdd:cd18579 35 LSEGYLLALALFLVSLLQSLLLHQYFFL-SFRLGMRVRSALSSliyrKALRLSSSARQETSTGEIVNLMSVDVQRIEDFF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 177 QqNLTQLITSIVTFVGVLWMM-LTISWQlTLIALATVPLSLIVVMVVAPRSQKHFAAQQKS----LGLLNnqveETYGGH 251
Cdd:cd18579 114 L-FLHYLWSAPLQIIVALYLLyRLLGWA-ALAGLGVLLLLIPLQAFLAKLISKLRKKLMKAtderVKLTN----EILSGI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 252 VVVKSFNHEESdqevFEKENEKL----YHAGRKAQFISAIIMPLMNFIKNLgyVFVAVLGGVKVANGMMDLGDVQAFLQY 327
Cdd:cd18579 188 KVIKLYAWEKP----FLKRIEELrkkeLKALRKFGYLRALNSFLFFSTPVL--VSLATFATYVLLGNPLTAAKVFTALSL 261
|
250 260
....*....|....*....|....*...
gi 488288408 328 TNQFSQPITQIANLMNTIQATVASAERV 355
Cdd:cd18579 262 FNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
392-574 |
5.41e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 41.87 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 392 PEKLLMKDFNLNVKP----------GEMVAIVGPTGAGKTTLINllerfydissgSIKYD--GVDTRDLSREELRAHFSM 459
Cdd:cd03279 3 PLKLELKNFGPFREEqvidftgldnNGLFLICGPTGAGKSTILD-----------AITYAlyGKTPRYGRQENLRSVFAP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 460 VLQDTWL-FTGSIYDNIHygneqaseeEVIRAAKAAHvDDFVRK--LPEG-YQTILNEEASNISQGQRQLITIARAF--- 532
Cdd:cd03279 72 GEDTAEVsFTFQLGGKKY---------RVERSRGLDY-DQFTRIvlLPQGeFDRFLARPVSTLSGGETFLASLSLALals 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488288408 533 --LANP-----DVLILDEATSSVDTRTEILIQAAMNRL-LENRTSFVVAH 574
Cdd:cd03279 142 evLQNRggarlEALFIDEGFGTLDPEALEAVATALELIrTENRMVGVISH 191
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
506-592 |
5.69e-04 |
|
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: 41.15 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 506 GYQTiLNEEASNISQGQRQLITIARAFLANPD--VLILDEATSSVDTRTEILIQAAMNRLL-ENRTSFVVAHRLSTIRDA 582
Cdd:cd03238 77 GYLT-LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSA 155
|
90
....*....|
gi 488288408 583 DTIIVMAEGS 592
Cdd:cd03238 156 DWIIDFGPGS 165
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
379-620 |
6.02e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.96 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 379 YRVSFEHVAFGYS-----PEKL--------------LMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIK 439
Cdd:PRK13545 3 YKVKFEHVTKKYKmynkpFDKLkdlffrskdgeyhyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 440 YDGvdtrdlsreelrahfsmvlQDTWLFTGSIYDNIHYGNEQASEEEVIRAAKAAHVDDFVRKLPEgYQTI---LNEEAS 516
Cdd:PRK13545 83 IKG-------------------SAALIAISSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIE-FADIgkfIYQPVK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 517 NISQGQRQLITIARAFLANPDVLILDEATSSVDTRTEILIQAAMNRLLEN-RTSFVVAHRLSTIRDADT-IIVMAEGSIV 594
Cdd:PRK13545 143 TYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQgKTIFFISHSLSQVKSFCTkALWLHYGQVK 222
|
250 260
....*....|....*....|....*.
gi 488288408 595 ETGTHDELMAKNGFYADLYNSQFSEE 620
Cdd:PRK13545 223 EYGDIKEVVDHYDEFLKKYNQMSVEE 248
|
|
| ABC_6TM_AarD_CydDC_like |
cd18781 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ... |
101-238 |
7.71e-04 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; This subgroup belongs to the ABC_6TM_AarD_CydDC_like subgroup of the ABC_6TM exporter family. The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs). The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350054 [Multi-domain] Cd Length: 290 Bit Score: 41.75 E-value: 7.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 101 IGQILLIVIAMYLISAVFNFLQQVIMTRVSQRTVYELRQELEAKMNKVPISYYDTHSNGDIMSRAINDMDNIASTLQQNL 180
Cdd:cd18781 36 LLIVLGILAIAIIVRFICTRLASRASYRASADVKKTLREKIYDKLLRLGPSYQEKVSTAEVVQLSVEGVEQLEIYFGRYL 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488288408 181 TQLITSI---VTFVGVLwmmLTISWQLTLIALATVPL---SLIVVMVVAPRSQKHFAAQQKSLG 238
Cdd:cd18781 116 PQFFYSMlapLTLFVVL---APINWKAALVLLICVPLipiSIIAVQKIAKKLLSKYWGSYTDLG 176
|
|
| Era_like |
cd00880 |
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ... |
411-518 |
2.64e-03 |
|
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.
Pssm-ID: 206646 [Multi-domain] Cd Length: 161 Bit Score: 38.77 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 411 AIVGPTGAGKTTLINLL--ERFYDISSgsikYDGVdTRDLSREELRAH--FSMVLQDtwlfTGSIYDNIHYGNEQasEEE 486
Cdd:cd00880 1 AIFGRPNVGKSSLLNALlgQNVGIVSP----IPGT-TRDPVRKEWELLplGPVVLID----TPGLDEEGGLGRER--VEE 69
|
90 100 110
....*....|....*....|....*....|....*.
gi 488288408 487 VIRAAKAA----HVDDFVRKLPEGYQTILNEEASNI 518
Cdd:cd00880 70 ARQVADRAdlvlLVVDSDLTPVEEEAKLGLLRERGK 105
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
390-556 |
2.74e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.47 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 390 YSPEKLLMKDFNLNVKPGEMVAIVGPTGAGKTTLINLLERFYDISSGSIKYDGVDTRDLSR-------EELRAHFSMVLQ 462
Cdd:PRK13541 9 FNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKpyctyigHNLGLKLEMTVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 463 DTWLFTGSIYDnihygneqaSEEEVIRAAKAAHVDDFvrklpegyqtiLNEEASNISQGQRQLITIARAFLANPDVLILD 542
Cdd:PRK13541 89 ENLKFWSEIYN---------SAETLYAAIHYFKLHDL-----------LDEKCYSLSSGMQKIVAIARLIACQSDLWLLD 148
|
170
....*....|....
gi 488288408 543 EATSSVDTRTEILI 556
Cdd:PRK13541 149 EVETNLSKENRDLL 162
|
|
| DO-GTPase2 |
pfam19993 |
Double-GTPase 2; GTPase of a GTPase-centric, NTP-dependent ternary systems. The domain belongs ... |
408-458 |
4.80e-03 |
|
Double-GTPase 2; GTPase of a GTPase-centric, NTP-dependent ternary systems. The domain belongs to a previously unrecognized family of the TRAFAC clade with a conserved glutamate in its Walker B motif.
Pssm-ID: 466247 Cd Length: 227 Bit Score: 38.83 E-value: 4.80e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 488288408 408 EMVAIVGPTGAGKTTLINLLerfYD-ISSGSIK-YDGVDTRDLSREELRAHFS 458
Cdd:pfam19993 1 RVIGIVGPPDAGKTTLLASL---YLlLLRGALAgFSFAGSRTLHAFEEIAHGA 50
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
410-512 |
5.56e-03 |
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50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 37.21 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488288408 410 VAIVGPTGAGKTTLINLLerfydISSGSI--KYDGVdTRDLSREELRAH-FSMVLQDtwlfTGSIYDNIHYGNEQASEEE 486
Cdd:pfam01926 2 VALVGRPNVGKSTLINAL-----TGAKAIvsDYPGT-TRDPNEGRLELKgKQIILVD----TPGLIEGASEGEGLGRAFL 71
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90 100
....*....|....*....|....*..
gi 488288408 487 VIRAAKAA-HVDDFVRKLPEGYQTILN 512
Cdd:pfam01926 72 AIIEADLIlFVVDSEEGITPLDEELLE 98
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| Gmk |
COG0194 |
Guanylate kinase [Nucleotide transport and metabolism]; |
406-452 |
8.28e-03 |
|
Guanylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 439964 Cd Length: 190 Bit Score: 37.74 E-value: 8.28e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 488288408 406 PGEMVAIVGPTGAGKTTLIN-LLERFYDISSgSIKY----------DGVDTRDLSREE 452
Cdd:COG0194 1 RGKLIVLSGPSGAGKTTLVKaLLERDPDLRF-SVSAttrpprpgevDGVDYHFVSREE 57
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| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
407-427 |
8.94e-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: 38.15 E-value: 8.94e-03
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