|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
9-626 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 640.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 9 PRAAKGTAGRLFRLiVEGNTLRLVVVLVAILISAAASVGASVFLESLIDDYIKPlllqdvPVFTGLVHALMGMAVLYLAG 88
Cdd:COG1132 2 SKSPRKLLRRLLRY-LRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAG------GDLSALLLLLLLLLGLALLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 89 LLATYLYNRIMVTVSQRTLKGIRDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFF 168
Cdd:COG1132 75 ALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 169 SMLVMSWQLTIVVLVCVAVMLVMVRVIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLA 248
Cdd:COG1132 155 VLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 249 GSARKANQYANILMPAMNNVGNLQYVVIAIIGGAIALHGGgLTLGAIAAFLQLSKSFTQPISQISQQMNAIVMALAGASR 328
Cdd:COG1132 235 RANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGS-LTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAER 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 329 VFELMDEEPEQDEGyvtlvnakylpdgsltetsertgiwawkhpheNGTTTYTKLTGDVRFFDVDFAYNPDKPILHDITL 408
Cdd:COG1132 314 IFELLDEPPEIPDP--------------------------------PGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 409 YAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQDTNLFTGTVRENIRYGRLDA 488
Cdd:COG1132 362 TIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDA 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 489 TDEEIEVAARLANADEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDTRTESLVQQGMDG 568
Cdd:COG1132 442 TDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALER 521
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 2541161597 569 LMYGRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEELIAQKGVYYQLYTGAFEME 626
Cdd:COG1132 522 LMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYRLQFGEE 579
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
11-621 |
7.25e-155 |
|
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: 462.38 E-value: 7.25e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 11 AAKGTAGRLFRLIVeGNTLRLVVVLVAILISAAASVGASVFLESLIDDYIKPLLLQDVPVFTGlvhalmGMAVLYLAGLL 90
Cdd:COG2274 139 EKPFGLRWFLRLLR-RYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVLAI------GLLLALLFEGL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 91 ATYLYNRIMVTVSQRTLKGIRDTLFSHMQALPIRYFDTHPHGDIMSVYtNDVDTLRQMISQSIPQAMSSVITILAVFFSM 170
Cdd:COG2274 212 LRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 171 LVMSWQLTIVVLVCVAVMLVMVRVIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGS 250
Cdd:COG2274 291 FFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNA 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 251 ARKANQYANILMPAMNNVGNLQYVVIaIIGGAIALHGGGLTLGAIAAFLQLSKSFTQPISQISQQMNAIVMALAGASRVF 330
Cdd:COG2274 371 RFKLRRLSNLLSTLSGLLQQLATVAL-LWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLD 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 331 ELMDEEPEQDEGYVTLVNAKylpdgsltetsertgiwawkhphengtttytkLTGDVRFFDVDFAYNPD-KPILHDITLY 409
Cdd:COG2274 450 DILDLPPEREEGRSKLSLPR--------------------------------LKGDIELENVSFRYPGDsPPVLDNISLT 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 410 AKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQDTNLFTGTVRENIRYGRLDAT 489
Cdd:COG2274 498 IKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDAT 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 490 DEEIEVAARLANADEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDTRTESLVQQGMDGL 569
Cdd:COG2274 578 DEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL 657
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 2541161597 570 MYGRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEELIAQKGVYYQLYTG 621
Cdd:COG2274 658 LKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQ 709
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
31-329 |
3.46e-140 |
|
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: 409.87 E-value: 3.46e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 31 LVVVLVAILISAAASVGASVFLESLIDDYIKPLLLQDVPVFTGLVHALMGMAVLYLAGLLATYLYNRIMVTVSQRTLKGI 110
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 111 RDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVMLV 190
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 191 MVRVIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANQYANILMPAMNNVGN 270
Cdd:cd18547 161 VTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFINN 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2541161597 271 LQYVVIAIIGGAIALHgGGLTLGAIAAFLQLSKSFTQPISQISQQMNAIVMALAGASRV 329
Cdd:cd18547 241 LGYVLVAVVGGLLVIN-GALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
30-623 |
1.61e-133 |
|
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: 402.94 E-value: 1.61e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 30 RLVVVLVAILISAAASVGASVFLESLIDDYI---KPLLLQDVPVFtglvhaLMGMAVLY-LAGLLATYLynriMVTVSQR 105
Cdd:TIGR02203 15 GLVLAGVAMILVAATESTLAALLKPLLDDGFggrDRSVLWWVPLV------VIGLAVLRgICSFVSTYL----LSWVSNK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 106 TLKGIRDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCV 185
Cdd:TIGR02203 85 VVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVML 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 186 AVMLVMVRVIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANQYANILMPAM 265
Cdd:TIGR02203 165 PVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPIT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 266 NNVGNLQYVVIAIIGGAIALhGGGLTLGAIAAFLQLSKSFTQPISQISQQMNAIVMALAGASRVFELMDEEPEQDEGYVT 345
Cdd:TIGR02203 245 QLIASLALAVVLFIALFQAQ-AGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKDTGTRA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 346 LVNAkylpdgsltetsertgiwawkhphengtttytklTGDVRFFDVDFAYNP-DKPILHDITLYAKPGQKLAFVGSTGA 424
Cdd:TIGR02203 324 IERA----------------------------------RGDVEFRNVTFRYPGrDRPALDSISLVIEPGETVALVGRSGS 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 425 GKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQDTNLFTGTVRENIRYGRL-DATDEEIEVAARLANAD 503
Cdd:TIGR02203 370 GKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQ 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 504 EFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDTRTESLVQQGMDGLMYGRTVFVIAHRLS 583
Cdd:TIGR02203 450 DFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLS 529
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2541161597 584 TVRNSNAIMVLEHGRIIERGSHEELIAQKGVYYQLYTGAF 623
Cdd:TIGR02203 530 TIEKADRIVVMDDGRIVERGTHNELLARNGLYAQLHNMQF 569
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
385-613 |
6.53e-121 |
|
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: 357.69 E-value: 6.53e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 385 GDVRFFDVDFAYNPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLG 464
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 465 IVLQDTNLFTGTVRENIRYGRLDATDEEIEVAARLANADEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPV 544
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2541161597 545 MILDEATSSIDTRTESLVQQGMDGLMYGRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEELIAQKG 613
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
31-619 |
1.09e-115 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 357.41 E-value: 1.09e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 31 LVVVLVAILISAAASVGASVFLESLIDDYIKPlllQDVPVFTGLVHALMGMAVLY-LAGLLATYLynriMVTVSQRTLKG 109
Cdd:PRK11176 27 LIVAGVALILNAASDTFMLSLLKPLLDDGFGK---ADRSVLKWMPLVVIGLMILRgITSFISSYC----ISWVSGKVVMT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 110 IRDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDtlrqMISQSIPQAMSSVI----TILAVFFSMLVMSWQLTIVVLVCV 185
Cdd:PRK11176 100 MRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSE----QVASSSSGALITVVregaSIIGLFIMMFYYSWQLSLILIVIA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 186 AVMLVMVRVIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANQYANILMPAM 265
Cdd:PRK11176 176 PIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASSISDPII 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 266 NNVGNLQYVVI---AIIGGAIA-LHGGGLTL--GAIAAFLQLSKSFTQPISQISQQMnaivmalAGASRVFELMDEEPEQ 339
Cdd:PRK11176 256 QLIASLALAFVlyaASFPSVMDtLTAGTITVvfSSMIALMRPLKSLTNVNAQFQRGM-------AACQTLFAILDLEQEK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 340 DEGYVTLVNAKylpdgsltetsertgiwawkhphengtttytkltGDVRFFDVDFAY-NPDKPILHDITLYAKPGQKLAF 418
Cdd:PRK11176 329 DEGKRVIERAK----------------------------------GDIEFRNVTFTYpGKEVPALRNINFKIPAGKTVAL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 419 VGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQDTNLFTGTVRENIRYGRLDA-TDEEIEVAA 497
Cdd:PRK11176 375 VGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAA 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 498 RLANADEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDTRTESLVQQGMDGLMYGRTVFV 577
Cdd:PRK11176 455 RMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLV 534
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 2541161597 578 IAHRLSTVRNSNAIMVLEHGRIIERGSHEELIAQKGVYYQLY 619
Cdd:PRK11176 535 IAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLH 576
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1-618 |
2.05e-114 |
|
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: 354.51 E-value: 2.05e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 1 MNENKKGAPRAAKGTAGRLFRLIVEGNTLRLVVVLVAILISAAASVGASVFLESLIDDYIKPLLLQDVPVFTGLVHALMG 80
Cdd:COG5265 4 ARAMSAPAAPPRLDLLLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALLVVPVGLLLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 81 MAVLYLAGLLATYLYNRIMVTVSQRTLKGIRDTLFSHMQALPIRYfdthpHGD--------IMSVYTNDVDTL-RQMISQ 151
Cdd:COG5265 84 YGLLRLLSVLFGELRDALFARVTQRAVRRLALEVFRHLHALSLRF-----HLErqtgglsrDIERGTKGIEFLlRFLLFN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 152 SIPQ----AMssVITILAVFFSmlvmsWQLTIVVLVCVAV-MLVMVRVIARRsgTFFIQQQTDL-GKLNGY-IEEMI--E 222
Cdd:COG5265 159 ILPTlleiAL--VAGILLVKYD-----WWFALITLVTVVLyIAFTVVVTEWR--TKFRREMNEAdSEANTRaVDSLLnyE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 223 gqkVVKVFCHEQKAKEDFDKLNDTLAGSARKaNQYANilmpAMNNVGnlQYVVIAI------IGGAIALHGGGLTLG--- 293
Cdd:COG5265 230 ---TVKYFGNEAREARRYDEALARYERAAVK-SQTSL----ALLNFG--QALIIALgltammLMAAQGVVAGTMTVGdfv 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 294 AIAAFL-QLsksfTQPIS-------QISQqmnaivmALAGASRVFELMDEEPE-QDEgyvtlVNAKYLPDGSltetsert 364
Cdd:COG5265 300 LVNAYLiQL----YIPLNflgfvyrEIRQ-------ALADMERMFDLLDQPPEvADA-----PDAPPLVVGG-------- 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 365 giwawkhphengtttytkltGDVRFFDVDFAYNPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKI 444
Cdd:COG5265 356 --------------------GEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRI 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 445 RYDGININKIKKSDLRHSLGIVLQDTNLFTGTVRENIRYGRLDATDEEIEVAARLANADEFIRRLPQGYDTMLTDNGASL 524
Cdd:COG5265 416 LIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKL 495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 525 SQGQRQLIAIARAAVADPPVMILDEATSSIDTRTESLVQQGMDGLMYGRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGS 604
Cdd:COG5265 496 SGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGT 575
|
650
....*....|....
gi 2541161597 605 HEELIAQKGVYYQL 618
Cdd:COG5265 576 HAELLAQGGLYAQM 589
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
387-619 |
5.89e-114 |
|
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: 340.36 E-value: 5.89e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 387 VRFFDVDFAYNPDK-PILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGI 465
Cdd:cd03251 1 VEFKNVTFRYPGDGpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 466 VLQDTNLFTGTVRENIRYGRLDATDEEIEVAARLANADEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVM 545
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2541161597 546 ILDEATSSIDTRTESLVQQGMDGLMYGRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEELIAQKGVYYQLY 619
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
30-613 |
8.03e-110 |
|
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: 341.35 E-value: 8.03e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 30 RLVVVLVAI-LISAAASVGASVFLESLIDDyikpLLLQDVPvFTGLVHALMGMAVLYLAGLLATYLYNRIMVTVSQRTLK 108
Cdd:COG4988 17 RWLALAVLLgLLSGLLIIAQAWLLASLLAG----LIIGGAP-LSALLPLLGLLLAVLLLRALLAWLRERAAFRAAARVKR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 109 GIRDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVM 188
Cdd:COG4988 92 RLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLILLVTAPLI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 189 ---LVMVRVIARRSGTffiQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLagsaRKAnqYANILMPAM 265
Cdd:COG4988 172 plfMILVGKGAAKASR---RQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDF----RKR--TMKVLRVAF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 266 NNVGNLQ---YVVIAIIGGAIALH--GGGLTLGAIAAFLQLSKSFTQPISQISQQMNAIVMALAGASRVFELMDEEPEqd 340
Cdd:COG4988 243 LSSAVLEffaSLSIALVAVYIGFRllGGSLTLFAALFVLLLAPEFFLPLRDLGSFYHARANGIAAAEKIFALLDAPEP-- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 341 egyvtlvnakylpdgsltETSERTGIWAWKHPHEngtttytkltgdVRFFDVDFAYNPDKPILHDITLYAKPGQKLAFVG 420
Cdd:COG4988 321 ------------------AAPAGTAPLPAAGPPS------------IELEDVSFSYPGGRPALDGLSLTIPPGERVALVG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 421 STGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQDTNLFTGTVRENIRYGRLDATDEEIEVAARLA 500
Cdd:COG4988 371 PSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAA 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 501 NADEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDTRTESLVQQGMDGLMYGRTVFVIAH 580
Cdd:COG4988 451 GLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITH 530
|
570 580 590
....*....|....*....|....*....|...
gi 2541161597 581 RLSTVRNSNAIMVLEHGRIIERGSHEELIAQKG 613
Cdd:COG4988 531 RLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
387-620 |
1.58e-105 |
|
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: 318.71 E-value: 1.58e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 387 VRFFDVDFAY--NPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLG 464
Cdd:cd03249 1 IEFKNVSFRYpsRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 465 IVLQDTNLFTGTVRENIRYGRLDATDEEIEVAARLANADEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPV 544
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2541161597 545 MILDEATSSIDTRTESLVQQGMDGLMYGRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEELIAQKGVYYQLYT 620
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVK 236
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
387-619 |
7.92e-100 |
|
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: 303.77 E-value: 7.92e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 387 VRFFDVDFAYNPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIV 466
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 467 LQDTNLFTGTVRENIRYGRLDATDEEIEVAARLANADEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMI 546
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2541161597 547 LDEATSSIDTRTESLVQQGMDGLMYGRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEELIAQKGVYYQLY 619
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMW 233
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
115-618 |
2.18e-99 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 314.98 E-value: 2.18e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 115 FSHMQALPIRYFDTHPHGDIMSVYTNDVDTL--------RQMISqsipqAMSSVITILAVFFSMlvmSWQLTIVVLVCVA 186
Cdd:PRK13657 96 FERIIQLPLAWHSQRGSGRALHTLLRGTDALfglwlefmREHLA-----TLVALVVLLPLALFM---NWRLSLVLVVLGI 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 187 VMLVMVRVIARRsgTFFIQQQTD--LGKLNGYIEEMIEGQKVVKVFcheQKAKEDFDKLNDTlagsarkANQYANILMP- 263
Cdd:PRK13657 168 VYTLITTLVMRK--TKDGQAAVEehYHDLFAHVSDAIGNVSVVQSY---NRIEAETQALRDI-------ADNLLAAQMPv 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 264 ----AMNNVGN-----LQYVVIAIIGgaIALHGGG-LTLGAIAAFLQLSKSFTQPISQISQQMNAIVMALAGASRVFELM 333
Cdd:PRK13657 236 lswwALASVLNraastITMLAILVLG--AALVQKGqLRVGEVVAFVGFATLLIGRLDQVVAFINQVFMAAPKLEEFFEVE 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 334 DEEPEQDEGyvtlVNAKYLPDgsltetsertgiwawkhphengtttytkLTGDVRFFDVDFAYNPDKPILHDITLYAKPG 413
Cdd:PRK13657 314 DAVPDVRDP----PGAIDLGR----------------------------VKGAVEFDDVSFSYDNSRQGVEDVSFEAKPG 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 414 QKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQDTNLFTGTVRENIRYGRLDATDEEI 493
Cdd:PRK13657 362 QTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEM 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 494 EVAARLANADEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDTRTESLVQQGMDGLMYGR 573
Cdd:PRK13657 442 RAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGR 521
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2541161597 574 TVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEELIAQKGVYYQL 618
Cdd:PRK13657 522 TTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAAL 566
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
13-618 |
1.71e-98 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 316.28 E-value: 1.71e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 13 KGTAGRLFRLI--VEGNTLRLVVVLVAILISAAASVGASVFLESLIDDyikplLLQDVPVFTgLVHALMGMAVLYLAGLL 90
Cdd:TIGR00958 143 SETADLLFRLLglSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDT-----LGGDKGPPA-LASAIFFMCLLSIASSV 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 91 ATYL----YNRIMVTVSQRtlkgIRDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAV 166
Cdd:TIGR00958 217 SAGLrggsFNYTMARINLR----IREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGL 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 167 FFSMLVMSWQLTIVVLVCVAVMLVMVRVIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVF-CHEQKAKEDFDKLND 245
Cdd:TIGR00958 293 LGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFaAEEGEASRFKEALEE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 246 TLAGSARKAnqYANILMPAMNNV-GNLQYVVIAIIGGAIALHGGgLTLGAIAAFLQLSKSFTQPISQISQQMNAIVMALA 324
Cdd:TIGR00958 373 TLQLNKRKA--LAYAGYLWTTSVlGMLIQVLVLYYGGQLVLTGK-VSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVG 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 325 GASRVFELMDEEPEQdegyvtlvnakylpdgsltetsertgiwawkhPHeNGTTTYTKLTGDVRFFDVDFAY--NPDKPI 402
Cdd:TIGR00958 450 ASEKVFEYLDRKPNI--------------------------------PL-TGTLAPLNLEGLIEFQDVSFSYpnRPDVPV 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 403 LHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQDTNLFTGTVRENIR 482
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIA 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 483 YGRLDATDEEIEVAARLANADEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDTRTESLV 562
Cdd:TIGR00958 577 YGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLL 656
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 2541161597 563 QQGMDglMYGRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEELIAQKGVYYQL 618
Cdd:TIGR00958 657 QESRS--RASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
105-619 |
9.51e-98 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 310.16 E-value: 9.51e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 105 RTLKGIRDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVC 184
Cdd:COG4987 85 RLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALALVLALG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 185 VAVMLVMVRVIARRSGTFFIQQQTDL-GKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANQyANILMP 263
Cdd:COG4987 165 LLLAGLLLPLLAARLGRRAGRRLAAArAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLAR-LSALAQ 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 264 AMNNVGNLQYVVIAIIGGAIALHGGGLTLGAIAAFLQLSKSFTQPISQISQQMNAIVMALAGASRVFELMDEEPEQDEgy 343
Cdd:COG4987 244 ALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDAPPAVTE-- 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 344 vtlvnakylPDGSLTETSErtgiwawkhphengtttytkltGDVRFFDVDFAY-NPDKPILHDITLYAKPGQKLAFVGST 422
Cdd:COG4987 322 ---------PAEPAPAPGG----------------------PSLELEDVSFRYpGAGRPVLDGLSLTLPPGERVAIVGPS 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 423 GAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQDTNLFTGTVRENIRYGRLDATDEEIEVAARLANA 502
Cdd:COG4987 371 GSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGL 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 503 DEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDTRTESLVQQGMDGLMYGRTVFVIAHRL 582
Cdd:COG4987 451 GDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRL 530
|
490 500 510
....*....|....*....|....*....|....*..
gi 2541161597 583 STVRNSNAIMVLEHGRIIERGSHEELIAQKGVYYQLY 619
Cdd:COG4987 531 AGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLY 567
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
387-619 |
6.09e-86 |
|
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: 268.20 E-value: 6.09e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 387 VRFFDVDFAYNPDKP-ILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGI 465
Cdd:cd03252 1 ITFEHVRFRYKPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 466 VLQDTNLFTGTVRENIRYGRLDATDEEIEVAARLANADEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVM 545
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2541161597 546 ILDEATSSIDTRTESLVQQGMDGLMYGRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEELIAQKGVYYQLY 619
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLY 234
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
13-618 |
8.29e-86 |
|
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: 282.60 E-value: 8.29e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 13 KGTAGRLFRLIVEGntlrLVVVLVAILISAAASVGASVFLESLIDDYIKPLLLqdvpvftglvhaLMGMAVLYLAGLlaT 92
Cdd:TIGR03796 150 RGSRGALLYLLLAG----LLLVLPGLVIPAFSQIFVDEILVQGRQDWLRPLLL------------GMGLTALLQGVL--T 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 93 YLYNRIMVTVSQRTLKGIRDTLFSHMQALPIRYFDTHPHGDIMS-VYTNDvdTLRQMISQSIPqamSSVITILAVFFSML 171
Cdd:TIGR03796 212 WLQLYYLRRLEIKLAVGMSARFLWHILRLPVRFFAQRHAGDIASrVQLND--QVAEFLSGQLA---TTALDAVMLVFYAL 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 172 VM---SWQLTIVVLVCVAVMLVMVRVIARRSGTFFIQQQTDLGKLNG-------YIEEM----IEGQKVVKVFCHEQKAK 237
Cdd:TIGR03796 287 LMllyDPVLTLIGIAFAAINVLALQLVSRRRVDANRRLQQDAGKLTGvaisglqSIETLkasgLESDFFSRWAGYQAKLL 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 238 EDFDKLNdtlagsarKANQYANILMPAMNNVGNlqyVVIAIIGGAIALhGGGLTLGAIAAFLQLSKSFTQPISQISQQMN 317
Cdd:TIGR03796 367 NAQQELG--------VLTQILGVLPTLLTSLNS---ALILVVGGLRVM-EGQLTIGMLVAFQSLMSSFLEPVNNLVGFGG 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 318 AIVMALAGASRVFELMDEEPEQDEgyvtlvnakylpdgsltetsERTGIWAWKHPHengtttYTKLTGDVRFFDVDFAYN 397
Cdd:TIGR03796 435 TLQELEGDLNRLDDVLRNPVDPLL--------------------EEPEGSAATSEP------PRRLSGYVELRNITFGYS 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 398 P-DKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQDTNLFTGT 476
Cdd:TIGR03796 489 PlEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGT 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 477 VRENIRYgrLDAT--DEEIEVAARLANADEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSI 554
Cdd:TIGR03796 569 VRDNLTL--WDPTipDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSAL 646
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2541161597 555 DTRTESLVqqgMDGLMY-GRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEELIAQKGVYYQL 618
Cdd:TIGR03796 647 DPETEKII---DDNLRRrGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARL 708
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
15-618 |
3.69e-82 |
|
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: 272.22 E-value: 3.69e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 15 TAGRLFRLIVEGNTLRLVVVLVAILISAAASVGASVFLESLIDDYI----KPLLLQdvpVFTGLVHALMGMAVLYLAGLL 90
Cdd:TIGR03797 122 GLRDLLRFALRGARRDLLAILAMGLLGTLLGMLVPIATGILIGTAIpdadRSLLVQ---IALALLAAAVGAAAFQLAQSL 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 91 ATYlynRIMVTVSQRTLKGIRDTLFShmqaLPIRYFDTHPHGDIMSvYTNDVDTLRQMISQSIpqamssVITILAVFFS- 169
Cdd:TIGR03797 199 AVL---RLETRMDASLQAAVWDRLLR----LPVSFFRQYSTGDLAS-RAMGISQIRRILSGST------LTTLLSGIFAl 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 170 -----MLVMSWQLTIV-VLVCVAVMLVMVrVIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKL 243
Cdd:TIGR03797 265 lnlglMFYYSWKLALVaVALALVAIAVTL-VLGLLQVRKERRLLELSGKISGLTVQLINGISKLRVAGAENRAFARWAKL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 244 NDTLAGSARKANQYANILmpAMNNVGNLQYVVIAIIGGAIALHGG-GLTLGAIAAFLQLSKSFTQPISQISQQMNAIVMA 322
Cdd:TIGR03797 344 FSRQRKLELSAQRIENLL--TVFNAVLPVLTSAALFAAAISLLGGaGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAV 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 323 LAGASRVFELMDEEPEQDEgyvtlvnAKYLPDgsltetsertgiwawkhphengtttytKLTGDVRFFDVDFAYNPDKP- 401
Cdd:TIGR03797 422 IPLWERAKPILEALPEVDE-------AKTDPG---------------------------KLSGAIEVDRVTFRYRPDGPl 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 402 ILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQDTNLFTGTVRENI 481
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENI 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 482 RYGRLDATDEEIEvAARLANADEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDTRTESL 561
Cdd:TIGR03797 548 AGGAPLTLDEAWE-AARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAI 626
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 2541161597 562 VQQGMDGLmyGRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEELIAQKGVYYQL 618
Cdd:TIGR03797 627 VSESLERL--KVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQL 681
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
19-619 |
8.33e-80 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 263.89 E-value: 8.33e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 19 LFRLIVEGNTLR--LVVVLVAILISAAASVGASVFLESLIDDYIK----PLLLqdvpvFTGLVHALMGMAVLylAGLLAT 92
Cdd:PRK10790 11 LKRLLAYGSPWRkpLGLAVLMLWVAAAAEVSGPLLISYFIDNMVAkgnlPLGL-----VAGLAAAYVGLQLL--AAGLHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 93 Y---LYNRIMVTVSQRTLKGIRDTlfshmqAL--PIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVF 167
Cdd:PRK10790 84 AqslLFNRAAVGVVQQLRTDVMDA------ALrqPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAML 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 168 FSMLVMSWQLTIV-VLVCVAVMLVMVrvIARRSGTFFIQQ-QTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFdklnd 245
Cdd:PRK10790 158 VAMFSLDWRMALVaIMIFPAVLVVMV--IYQRYSTPIVRRvRAYLADINDGFNEVINGMSVIQQFRQQARFGERM----- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 246 tlaGSARKANQYANilMPAMNNVGNLQYVVIA-----IIGGAIALHG----GGLTLGAIAAFLQLSKSFTQPISQISQQM 316
Cdd:PRK10790 231 ---GEASRSHYMAR--MQTLRLDGFLLRPLLSlfsalILCGLLMLFGfsasGTIEVGVLYAFISYLGRLNEPLIELTTQQ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 317 NAIVMALAGASRVFELMDEePEQdeGYvtlvnakylpdgsltetsertgiwawkhphenGTTTYTKLTGDVRFFDVDFAY 396
Cdd:PRK10790 306 SMLQQAVVAGERVFELMDG-PRQ--QY--------------------------------GNDDRPLQSGRIDIDNVSFAY 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 397 NPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQDTNLFTGT 476
Cdd:PRK10790 351 RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADT 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 477 VRENIRYGRlDATDEEIEVAARLANADEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDT 556
Cdd:PRK10790 431 FLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDS 509
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2541161597 557 RTESLVQQGMDGLMYGRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEELIAQKGVYYQLY 619
Cdd:PRK10790 510 GTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMY 572
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
129-619 |
1.35e-75 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 251.94 E-value: 1.35e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 129 HPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLV-MSWQLTIVVLVCVAVMLVMVRVIARRSGTFFIQQQ 207
Cdd:PRK10789 90 HRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMSTqISWQLTLLALLPMPVMAIMIKRYGDQLHERFKLAQ 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 208 TDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKL-NDTLAGSARKANQYA----NILMP-AMNNVgnlqyvvIAIIGG 281
Cdd:PRK10789 170 AAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADaEDTGKKNMRVARIDArfdpTIYIAiGMANL-------LAIGGG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 282 AIALHGGGLTLGAIAAFLQLSKSFTQPISQISQQMNAIVMALAGASRVFELMDEEPEQDEGYVTLvnakylpdgsltets 361
Cdd:PRK10789 243 SWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVKDGSEPV--------------- 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 362 ertgiwawkhPHENGTttytkLTGDVRffdvDFAY-NPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIA 440
Cdd:PRK10789 308 ----------PEGRGE-----LDVNIR----QFTYpQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVS 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 441 DGKIRYDGININKIKKSDLRHSLGIVLQDTNLFTGTVRENIRYGRLDATDEEIEVAARLANADEFIRRLPQGYDTMLTDN 520
Cdd:PRK10789 369 EGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGER 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 521 GASLSQGQRQLIAIARAAVADPPVMILDEATSSIDTRTESLVQQGMDGLMYGRTVFVIAHRLSTVRNSNAIMVLEHGRII 600
Cdd:PRK10789 449 GVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIA 528
|
490
....*....|....*....
gi 2541161597 601 ERGSHEELIAQKGVYYQLY 619
Cdd:PRK10789 529 QRGNHDQLAQQSGWYRDMY 547
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
385-604 |
2.31e-74 |
|
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: 237.39 E-value: 2.31e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 385 GDVRFFDVDFAYNPD-KPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSL 463
Cdd:cd03244 1 GDIEFKNVSLRYRPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 464 GIVLQDTNLFTGTVRENirygrLD----ATDEEIEVAARLANADEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAV 539
Cdd:cd03244 81 SIIPQDPVLFSGTIRSN-----LDpfgeYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2541161597 540 ADPPVMILDEATSSIDTRTESLVQQGMDGLMYGRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGS 604
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
19-620 |
9.47e-72 |
|
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: 245.03 E-value: 9.47e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 19 LFRLIVEGNTLRLVVVLVAILISAAaSVGASVFLESLIDDYIKPLLLQDVPVFTglvhalMGMAVLYLAGLLATYLYNRI 98
Cdd:TIGR01193 147 FIPLITRQKKLIVNIVIAAIIVTLI-SIAGSYYLQKIIDTYIPHKMMGTLGIIS------IGLIIAYIIQQILSYIQIFL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 99 MVTVSQRTLKGIRDTLFSHMQALPIRYFDTHPHGDIMSVYTnDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLT 178
Cdd:TIGR01193 220 LNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFT-DASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLF 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 179 IVVLVCVAVMLVMVRVIARRsgtfFIQQQTDLGK----LNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKa 254
Cdd:TIGR01193 299 LLSLLSIPVYAVIIILFKRT----FNKLNHDAMQanavLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFK- 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 255 NQYANILMPAMNNVGNLQYVVIAIIGGAIALHGGGLTLGAIAAFLQLSKSFTQPISQISQQMNAIVMALAGASRVFElmd 334
Cdd:TIGR01193 374 YQKADQGQQAIKAVTKLILNVVILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNE--- 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 335 eepeqdegyVTLVNAKYLPDGSLTETsertgiwawkhphengtttyTKLTGDVRFFDVDFAYNPDKPILHDITLYAKPGQ 414
Cdd:TIGR01193 451 ---------VYLVDSEFINKKKRTEL--------------------NNLNGDIVINDVSYSYGYGSNILSDISLTIKMNS 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 415 KLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQDTNLFTGTVRENIRYG-RLDATDEEI 493
Cdd:TIGR01193 502 KTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEI 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 494 EVAARLANADEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDTRTEslvQQGMDGLMY-- 571
Cdd:TIGR01193 582 WAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITE---KKIVNNLLNlq 658
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 2541161597 572 GRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEELIAQKGVYYQLYT 620
Cdd:TIGR01193 659 DKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIH 707
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
387-598 |
1.60e-68 |
|
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: 220.33 E-value: 1.60e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 387 VRFFDVDFAYNP-DKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGI 465
Cdd:cd03228 1 IEFKNVSFSYPGrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 466 VLQDTNLFTGTVRENIrygrldatdeeievaarlanadefirrlpqgydtmltdngasLSQGQRQLIAIARAAVADPPVM 545
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2541161597 546 ILDEATSSIDTRTESLVQQGMDGLMYGRTVFVIAHRLSTVRNSNAIMVLEHGR 598
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
385-603 |
1.91e-67 |
|
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: 219.38 E-value: 1.91e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 385 GDVRFFDVDFAYNPDK-PILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSL 463
Cdd:cd03245 1 GRIEFRNVSFSYPNQEiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 464 GIVLQDTNLFTGTVRENIRYGRLDATDEEIEVAARLANADEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPP 543
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 544 VMILDEATSSIDTRTESLVQQGMDGLMYGRTVFVIAHRLSTVRNSNAIMVLEHGRIIERG 603
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
31-329 |
1.04e-64 |
|
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: 214.56 E-value: 1.04e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 31 LVVVLVAILISAAASVGASVFLESLIDDYIKPlllqDVPVFTGLVHALMGMAVLYLAGLLATYLYNRIMVTVSQRTLKGI 110
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIVP----GQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 111 RDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVMLV 190
Cdd:cd18544 77 RRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 191 MVRVIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANQYANILMPAMNNVGN 270
Cdd:cd18544 157 ATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSS 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 271 LqyVVIAIIG-GAIALHGGGLTLGAIAAFLQLSKSFTQPISQISQQMNAIVMALAGASRV 329
Cdd:cd18544 237 L--ALALVLWyGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
30-594 |
2.66e-64 |
|
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: 220.62 E-value: 2.66e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 30 RLVVVLVAIL--ISAAASVGASVFLESLIDDyikplLLQDVPVFTGLVHALMGMAVLYLAGLLATYLYNRIMVTVSQRTL 107
Cdd:TIGR02857 2 RRALALLALLgvLGALLIIAQAWLLARVVDG-----LISAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 108 KGIRDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAV 187
Cdd:TIGR02857 77 SQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 188 MLVMVRVIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFcheQKAKEdfdklndTLAGSARKANQYANILMP---- 263
Cdd:TIGR02857 157 IPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLF---GRAKA-------QAAAIRRSSEEYRERTMRvlri 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 264 ------AMNNVGNLQYVVIAI-IGgaIALHGGGLTLGAIAAFLQLSKSFTQPISQISQQMNAIVMALAGASRVFELMDEE 336
Cdd:TIGR02857 227 aflssaVLELFATLSVALVAVyIG--FRLLAGDLDLATGLFVLLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 337 PeqdegyvtlvnAKYLPDGSLTETSERTgiwawkhphengtttytkltgdVRFFDVDFAYNPDKPILHDITLYAKPGQKL 416
Cdd:TIGR02857 305 P-----------RPLAGKAPVTAAPASS----------------------LEFSGVSVAYPGRRPALRPVSFTVPPGERV 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 417 AFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQDTNLFTGTVRENIRYGRLDATDEEIEVA 496
Cdd:TIGR02857 352 ALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREA 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 497 ARLANADEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDTRTESLVQQGMDGLMYGRTVF 576
Cdd:TIGR02857 432 LERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVL 511
|
570
....*....|....*...
gi 2541161597 577 VIAHRLSTVRNSNAIMVL 594
Cdd:TIGR02857 512 LVTHRLALAALADRIVVL 529
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
376-599 |
3.70e-64 |
|
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: 210.79 E-value: 3.70e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 376 GTTTYTKLTGDVRFFDVDFAY--NPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININK 453
Cdd:cd03248 1 GSLAPDHLKGIVKFQNVTFAYptRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 454 IKKSDLRHSLGIVLQDTNLFTGTVRENIRYGRLDATDEEIEVAARLANADEFIRRLPQGYDTMLTDNGASLSQGQRQLIA 533
Cdd:cd03248 81 YEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2541161597 534 IARAAVADPPVMILDEATSSIDTRTESLVQQGMDGLMYGRTVFVIAHRLSTVRNSNAIMVLEHGRI 599
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
30-329 |
3.71e-64 |
|
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: 213.10 E-value: 3.71e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 30 RLVVVLVAILISAAASVGASVFLESLIDDYIKPlllQDVPvftGLVHALMGMAVLYLAGLLATYLYNRIMVTVSQRTLKG 109
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKIAIDEYIPN---GDLS---GLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 110 IRDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVML 189
Cdd:cd18545 75 LRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 190 VMVRVIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANQYANILMPAMNNVG 269
Cdd:cd18545 155 LVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELIS 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 270 NLQYVVIaIIGGAIALHGGGLTLGAIAAFLQLSKSFTQPISQISQQMNAIVMALAGASRV 329
Cdd:cd18545 235 ALGTALV-YWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
31-329 |
1.73e-56 |
|
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: 192.77 E-value: 1.73e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 31 LVVVLVAILISAAASVGASVFLESLIDDYIKPlllqdvPVFTGLVHALMGMAVLYLAGLLATYLYNRIMVTVSQRTLKGI 110
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPA------GDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 111 RDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVMLV 190
Cdd:cd07346 75 RRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 191 MVRVIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANQYANILMPAMNNVGN 270
Cdd:cd07346 155 ILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTA 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2541161597 271 LQYVVIAIIGGAIALHgGGLTLGAIAAFLQLSKSFTQPISQISQQMNAIVMALAGASRV 329
Cdd:cd07346 235 LGTALVLLYGGYLVLQ-GSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
132-582 |
1.63e-54 |
|
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: 194.12 E-value: 1.63e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 132 GDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVMLVMVRVIARRSGTFFIQQQTDL- 210
Cdd:TIGR02868 110 GDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAAGLLLAGFVAPLVSLRAARAAEQALARLr 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 211 GKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANQYANILMPAMNNVGNLQyVVIAIIGGAIALHGGGL 290
Cdd:TIGR02868 190 GELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALGAALTLLAAGLA-VLGALWAGGPAVADGRL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 291 TLGAIAAFLQLSKSFTQPISQISQQMNAIVMALAGASRVFELMDEEPEQDEGyvtlvnakylpdgslteTSERTGIWAWK 370
Cdd:TIGR02868 269 APVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAGPVAEG-----------------SAPAAGAVGLG 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 371 HPhengtttytkltgDVRFFDVDFAYNPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGIN 450
Cdd:TIGR02868 332 KP-------------TLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVP 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 451 INKIKKSDLRHSLGIVLQDTNLFTGTVRENIRYGRLDATDEEIEVAARLANADEFIRRLPQGYDTMLTDNGASLSQGQRQ 530
Cdd:TIGR02868 399 VSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQ 478
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2541161597 531 LIAIARAAVADPPVMILDEATSSIDTRTESLVQQGMDGLMYGRTVFVIAHRL 582
Cdd:TIGR02868 479 RLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
112-618 |
5.71e-54 |
|
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: 199.79 E-value: 5.71e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 112 DTLFSHMQAlPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVMLVM 191
Cdd:TIGR00957 1043 DLLHNKLRS-PMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFV 1121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 192 VRVIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFcheqKAKEDFDKLNDTLAGSARKAnQYANI-----LMPAMN 266
Cdd:TIGR00957 1122 QRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAF----EEQERFIHQSDLKVDENQKA-YYPSIvanrwLAVRLE 1196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 267 NVGNLqYVVIAIIGGAIALHGggLTLGAIAAFLQLSKSFTQPISQISQQMNAIVMALAGASRVFELMDEEPEqdegyvtl 346
Cdd:TIGR00957 1197 CVGNC-IVLFAALFAVISRHS--LSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKE-------- 1265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 347 vnAKYLPDGSLTETSertgiwaWKHphengtttytklTGDVRFFDVDFAYNPD-KPILHDITLYAKPGQKLAFVGSTGAG 425
Cdd:TIGR00957 1266 --APWQIQETAPPSG-------WPP------------RGRVEFRNYCLRYREDlDLVLRHINVTIHGGEKVGIVGRTGAG 1324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 426 KTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQDTNLFTGTVRENIR-YGRLdaTDEEIEVAARLANADE 504
Cdd:TIGR00957 1325 KSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDpFSQY--SDEEVWWALELAHLKT 1402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 505 FIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDTRTESLVQQGMDGLMYGRTVFVIAHRLST 584
Cdd:TIGR00957 1403 FVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNT 1482
|
490 500 510
....*....|....*....|....*....|....
gi 2541161597 585 VRNSNAIMVLEHGRIIERGSHEELIAQKGVYYQL 618
Cdd:TIGR00957 1483 IMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
384-604 |
2.93e-53 |
|
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: 181.07 E-value: 2.93e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 384 TGDVRFFDVDFAYNPDKP-ILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHS 462
Cdd:cd03369 4 HGEIEVENLSVRYAPDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 463 LGIVLQDTNLFTGTVRENI-RYGRLDatDEEIEVAARLanadefirrlpqgydtmlTDNGASLSQGQRQLIAIARAAVAD 541
Cdd:cd03369 84 LTIIPQDPTLFSGTIRSNLdPFDEYS--DEEIYGALRV------------------SEGGLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2541161597 542 PPVMILDEATSSIDTRTESLVQQGMDGLMYGRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGS 604
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
81-611 |
1.61e-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: 189.57 E-value: 1.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 81 MAVLYLAGLLATYLYNRIMVTVSQRTLKGIRDTLFSHMQALPIRYFDTHPHGDImsvytNDVDTLRQMISQSIPQAMS-- 158
Cdd:COG4618 66 ALGLYAVMGLLDAVRSRILVRVGARLDRRLGPRVFDAAFRAALRGGGGAAAQAL-----RDLDTLRQFLTGPGLFALFdl 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 159 --SVITILAVFfsmlVMSWQLTIVVLVCVAVMLV-------MVRVIARRSGTFFIQQqtdlgklNGYIEEMIEGQKVVKV 229
Cdd:COG4618 141 pwAPIFLAVLF----LFHPLLGLLALVGALVLVAlallnerLTRKPLKEANEAAIRA-------NAFAEAALRNAEVIEA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 230 FCHEQKAKEDFDKLNDTLAGSARKANQYANILMpAMNNVgnLQYVV-IAIIG-GA-IALHGGgLTLGA-IAAFLQLSKSF 305
Cdd:COG4618 210 MGMLPALRRRWQRANARALALQARASDRAGGFS-ALSKF--LRLLLqSAVLGlGAyLVIQGE-ITPGAmIAASILMGRAL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 306 tQPISQISQQMNAIVMALAGASRVFELMDEEPEQDEGyvtlvnaKYLPdgsltetsertgiwawkhphengtttytKLTG 385
Cdd:COG4618 286 -APIEQAIGGWKQFVSARQAYRRLNELLAAVPAEPER-------MPLP----------------------------RPKG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 386 DVRFFDVDFAY-NPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLG 464
Cdd:COG4618 330 RLSVENLTVVPpGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 465 IVLQDTNLFTGTVRENI-RYGrlDATDEEIEVAARLANADEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPP 543
Cdd:COG4618 410 YLPQDVELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPR 487
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2541161597 544 VMILDEATSSIDTRTESLVQQGMDGLMY-GRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEELIAQ 611
Cdd:COG4618 488 LVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
131-619 |
2.42e-52 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 189.27 E-value: 2.42e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 131 HGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVMLVMVRVIARRSGTFFIQQQTDL 210
Cdd:PRK11160 116 QGDLLNRLVADVDTLDHLYLRLISPLVAALVVILVLTIGLSFFDLTLALTLGGILLLLLLLLPLLFYRLGKKPGQDLTHL 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 211 -GKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDT-LAGSARKAN-----QYANILMPAMNNVGNLqYVVIAIIGGA- 282
Cdd:PRK11160 196 rAQYRVQLTEWLQGQAELTLFGAEDRYRQQLEQTEQQwLAAQRRQANltglsQALMILANGLTVVLML-WLAAGGVGGNa 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 283 -----IALhgggLTLGAIAAFLQLsksftQPISQISQQMNAIVmalAGASRVFELMDEEPEqdegyVTLvnakylpdgsl 357
Cdd:PRK11160 275 qpgalIAL----FVFAALAAFEAL-----MPVAGAFQHLGQVI---ASARRINEITEQKPE-----VTF----------- 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 358 tetsertgiwawkhpheNGTTTYTKLTGDVRFFDVDFAY-NPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRF 436
Cdd:PRK11160 327 -----------------PTTSTAAADQVSLTLNNVSFTYpDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRA 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 437 YDIADGKIRYDGININKIKKSDLRHSLGIVLQDTNLFTGTVRENIRYGRLDATDEE-IEVAAR-----LANADEfirrlp 510
Cdd:PRK11160 390 WDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEAlIEVLQQvglekLLEDDK------ 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 511 qGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDTRTESLVQQGMDGLMYGRTVFVIAHRLSTVRNSNA 590
Cdd:PRK11160 464 -GLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDR 542
|
490 500
....*....|....*....|....*....
gi 2541161597 591 IMVLEHGRIIERGSHEELIAQKGVYYQLY 619
Cdd:PRK11160 543 ICVMDNGQIIEQGTHQELLAQQGRYYQLK 571
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
399-620 |
1.50e-50 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 184.28 E-value: 1.50e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 399 DKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRF--YDiadGKIRYDGININKIKKSDLRHSLGIVLQDTNLFTGT 476
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpYQ---GSLKINGIELRELDPESWRKHLSWVGQNPQLPHGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 477 VRENIRYGRLDATDEEIEVAARLANADEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDT 556
Cdd:PRK11174 439 LRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2541161597 557 RTESLVQQGMDGLMYGRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEELIAQKGVYYQLYT 620
Cdd:PRK11174 519 HSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLA 582
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
81-611 |
9.53e-50 |
|
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: 181.39 E-value: 9.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 81 MAVLYLAGLLATYLYNRIMVTVSQRTLKGIRDTLFSHMQALPIRyfdthpHGDIMSVYT-NDVDTLRQMISQSIPQAMSS 159
Cdd:TIGR01842 52 ALGLYLFLGLLDALRSFVLVRIGEKLDGALNQPIFAASFSATLR------RGSGDGLQAlRDLDQLRQFLTGPGLFAFFD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 160 ---------VITILAVFFSMLVMswqLTIVVLVCVAVML-VMVRVIARRSGTFFIQQQTDLGKLNGYIEemiegqkVVKV 229
Cdd:TIGR01842 126 apwmpiyllVCFLLHPWIGILAL---GGAVVLVGLALLNnRATKKPLKEATEASIRANNLADSALRNAE-------VIEA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 230 FCHEQKAKEDFDKLNDTLAGSARKANQYANILMPAMNNVGNLQYVVIAIIGGAIALHGGgLTLGAIAAFLQLSKSFTQPI 309
Cdd:TIGR01842 196 MGMMGNLTKRWGRFHSKYLSAQSAASDRAGMLSNLSKYFRIVLQSLVLGLGAYLAIDGE-ITPGMMIAGSILVGRALAPI 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 310 SQISQQMNAIVMALAGASRVFELMDEEPEQD--------EGYVTLVNAKYLPDGsltetsertgiwawkhphengtttyt 381
Cdd:TIGR01842 275 DGAIGGWKQFSGARQAYKRLNELLANYPSRDpamplpepEGHLSVENVTIVPPG-------------------------- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 382 kltgdvrffdvdfaynPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRH 461
Cdd:TIGR01842 329 ----------------GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 462 SLGIVLQDTNLFTGTVRENI-RYGRlDATDEEIEVAARLANADEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVA 540
Cdd:TIGR01842 393 HIGYLPQDVELFPGTVAENIaRFGE-NADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYG 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2541161597 541 DPPVMILDEATSSIDTRTESLVQQGMDGL-MYGRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEELIAQ 611
Cdd:TIGR01842 472 DPKLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
383-612 |
8.98e-49 |
|
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: 170.86 E-value: 8.98e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 383 LTGDVRFFDVDFAY-NPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRH 461
Cdd:cd03288 16 LGGEIKIHDLCVRYeNNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 462 SLGIVLQDTNLFTGTVRENIRYGRlDATDEEIEVAARLANADEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVAD 541
Cdd:cd03288 96 RLSIILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2541161597 542 PPVMILDEATSSIDTRTESLVQQGMDGLMYGRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEELIAQK 612
Cdd:cd03288 175 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQE 245
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
31-329 |
1.27e-48 |
|
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: 171.54 E-value: 1.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 31 LVVVLVAILISAAASVGASVFLESLIDDYIKPLLLQdvPVFTGLVHALMGMAVLYLAGLLATYLYNRIMVTVSQRTLKGI 110
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDVLIQLGPG--GNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 111 RDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVMLV 190
Cdd:cd18563 79 RRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 191 MVRVIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANQYANILMPAMNNVGN 270
Cdd:cd18563 159 GSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTS 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2541161597 271 LQYVVIAIIGGaIALHGGGLTLGAIAAFLQLSKSFTQPISQISQQMNAIVMALAGASRV 329
Cdd:cd18563 239 LGTLIVWYFGG-RQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
31-329 |
8.12e-48 |
|
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: 169.53 E-value: 8.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 31 LVVVLVAILISAAASVGASVFLESLIDDYIKPLLLQdvpvftGLVHALMGMAVLYLAGLLATYLYNRIMVTVSQRTLKGI 110
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRE------LLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 111 RDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVMLV 190
Cdd:cd18542 75 RNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 191 MVRVIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANQYANILMPAMNNVGN 270
Cdd:cd18542 155 FSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSG 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2541161597 271 LQYVVIAIIGGAIALHgGGLTLGAIAAFLQLSKSFTQPISQISQQMNAIVMALAGASRV 329
Cdd:cd18542 235 LQIVLVLWVGGYLVIN-GEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
31-309 |
1.20e-46 |
|
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: 165.51 E-value: 1.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 31 LVVVLVAILISAAASVGASVFLESLIDDYIKplllQDVPVFTGLVHALMGMAVLYLAGLLATYLYNRIMVTVSQRTLKGI 110
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLP----DGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 111 RDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVMLV 190
Cdd:pfam00664 77 RRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 191 MVRVIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANQYANILMPAMNNVGN 270
Cdd:pfam00664 157 VSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGY 236
|
250 260 270
....*....|....*....|....*....|....*....
gi 2541161597 271 LQYVVIAIIGGAIaLHGGGLTLGAIAAFLQLSKSFTQPI 309
Cdd:pfam00664 237 LSYALALWFGAYL-VISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
69-613 |
1.50e-46 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 177.48 E-value: 1.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 69 PVFTGLVHALMGMavlylaGLLATYLYNRI-MVTVSQRTLKGIRDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQ 147
Cdd:PLN03232 949 PGFYIVVYALLGF------GQVAVTFTNSFwLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDR 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 148 MISQSIPQAMSSVITILAVFFSMLVMSwqlTIVVLvcvAVMLVMVRVIArrsgTFFIQQQT--DLGKLNGYIEEMIEGQk 225
Cdd:PLN03232 1023 NVANLMNMFMNQLWQLLSTFALIGTVS---TISLW---AIMPLLILFYA----AYLYYQSTsrEVRRLDSVTRSPIYAQ- 1091
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 226 vvkvfcheqkakedF-DKLNDTLAGSARKA-NQYANILMPAMNNvgNLQYVVIAIIGG---AIALHG-GGLTLGAIAAFL 299
Cdd:PLN03232 1092 --------------FgEALNGLSSIRAYKAyDRMAKINGKSMDN--NIRFTLANTSSNrwlTIRLETlGGVMIWLTATFA 1155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 300 QLSKSFTQPISQISQQMNaivMALAGASRVFELMDEEPEQDEGYVTLVNAKYLPDGSLTETSERTGIwawkhPHENGTTT 379
Cdd:PLN03232 1156 VLRNGNAENQAGFASTMG---LLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAI-----IENNRPVS 1227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 380 YTKLTGDVRFFDVDFAYNPD-KPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSD 458
Cdd:PLN03232 1228 GWPSRGSIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTD 1307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 459 LRHSLGIVLQDTNLFTGTVRENIRYGRlDATDEEIEVAARLANADEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAA 538
Cdd:PLN03232 1308 LRRVLSIIPQSPVLFSGTVRFNIDPFS-EHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARAL 1386
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2541161597 539 VADPPVMILDEATSSIDTRTESLVQQGMDGLMYGRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEELIAQKG 613
Cdd:PLN03232 1387 LRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
31-329 |
3.73e-46 |
|
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: 164.90 E-value: 3.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 31 LVVVLVAILISAAASVGASVFLESLIDDyikpllLQDVPVFTGLVHALMGMAVLYLAGLLATYLYNRIMVTVSQRTLKGI 110
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDD------IFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 111 RDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVMLV 190
Cdd:cd18552 75 RNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 191 MVRVIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANQYANILMPAMNNVGn 270
Cdd:cd18552 155 PIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLG- 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2541161597 271 lqYVVIAII---GGAIALHgGGLTLGA----IAAFLQLsksfTQPISQISQQMNAIVMALAGASRV 329
Cdd:cd18552 234 --AIAIALVlwyGGYQVIS-GELTPGEfisfITALLLL----YQPIKRLSNVNANLQRGLAAAERI 292
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
383-615 |
1.62e-45 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 174.06 E-value: 1.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 383 LTGDVRFFDVDFAY--NPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIAD------------------- 441
Cdd:PTZ00265 1162 IKGKIEIMDVNFRYisRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNdhhivfknehtndmtneqd 1241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 442 -----------------------------------GKIRYDGININKIKKSDLRHSLGIVLQDTNLFTGTVRENIRYGRL 486
Cdd:PTZ00265 1242 yqgdeeqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKE 1321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 487 DATDEEIEVAARLANADEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDTRTESLVQQGM 566
Cdd:PTZ00265 1322 DATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1401
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2541161597 567 DGL--MYGRTVFVIAHRLSTVRNSNAIMVLEH----GRIIE-RGSHEELI-AQKGVY 615
Cdd:PTZ00265 1402 VDIkdKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLsVQDGVY 1458
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
31-329 |
1.75e-45 |
|
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: 163.09 E-value: 1.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 31 LVVVLVAILISAAASVGASVFLESLIDD-YIKPlllQDVPVFTGLVhalMGMAVLYLAGLLATYLYNRIMVTVSQRTLKG 109
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLvTIGS---KSLGLLLGLA---LLLLGAYLLRALLNFLRIYLNHVAEQKVVAD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 110 IRDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVML 189
Cdd:cd18778 75 LRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 190 VMVRVIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANQYANILMPAMNNVG 269
Cdd:cd18778 155 LGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLT 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 270 NLQYVVIAIIGGAIALHgGGLTLGAIAAFLQLSKSFTQPISQISQQMNAIVMALAGASRV 329
Cdd:cd18778 235 SLGTVLVLGFGGRLVLA-GELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
31-329 |
2.81e-43 |
|
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: 156.88 E-value: 2.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 31 LVVVLVAILISAAASVGASVFLESLIDDYIKPlllQDVPVftgLVHALMGMAVLYLAGLLATYLYNRIMVTVSQRTLKGI 110
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDSGVRA---GDLGV---LLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 111 RDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVMLV 190
Cdd:cd18546 75 RLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 191 MVRVIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANQYANILMPAMNNVGN 270
Cdd:cd18546 155 ATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGN 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2541161597 271 LQYVVIAIIGGAIALHgGGLTLGAIAAFLQLSKSFTQPISQISQQMNAIVMALAGASRV 329
Cdd:cd18546 235 LATAAVLLVGAWRVAA-GTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
384-613 |
1.15e-42 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 165.68 E-value: 1.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 384 TGDVRFFDVDFAYNPD-KPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHS 462
Cdd:PLN03130 1235 SGSIKFEDVVLRYRPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKV 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 463 LGIVLQDTNLFTGTVRENirygrLDA----TDEEIEVAARLANADEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAA 538
Cdd:PLN03130 1315 LGIIPQAPVLFSGTVRFN-----LDPfnehNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARAL 1389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2541161597 539 VADPPVMILDEATSSIDTRTESLVQQGMDGLMYGRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEELIAQKG 613
Cdd:PLN03130 1390 LRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
31-329 |
3.10e-42 |
|
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: 154.13 E-value: 3.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 31 LVVVLVAILISAAASVGASVFLESLIDDyikplllqdvpVFTGLVHA--LMGMAVLYLAGLLATYLYNRIMVTVSQRTLK 108
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDA-----------LSAGGSSGglLALLVALFLLQAVLSALSSYLLGRTGERVVL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 109 GIRDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVM 188
Cdd:cd18551 70 DLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 189 LVMVRVIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANQYANILMPAMNNV 268
Cdd:cd18551 150 FLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLA 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2541161597 269 gnLQYVVIAIIG-GAIALHGGGLTLGAIAAFL----QLsksfTQPISQISQQMNAIVMALAGASRV 329
Cdd:cd18551 230 --VQLALLVVLGvGGARVASGALTVGTLVAFLlylfQL----ITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
31-299 |
2.23e-40 |
|
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: 149.10 E-value: 2.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 31 LVVVLVAILISAAASVGASVFLESLIDDYIKPLLLQDvpvftGLVHALMGMAVLYLAGLLATYLYNRIMVTVSQRTLKGI 110
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGTLTAS-----QLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 111 RDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVMLV 190
Cdd:cd18541 76 RNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 191 MVRVIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANQYANILMPAMNNVGN 270
Cdd:cd18541 156 LVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIG 235
|
250 260
....*....|....*....|....*....
gi 2541161597 271 LQYVVIAIIGGAIALHgGGLTLGAIAAFL 299
Cdd:cd18541 236 LSFLIVLWYGGRLVIR-GTITLGDLVAFN 263
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
391-612 |
3.35e-40 |
|
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: 146.32 E-value: 3.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 391 DVDFAYNPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQ-- 468
Cdd:COG1122 5 NLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLVFQnp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 469 DTNLFTGTVRENIRYG--RLDATDEEIEV----AARLANADEFIRRLPQgydtmltdngaSLSQGQRQLIAIARAAVADP 542
Cdd:COG1122 85 DDQLFAPTVEEDVAFGpeNLGLPREEIRErveeALELVGLEHLADRPPH-----------ELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2541161597 543 PVMILDEATSSIDTRTESLVQQGMDGL-MYGRTVFVIAHRLSTV-RNSNAIMVLEHGRIIERGSHEELIAQK 612
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
31-314 |
4.59e-38 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 142.62 E-value: 4.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 31 LVVVLVAILISAAASVGASVFLESLIDDYIkplLLQDVPVFTGLVHALMGMAVLY-LAGLLATYLYNRImvtvSQRTLKG 109
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDAL---PQGDLGLLVLLALGMVAVAVASaLLGVVQTYLSARI----GQGVMYD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 110 IRDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVML 189
Cdd:cd18550 74 LRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 190 VMVRVIARRSGTFFIQQQTDLGKLNGYIEEM--IEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANQYANILMPAMNN 267
Cdd:cd18550 154 LPTRRVGRRRRKLTREQQEKLAELNSIMQETlsVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGL 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2541161597 268 VGNLQYVVIAIIGGAIALHgGGLTLGAIAAFLQLSKSFTQPISQISQ 314
Cdd:cd18550 234 FTAIGPALVYWVGGLLVIG-GGLTIGTLVAFTALLGRLYGPLTQLLN 279
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
31-329 |
5.68e-38 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 142.65 E-value: 5.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 31 LVVVLVAILISAAASVGASVFLESLIDDYIKPLLLQDVPVFTGL-----VHAL----MGMAVLYLAGLLATYLYNRIMVT 101
Cdd:cd18564 1 LALALLALLLETALRLLEPWPLKVVIDDVLGDKPLPGLLGLAPLlgpdpLALLllaaAALVGIALLRGLASYAGTYLTAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 102 VSQRTLKGIRDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVV 181
Cdd:cd18564 81 VGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 182 LVCVAVMLVMVRVIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANQYANIL 261
Cdd:cd18564 161 LAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQALL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2541161597 262 MPAMNnvgnlqyVVIAIIGGAIALHG------GGLTLGAIAAFLQLSKSFTQPISQISQQMNAIVMALAGASRV 329
Cdd:cd18564 241 SPVVD-------VLVAVGTALVLWFGawlvlaGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
403-552 |
2.69e-37 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 135.85 E-value: 2.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 403 LHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQDTNLFTG-TVRENI 481
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2541161597 482 RYGRLDATDEEIEVAARlanADEFIRRLPQGY--DTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATS 552
Cdd:pfam00005 81 RLGLLLKGLSKREKDAR---AEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
387-608 |
1.98e-36 |
|
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: 136.16 E-value: 1.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 387 VRFFDVDFAYNpDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDI-----ADGKIRYDGININKIKKSD--L 459
Cdd:cd03260 1 IELRDLNVYYG-DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVleL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 460 RHSLGIVLQDTNLFTGTVRENIRYG-RL------DATDEEIEVAARLAN-ADEFIRRLpqgydtmltdNGASLSQGQRQL 531
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGlRLhgiklkEELDERVEEALRKAAlWDEVKDRL----------HALGLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2541161597 532 IAIARAAVADPPVMILDEATSSIDTRTESLVQQGMDGLMYGRTVFVIAHRLSTV-RNSNAIMVLEHGRIIERGSHEEL 608
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAaRVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
31-329 |
8.74e-36 |
|
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: 136.07 E-value: 8.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 31 LVVVLVAILISAAASVGASVFLESLIDDyikPLLLQDvpvFTGLVHALMGMAVLYLAGLLATYLYNRIMVTVSQRTLKGI 110
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDG---PIAHGD---RSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 111 RDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQsIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVMLV 190
Cdd:cd18543 75 RTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAF-GPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 191 MVRVIARRSG--TFFIQQQTdlGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANQYANILMPAMNNV 268
Cdd:cd18543 154 VARRFRRRYFpaSRRAQDQA--GDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEAL 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2541161597 269 GNLQYVVIAIIGGAIALHgGGLTLGAIAAFLQLSKSFTQPISQISQQMNAIVMALAGASRV 329
Cdd:cd18543 232 PELGLAAVLALGGWLVAN-GSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
70-604 |
6.66e-35 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 141.71 E-value: 6.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 70 VFTGLVHALMGMAVLYLAGLLATylynRIMVTVSQRTLKGIrdtLFSHMQalpirYFDTHPHgdimSVYTNDVDTLRQMI 149
Cdd:PTZ00265 104 VLIGIFQFILSFISSFCMDVVTT----KILKTLKLEFLKSV---FYQDGQ-----FHDNNPG----SKLTSDLDFYLEQV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 150 SQSIPQAMSSVIT----ILAVFFSMLVMSWQLTIVVlVCVAVMLVMVRVIARRSGTffIQQQTDLGKLN---GYIEEMIE 222
Cdd:PTZ00265 168 NAGIGTKFITIFTyasaFLGLYIWSLFKNARLTLCI-TCVFPLIYICGVICNKKVK--INKKTSLLYNNntmSIIEEALV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 223 GQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANQYANILMPAMNNVGNLQY---------VVIAIIGGAIA---LHGGG- 289
Cdd:PTZ00265 245 GIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLHIGMINGFILASYafgfwygtrIIISDLSNQQPnndFHGGSv 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 290 --LTLGAIAAFLQLsksfTQPISQISQQMNAivmaLAGASRVFELMDEEP---EQDEGyvtlvnaKYLPDgsltetsert 364
Cdd:PTZ00265 325 isILLGVLISMFML----TIILPNITEYMKS----LEATNSLYEIINRKPlveNNDDG-------KKLKD---------- 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 365 giwawkhphengtttytklTGDVRFFDVDFAYN--PDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADG 442
Cdd:PTZ00265 380 -------------------IKKIQFKNVRFHYDtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEG 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 443 KIRY-DGININKIKKSDLRHSLGIVLQDTNLFTGTVRENIRYG-----RLDATDEEIEVAARLANAD------------- 503
Cdd:PTZ00265 441 DIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkDLEALSNYYNEDGNDSQENknkrnscrakcag 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 504 ---------------------------------------EFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPV 544
Cdd:PTZ00265 521 dlndmsnttdsneliemrknyqtikdsevvdvskkvlihDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKI 600
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2541161597 545 MILDEATSSIDTRTESLVQQGMDGLM--YGRTVFVIAHRLSTVRNSNAIMVLEHGriiERGS 604
Cdd:PTZ00265 601 LILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSNR---ERGS 659
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
398-611 |
1.05e-34 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 138.11 E-value: 1.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 398 PDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSD---LRHSLGIVLQDTN--L 472
Cdd:COG1123 276 GGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlreLRRRVQMVFQDPYssL 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 473 FTG-TVRENIRYG-RLDATDEEIEVAARLANA-------DEFIRRLPqgydtmltdngASLSQGQRQLIAIARAAVADPP 543
Cdd:COG1123 356 NPRmTVGDIIAEPlRLHGLLSRAERRERVAELlervglpPDLADRYP-----------HELSGGQRQRVAIARALALEPK 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2541161597 544 VMILDEATSSIDTRteslVQQGMDGLM------YGRTVFVIAHRLSTVRN-SNAIMVLEHGRIIERGSHEELIAQ 611
Cdd:COG1123 425 LLILDEPTSALDVS----VQAQILNLLrdlqreLGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
70-329 |
1.23e-34 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 133.46 E-value: 1.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 70 VFTGLVhalmgMAVLYLAGLLATYLYNRIMVTVSQRTLKGIRDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMI 149
Cdd:cd18565 54 WLLGGL-----TVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 150 SQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVMLVMVRVIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKV 229
Cdd:cd18565 129 DDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 230 FCHEQKAKEDFDKLNDTLAGSARKANQYANILMPAMNNVGNLQYVVIAIIGGAIALHG-----GGLTLGAIAAFLQLSKS 304
Cdd:cd18565 209 FTAEDFERERVADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVLDGpplftGTLTVGTLVTFLFYTQR 288
|
250 260
....*....|....*....|....*
gi 2541161597 305 FTQPISQISQQMNAIVMALAGASRV 329
Cdd:cd18565 289 LLWPLTRLGDLIDQYQRAMASAKRV 313
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
31-329 |
5.50e-34 |
|
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: 131.03 E-value: 5.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 31 LVVVLVAILISAAASVGASVFLESLIDDYIkplLLQDvpvFTGLVHALMGMAVLYLAGLLATYLYNRIMVTVSQRTLKGI 110
Cdd:cd18570 4 LILILLLSLLITLLGIAGSFFFQILIDDII---PSGD---INLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 111 RDTLFSHMQALPIRYFDTHPHGDIMSVYtNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVMLV 190
Cdd:cd18570 78 ILGYFKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 191 MVRVIARRsgtfFIQQQTDL----GKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANQYANILMPAMN 266
Cdd:cd18570 157 IILLFNKP----FKKKNREVmesnAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKG 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2541161597 267 NVGNLQYVVIAIIGGAIALHgGGLTLGAIAAFLQLSKSFTQPISQISQQMNAIVMALAGASRV 329
Cdd:cd18570 233 LISLIGSLLILWIGSYLVIK-GQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
31-329 |
5.59e-34 |
|
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: 130.98 E-value: 5.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 31 LVVVLVAILISAAASVGASVFLESLIDDYIKPLLLQDVpVFTGLVhalmgMAVLYLAGLLATYLYNRIMVTVSQRTLKGI 110
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYI-LRTGLL-----MLLLALLGLIAGILAGYFAAKASQGFGRDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 111 RDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVMLV 190
Cdd:cd18548 75 RKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 191 MVRVIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANQYANILMPAMNNVGN 270
Cdd:cd18548 155 VVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMN 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 271 LqyVVIAIIG-GAIALHGGGLTLGAIAAFLQLSKSFTQPISQISQQMNAIVMALAGASRV 329
Cdd:cd18548 235 L--AIVAILWfGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKRI 292
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
391-599 |
8.07e-34 |
|
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: 126.95 E-value: 8.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 391 DVDFAY-NPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQD 469
Cdd:cd03246 5 NVSFRYpGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 470 TNLFTGTVRENIrygrldatdeeievaarlanadefirrlpqgydtmltdngasLSQGQRQLIAIARAAVADPPVMILDE 549
Cdd:cd03246 85 DELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2541161597 550 ATSSIDTRTESLVQQGMDGL-MYGRTVFVIAHRLSTVRNSNAIMVLEHGRI 599
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
35-329 |
1.09e-33 |
|
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: 130.30 E-value: 1.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 35 LVAILISAAASVGASVFLESLIDDyikplllqdvpVFTGLVHALMGMAVLYLAGLLA-----TYLYNRIMVTVSQRTLKG 109
Cdd:cd18576 2 LILLLLSSAIGLVFPLLAGQLIDA-----------ALGGGDTASLNQIALLLLGLFLlqavfSFFRIYLFARVGERVVAD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 110 IRDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVML 189
Cdd:cd18576 71 LRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 190 VMVRVIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANQYANILMPAMNNVG 269
Cdd:cd18576 151 LVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLL 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 270 NLQYVVIAIIGGAIALHgGGLTLGAIAAFLQLSKSFTQPISQISQQMNAIVMALAGASRV 329
Cdd:cd18576 231 FGAIVAVLWYGGRLVLA-GELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
387-603 |
2.12e-33 |
|
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: 125.89 E-value: 2.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 387 VRFFDVDFAYNP-DKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSdLRHSLGI 465
Cdd:cd03247 1 LSINNVSFSYPEqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 466 VLQDTNLFTGTVRENIrygrldatdeeievaarlanadefirrlpqgydtmltdnGASLSQGQRQLIAIARAAVADPPVM 545
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2541161597 546 ILDEATSSIDTRTESLVQQGMDGLMYGRTVFVIAHRLSTVRNSNAIMVLEHGRIIERG 603
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
391-613 |
5.09e-33 |
|
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: 126.90 E-value: 5.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 391 DVDFAYNpDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGINInKIKKSDLRHSLGIVLQDT 470
Cdd:COG4555 6 NLSKKYG-KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDV-RKEPREARRQIGVLPDER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 471 NLFTG-TVRENIRY-GRL-DATDEEIEvaarlANADEFIRRLpqGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMIL 547
Cdd:COG4555 84 GLYDRlTVRENIRYfAELyGLFDEELK-----KRIEELIELL--GLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2541161597 548 DEATSSIDTRTESLVQQGMDGLM-YGRTVFVIAHRLSTVRN-SNAIMVLEHGRIIERGSHEELIAQKG 613
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
123-609 |
8.32e-33 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 135.29 E-value: 8.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 123 IRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAvffSMLVMSWQLTIVVLVCVAVMLVMVRVI-----AR 197
Cdd:PTZ00243 1046 MSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICS---SILVTSASQPFVLVALVPCGYLYYRLMqfynsAN 1122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 198 RSgtffIQQQTDLGK--LNGYIEEMIEGQKVVKVFcHEQKA--KEDFDKLNDTLAGSARK--ANQYANILMPAMNNVGNL 271
Cdd:PTZ00243 1123 RE----IRRIKSVAKspVFTLLEEALQGSATITAY-GKAHLvmQEALRRLDVVYSCSYLEnvANRWLGVRVEFLSNIVVT 1197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 272 QYVVIAIIGGAiaLHGGGLTLGAIAAFLQLSKSFTQPISQISQQMNAIVMALAGASRVFELMDE-----EPEQDEGYVTL 346
Cdd:PTZ00243 1198 VIALIGVIGTM--LRATSQEIGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTDEvphedMPELDEEVDAL 1275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 347 VNAKYLPdgsltetSERTGIWAWKHPHENGTTTYTKLTGDVRFFDVDFAYNPDKP-ILHDITLYAKPGQKLAFVGSTGAG 425
Cdd:PTZ00243 1276 ERRTGMA-------ADVTGTVVIEPASPTSAAPHPVQAGSLVFEGVQMRYREGLPlVLRGVSFRIAPREKVGIVGRTGSG 1348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 426 KTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQDTNLFTGTVRENIRyGRLDATDEEIEVAARLANADEF 505
Cdd:PTZ00243 1349 KSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVD-PFLEASSAEVWAALELVGLRER 1427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 506 IRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMIL-DEATSSIDTRTESLVQQGMDGLMYGRTVFVIAHRLST 584
Cdd:PTZ00243 1428 VASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHT 1507
|
490 500
....*....|....*....|....*
gi 2541161597 585 VRNSNAIMVLEHGRIIERGSHEELI 609
Cdd:PTZ00243 1508 VAQYDKIIVMDHGAVAEMGSPRELV 1532
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
30-329 |
1.52e-32 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 127.21 E-value: 1.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 30 RLVVVLVAILISAAASVGASVFLESLIDDYIKPLLLQDVPVFTGLVHALMGMAVLylagllATYLYNRIMVTVSQRTLKG 109
Cdd:cd18540 3 LLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQAL------SVFLFIRLAGKIEMGVSYD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 110 IRDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVML 189
Cdd:cd18540 77 LRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 190 VMVRVIARRsgtfFIQQQTDLGKLNGYI----EEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANQYANILMPAM 265
Cdd:cd18540 157 VVSIYFQKK----ILKAYRKVRKINSRItgafNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIV 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2541161597 266 NNVGnlqYVVIAII---GGAIALhGGGLTLGAIAAFLQLSKSFTQPISQISQQMNAIVMALAGASRV 329
Cdd:cd18540 233 LFLG---SIATALVlwyGGILVL-AGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
391-598 |
3.05e-32 |
|
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: 123.73 E-value: 3.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 391 DVDFAYNP-DKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQD 469
Cdd:cd03225 4 NLSFSYPDgARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 470 TN--LFTGTVRENIRYGRLDATDEEIEVAARLANA------DEFIRRLPQgydtmltdngaSLSQGQRQLIAIARAAVAD 541
Cdd:cd03225 84 PDdqFFGPTVEEEVAFGLENLGLPEEEIEERVEEAlelvglEGLRDRSPF-----------TLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2541161597 542 PPVMILDEATSSIDTRT--------ESLVQQGMdglmygrTVFVIAHRLSTVRN-SNAIMVLEHGR 598
Cdd:cd03225 153 PDILLLDEPTAGLDPAGrrellellKKLKAEGK-------TIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
401-603 |
4.05e-32 |
|
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: 123.77 E-value: 4.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 401 PILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDL---RHSLGIVLQD--TNL-FT 474
Cdd:cd03257 19 KALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirRKEIQMVFQDpmSSLnPR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 475 GTVRENIR-----YGRLDATDEEIEVAARLA----NADEFIRRLPqgydtmltdngASLSQGQRQLIAIARAAVADPPVM 545
Cdd:cd03257 99 MTIGEQIAeplriHGKLSKKEARKEAVLLLLvgvgLPEEVLNRYP-----------HELSGGQRQRVAIARALALNPKLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2541161597 546 ILDEATSSIDTRTESLVQQGMDGL--MYGRTVFVIAHRLSTVRN-SNAIMVLEHGRIIERG 603
Cdd:cd03257 168 IADEPTSALDVSVQAQILDLLKKLqeELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
399-611 |
2.59e-31 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 121.71 E-value: 2.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 399 DKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKiKKSDLRHSLGIVLQDTNLFTG-TV 477
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYVPQEPALYPDlTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 478 RENIRY-GRLDATDEEiEVAARlanADEFIRRLpqGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSID- 555
Cdd:COG1131 91 RENLRFfARLYGLPRK-EARER---IDELLELF--GLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDp 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2541161597 556 -TRTE------SLVQQGMdglmygrTVFVIAHRLSTV-RNSNAIMVLEHGRIIERGSHEELIAQ 611
Cdd:COG1131 165 eARRElwellrELAAEGK-------TVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
387-601 |
4.10e-31 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 120.93 E-value: 4.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 387 VRFFDVDFAYNPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSD---LRHSL 463
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 464 GIVLQDTNLFTG-TVRENIRYGrLDATDEEIEVAARLANA-------DEFIRRLPqgydtmltdngASLSQGQRQLIAIA 535
Cdd:COG2884 82 GVVFQDFRLLPDrTVYENVALP-LRVTGKSRKEIRRRVREvldlvglSDKAKALP-----------HELSGGEQQRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2541161597 536 RAAVADPPVMILDEATSSIDTRT--------ESLVQQGMdglmygrTVFVIAHRLSTVRNSNA-IMVLEHGRIIE 601
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETsweimellEEINRRGT-------TVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
31-328 |
5.41e-31 |
|
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: 122.56 E-value: 5.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 31 LVVVLVAILISAAASVGASVFLESLIDDYIKPLLLQDVPVFTGLvhalmgMAVLYLAGLLATYLYNRIMVTVSQRTLKGI 110
Cdd:cd18549 4 FFLDLFCAVLIAALDLVFPLIVRYIIDDLLPSKNLRLILIIGAI------LLALYILRTLLNYFVTYWGHVMGARIETDM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 111 RDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVMLV 190
Cdd:cd18549 78 RRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALLPLMII 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 191 MVRVIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANQYANILMPAMNNVGN 270
Cdd:cd18549 158 FTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMNFFTN 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2541161597 271 LQYVVIaIIGGAIALHGGGLTLGAIAAFLQLSKSFTQPISQISQQMNAIVMALAGASR 328
Cdd:cd18549 238 LLNLVV-LVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQKGMAGFER 294
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
387-610 |
1.10e-30 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 120.48 E-value: 1.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 387 VRFFDVDFAYNPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIV 466
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 467 LQDTNLFTG-TVRENIrygRLDATDEEIEVAARLANADEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVM 545
Cdd:cd03295 81 IQQIGLFPHmTVEENI---ALVPKLLKWPKEKIRERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2541161597 546 ILDEATSSIDTRTESLVQQGMDGL--MYGRTVFVIAHRL-STVRNSNAIMVLEHGRIIERGSHEELIA 610
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLqqELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
388-598 |
3.39e-29 |
|
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: 113.49 E-value: 3.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 388 RFFDVDFAYNpDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVL 467
Cdd:cd00267 1 EIENLSFRYG-GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 468 QdtnlftgtvrenirygrldatdeeievaarlanadefirrlpqgydtmltdngasLSQGQRQLIAIARAAVADPPVMIL 547
Cdd:cd00267 80 Q-------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2541161597 548 DEATSSIDTRTESLVQQGMDGLMY-GRTVFVIAHRLSTVRN-SNAIMVLEHGR 598
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
401-611 |
6.44e-29 |
|
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: 114.99 E-value: 6.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 401 PILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDL---RHSLGIVLQDTNLFTG-T 476
Cdd:cd03258 19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaRRRIGMIFQHFNLLSSrT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 477 VRENIRYGRLDATDEEIEVAAR------LANADEFIRRLPqgydtmltdngASLSQGQRQLIAIARAAVADPPVMILDEA 550
Cdd:cd03258 99 VFENVALPLEIAGVPKAEIEERvlelleLVGLEDKADAYP-----------AQLSGGQKQRVGIARALANNPKVLLCDEA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2541161597 551 TSSID-TRTESLVQqgmdgLMY------GRTVFVIAHRLSTVRN-SNAIMVLEHGRIIERGSHEELIAQ 611
Cdd:cd03258 168 TSALDpETTQSILA-----LLRdinrelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
399-598 |
6.67e-29 |
|
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: 113.05 E-value: 6.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 399 DKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKS--DLRHSLGIVLQDTNLFTG- 475
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRIGMVFQDFALFPHl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 476 TVRENIRYGrldatdeeievaarlanadefirrlpqgydtmltdngasLSQGQRQLIAIARAAVADPPVMILDEATSSID 555
Cdd:cd03229 92 TVLENIALG---------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALD 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2541161597 556 TRTESLVQQGMDGL--MYGRTVFVIAHRLSTVRN-SNAIMVLEHGR 598
Cdd:cd03229 133 PITRREVRALLKSLqaQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
391-609 |
6.86e-29 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 115.53 E-value: 6.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 391 DVDFAYnPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQDT 470
Cdd:COG1120 6 NLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 471 NL-FTGTVRENIRYGR---------LDATDEEI-EVAARLANADEFIRRLpqgYDTmltdngasLSQGQRQLIAIARAAV 539
Cdd:COG1120 85 PApFGLTVRELVALGRyphlglfgrPSAEDREAvEEALERTGLEHLADRP---VDE--------LSGGERQRVLIARALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2541161597 540 ADPPVMILDEATSSIDTRTESLVQQGMDGL--MYGRTVFVIAHRLS-TVRNSNAIMVLEHGRIIERGSHEELI 609
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
35-329 |
8.01e-29 |
|
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: 116.51 E-value: 8.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 35 LVAILISAAASVGASVFLESLIDDYIKpllLQDVPVFTGLvhaLMGMAVLYLAGLLATYLYNRIMVTVSQRTLKGIRDTL 114
Cdd:cd18557 2 LLFLLISSAAQLLLPYLIGRLIDTIIK---GGDLDVLNEL---ALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 115 FSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVMLVMVRV 194
Cdd:cd18557 76 FSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 195 IARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFD-KLNDTLAGSARKANQYAnILMPAMNNVGNLQY 273
Cdd:cd18557 156 YGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSeALDRSYRLARKKALANA-LFQGITSLLIYLSL 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2541161597 274 VVIAIIGGAIALhGGGLTLGAIAAFLQLSKSFTQPISQISQQMNAIVMALAGASRV 329
Cdd:cd18557 235 LLVLWYGGYLVL-SGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
399-603 |
1.41e-28 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 113.38 E-value: 1.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 399 DKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSdlRHSLGIVLQDTNLFTG-TV 477
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFPHlTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 478 RENIRYG----RLDATDEEIEV--AARLANADEFIRRLPqgydtmltdngASLSQGQRQLIAIARAAVADPPVMILDEAT 551
Cdd:cd03259 90 AENIAFGlklrGVPKAEIRARVreLLELVGLEGLLNRYP-----------HELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2541161597 552 SSIDTRTESLVQQGMDGLM--YGRTVFVIAHRLS-TVRNSNAIMVLEHGRIIERG 603
Cdd:cd03259 159 SALDAKLREELREELKELQreLGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
387-612 |
1.51e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 115.09 E-value: 1.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 387 VRFFDVDFAYNPD-KPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGI 465
Cdd:PRK13632 8 IKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 466 VLQD-TNLFTG-TVRENIRYG----RLDATD--EEIEVAARLANADEFIRRLPQgydtmltdngaSLSQGQRQLIAIARA 537
Cdd:PRK13632 88 IFQNpDNQFIGaTVEDDIAFGlenkKVPPKKmkDIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2541161597 538 AVADPPVMILDEATSSIDTRTESLVQQGMDGLMYGR--TVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEELIAQK 612
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
387-610 |
7.58e-28 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 112.00 E-value: 7.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 387 VRFFDVDFAYNpDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDL---RHSL 463
Cdd:COG1127 6 IEVRNLTKSFG-DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELyelRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 464 GIVLQDTNLFTG-TVRENI-----RYGRLDatDEEIE--VAARLANA--DEFIRRLPqgydtmltdngASLSQGQRQLIA 533
Cdd:COG1127 85 GMLFQGGALFDSlTVFENVafplrEHTDLS--EAEIRelVLEKLELVglPGAADKMP-----------SELSGGMRKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 534 IARAAVADPPVMILDEATSSID----TRTESLVQQGMDglMYGRTVFVIAHRLSTVRN-SNAIMVLEHGRIIERGSHEEL 608
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDpitsAVIDELIRELRD--ELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEEL 229
|
..
gi 2541161597 609 IA 610
Cdd:COG1127 230 LA 231
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
391-611 |
1.32e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 112.42 E-value: 1.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 391 DVDFAY-NPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQD 469
Cdd:PRK13635 10 HISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 470 -TNLFTG-TVRENIRYG-------RLDATdEEIEVAARLANADEFIRRLPqgydtmltdngASLSQGQRQLIAIARAAVA 540
Cdd:PRK13635 90 pDNQFVGaTVQDDVAFGlenigvpREEMV-ERVDQALRQVGMEDFLNREP-----------HRLSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2541161597 541 DPPVMILDEATSSIDT--RTE------SLVQQGMdglmygRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEELIAQ 611
Cdd:PRK13635 158 QPDIIILDEATSMLDPrgRREvletvrQLKEQKG------ITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
386-611 |
1.86e-27 |
|
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: 116.54 E-value: 1.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 386 DVRFFDVDFAyNPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIA---DGKIRYDGININKIKKSDLRHS 462
Cdd:COG1123 6 EVRDLSVRYP-GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 463 LGIVLQD--TNLFTGTVRENIRYG--RLDATDEEIEvaarlANADEFIRRLpqGYDTMLTDNGASLSQGQRQLIAIARAA 538
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQIAEAleNLGLSRAEAR-----ARVLELLEAV--GLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2541161597 539 VADPPVMILDEATSSIDTRTESLVQQGMDGLM--YGRTVFVIAHRLSTV-RNSNAIMVLEHGRIIERGSHEELIAQ 611
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQreRGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
31-622 |
1.87e-27 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 118.86 E-value: 1.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 31 LVVVLVAILISAAASVGASVFLESLIDDYIKPLLLQD-------------------------VPVFTGLVHALMGMAVLY 85
Cdd:TIGR01271 866 LVFVLIFCLVIFLAEVAASLLGLWLITDNPSAPNYVDqqhanasspdvqkpviitptsayyiFYIYVGTADSVLALGFFR 945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 86 LAGLLATylynriMVTVSQRTLKGIrdtLFSHMQAlPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILA 165
Cdd:TIGR01271 946 GLPLVHT------LLTVSKRLHEQM---LHSVLQA-PMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLG 1015
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 166 VFFSMLVMSwQLTIVVLVCVAVMLVMVRVIARRSGTFFIQQQTDL-GKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKln 244
Cdd:TIGR01271 1016 AIFVVSVLQ-PYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEArSPIFSHLITSLKGLWTIRAFGRQSYFETLFHK-- 1092
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 245 dtlAGSARKAN--QYANILMPAMNNVgNLQYVV--IAIIGGAIALHGGGL-TLGAIAAFLQLSKSFTQPISQISQQMNAI 319
Cdd:TIGR01271 1093 ---ALNLHTANwfLYLSTLRWFQMRI-DIIFVFffIAVTFIAIGTNQDGEgEVGIILTLAMNILSTLQWAVNSSIDVDGL 1168
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 320 VMALagaSRVFELMD---EEPEQDEGYvtlvNAKYLPDGSLTETSERTGIWAwkhphENGTTTYTKLTGDvrffdvdfaY 396
Cdd:TIGR01271 1169 MRSV---SRVFKFIDlpqEEPRPSGGG----GKYQLSTVLVIENPHAQKCWP-----SGGQMDVQGLTAK---------Y 1227
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 397 NPD-KPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDiADGKIRYDGININKIKKSDLRHSLGIVLQDTNLFTG 475
Cdd:TIGR01271 1228 TEAgRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSG 1306
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 476 TVRENIR-YGRLdaTDEEIEVAARLANADEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSI 554
Cdd:TIGR01271 1307 TFRKNLDpYEQW--SDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHL 1384
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2541161597 555 DTRTESLVQQGMDGLMYGRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEELIAQKGVYYQLYTGA 622
Cdd:TIGR01271 1385 DPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAMSAA 1452
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
387-610 |
6.54e-27 |
|
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: 109.51 E-value: 6.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 387 VRFFDVDFAYNpDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHS---L 463
Cdd:cd03261 1 IELRGLTKSFG-GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrrM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 464 GIVLQDTNLFTG-TVRENI-----RYGRLDatDEEIE--VAARLA--NADEFIRRLPqgydtmltdngASLSQGQRQLIA 533
Cdd:cd03261 80 GMLFQSGALFDSlTVFENVafplrEHTRLS--EEEIReiVLEKLEavGLRGAEDLYP-----------AELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 534 IARAAVADPPVMILDEATSSIDTRTESLVQQGMDGL--MYGRTVFVIAHRLSTVRN-SNAIMVLEHGRIIERGSHEELIA 610
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
403-609 |
1.23e-26 |
|
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: 108.58 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 403 LHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSdlRHSLGIVLQDTNLFTG-TVRENI 481
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPHmTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 482 RYGRLDATDEEIEVAARLANADEFIrrlpqGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDTRTESL 561
Cdd:cd03299 93 AYGLKKRKVDKKEIERKVLEIAEML-----GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2541161597 562 VQQGMDGLM--YGRTVFVIAHRLSTVRN-SNAIMVLEHGRIIERGSHEELI 609
Cdd:cd03299 168 LREELKKIRkeFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
387-598 |
1.87e-26 |
|
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: 107.17 E-value: 1.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 387 VRFFDVDFAYNPD----KPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGininkikksdlrhS 462
Cdd:cd03250 1 ISVEDASFTWDSGeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 463 LGIVLQDTNLFTGTVRENIRYGR-LDAT--DEEIEVAArLanaDEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAV 539
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKpFDEEryEKVIKACA-L---EPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2541161597 540 ADPPVMILDEATSSIDTRTES-LVQQGMDG-LMYGRTVFVIAHRLSTVRNSNAIMVLEHGR 598
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHVGRhIFENCILGlLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
405-610 |
2.34e-26 |
|
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: 107.91 E-value: 2.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 405 DITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKiKKSDLRHSLGIV--LQDTNLFTG-TVRENI 481
Cdd:cd03219 18 DVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITG-LPPHEIARLGIGrtFQIPRLFPElTVLENV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 482 RYGRLDAT----------DEEIEVAARlanADEFIRRLpqGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEAT 551
Cdd:cd03219 97 MVAAQARTgsglllararREEREARER---AEELLERV--GLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2541161597 552 SSIdTRTESlvqQGMDGLM-----YGRTVFVIAHRLSTVRN-SNAIMVLEHGRIIERGSHEELIA 610
Cdd:cd03219 172 AGL-NPEET---EELAELIrelreRGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
402-617 |
4.07e-26 |
|
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: 108.40 E-value: 4.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 402 ILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIaDGKIRYDGININKIKKSDLRHSLGIVLQDTNLFTGTVRENI 481
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 482 R-YGRLdaTDEEIEVAARLANADEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDTRTES 560
Cdd:cd03289 98 DpYGKW--SDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQ 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2541161597 561 LVQQGMDGLMYGRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEELIAQKGVYYQ 617
Cdd:cd03289 176 VIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQ 232
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
399-610 |
4.45e-26 |
|
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: 107.20 E-value: 4.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 399 DKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQD--TNL---F 473
Cdd:COG1124 17 RVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDpyASLhprH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 474 T--GTVRENIRYGRLDATDEEIEVAARLAN-ADEFIRRLPqgydtmltdngASLSQGQRQLIAIARAAVADPPVMILDEA 550
Cdd:COG1124 97 TvdRILAEPLRIHGLPDREERIAELLEQVGlPPSFLDRYP-----------HQLSGGQRQRVAIARALILEPELLLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2541161597 551 TSSID--TRTE------SLVQQgmdglmYGRTVFVIAHRLSTV-RNSNAIMVLEHGRIIERGSHEELIA 610
Cdd:COG1124 166 TSALDvsVQAEilnllkDLREE------RGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
391-599 |
5.40e-26 |
|
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: 106.03 E-value: 5.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 391 DVDFAYNPDK---PILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDL----RHSL 463
Cdd:cd03255 5 NLSKTYGGGGekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafrRRHI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 464 GIVLQDTNLFTG-TVRENIRYGRLDATDEEIEVAARlanADEFIRRLpqGYDTMLTDNGASLSQGQRQLIAIARAAVADP 542
Cdd:cd03255 85 GFVFQSFNLLPDlTALENVELPLLLAGVPKKERRER---AEELLERV--GLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2541161597 543 PVMILDEATSSIDTRTESLVqqgMDGLM-----YGRTVFVIAHRLSTVRNSNAIMVLEHGRI 599
Cdd:cd03255 160 KIILADEPTGNLDSETGKEV---MELLRelnkeAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
401-601 |
1.85e-25 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 104.74 E-value: 1.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 401 PILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDL----RHSLGIVLQDTNLFTG- 475
Cdd:COG1136 22 TALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlrRRHIGFVFQFFNLLPEl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 476 TVRENI----RYGRLDAtdeeievAARLANADEFIRRLpqGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEAT 551
Cdd:COG1136 102 TALENValplLLAGVSR-------KERRERARELLERV--GLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2541161597 552 SSIDTRTESLVQQGMDGL--MYGRTVFVIAHRLSTVRNSNAIMVLEHGRIIE 601
Cdd:COG1136 173 GNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
391-580 |
2.23e-25 |
|
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: 103.88 E-value: 2.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 391 DVDFAYNPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGiniNKIKKSDLRHSLGIVLQDT 470
Cdd:cd03226 4 NISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 471 N--LFTGTVRENIRYGrLDATDEEIEVAA---RLANADEFIRRLPQgydtmltdngaSLSQGQRQLIAIARAAVADPPVM 545
Cdd:cd03226 81 DyqLFTDSVREELLLG-LKELDAGNEQAEtvlKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 2541161597 546 ILDEATSSIDTRTESLVQQGMDGLM-YGRTVFVIAH 580
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITH 184
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
388-608 |
4.40e-25 |
|
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: 104.19 E-value: 4.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 388 RFFDVDFAYNPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDL---RHSLG 464
Cdd:cd03256 2 EVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 465 IVLQDTNLFTG-TVRENIRYGRLDA-----------TDEEIEVAARLanadefIRRLpqGYDTMLTDNGASLSQGQRQLI 532
Cdd:cd03256 82 MIFQQFNLIERlSVLENVLSGRLGRrstwrslfglfPKEEKQRALAA------LERV--GLLDKAYQRADQLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 533 AIARAAVADPPVMILDEATSSIDTRTEslvQQGMDGLM-----YGRTVFVIAHRLSTVR-NSNAIMVLEHGRIIERGSHE 606
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASS---RQVMDLLKrinreEGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPPA 230
|
..
gi 2541161597 607 EL 608
Cdd:cd03256 231 EL 232
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
399-599 |
5.56e-25 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 101.71 E-value: 5.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 399 DKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKiKKSDLRHSLGIVLQDTNLFTG-TV 477
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPEEPSLYENlTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 478 RENIRYgrldatdeeievaarlanadefirrlpqgydtmltdngaslSQGQRQLIAIARAAVADPPVMILDEATSSIDTR 557
Cdd:cd03230 91 RENLKL-----------------------------------------SGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2541161597 558 TESLVQQGMDGLM-YGRTVFVIAHRLSTVRN-SNAIMVLEHGRI 599
Cdd:cd03230 130 SRREFWELLRELKkEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
403-607 |
8.36e-25 |
|
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: 103.97 E-value: 8.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 403 LHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKiKKSDLRHSLGIV--LQDTNLFTG-TVRE 479
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITG-LPPHRIARLGIArtFQNPRLFPElTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 480 NIRYGRLDAT---------------DEEIEVAARlanADEFIRRLpqGYDTMLTDNGASLSQGQRQLIAIARAAVADPPV 544
Cdd:COG0411 99 NVLVAAHARLgrgllaallrlprarREEREARER---AEELLERV--GLADRADEPAGNLSYGQQRRLEIARALATEPKL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2541161597 545 MILDEATSsidtrteslvqqGM-----DGLM---------YGRTVFVIAHRLSTVRN-SNAIMVLEHGRIIERGSHEE 607
Cdd:COG0411 174 LLLDEPAA------------GLnpeetEELAelirrlrdeRGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAE 239
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
401-610 |
9.31e-25 |
|
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: 102.90 E-value: 9.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 401 PILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKiKKSDLRHSLGI--VLQDTNLFTG-TV 477
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITG-LPPHERARAGIgyVPEGRRIFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 478 RENIRYGRLDATDEEIEvaARLANADEFIRRLPQgydtMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIdtr 557
Cdd:cd03224 93 EENLLLGAYARRRAKRK--ARLERVYELFPRLKE----RRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL--- 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2541161597 558 TESLVQQGMDGLMY----GRTVFVIAHRLSTVRN-SNAIMVLEHGRIIERGSHEELIA 610
Cdd:cd03224 164 APKIVEEIFEAIRElrdeGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
406-611 |
1.07e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 102.91 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 406 ITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDlRhSLGIVLQDTNLFTG-TVRENIRYG 484
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-R-PVSMLFQENNLFPHlTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 485 -----RLDATD-EEIEVAARLANADEFIRRLPqgydtmltdngASLSQGQRQLIAIARAAVADPPVMILDEATSSIDT-- 556
Cdd:COG3840 96 lrpglKLTAEQrAQVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPal 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2541161597 557 RTE--SLVQQGMDGlmYGRTVFVIAHRLSTVRN-SNAIMVLEHGRIIERGSHEELIAQ 611
Cdd:COG3840 165 RQEmlDLVDELCRE--RGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDG 220
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
34-299 |
1.14e-24 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 104.49 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 34 VLVAILISAAASVGASVFLESLIDdyiKPLLLQDVPVFTGLVHALMGMAVLyLAglLATYLYNRIMVTVSQRTLKGIRDT 113
Cdd:cd18575 1 ALIALLIAAAATLALGQGLRLLID---QGFAAGNTALLNRAFLLLLAVALV-LA--LASALRFYLVSWLGERVVADLRKA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 114 LFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVMLVMVR 193
Cdd:cd18575 75 VFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPII 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 194 VIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKanqyaNILMPAMnnvgnLQY 273
Cdd:cd18575 155 LFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALR-----RIRARAL-----LTA 224
|
250 260 270
....*....|....*....|....*....|....*
gi 2541161597 274 VVIAIIGGAIAL------HG---GGLTLGAIAAFL 299
Cdd:cd18575 225 LVIFLVFGAIVFvlwlgaHDvlaGRMSAGELSQFV 259
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
386-603 |
1.39e-24 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 101.47 E-value: 1.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 386 DVRFFDVDFAYNPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLIN--RFYDIADGKIRYDGINinkIKKSDLRHSL 463
Cdd:cd03213 8 NLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRP---LDKRSFRKII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 464 GIVLQDTNLF-TGTVRENIRYgrldatdeeievAARLanadefirrlpqgydtmltdngASLSQGQRQLIAIARAAVADP 542
Cdd:cd03213 85 GYVPQDDILHpTLTVRETLMF------------AAKL----------------------RGLSGGERKRVSIALELVSNP 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2541161597 543 PVMILDEATSSIDTRTESLVQQGMDGLMY-GRTVFVIAHRLST--VRNSNAIMVLEHGRIIERG 603
Cdd:cd03213 131 SLLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
387-609 |
2.70e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 102.09 E-value: 2.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 387 VRFFDVDFAYNPdKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININ--KIKKSDLRHSLG 464
Cdd:PRK09493 2 IEFKNVSKHFGP-TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 465 IVLQDTNLFTG-TVRENIRYGRLD---ATDEEIEVAARlanadEFIRRLpqGYDTMLTDNGASLSQGQRQLIAIARAAVA 540
Cdd:PRK09493 81 MVFQQFYLFPHlTALENVMFGPLRvrgASKEEAEKQAR-----ELLAKV--GLAERAHHYPSELSGGQQQRVAIARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2541161597 541 DPPVMILDEATSSIDT--RTE------SLVQQGMdglmygrTVFVIAHRLSTVRN-SNAIMVLEHGRIIERGSHEELI 609
Cdd:PRK09493 154 KPKLMLFDEPTSALDPelRHEvlkvmqDLAEEGM-------TMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
31-329 |
3.70e-24 |
|
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: 102.94 E-value: 3.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 31 LVVVLVAILISAAASVGASVFLESLIDDYIKPLLLQDVP--VFTGLVHALMGMAVLYLAGLLATYLYNRIMVTVSQRTLK 108
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGSGESSPdeFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 109 GIRDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVM 188
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 189 LVMVRVIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANQYANILMPAMNNV 268
Cdd:cd18577 161 AIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2541161597 269 GNLQYvVIAIIGGAIALHGGGLTLGAI-AAFLqlskSF---TQPISQISQQMNAIVMALAGASRV 329
Cdd:cd18577 241 IFAMY-ALAFWYGSRLVRDGEISPGDVlTVFF----AVligAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
391-603 |
5.28e-24 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 99.43 E-value: 5.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 391 DVDFAYNpDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQdt 470
Cdd:cd03214 4 NLSVGYG-GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 471 nlftgtvrenirygrldatdeeievAARLANADEFIRRlpqGYDTmltdngasLSQGQRQLIAIARAAVADPPVMILDEA 550
Cdd:cd03214 81 -------------------------ALELLGLAHLADR---PFNE--------LSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2541161597 551 TSSIDTRTESLVQQGMDGL--MYGRTVFVIAHRLS-TVRNSNAIMVLEHGRIIERG 603
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLarERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
391-602 |
5.82e-24 |
|
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: 100.24 E-value: 5.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 391 DVDFAY---NPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININkikksDLRHSLGIVL 467
Cdd:cd03293 5 NVSKTYgggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT-----GPGPDRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 468 QDTNLFT-GTVRENIRYG---RLDATDEEIEVAARLANA---DEFIRRLPqgydtmltdngASLSQGQRQLIAIARAAVA 540
Cdd:cd03293 80 QQDALLPwLTVLDNVALGlelQGVPKAEARERAEELLELvglSGFENAYP-----------HQLSGGMRQRVALARALAV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2541161597 541 DPPVMILDEATSSIDTRTESLVQQGMDGLM--YGRTVFVIAHRLS-TVRNSNAIMVLE--HGRIIER 602
Cdd:cd03293 149 DPDVLLLDEPFSALDALTREQLQEELLDIWreTGKTVLLVTHDIDeAVFLADRVVVLSarPGRIVAE 215
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
18-549 |
9.28e-24 |
|
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: 105.65 E-value: 9.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 18 RLFRLIVEGNTLRLVVVLVAILISAAASVGasvfLESLIDDYIK---PLLLQDVPVFTGLVHALMgmAVLYLAGLLATYL 94
Cdd:COG4615 2 NLLRLLLRESRWLLLLALLLGLLSGLANAG----LIALINQALNatgAALARLLLLFAGLLVLLL--LSRLASQLLLTRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 95 YNRIMVTVSQRTLKGIRDTlfshmqalPIRYFDTHPHGDIMSVYTNDVDTLRQmISQSIPQAMSSVITILAVFFSMLVMS 174
Cdd:COG4615 76 GQHAVARLRLRLSRRILAA--------PLERLERIGAARLLAALTEDVRTISQ-AFVRLPELLQSVALVLGCLAYLAWLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 175 WQLTIVVLVCVAVMLVMVRVIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVfcHEQKAKEDFDKLNDTLAGSARKA 254
Cdd:COG4615 147 PPLFLLTLVLLGLGVAGYRLLVRRARRHLRRAREAEDRLFKHFRALLEGFKELKL--NRRRRRAFFDEDLQPTAERYRDL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 255 NQYANILMPAMNNVGNLqyVVIAIIGGAIALHGGGLTL------GAIAAFLQLSksftQPISQISQQMNAIVMALAGASR 328
Cdd:COG4615 225 RIRADTIFALANNWGNL--LFFALIGLILFLLPALGWAdpavlsGFVLVLLFLR----GPLSQLVGALPTLSRANVALRK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 329 VFELMDEEPEQDEGYVTLVNAKYLPDgsltetsertgiwaWKHphengtttytkltgdVRFFDVDFAYNPDK-------- 400
Cdd:COG4615 299 IEELELALAAAEPAAADAAAPPAPAD--------------FQT---------------LELRGVTYRYPGEDgdegftlg 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 401 PIlhDITLyaKPGQkLAF-VGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQDTNLFTGTvre 479
Cdd:COG4615 350 PI--DLTI--RRGE-LVFiVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRL--- 421
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2541161597 480 nirYGRLDATDEEIevaarlanADEFIRRLpqGYDTMLT-DNGA----SLSQGQRQLIAIARAAVADPPVMILDE 549
Cdd:COG4615 422 ---LGLDGEADPAR--------ARELLERL--ELDHKVSvEDGRfsttDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
387-608 |
2.08e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 100.64 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 387 VRFFDVDFAYnPD--KPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFY---DIADGKIRYDGININKIKKSDLRH 461
Cdd:PRK13640 6 VEFKHVSFTY-PDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 462 SLGIVLQD-TNLFTG-TVRENIRYG---RLDATDEEIEVAAR-LANAD--EFIRRLPQgydtmltdngaSLSQGQRQLIA 533
Cdd:PRK13640 85 KVGIVFQNpDNQFVGaTVGDDVAFGlenRAVPRPEMIKIVRDvLADVGmlDYIDSEPA-----------NLSGGQKQRVA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2541161597 534 IARAAVADPPVMILDEATSSIDTRTESLVQQGMDGLMY--GRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEEL 608
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
35-299 |
2.36e-23 |
|
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: 100.67 E-value: 2.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 35 LVAILISAAASVGASVFLESLIDdYIKPLLLQDVPVFTGLVHALMGMAVLYLAGLLATYLYNRIMVTVSQRTLKGIRDTL 114
Cdd:cd18573 2 LALLLVSSAVTMSVPFAIGKLID-VASKESGDIEIFGLSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 115 FSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLV---CVAVMLVM 191
Cdd:cd18573 81 FKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLvvpPIAVGAVF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 192 ----VRVIARrsgtffiQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANQYANILMPAMNN 267
Cdd:cd18573 161 ygryVRKLSK-------QVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGF 233
|
250 260 270
....*....|....*....|....*....|..
gi 2541161597 268 VGNLQYVVIAIIGGAIALhGGGLTLGAIAAFL 299
Cdd:cd18573 234 SGNLSLLSVLYYGGSLVA-SGELTVGDLTSFL 264
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
387-599 |
2.69e-23 |
|
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: 98.25 E-value: 2.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 387 VRFFDVDFAYNPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSD---LRHSL 463
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 464 GIVLQDTNLF-TGTVRENIRYGrLDATDEE-IEVAARLANADEFIrRLPQGYDTMltdnGASLSQGQRQLIAIARAAVAD 541
Cdd:cd03292 81 GVVFQDFRLLpDRNVYENVAFA-LEVTGVPpREIRKRVPAALELV-GLSHKHRAL----PAELSGGEQQRVAIARAIVNS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 542 PPVMILDEATSSIDTRTESLVQQGMDGL-MYGRTVFVIAHRLSTVRN-SNAIMVLEHGRI 599
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATHAKELVDTtRHRVIALERGKL 214
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
31-322 |
4.21e-23 |
|
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: 99.89 E-value: 4.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 31 LVVVLVAILISAAASVGASVFLESLIDDYIKPlllQDVPVFTGLVHALMGMAVLYLaglLATYLYNRIMVTVSQRTLKGI 110
Cdd:cd18555 4 LISILLLSLLLQLLTLLIPILTQYVIDNVIVP---GNLNLLNVLGIGILILFLLYG---LFSFLRGYIIIKLQTKLDKSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 111 RDTLFSHMQALPIRYFDTHPHGDIMSvYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVMlV 190
Cdd:cd18555 78 MSDFFEHLLKLPYSFFENRSSGDLLF-RANSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLI-V 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 191 MVRVIARRSGTFFIQQQ-TDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANQYANILMPAMNNVG 269
Cdd:cd18555 156 LLLLLTRKKIKKLNQEEiVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQ 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2541161597 270 NLQYVVIAIIgGAIALHGGGLTLGAIAAFLQLSKSFTQPISQISQQMNAIVMA 322
Cdd:cd18555 236 FIAPLLILWI-GAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILL 287
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
403-611 |
9.10e-23 |
|
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: 98.48 E-value: 9.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 403 LHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDL----RHSLGIVLQDTNLFTG-TV 477
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPHrTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 478 RENIRYGrldatdeeIEV-----AARLANADEFIRRLP-QGYDTMLTDngaSLSQGQRQLIAIARAAVADPPVMILDEAT 551
Cdd:cd03294 120 LENVAFG--------LEVqgvprAEREERAAEALELVGlEGWEHKYPD---ELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2541161597 552 SSIDtrteSLVQQGM-DGLM-----YGRTVFVIAHRLS-TVRNSNAIMVLEHGRIIERGSHEELIAQ 611
Cdd:cd03294 189 SALD----PLIRREMqDELLrlqaeLQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
405-611 |
1.02e-22 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 99.42 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 405 DITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRH---SLGIVLQDTnlFTG-----T 476
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPlrrRMQMVFQDP--YASlnprmT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 477 VRENIR-----YGRLDATDEEIEVAARLA----NAdEFIRRLPQgydtmltdngaSLSQGQRQLIAIARAAVADPPVMIL 547
Cdd:COG4608 114 VGDIIAeplriHGLASKAERRERVAELLElvglRP-EHADRYPH-----------EFSGGQRQRIGIARALALNPKLIVC 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2541161597 548 DEATSSIDTRTESLV-------QQGMdGLMYgrtVFvIAHRLSTVRN-SNAIMVLEHGRIIERGSHEELIAQ 611
Cdd:COG4608 182 DEPVSALDVSIQAQVlnlledlQDEL-GLTY---LF-ISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
403-611 |
1.07e-22 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 99.36 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 403 LHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYD---IADGKIRYDGININKIKKSDLRH----SLGIVLQD--TNL- 472
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELRKirgrEIQMIFQDpmTSLn 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 473 --------FTGTVRENIRYGRLDATDEEIEVAAR--LANADEFIRRLP-QgydtmltdngasLSQGQRQLIAIARAAVAD 541
Cdd:COG0444 101 pvmtvgdqIAEPLRIHGGLSKAEARERAIELLERvgLPDPERRLDRYPhE------------LSGGMRQRVMIARALALE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2541161597 542 PPVMILDEATSSIDTrtesLVQ-QGMDgLM------YGRTVFVIAHRLSTVRN-SNAIMVLEHGRIIERGSHEELIAQ 611
Cdd:COG0444 169 PKLLIADEPTTALDV----TIQaQILN-LLkdlqreLGLAILFITHDLGVVAEiADRVAVMYAGRIVEEGPVEELFEN 241
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
399-599 |
1.20e-22 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 96.44 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 399 DKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKK--SDLRHSLGIVLQDTNLFTG- 475
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKniNELRQKVGMVFQQFNLFPHl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 476 TVRENIRYG---RLDATDEEIEvaarlANADEFIRRLpqGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATS 552
Cdd:cd03262 92 TVLENITLApikVKGMSKAEAE-----ERALELLEKV--GLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTS 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2541161597 553 SIDTRTESLVQQGMDGLMY-GRTVFVIAHRLSTVRN-SNAIMVLEHGRI 599
Cdd:cd03262 165 ALDPELVGEVLDVMKDLAEeGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
391-618 |
1.24e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 98.27 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 391 DVDFAYNPD--KPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQ 468
Cdd:PRK13650 9 NLTFKYKEDqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 469 D-TNLFTG-TVRENIRYG------RLDATDEEIEVAARLANADEFIRRLPqgydtmltdngASLSQGQRQLIAIARAAVA 540
Cdd:PRK13650 89 NpDNQFVGaTVEDDVAFGlenkgiPHEEMKERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 541 DPPVMILDEATSSIDTRTESLVQQGMDGLM--YGRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEELIAQKGVYYQL 618
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRddYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGNDLLQL 237
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
403-603 |
1.47e-22 |
|
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: 96.28 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 403 LHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKiKKSDLRHSLGIVLQDTNLFTG-TVRENI 481
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYDRlTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 482 RY-GRLDAtdeeIEVAARLANADEFIRRLpqGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSID---TR 557
Cdd:cd03266 100 EYfAGLYG----LKGDELTARLEELADRL--GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDvmaTR 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2541161597 558 T-ESLVQQGMDGlmyGRTVFVIAHRLSTV-RNSNAIMVLEHGRIIERG 603
Cdd:cd03266 174 AlREFIRQLRAL---GKCILFSTHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
391-599 |
3.13e-22 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 95.93 E-value: 3.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 391 DVDFAYNpDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKikksdLRHSLGIVLQDT 470
Cdd:COG1121 11 NLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIGYVPQRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 471 NL---FTGTVRENI---RYG------RLDATDEEIeVAARLA--NADEFIRRlPQGydtmltdngaSLSQGQRQLIAIAR 536
Cdd:COG1121 85 EVdwdFPITVRDVVlmgRYGrrglfrRPSRADREA-VDEALErvGLEDLADR-PIG----------ELSGGQQQRVLLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2541161597 537 AAVADPPVMILDEATSSIDTRTESLVQQGMDGL-MYGRTVFVIAHRLSTVR-NSNAIMVLEHGRI 599
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVReYFDRVLLLNRGLV 217
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
391-610 |
3.81e-22 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 95.43 E-value: 3.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 391 DVDFAYNpDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDL-RHSLGIVLQD 469
Cdd:COG0410 8 NLHAGYG-GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 470 TNLFTG-TVRENIRYGRLDATDEEiEVAARLANADEFIRRLPQgydtMLTDNGASLSQGQRQLIAIARAAVADPPVMILD 548
Cdd:COG0410 87 RRIFPSlTVEENLLLGAYARRDRA-EVRADLERVYELFPRLKE----RRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 549 EAT--------SSIDTRTESLVQQGMdglmygrTVFV----------IAHRlstvrnsnaIMVLEHGRIIERGSHEELIA 610
Cdd:COG0410 162 EPSlglaplivEEIFEIIRRLNREGV-------TILLveqnarfaleIADR---------AYVLERGRIVLEGTAAELLA 225
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
391-555 |
4.08e-22 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 96.26 E-value: 4.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 391 DVDFAYNpDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDI-----ADGKIRYDGININ--KIKKSDLRHSL 463
Cdd:COG1117 16 NLNVYYG-DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLipgarVEGEILLDGEDIYdpDVDVVELRRRV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 464 GIVLQDTNLFTGTVRENIRYG-RL------DATDEEIEVAARLANA-DEFIRRLpqgydtmlTDNGASLSQGQRQLIAIA 535
Cdd:COG1117 95 GMVFQKPNPFPKSIYDNVAYGlRLhgikskSELDEIVEESLRKAALwDEVKDRL--------KKSALGLSGGQQQRLCIA 166
|
170 180
....*....|....*....|.
gi 2541161597 536 RA-AVaDPPVMILDEATSSID 555
Cdd:COG1117 167 RAlAV-EPEVLLMDEPTSALD 186
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
35-328 |
4.32e-22 |
|
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: 96.84 E-value: 4.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 35 LVAILISAAASVGASVFLESLIDDYIKpllLQDVPVFTglvHALMGMAVLYLAGLLATYLYNRIMVTVSQRTLKGIRDTL 114
Cdd:cd18572 2 FVFLVVAALSELAIPHYTGAVIDAVVA---DGSREAFY---RAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 115 FSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVMLVMVRV 194
Cdd:cd18572 76 FRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 195 IARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFD-KLNDTLAGSARKANQYAnILMPAMNNVGNLQY 273
Cdd:cd18572 156 YGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYErALDKALKLSVRQALAYA-GYVAVNTLLQNGTQ 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2541161597 274 VVIAIIGGAIALHgGGLTLGAIAAFLQLSKSFTQPISQISQQMNAIvMALAGASR 328
Cdd:cd18572 235 VLVLFYGGHLVLS-GRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSL-MQAVGAAE 287
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
387-603 |
8.51e-22 |
|
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: 94.10 E-value: 8.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 387 VRFFDVDFAYNpDKPILHDITLYAkpGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDlrHSLGIV 466
Cdd:cd03298 1 VRLDKIRFSYG-EQPMHFDLTFAQ--GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 467 LQDTNLFTG-TVRENIRYG-----RLDATDEE-IEVAARLANADEFIRRLPQgydtmltdngaSLSQGQRQLIAIARAAV 539
Cdd:cd03298 76 FQENNLFAHlTVEQNVGLGlspglKLTAEDRQaIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2541161597 540 ADPPVMILDEATSSIDtrteSLVQQGMDGLMY------GRTVFVIAHRLSTVRN-SNAIMVLEHGRIIERG 603
Cdd:cd03298 145 RDKPVLLLDEPFAALD----PALRAEMLDLVLdlhaetKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
394-607 |
8.67e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 95.88 E-value: 8.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 394 FAYNPDKPI----LHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGINI--NKIKKSDLRHSLGIVL 467
Cdd:PRK13637 10 HIYMEGTPFekkaLDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 468 Q--DTNLFTGTVRENIRYG--RLDATDEEIEVAARLAnadefIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPP 543
Cdd:PRK13637 90 QypEYQLFEETIEKDIAFGpiNLGLSEEEIENRVKRA-----MNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2541161597 544 VMILDEATSSID--TRTESLVQQGMDGLMYGRTVFVIAHRLSTV-RNSNAIMVLEHGRIIERGSHEE 607
Cdd:PRK13637 165 ILILDEPTAGLDpkGRDEILNKIKELHKEYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE 231
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
35-328 |
1.04e-21 |
|
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: 95.78 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 35 LVAILISAAASVGASVFLESLIDDYIKPLLLQDVPVFTGLVHALMGMAVLYLAGLLATYLYNRIMVTVSQRTLKGIRDTL 114
Cdd:cd18780 2 TIALLVSSGTNLALPYFFGQVIDAVTNHSGSGGEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 115 FSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVMLVMVRV 194
Cdd:cd18780 82 FSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 195 IARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFD-KLNDTLaGSARKANQYANILMPAMNNVGNLQY 273
Cdd:cd18780 162 YGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSeKINESY-LLGKKLARASGGFNGFMGAAAQLAI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2541161597 274 VVIAIIGGAIALHgGGLTLGAIAAF----LQLSKSFTQPISQISQQMNAIvmalaGASR 328
Cdd:cd18780 241 VLVLWYGGRLVID-GELTTGLLTSFllytLTVAMSFAFLSSLYGDFMQAV-----GASV 293
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
398-557 |
1.21e-21 |
|
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: 93.47 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 398 PDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDlrHSLGIVLQDTNLFTG-T 476
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVFQNYALYPHmT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 477 VRENIRYG------RLDATDEEIEVAARLANADEFIRRLPqgydtmltdngASLSQGQRQLIAIARAAVADPPVMILDEA 550
Cdd:cd03301 89 VYDNIAFGlklrkvPKDEIDERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
....*..
gi 2541161597 551 TSSIDTR 557
Cdd:cd03301 158 LSNLDAK 164
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
391-587 |
1.74e-21 |
|
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: 92.98 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 391 DVDFAYNpDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGINInkikkSDLRHSLGIVLQDT 470
Cdd:cd03235 4 DLTVSYG-GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-----EKERKRIGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 471 NL---FTGTVRENIRYGRL----------DATDEEIEVAARLANADEFIRRlpqgydtmltdNGASLSQGQRQLIAIARA 537
Cdd:cd03235 78 SIdrdFPISVRDVVLMGLYghkglfrrlsKADKAKVDEALERVGLSELADR-----------QIGELSGGQQQRVLLARA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2541161597 538 AVADPPVMILDEATSSIDTRTESLVQQGMDGL-MYGRTVFVIAHRLSTVRN 587
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLE 197
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
403-611 |
1.78e-21 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 95.92 E-value: 1.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 403 LHDITLYAKPGQKLAFVGSTGAGKTTITNLINRF--YDiaDGKIRYDGININKIKKSDL---RHSLGIVLQDTNLFTG-T 476
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLerPT--SGSVLVDGVDLTALSERELraaRRKIGMIFQHFNLLSSrT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 477 VRENIRYG-RLDATDEEiEVAARlanADEFIRRLpqGydtmLTDNGAS----LSQGQRQLIAIARAAVADPPVMILDEAT 551
Cdd:COG1135 99 VAENVALPlEIAGVPKA-EIRKR---VAELLELV--G----LSDKADAypsqLSGGQKQRVGIARALANNPKVLLCDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2541161597 552 SSIDTRT--------ESLVQQgmdglmYGRTVFVIAHRLSTVRN-SNAIMVLEHGRIIERGSHEELIAQ 611
Cdd:COG1135 169 SALDPETtrsildllKDINRE------LGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGPVLDVFAN 231
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
387-609 |
1.88e-21 |
|
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: 94.00 E-value: 1.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 387 VRFFDVDFAYNpDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGK------IRYDGINInkikkSDLR 460
Cdd:COG1119 4 LELRNVTVRRG-GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrlfgERRGGEDV-----WELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 461 HSLGIV---LQDTNLFTGTVRENIRYGRLD-------ATDEEIEVAARLA---NADEFIRRLPQgydtmltdngaSLSQG 527
Cdd:COG1119 78 KRIGLVspaLQLRFPRDETVLDVVLSGFFDsiglyrePTDEQRERARELLellGLAHLADRPFG-----------TLSQG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 528 QRQLIAIARAAVADPPVMILDEATSSIDTRTESLVQQGMDGLMYGR---TVFViAHRLSTVRNS-NAIMVLEHGRIIERG 603
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaptLVLV-THHVEEIPPGiTHVLLLKDGRVVAAG 225
|
....*.
gi 2541161597 604 SHEELI 609
Cdd:COG1119 226 PKEEVL 231
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
402-610 |
2.16e-21 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 93.66 E-value: 2.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 402 ILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKK--------SDLRHSLGIVLQDTNLF 473
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqqkgliRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 474 TG-TVRENIRYGRLDATDEEIEVAARLANA-----------DEFIRRLpqgydtmltdngaslSQGQRQLIAIARAAVAD 541
Cdd:PRK11264 98 PHrTVLENIIEGPVIVKGEPKEEATARAREllakvglagkeTSYPRRL---------------SGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2541161597 542 PPVMILDEATSSIDTRTESLVQQGMDGLMY-GRTVFVIAHRLSTVRN-SNAIMVLEHGRIIERGSHEELIA 610
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
130-626 |
3.30e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 98.89 E-value: 3.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 130 PHGDIMSVYTNDVDTLrQMISQSIPQAMSSVITILAvffSMLVMSWQLTIVVLVCVAVMLVMV---RVIARRSGTFFIQ- 205
Cdd:PLN03232 396 ASGKVTNMITTDANAL-QQIAEQLHGLWSAPFRIIV---SMVLLYQQLGVASLFGSLILFLLIplqTLIVRKMRKLTKEg 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 206 -QQTDlgKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANqyaniLMPAMNN--VGNLQYVVIAIIGGA 282
Cdd:PLN03232 472 lQWTD--KRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQ-----LLSAFNSfiLNSIPVVVTLVSFGV 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 283 IALHGGGLTLGAIAAFLQLSKSFTQPISQISQQMNAIVMALAGASRVFELMDEEpeqdegyvtlvnakylpdgsltetsE 362
Cdd:PLN03232 545 FVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSE-------------------------E 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 363 RtgIWAWKHPHENGTTTYTKLTGdvrFFDVDFayNPDKPILHDITLYAKPGQKLAFVGSTGAGKTT-ITNLINRFYDIAD 441
Cdd:PLN03232 600 R--ILAQNPPLQPGAPAISIKNG---YFSWDS--KTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSlISAMLGELSHAET 672
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 442 GKIrydgininkikksDLRHSLGIVLQDTNLFTGTVRENI---------RYGRldatdeEIEVAARLANADEFirrlpQG 512
Cdd:PLN03232 673 SSV-------------VIRGSVAYVPQVSWIFNATVRENIlfgsdfeseRYWR------AIDVTALQHDLDLL-----PG 728
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 513 YD-TMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDTRT-----ESLVQQGMDglmyGRTVFVIAHRLSTVR 586
Cdd:PLN03232 729 RDlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVahqvfDSCMKDELK----GKTRVLVTNQLHFLP 804
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2541161597 587 NSNAIMVLEHGRIIERGSHEELIAQKGVYYQLYTGAFEME 626
Cdd:PLN03232 805 LMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGKMD 844
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
391-608 |
4.72e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 92.92 E-value: 4.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 391 DVDFAYNpDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDI-----ADGKIRYDGINI--NKIKKSDLRHSL 463
Cdd:PRK14239 10 DLSVYYN-KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNGHNIysPRTDTVDLRKEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 464 GIVLQDTNLFTGTVRENIRYG-RLDAT------DEEIEVAARLANA-DEFIRRLpqgydtmlTDNGASLSQGQRQLIAIA 535
Cdd:PRK14239 89 GMVFQQPNPFPMSIYENVVYGlRLKGIkdkqvlDEAVEKSLKGASIwDEVKDRL--------HDSALGLSGGQQQRVCIA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2541161597 536 RAAVADPPVMILDEATSSIDTRTESLVQQGMDGLMYGRTVFVIAHRLSTV-RNSNAIMVLEHGRIIERGSHEEL 608
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
387-612 |
4.87e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 93.74 E-value: 4.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 387 VRFFDVDFAYNPDKPI----LHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDG--ININKIKKS--D 458
Cdd:PRK13641 3 IKFENVDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhITPETGNKNlkK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 459 LRHSLGIVLQ--DTNLFTGTVRENIRYGRLD--ATDEEIEVAARlanadEFIRRLpqGYDTMLTDNGA-SLSQGQRQLIA 533
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAKEKAL-----KWLKKV--GLSEDLISKSPfELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 534 IARAAVADPPVMILDEATSSIDTRT-ESLVQQGMDGLMYGRTVFVIAHRLSTVRN-SNAIMVLEHGRIIERGSHEELIAQ 611
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSD 235
|
.
gi 2541161597 612 K 612
Cdd:PRK13641 236 K 236
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
385-608 |
6.43e-21 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 94.75 E-value: 6.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 385 GDVRFFDVDFAYNpDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKI--KKSDLrhs 462
Cdd:COG3839 2 ASLELENVSKSYG-GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLppKDRNI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 463 lGIVLQDTNLF-TGTVRENIRYG----RLDAT--DEEIEVAARLANADEFIRRLPqgydtmltdngASLSQGQRQLIAIA 535
Cdd:COG3839 78 -AMVFQSYALYpHMTVYENIAFPlklrKVPKAeiDRRVREAAELLGLEDLLDRKP-----------KQLSGGQRQRVALG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 536 RAAVADPPVMILDEATSSID------TRTE--SLVQQgmdglmYGRT-VFV---------IAHRlstvrnsnaIMVLEHG 597
Cdd:COG3839 146 RALVREPKVFLLDEPLSNLDaklrveMRAEikRLHRR------LGTTtIYVthdqveamtLADR---------IAVMNDG 210
|
250
....*....|.
gi 2541161597 598 RIIERGSHEEL 608
Cdd:COG3839 211 RIQQVGTPEEL 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
403-611 |
8.07e-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: 96.29 E-value: 8.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 403 LHDITLYAKPGQKLAFVGSTGAGKTT----ITNLINrfydiADGKIRYDGININKIKKSD---LRHSLGIVLQDTNlftG 475
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLIP-----SEGEIRFDGQDLDGLSRRAlrpLRRRMQVVFQDPF---G 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 476 ------TVRENIRYG------RLDATDEEIEVAARLAN---ADEFIRRLPqgydtmltdngASLSQGQRQLIAIARAAVA 540
Cdd:COG4172 374 slsprmTVGQIIAEGlrvhgpGLSAAERRARVAEALEEvglDPAARHRYP-----------HEFSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 541 DPPVMILDEATSSIDtRTeslVQ-QGMD---------GLMYgrtVFvIAHRLSTVRN-SNAIMVLEHGRIIERGSHEELI 609
Cdd:COG4172 443 EPKLLVLDEPTSALD-VS---VQaQILDllrdlqrehGLAY---LF-ISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVF 514
|
..
gi 2541161597 610 AQ 611
Cdd:COG4172 515 DA 516
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
110-612 |
9.19e-21 |
|
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: 97.29 E-value: 9.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 110 IRDTLFS----HMQALPIRYFDTHPHGDIMSVYTNDVDTLrqmiSQSIPQAMSSVITILAVFFSMLVMsWQLTIVVLVCV 185
Cdd:TIGR01271 153 MRIALFSliykKTLKLSSRVLDKISTGQLVSLLSNNLNKF----DEGLALAHFVWIAPLQVILLMGLI-WELLEVNGFCG 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 186 AVMLVMVRVIARRSGTFFIQ-QQTDLGKLNGYI---EEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANqYANIL 261
Cdd:TIGR01271 228 LGFLILLALFQACLGQKMMPyRDKRAGKISERLaitSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIA-YLRYF 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 262 MPAMNNVGNLQYVVIAIIGGAIAlhgGGLTLGAIaaFLQLSKSFTQPISQISQQMNAIVM---ALAGASRVFELMDEEPE 338
Cdd:TIGR01271 307 YSSAFFFSGFFVVFLSVVPYALI---KGIILRRI--FTTISYCIVLRMTVTRQFPGAIQTwydSLGAITKIQDFLCKEEY 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 339 QDEGY------VTLVNAKYLPDGSLTETSERtgiwAWKHPHENGTTTytkltGDVRFFDVDFAYNPdKPILHDITLYAKP 412
Cdd:TIGR01271 382 KTLEYnlttteVEMVNVTASWDEGIGELFEK----IKQNNKARKQPN-----GDDGLFFSNFSLYV-TPVLKNISFKLEK 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 413 GQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGininKIKKSDlrhslgivlQDTNLFTGTVRENIRYGrLDATDEE 492
Cdd:TIGR01271 452 GQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG----RISFSP---------QTSWIMPGTIKDNIIFG-LSYDEYR 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 493 IEVAARLANADEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDTRTE-SLVQQGMDGLMY 571
Cdd:TIGR01271 518 YTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEkEIFESCLCKLMS 597
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2541161597 572 GRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEELIAQK 612
Cdd:TIGR01271 598 NKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
387-608 |
9.79e-21 |
|
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: 91.53 E-value: 9.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 387 VRFFDVDFAYNpDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSdlRHSLGIV 466
Cdd:cd03300 1 IELENVSKFYG-GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 467 LQDTNLFTG-TVRENIRYG----RLDATD--EEIEVAARLANADEFIRRLPqgydtmltdngASLSQGQRQLIAIARAAV 539
Cdd:cd03300 78 FQNYALFPHlTVFENIAFGlrlkKLPKAEikERVAEALDLVQLEGYANRKP-----------SQLSGGQQQRVAIARALV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2541161597 540 ADPPVMILDEATSSIDTRTESLVQQGMDGL--MYGRTVFVIAHRLS---TVrnSNAIMVLEHGRIIERGSHEEL 608
Cdd:cd03300 147 NEPKVLLLDEPLGALDLKLRKDMQLELKRLqkELGITFVFVTHDQEealTM--SDRIAVMNKGKIQQIGTPEEI 218
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
163-615 |
1.79e-20 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 96.55 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 163 ILAVFFSmlvmsWQ-LTIVVLVCVAVMLVMV---RVIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKE 238
Cdd:TIGR00957 446 ILALYFL-----WLnLGPSVLAGVAVMVLMVplnAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFLD 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 239 DFDKLNDTLAGSARKAnqyanilmPAMNNVGNLQYV----VIAIIGGAIALH-GGGLTLGAIAAFLQLS--KSFTQPISQ 311
Cdd:TIGR00957 521 KVEGIRQEELKVLKKS--------AYLHAVGTFTWVctpfLVALITFAVYVTvDENNILDAEKAFVSLAlfNILRFPLNI 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 312 ISQQMNAIVMALAGASRVFE-LMDEEPEQDEgyvtlVNAKYLPDGSLTETSERTGIWAWKHPhengtttytkltgdvrff 390
Cdd:TIGR00957 593 LPMVISSIVQASVSLKRLRIfLSHEELEPDS-----IERRTIKPGEGNSITVHNATFTWARD------------------ 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 391 dvdfaynpDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGininkikksdlrhSLGIVLQDT 470
Cdd:TIGR00957 650 --------LPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQA 708
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 471 NLFTGTVRENIRYGRldATDEE-----IEVAARLANadefIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVM 545
Cdd:TIGR00957 709 WIQNDSLRENILFGK--ALNEKyyqqvLEACALLPD----LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIY 782
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2541161597 546 ILDEATSSIDTRTESLVQQ---GMDGLMYGRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEELIAQKGVY 615
Cdd:TIGR00957 783 LFDDPLSAVDAHVGKHIFEhviGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
387-601 |
3.18e-20 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 90.53 E-value: 3.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 387 VRFFDVDFAYNPDK---PILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKikksdLRHSL 463
Cdd:COG1116 8 LELRGVSKRFPTGGggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 464 GIVLQDTNLF---TgtVRENIRYGrLDATDEEIEVAARLANA-------DEFIRRLPqgydtmltdngASLSQGQRQLIA 533
Cdd:COG1116 83 GVVFQEPALLpwlT--VLDNVALG-LELRGVPKAERRERAREllelvglAGFEDAYP-----------HQLSGGMRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 534 IARAAVADPPVMILDEATSSID--TRTE------SLVQQgmdglmYGRTVFVIAH------RLSTvRnsnaIMVLEH--G 597
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDalTRERlqdellRLWQE------TGKTVLFVTHdvdeavFLAD-R----VVVLSArpG 217
|
....
gi 2541161597 598 RIIE 601
Cdd:COG1116 218 RIVE 221
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
387-608 |
4.34e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 90.58 E-value: 4.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 387 VRFFDVDFAYNPDKPI-LHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGI 465
Cdd:PRK13648 8 IVFKNVSFQYQSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 466 VLQD-TNLFTGTVrenIRYgrldatdeeiEVAARLAN----ADEFIRRLPQGY-DTMLTDNG----ASLSQGQRQLIAIA 535
Cdd:PRK13648 88 VFQNpDNQFVGSI---VKY----------DVAFGLENhavpYDEMHRRVSEALkQVDMLERAdyepNALSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2541161597 536 RAAVADPPVMILDEATSSIDTRTE----SLVQQGMDGlmYGRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEEL 608
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARqnllDLVRKVKSE--HNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
399-580 |
4.69e-20 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 88.69 E-value: 4.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 399 DKPILHDITLYAKPGQKLAFVGSTGAGKTT----ITNLINRFydiaDGKIRYDGININKiKKSDLRHSLGIVLQDTNLFT 474
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTllriLAGLLPPS----AGEVLWNGEPIRD-AREDYRRRLAYLGHADGLKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 475 G-TVRENIRY----GRLDATDEEIEVAARLANADEFIRRLPqgydtmltdngASLSQGQRQLIAIARAAVADPPVMILDE 549
Cdd:COG4133 89 ElTVRENLRFwaalYGLRADREAIDEALEAVGLAGLADLPV-----------RQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190
....*....|....*....|....*....|..
gi 2541161597 550 ATSSIDTRTESLVQQGMDG-LMYGRTVFVIAH 580
Cdd:COG4133 158 PFTALDAAGVALLAELIAAhLARGGAVLLTTH 189
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
391-624 |
5.97e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 90.18 E-value: 5.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 391 DVDFAYNPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQDT 470
Cdd:PRK13647 9 DLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 471 N--LFTGTVRENIRYG------RLDATDEEIEVAARLANADEFIRRLPQgydtmltdngaSLSQGQRQLIAIARAAVADP 542
Cdd:PRK13647 89 DdqVFSSTVWDDVAFGpvnmglDKDEVERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 543 PVMILDEATSSIDTRTESLVQQGMDGL-MYGRTVFVIAHRLSTVRN-SNAIMVLEHGRIIERG-----SHEELIAQKGVY 615
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGdksllTDEDIVEQAGLR 237
|
....*....
gi 2541161597 616 YQLYTGAFE 624
Cdd:PRK13647 238 LPLVAQIFE 246
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
407-612 |
7.78e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 88.87 E-value: 7.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 407 TLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSdlRHSLGIVLQDTNLFTG-TVRENIRYG- 484
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFSHlTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 485 ----RLDATD-EEIEVAARLANADEFIRRLPqgydtmltdngASLSQGQRQLIAIARAAVADPPVMILDEATSSIDT--R 557
Cdd:PRK10771 97 npglKLNAAQrEKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPalR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2541161597 558 TESLV-------QQGMDGLMygrtvfvIAHRLS-TVRNSNAIMVLEHGRIIERGSHEELIAQK 612
Cdd:PRK10771 166 QEMLTlvsqvcqERQLTLLM-------VSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
386-608 |
8.26e-20 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 91.31 E-value: 8.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 386 DVRFFDVDFAYNpDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGINInkikkSDL----RH 461
Cdd:COG3842 5 ALELENVSKRYG-DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-----TGLppekRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 462 sLGIVLQDTNLFTG-TVRENIRYG-RLDATDEEiEVAARLANA------DEFIRRLPqgydtmltdngASLSQGQRQLIA 533
Cdd:COG3842 79 -VGMVFQDYALFPHlTVAENVAFGlRMRGVPKA-EIRARVAELlelvglEGLADRYP-----------HQLSGGQQQRVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 534 IARAAVADPPVMILDEATSSID------TRTE--SLVQQgmdglmYGRT-VFV---------IAHRlstvrnsnaIMVLE 595
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDaklreeMREElrRLQRE------LGITfIYVthdqeealaLADR---------IAVMN 210
|
250
....*....|...
gi 2541161597 596 HGRIIERGSHEEL 608
Cdd:COG3842 211 DGRIEQVGTPEEI 223
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
403-582 |
9.62e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 89.46 E-value: 9.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 403 LHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDI-----ADGKIRYDGININ--KIKKSDLRHSLGIVLQDTNLFTG 475
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLYapDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 476 TVRENIRYG-RLDA----TDEEIEVAARLANA-DEFIRRLPQgydtmltdNGASLSQGQRQLIAIARAAVADPPVMILDE 549
Cdd:PRK14243 106 SIYDNIAYGaRINGykgdMDELVERSLRQAALwDEVKDKLKQ--------SGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190
....*....|....*....|....*....|...
gi 2541161597 550 ATSSIDTRTESLVQQGMDGLMYGRTVFVIAHRL 582
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
391-614 |
1.35e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 89.52 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 391 DVDFAYNPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKS--DLRHSLGIVLQ 468
Cdd:PRK13636 10 ELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmKLRESVGMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 469 --DTNLFTGTVRENIRYGRLDATDEEIEVAARLANADEfirrlPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMI 546
Cdd:PRK13636 90 dpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALK-----RTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2541161597 547 LDEATSSIDTRTES----LVQQGMDGLmyGRTVFVIAHRLSTVR-NSNAIMVLEHGRIIERGSHEELIAQKGV 614
Cdd:PRK13636 165 LDEPTAGLDPMGVSeimkLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEKEM 235
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
386-609 |
1.75e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 91.06 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 386 DVRFFDVDFAynpDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGI 465
Cdd:PRK09536 5 DVSDLSVEFG---DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 466 VLQDTNL-FTGTVRENIRYGR---------LDATDEE-IEVAARLANADEFIRRlpqgydtmltdNGASLSQGQRQLIAI 534
Cdd:PRK09536 82 VPQDTSLsFEFDVRQVVEMGRtphrsrfdtWTETDRAaVERAMERTGVAQFADR-----------PVTSLSGGERQRVLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 535 ARAAVADPPVMILDEATSSID----TRTESLVQQGMDGlmyGRTVFVIAHRLS-TVRNSNAIMVLEHGRIIERGSHEELI 609
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLDinhqVRTLELVRRLVDD---GKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
402-608 |
2.57e-19 |
|
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: 87.20 E-value: 2.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 402 ILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDL-RHSLGIVLQDTNLFTG-TVRE 479
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYVPQGREIFPRlTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 480 NIRYGrLDATdeeievAARLANADEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDTrte 559
Cdd:TIGR03410 95 NLLTG-LAAL------PRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQP--- 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2541161597 560 SLVQQGMDGLMY-----GRTVFVIAHRLSTVRN-SNAIMVLEHGRIIERGSHEEL 608
Cdd:TIGR03410 165 SIIKDIGRVIRRlraegGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
394-608 |
2.72e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 87.80 E-value: 2.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 394 FAYNPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDI------ADGKIRYDGININKIKKSDLRHSLGIVL 467
Cdd:PRK14246 17 YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIydskikVDGKVLYFGKDIFQIDAIKLRKEVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 468 QDTNLFTG-TVRENIRYG-RLDATDEEIEVAARLANADEFIRRLPQGYDTmLTDNGASLSQGQRQLIAIARAAVADPPVM 545
Cdd:PRK14246 97 QQPNPFPHlSIYDNIAYPlKSHGIKEKREIKKIVEECLRKVGLWKEVYDR-LNSPASQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2541161597 546 ILDEATSSIDTRTESLVQQGMDGLMYGRTVFVIAHRLSTV-RNSNAIMVLEHGRIIERGSHEEL 608
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
101-329 |
3.91e-19 |
|
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: 88.25 E-value: 3.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 101 TVSQRTLKGIRDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIV 180
Cdd:cd18554 72 WIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 181 VLVCVAVMLVMVRVIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANQYANI 260
Cdd:cd18554 152 SLVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAK 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2541161597 261 LMPAMNNVGNLQYVVIAIIGGAIALHgGGLTLGAIAAFLQLSKSFTQPISQISQQMNAIVMALAGASRV 329
Cdd:cd18554 232 TFSAVNTITDLAPLLVIGFAAYLVIE-GNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
399-607 |
4.25e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 89.62 E-value: 4.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 399 DKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDlRHsLGIVLQDTNLFTG-TV 477
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN-RH-VNTVFQSYALFPHmTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 478 RENIRYG-RLDATDEEiEVAARLANA------DEFIRRLPQgydtmltdngaSLSQGQRQLIAIARAAVADPPVMILDEA 550
Cdd:PRK09452 104 FENVAFGlRMQKTPAA-EITPRVMEAlrmvqlEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 551 TSSIDTRTESLVQQGMDGLM--YGRT-VFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEE 607
Cdd:PRK09452 172 LSALDYKLRKQMQNELKALQrkLGITfVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
398-608 |
4.62e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 91.26 E-value: 4.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 398 PDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINrFYDIADGKIRYD-GININKIKKSDLRHSLGIVLQDtNLFTG- 475
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKGVKGSGSvLLNGMPIDAKEMRAISAYVQQD-DLFIPt 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 476 -TVRENI------RYGRLDATDEeievaaRLANADEFIRR--LPQGYDTMLTDNGA--SLSQGQRQLIAIARAAVADPPV 544
Cdd:TIGR00955 114 lTVREHLmfqahlRMPRRVTKKE------KRERVDEVLQAlgLRKCANTRIGVPGRvkGLSGGERKRLAFASELLTDPPL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2541161597 545 MILDEATSSIDTRTESLVQQGMDGL-MYGRTVFVIAHRLST--VRNSNAIMVLEHGRIIERGSHEEL 608
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGLaQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
403-610 |
4.68e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 90.46 E-value: 4.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 403 LHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDG--ININKIKKSdLRHSLGIVLQDTNLFTG-TVRE 479
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSPRDA-QAAGIAIIHQELNLVPNlSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 480 NIRYGRLDATDEEIEVAARLANADEFIRRLpqGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIdTRTE 559
Cdd:COG1129 99 NIFLGREPRRGGLIDWRAMRRRARELLARL--GLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASL-TERE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2541161597 560 S---------LVQQGMdglmygrTVFVIAHRLSTVRN-SNAIMVLEHGRIIERG-----SHEELIA 610
Cdd:COG1129 176 VerlfriirrLKAQGV-------AIIYISHRLDEVFEiADRVTVLRDGRLVGTGpvaelTEDELVR 234
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
387-610 |
4.92e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 87.74 E-value: 4.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 387 VRFFDVDFAYNPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKK-SDLRHSLGI 465
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 466 VLQ--DTNLFTGTVRENIRYGRLDATDEEIEVAARLANA------DEFIRRLPQgydtmltdngaSLSQGQRQLIAIARA 537
Cdd:PRK13644 82 VFQnpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRAlaeiglEKYRHRSPK-----------TLSGGQGQCVALAGI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2541161597 538 AVADPPVMILDEATSSIDTRTESLVQQGMDGLM-YGRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEELIA 610
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHeKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
391-612 |
8.86e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 86.67 E-value: 8.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 391 DVDFAYNPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKS--DLRHSLGIVLQ 468
Cdd:PRK13639 6 DLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllEVRKTVGIVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 469 --DTNLFTGTVRENIRYGRLDATDEEIEVAARLANA------DEFIRRLPQgydtmltdngaSLSQGQRQLIAIARAAVA 540
Cdd:PRK13639 86 npDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEAlkavgmEGFENKPPH-----------HLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2541161597 541 DPPVMILDEATSSIDTRTESLVQQgmdgLMY-----GRTVFVIAHRLSTV-RNSNAIMVLEHGRIIERGSHEELIAQK 612
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMK----LLYdlnkeGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
31-338 |
1.51e-18 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 86.74 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 31 LVVVLVAILISAAASVGASVFLESLIDDYIKPLllQDVPVFTGLVHALMgMAVLYLAGLLATYLYNRIMVTVSQRTLKGI 110
Cdd:cd18578 11 LLLGLIGAIIAGAVFPVFAILFSKLISVFSLPD--DDELRSEANFWALM-FLVLAIVAGIAYFLQGYLFGIAGERLTRRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 111 RDTLFSHMQALPIRYFDTHPH--GDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVM 188
Cdd:cd18578 88 RKLAFRAILRQDIAWFDDPENstGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVGLATVPLL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 189 LVMVRVIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANQYANILMpAMNNV 268
Cdd:cd18578 168 LLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGF-GLSQS 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2541161597 269 gnLQYVVIAII---GGAIALHGGgltlgaiAAFLQLSKSFT------QPISQISQQMNAIVMALAGASRVFELMDEEPE 338
Cdd:cd18578 247 --LTFFAYALAfwyGGRLVANGE-------YTFEQFFIVFMalifgaQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPE 316
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
402-611 |
1.65e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 85.79 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 402 ILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSD-------------LRHSLGIVLQ 468
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkvadknqlrlLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 469 DTNLFTG-TVRENIRYGRLD----ATDEEIEVAARLANADEFIRRLPQGYDtmltdngASLSQGQRQLIAIARAAVADPP 543
Cdd:PRK10619 100 HFNLWSHmTVLENVMEAPIQvlglSKQEARERAVKYLAKVGIDERAQGKYP-------VHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 544 VMILDEATSSIDTRTESLVQQGMDGLM-YGRTVFVIAHRLSTVRN-SNAIMVLEHGRIIERGSHEELIAQ 611
Cdd:PRK10619 173 VLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
130-626 |
2.13e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 89.80 E-value: 2.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 130 PHGDIMSVYTNDVDTLRQmISQSIPQAMSSVITILavfFSMLVMSWQLTIVVLVCVAVMLVMVRViarrsGTFFIQ---- 205
Cdd:PLN03130 396 TSGKITNLMTTDAEALQQ-ICQQLHTLWSAPFRII---IAMVLLYQQLGVASLIGSLMLVLMFPI-----QTFIISkmqk 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 206 ------QQTDlgKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANqyaniLMPAMNN--VGNLQYVVIA 277
Cdd:PLN03130 467 ltkeglQRTD--KRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQ-----LLSAFNSfiLNSIPVLVTV 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 278 IIGGAIALHGGGLTlgAIAAFLQLS-------KSFTQPiSQISQQMNAIVmalaGASRVFELMDEEPEqdegyVTLVNAK 350
Cdd:PLN03130 540 VSFGVFTLLGGDLT--PARAFTSLSlfavlrfPLFMLP-NLITQAVNANV----SLKRLEELLLAEER-----VLLPNPP 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 351 YLPDgsLTETSERTGIWAWKHPHEngtttytkltgdvrffdvdfaynpdKPILHDITLYAKPGQKLAFVGSTGAGKTT-I 429
Cdd:PLN03130 608 LEPG--LPAISIKNGYFSWDSKAE-------------------------RPTLSNINLDVPVGSLVAIVGSTGEGKTSlI 660
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 430 TNLINRFYDIADGKIRydgininkikksdLRHSLGIVLQDTNLFTGTVRENIRYGrLDATDEEIEVAARLANADEFIRRL 509
Cdd:PLN03130 661 SAMLGELPPRSDASVV-------------IRGTVAYVPQVSWIFNATVRDNILFG-SPFDPERYERAIDVTALQHDLDLL 726
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 510 PQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDTRTESLV-QQGMDGLMYGRTVFVIAHRLSTVRNS 588
Cdd:PLN03130 727 PGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVfDKCIKDELRGKTRVLVTNQLHFLSQV 806
|
490 500 510
....*....|....*....|....*....|....*...
gi 2541161597 589 NAIMVLEHGRIIERGSHEELIAQKGVYYQLYTGAFEME 626
Cdd:PLN03130 807 DRIILVHEGMIKEEGTYEELSNNGPLFQKLMENAGKME 844
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
400-607 |
2.72e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 84.82 E-value: 2.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 400 KPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQDTNL-FTGTVR 478
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 479 ENIRYGRL------DATDEEIEVAARLANADEFIRRLPQgydtmltdngaSLSQGQRQLIAIARA------AVADPPVMI 546
Cdd:PRK13548 95 EVVAMGRAphglsrAEDDALVAAALAQVDLAHLAGRDYP-----------QLSGGEQQRVQLARVlaqlwePDGPPRWLL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 547 LDEATSSIDTR--------TESLVQQGmdglmyGRTVFVIAHRLS-TVRNSNAIMVLEHGRIIERGSHEE 607
Cdd:PRK13548 164 LDEPTSALDLAhqhhvlrlARQLAHER------GLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAE 227
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
399-612 |
3.30e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 86.42 E-value: 3.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 399 DKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSdLRHSLGIVLQDTNL-FTGTV 477
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARL-ARARIGVVPQFDNLdLEFTV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 478 RENI----RYGRLDATDEEIEVAARLanadEFIRrLPQGYDTMLTDngasLSQGQRQLIAIARAAVADPPVMILDEATSS 553
Cdd:PRK13536 132 RENLlvfgRYFGMSTREIEAVIPSLL----EFAR-LESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTG 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2541161597 554 IDTRTESLVQQGMDGLM-YGRTVFVIAHRLSTV-RNSNAIMVLEHGRIIERGSHEELIAQK 612
Cdd:PRK13536 203 LDPHARHLIWERLRSLLaRGKTILLTTHFMEEAeRLCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
387-611 |
3.77e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 85.17 E-value: 3.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 387 VRFFDVDFAYNPDKPI----LHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSD---- 458
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFasraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 459 LRHSLGIVLQ--DTNLFTGTVRENIRYG--RLDATDEEIE-VAAR----LANADEFIRRLPqgydtmltdngASLSQGQR 529
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGpqNFGIPKEKAEkIAAEklemVGLADEFWEKSP-----------FELSGGQM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 530 QLIAIARAAVADPPVMILDEATSSIDTRTESLVQQGMDGL-MYGRTVFVIAHRLSTVRN-SNAIMVLEHGRIIERGSHEE 607
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSD 230
|
....
gi 2541161597 608 LIAQ 611
Cdd:PRK13643 231 VFQE 234
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
396-611 |
4.91e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 85.62 E-value: 4.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 396 YNPDKPI--LHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDL---RHSLGIVLQDT 470
Cdd:PRK11153 12 PQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkaRRQIGMIFQHF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 471 NLFTG-TVRENIRYG-RLDATDEEiEVAARlanADEFIRRLpqGydtmLTDNG----ASLSQGQRQLIAIARAAVADPPV 544
Cdd:PRK11153 92 NLLSSrTVFDNVALPlELAGTPKA-EIKAR---VTELLELV--G----LSDKAdrypAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2541161597 545 MILDEATSSIDTR-TESLVQqgmdgLM------YGRTVFVIAHRLSTVRN-SNAIMVLEHGRIIERGSHEELIAQ 611
Cdd:PRK11153 162 LLCDEATSALDPAtTRSILE-----LLkdinreLGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGTVSEVFSH 231
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
401-612 |
6.03e-18 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 84.52 E-value: 6.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 401 PILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGininKIKKSDlrhslgivlQDTNLFTGTVREN 480
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG----RISFSS---------QFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 481 IRYGrLDATDEEIEVAARLANADEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDTRTES 560
Cdd:cd03291 118 IIFG-VSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEK 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2541161597 561 LV-QQGMDGLMYGRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEELIAQK 612
Cdd:cd03291 197 EIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
79-314 |
8.70e-18 |
|
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: 84.09 E-value: 8.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 79 MGMAVLYLA----GLLATYLY----NRIMVTVSQRtlkgirdtLFSHMQALPIRYFDTHPHGDIMSvYTNDVDTLRQMIS 150
Cdd:cd18588 46 IGLLVVALFeavlSGLRTYLFshttNRIDAELGAR--------LFRHLLRLPLSYFESRQVGDTVA-RVRELESIRQFLT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 151 QSipqAMSSVITIL--AVFFS-MLVMSWQLTIVVLVCVAVM----LVMVRVIARRsgtffIQQQTDLGKLN-GYIEEMIE 222
Cdd:cd18588 117 GS---ALTLVLDLVfsVVFLAvMFYYSPTLTLIVLASLPLYallsLLVTPILRRR-----LEEKFQRGAENqSFLVETVT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 223 GQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANQYANIlmpAMNNVGNLQYVVIAII--GGAIALHGGGLTLGAIAAFLQ 300
Cdd:cd18588 189 GIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNL---ASQIVQLIQKLTTLAIlwFGAYLVMDGELTIGQLIAFNM 265
|
250
....*....|....
gi 2541161597 301 LSKSFTQPISQISQ 314
Cdd:cd18588 266 LAGQVSQPVLRLVQ 279
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
391-611 |
1.03e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 83.70 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 391 DVDFAYNPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQ-- 468
Cdd:PRK13652 8 DLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQnp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 469 DTNLFTGTVRENIRYGRLDATDEEIEVAARLanaDEFIRRLpqGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILD 548
Cdd:PRK13652 88 DDQIFSPTVEQDIAFGPINLGLDEETVAHRV---SSALHML--GLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2541161597 549 EATSSIDTrteslvqQGMDGLM---------YGRTVFVIAHRLSTVRN-SNAIMVLEHGRIIERGSHEELIAQ 611
Cdd:PRK13652 163 EPTAGLDP-------QGVKELIdflndlpetYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
387-612 |
1.33e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 83.68 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 387 VRFFDVDFAYNPDKPI----LHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGINI-NKIKKSDLRH 461
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqaIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 462 ---SLGIVLQ--DTNLFTGTVRENIRYGRLDATDEEIEVAARlanADEFIRRLPQGYDTMlTDNGASLSQGQRQLIAIAR 536
Cdd:PRK13646 83 vrkRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKNY---AHRLLMDLGFSRDVM-SQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2541161597 537 AAVADPPVMILDEATSSIDTRTESLVQQGMDGLMY--GRTVFVIAHRLSTV-RNSNAIMVLEHGRIIERGSHEELIAQK 612
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTdeNKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKDK 237
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
397-608 |
1.43e-17 |
|
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: 81.78 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 397 NPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKiKKSDLRHSLGIVLQDTNLFTG- 475
Cdd:cd03263 12 KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALFDEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 476 TVRENIR-YGRL-----DATDEEIEVAARLANADEFIRRLPQgydtmltdngaSLSQGQRQLIAIARAAVADPPVMILDE 549
Cdd:cd03263 91 TVREHLRfYARLkglpkSEIKEEVELLLRVLGLTDKANKRAR-----------TLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2541161597 550 ATSSIDTRTESLVQQGMDGLMYGRTVF----------VIAHRLstvrnsnAIMVleHGRIIERGSHEEL 608
Cdd:cd03263 160 PTSGLDPASRRAIWDLILEVRKGRSIIltthsmdeaeALCDRI-------AIMS--DGKLRCIGSPQEL 219
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
387-604 |
2.30e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 82.87 E-value: 2.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 387 VRFFDVDFAYNPDKPI----LHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGINI-----NKIKKS 457
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegraLFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstskNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 458 dLRHSLGIVLQ--DTNLFTGTVRENIRYG--RLDATDEEIEVAARlanadEFIRRLpqGYDTMLTD-NGASLSQGQRQLI 532
Cdd:PRK13649 83 -IRKKVGLVFQfpESQLFEETVLKDVAFGpqNFGVSQEEAEALAR-----EKLALV--GISESLFEkNPFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 533 AIARAAVADPPVMILDEATSSID--------TRTESLVQQGMdglmygrTVFVIAHRLSTVRN-SNAIMVLEHGRIIERG 603
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDpkgrkelmTLFKKLHQSGM-------TIVLVTHLMDDVANyADFVYVLEKGKLVLSG 227
|
.
gi 2541161597 604 S 604
Cdd:PRK13649 228 K 228
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
394-610 |
2.58e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 82.45 E-value: 2.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 394 FAYNPDKPI--LHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQD-T 470
Cdd:PRK13642 12 FKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNpD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 471 NLFTG-TVRENIRYGRLDATDEEIEVAARLANADEFIRRLpqgydTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDE 549
Cdd:PRK13642 92 NQFVGaTVEDDVAFGMENQGIPREEMIKRVDEALLAVNML-----DFKTREPARLSGGQKQRVAVAGIIALRPEIIILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2541161597 550 ATSSIDTRTESLVQQGMDGL--MYGRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEELIA 610
Cdd:PRK13642 167 STSMLDPTGRQEIMRVIHEIkeKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
386-610 |
4.50e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 81.99 E-value: 4.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 386 DVRFFDVDFAYNPDKPI----LHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKS---- 457
Cdd:PRK13634 2 DITFQKVEHRYQYKTPFerraLYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 458 DLRHSLGIVLQ--DTNLFTGTVRENIRYGRLD--ATDEEIEvaarlANADEFIRR--LPQGYdtmLTDNGASLSQGQRQL 531
Cdd:PRK13634 82 PLRKKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEEDAK-----QKAREMIELvgLPEEL---LARSPFELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 532 IAIARAAVADPPVMILDEATSSIDTRTeslvQQGMDGLMY------GRTVFVIAHRLSTVRN-SNAIMVLEHGRIIERGS 604
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDPKG----RKEMMEMFYklhkekGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGT 229
|
....*.
gi 2541161597 605 HEELIA 610
Cdd:PRK13634 230 PREIFA 235
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
411-611 |
4.53e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 82.70 E-value: 4.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 411 KPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGINI---NKIKKSDLRHSLGIVLQDTnlftgtvrenirYGRLD 487
Cdd:PRK11308 39 ERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPEAQKLLRQKIQIVFQNP------------YGSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 488 ------ATDEE-------IEVAARLANADEFIRRL---PQGYDT---MLtdngaslSQGQRQLIAIARAAVADPPVMILD 548
Cdd:PRK11308 107 prkkvgQILEEpllintsLSAAERREKALAMMAKVglrPEHYDRyphMF-------SGGQRQRIAIARALMLDPDVVVAD 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2541161597 549 EATSSIDTRTESLV-------QQGMdGLMYgrtVFvIAHRLSTVRN-SNAIMVLEHGRIIERGSHEELIAQ 611
Cdd:PRK11308 180 EPVSALDVSVQAQVlnlmmdlQQEL-GLSY---VF-ISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
398-608 |
5.07e-17 |
|
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: 80.85 E-value: 5.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 398 PDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDlrHSLGIVLQDTNLFTG-T 476
Cdd:cd03296 13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVFQHYALFRHmT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 477 VRENIRYGRldatdeEIEVAARLANADEFIRRLPQGYDTMLTDNGAS-----LSQGQRQLIAIARAAVADPPVMILDEAT 551
Cdd:cd03296 91 VFDNVAFGL------RVKPRSERPPEAEIRAKVHELLKLVQLDWLADrypaqLSGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 552 SSIDTRTESLVQQGMDGL---MYGRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEEL 608
Cdd:cd03296 165 GALDAKVRKELRRWLRRLhdeLHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
394-601 |
5.16e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 81.27 E-value: 5.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 394 FAYNPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSD---LRHSLGIVLQDT 470
Cdd:PRK10419 19 SGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkaFRRDIQMVFQDS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 471 nlfTG------TVRENIR-----YGRLDATDEEIEVAARLAN---ADEFIRRLPQgydtmltdngaSLSQGQRQLIAIAR 536
Cdd:PRK10419 99 ---ISavnprkTVREIIReplrhLLSLDKAERLARASEMLRAvdlDDSVLDKRPP-----------QLSGGQLQRVCLAR 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2541161597 537 AAVADPPVMILDEATSSIDTrtesLVQQGMDGLM------YGRTVFVIAHRLSTV-RNSNAIMVLEHGRIIE 601
Cdd:PRK10419 165 ALAVEPKLLILDEAVSNLDL----VLQAGVIRLLkklqqqFGTACLFITHDLRLVeRFCQRVMVMDNGQIVE 232
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
387-599 |
9.86e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 79.53 E-value: 9.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 387 VRFFDVDFAYNPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSD---LRHSL 463
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 464 GIVLQDTNLFTG-TVRENIrygrldatdeEIEVAARLANADEFIRRLPQGYDTM-LTDNGAS----LSQGQRQLIAIARA 537
Cdd:PRK10908 82 GMIFQDHHLLMDrTVYDNV----------AIPLIIAGASGDDIRRRVSAALDKVgLLDKAKNfpiqLSGGEQQRVGIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2541161597 538 AVADPPVMILDEATSSIDTR-TESLVQQGMDGLMYGRTVFVIAHRLSTV-RNSNAIMVLEHGRI 599
Cdd:PRK10908 152 VVNKPAVLLADEPTGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLIsRRSYRMLTLSDGHL 215
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
88-323 |
9.95e-17 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 81.10 E-value: 9.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 88 GLLATYLYNRIMVTVSQRTLkgirDTLFSHMQALPIRYFDTHPHGDIMSvYTNDVDTLRQ-MISQSIPQAMSSVITILAV 166
Cdd:cd18782 59 TALRTYLFTDTANRIDLELG----GTIIDHLLRLPLGFFDKRPVGELST-RISELDTIRGfLTGTALTTLLDVLFSVIYI 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 167 FFsMLVMSWQLTIVVLVCV----AVMLVMVRVIARRsgtffIQQQTDL-GKLNGYIEEMIEGQKVVKVFCHEQKAKedfD 241
Cdd:cd18782 134 AV-LFSYSPLLTLVVLATVplqlLLTFLFGPILRRQ-----IRRRAEAsAKTQSYLVESLTGIQTVKAQNAELKAR---W 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 242 KLNDTLAGSARKANQYANILMpAMNNVGNL--QYVVIAIIG-GAIALHGGGLTLGAIAAFLQLSKSFTQPI---SQISQQ 315
Cdd:cd18782 205 RWQNRYARSLGEGFKLTVLGT-TSGSLSQFlnKLSSLLVLWvGAYLVLRGELTLGQLIAFRILSGYVTGPIlrlSTLWQQ 283
|
....*...
gi 2541161597 316 MNAIVMAL 323
Cdd:cd18782 284 FQELRVSL 291
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
412-603 |
1.18e-16 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 79.26 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 412 PGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGINI----NKIKKSDLRHSLGIVLQDTNLFTG-TVRENIRYGRL 486
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYALFPHlNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 487 DATDEEIEVAAR----LANADEFIRRLPQGydtmltdngasLSQGQRQLIAIARAAVADPPVMILDEATSSIDTRTESLV 562
Cdd:cd03297 102 RKRNREDRISVDelldLLGLDHLLNRYPAQ-----------LSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2541161597 563 QQGMDGLM--YGRTVFVIAHRLSTV-RNSNAIMVLEHGRIIERG 603
Cdd:cd03297 171 LPELKQIKknLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
399-603 |
1.68e-16 |
|
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: 78.41 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 399 DKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKiKKSDLRHsLGiVLQDTNLFTG--T 476
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-NIEALRR-IG-ALIEAPGFYPnlT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 477 VRENIRYGR--LDATDEEIEVAARLANADEFIRRLPQGYdtmltdngaslSQGQRQLIAIARAAVADPPVMILDEATSSI 554
Cdd:cd03268 89 ARENLRLLArlLGIRKKRIDEVLDVVGLKDSAKKKVKGF-----------SLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2541161597 555 DTRTESLVQQGMDGLM-YGRTVFVIAHRLSTVRN-SNAIMVLEHGRIIERG 603
Cdd:cd03268 158 DPDGIKELRELILSLRdQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
383-610 |
2.05e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 80.05 E-value: 2.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 383 LTGDVRFFDVDFAYNPDKPI----LHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGK-IRYD---GININKI 454
Cdd:PRK13645 3 FSKDIILDNVSYTYAKKTPFefkaLNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtIVGDyaiPANLKKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 455 KK-SDLRHSLGIVLQ--DTNLFTGTVRENIRYGRLDATDEEIEVAARLANADEFIRrLPQGYdtmLTDNGASLSQGQRQL 531
Cdd:PRK13645 83 KEvKRLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQ-LPEDY---VKRSPFELSGGQKRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 532 IAIARAAVADPPVMILDEATSSIDTRTESLVQQGMDGL--MYGRTVFVIAHRLSTV-RNSNAIMVLEHGRIIERGSHEEL 608
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnkEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSPFEI 238
|
..
gi 2541161597 609 IA 610
Cdd:PRK13645 239 FS 240
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
399-612 |
2.49e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 79.29 E-value: 2.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 399 DKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQDTNLFTG-TV 477
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 478 RENIRYGR---------LDATDEE-IEVAARLANADEFIRRLpqgydtmLTDngasLSQGQRQLIAIARAAVADPPVMIL 547
Cdd:PRK11231 94 RELVAYGRspwlslwgrLSAEDNArVNQAMEQTRINHLADRR-------LTD----LSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 548 DEATSSIDTRTE----SLVQQGMDGlmyGRTVFVIAHRLSTV-RNSNAIMVLEHGRIIERGSHEELIAQK 612
Cdd:PRK11231 163 DEPTTYLDINHQvelmRLMRELNTQ---GKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
394-597 |
3.36e-16 |
|
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: 77.76 E-value: 3.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 394 FAYNPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDL----RHSLGIVLQD 469
Cdd:cd03290 8 FSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 470 TNLFTGTVRENIRYGRlDATDEEIEVAARLANADEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDE 549
Cdd:cd03290 88 PWLLNATVEENITFGS-PFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2541161597 550 ATSSIDTR-TESLVQQGMDGLMYG--RTVFVIAHRLSTVRNSNAIMVLEHG 597
Cdd:cd03290 167 PFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
72-307 |
4.21e-16 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 79.04 E-value: 4.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 72 TGLVHAL-MGMAVLYLAGLLATYLYNRIMVTVSQRTLKGIRDTLFSHMQALPIRYFDTHPHGDIMSVYtNDVDTLRQMIS 150
Cdd:cd18567 38 RDLLTVLaIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFEKRHLGDIVSRF-GSLDEIQQTLT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 151 QSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVMLVmVRVIA----RRSGTFFIQQQTdlgKLNGYIEEMIEGQKV 226
Cdd:cd18567 117 TGFVEALLDGLMAILTLVMMFLYSPKLALIVLAAVALYAL-LRLALypplRRATEEQIVASA---KEQSHFLETIRGIQT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 227 VKVFCHEQKAKEDF-DKLNDTLAGSARKanQYANILMPAMNN-VGNLQYVVIAIIGGAIALHgGGLTLGAIAAFLQLSKS 304
Cdd:cd18567 193 IKLFGREAEREARWlNLLVDAINADIRL--QRLQILFSAANGlLFGLENILVIYLGALLVLD-GEFTVGMLFAFLAYKDQ 269
|
...
gi 2541161597 305 FTQ 307
Cdd:cd18567 270 FSS 272
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
399-610 |
4.92e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 79.08 E-value: 4.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 399 DKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKiKKSDLRHSLGIVLQDTNL---FTg 475
Cdd:PRK13537 19 DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGVVPQFDNLdpdFT- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 476 tVRENI----RYGRLDATdeeiEVAARLANADEFIRrLPQGYDTMLTDngasLSQGQRQLIAIARAAVADPPVMILDEAT 551
Cdd:PRK13537 97 -VRENLlvfgRYFGLSAA----AARALVPPLLEFAK-LENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2541161597 552 SSIDTRTESLVQQGMDGLM-YGRTVFVIAHRLSTV-RNSNAIMVLEHGRIIERGSHEELIA 610
Cdd:PRK13537 167 TGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
391-611 |
5.94e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 78.59 E-value: 5.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 391 DVDFAYNPD-----KPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKS-DLRHSLG 464
Cdd:PRK13633 9 NVSYKYESNeesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDIRNKAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 465 IVLQ--DTNLFTGTVRENIRYG--RLDATDEEI----EVAARLANADEFIRRLPQgydtmltdngaSLSQGQRQLIAIAR 536
Cdd:PRK13633 89 MVFQnpDNQIVATIVEEDVAFGpeNLGIPPEEIrervDESLKKVGMYEYRRHAPH-----------LLSGGQKQRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2541161597 537 AAVADPPVMILDEATSSIDTRTESLVQQGMDGL--MYGRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEELIAQ 611
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnkKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
392-606 |
1.03e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 76.98 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 392 VDFAYNPDKpILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRF-------YDIADGKIRYDG-ININKIKKsdLRHSL 463
Cdd:PRK11124 8 INCFYGAHQ-ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLemprsgtLNIAGNHFDFSKtPSDKAIRE--LRRNV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 464 GIVLQDTNLFTG-TVREN-----IRYGRLD---ATDEEIEVAARLANADeFIRRLPQgydtmltdngaSLSQGQRQLIAI 534
Cdd:PRK11124 85 GMVFQQYNLWPHlTVQQNlieapCRVLGLSkdqALARAEKLLERLRLKP-YADRFPL-----------HLSGGQQQRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2541161597 535 ARAAVADPPVMILDEATSSIDTR-TESLVQQGMDGLMYGRTVFVIAHRLSTVRN-SNAIMVLEHGRIIERGSHE 606
Cdd:PRK11124 153 ARALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
400-610 |
1.04e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 77.83 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 400 KPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGkIRYDGINI-------NKIKKSDLRHSLGIVLQDTNL 472
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVLlggrsifNYRDVLEFRRRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 473 FTGTVRENI----RYGRLDATDEEIEVA-ARLANADefirrLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMIL 547
Cdd:PRK14271 113 FPMSIMDNVlagvRAHKLVPRKEFRGVAqARLTEVG-----LWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2541161597 548 DEATSSIDTRTESLVQQGMDGLMYGRTVFVIAHRLS-TVRNSNAIMVLEHGRIIERGSHEELIA 610
Cdd:PRK14271 188 DEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
394-580 |
1.29e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 77.05 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 394 FAYNPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGINInkikkSDLRHSLGIVLQDTNLF 473
Cdd:PRK11248 8 YADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV-----EGPGAERGVVFQNEGLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 474 T-GTVRENIRYG-RLDATD-EEIEVAAR-------LANADEfiRRLPQgydtmltdngasLSQGQRQLIAIARAAVADPP 543
Cdd:PRK11248 83 PwRNVQDNVAFGlQLAGVEkMQRLEIAHqmlkkvgLEGAEK--RYIWQ------------LSGGQRQRVGIARALAANPQ 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 2541161597 544 VMILDEATSSIDTRTESLVQQGMDGLMY--GRTVFVIAH 580
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKLWQetGKQVLLITH 187
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
74-314 |
1.51e-15 |
|
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: 77.60 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 74 LVHALM-GMAVLYLAGLLATYLYNRIMVTVSQRTLKGIRDTLFSHMQALPIRYFDTHPHGDIMS-VYTNDvdTLRQMISQ 151
Cdd:cd18568 40 LLNLILiGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITrFQENQ--KIRRFLTR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 152 SIPQAMSSVITILAVFFSMLVMSWQLTIVVL---VCVAVMLVMVRVIARRSGTFFIQQQTdlgKLNGYIEEMIEGQKVVK 228
Cdd:cd18568 118 SALTTILDLLMVFIYLGLMFYYNLQLTLIVLafiPLYVLLTLLSSPKLKRNSREIFQANA---EQQSFLVEALTGIATIK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 229 VFCHEQ----KAKEDFDK-LNDTLagsarKANQYANILMPAMNNVGNLQYVVIaIIGGAIALHGGGLTLGAIAAFLQLSK 303
Cdd:cd18568 195 ALAAERpirwRWENKFAKaLNTRF-----RGQKLSIVLQLISSLINHLGTIAV-LWYGAYLVISGQLTIGQLVAFNMLFG 268
|
250
....*....|.
gi 2541161597 304 SFTQPISQISQ 314
Cdd:cd18568 269 SVINPLLALVG 279
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
405-609 |
1.83e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 78.92 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 405 DITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRH----SLGIVLQDTNLFTG-TVRE 479
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPHmTVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 480 NIRYGRLDATdeeIEVAARLANADEFIRRLpqGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDTRTE 559
Cdd:PRK10070 126 NTAFGMELAG---INAEERREKALDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2541161597 560 SLVQQGMDGLM--YGRTVFVIAHRL-STVRNSNAIMVLEHGRIIERGSHEELI 609
Cdd:PRK10070 201 TEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
391-609 |
2.05e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 76.28 E-value: 2.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 391 DVDFAYNpDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQDT 470
Cdd:COG4604 6 NVSKRYG-GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQEN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 471 NLFTG-TVRENI---RY----GRLDATDEE-IEVAARLAN----ADEFIrrlpqgyDTmltdngasLSQGQRQliaiaRA 537
Cdd:COG4604 85 HINSRlTVRELVafgRFpyskGRLTAEDREiIDEAIAYLDledlADRYL-------DE--------LSGGQRQ-----RA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 538 AVA-----DPPVMILDEATSSIDTRTEslVQqgmdgLM---------YGRTVFVIAHRLstvrN-----SNAIMVLEHGR 598
Cdd:COG4604 145 FIAmvlaqDTDYVLLDEPLNNLDMKHS--VQ-----MMkllrrladeLGKTVVIVLHDI----NfascyADHIVAMKDGR 213
|
250
....*....|.
gi 2541161597 599 IIERGSHEELI 609
Cdd:COG4604 214 VVAQGTPEEII 224
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
386-608 |
2.33e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 78.15 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 386 DVRFFDVDFAYNpDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDlrHSLGI 465
Cdd:PRK11000 3 SVTLRNVTKAYG-DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 466 VLQDTNLFTG-TVRENIRYGRLDATDEEIEVAARLANADEfIRRLpqgyDTMLTDNGASLSQGQRQLIAIARAAVADPPV 544
Cdd:PRK11000 80 VFQSYALYPHlSVAENMSFGLKLAGAKKEEINQRVNQVAE-VLQL----AHLLDRKPKALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2541161597 545 MILDEATSSIDT------RTE-SLVQQGMdglmyGRTVFVIAH-RLSTVRNSNAIMVLEHGRIIERGSHEEL 608
Cdd:PRK11000 155 FLLDEPLSNLDAalrvqmRIEiSRLHKRL-----GRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
419-615 |
2.43e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 77.58 E-value: 2.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 419 VGSTGAGKTTITNLINRFYDIADGKIRYDGININ---------------KIKK-SDLRHSLGIVLQ--DTNLFTGTVREN 480
Cdd:PRK13631 58 IGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGdkknnhelitnpyskKIKNfKELRRRVSMVFQfpEYQLFKDTIEKD 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 481 IRYGRLDATDEEIEVAARlanADEFIRRLPQGYDtMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDTRTES 560
Cdd:PRK13631 138 IMFGPVALGVKKSEAKKL---AKFYLNKMGLDDS-YLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEH 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2541161597 561 -LVQQGMDGLMYGRTVFVIAHRLSTVRN-SNAIMVLEHGRIIERGSHEELIAQKGVY 615
Cdd:PRK13631 214 eMMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIFTDQHII 270
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
381-585 |
2.72e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 76.23 E-value: 2.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 381 TKLTGDVRFFDVDFAYNPDKpILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDI-----ADGKIRYDGINI--NK 453
Cdd:PRK14258 2 SKLIPAIKVNNLSFYYDTQK-ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELesevrVEGRVEFFNQNIyeRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 454 IKKSDLRHSLGIVLQDTNLFTGTVRENIRYG--------RLDaTDEEIEVAARLANA-DEFIRRLPQgydtmltdNGASL 524
Cdd:PRK14258 81 VNLNRLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwrpKLE-IDDIVESALKDADLwDEIKHKIHK--------SALDL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2541161597 525 SQGQRQLIAIARAAVADPPVMILDEATSSID----TRTESLVQQGMdgLMYGRTVFVIAHRLSTV 585
Cdd:PRK14258 152 SGGQQQRLCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSLR--LRSELTMVIVSHNLHQV 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
398-608 |
4.44e-15 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 77.11 E-value: 4.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 398 PDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLInrfydiA-----D-GKIRYDGININKIKKSDLRHsLGIVLQDTN 471
Cdd:COG1118 13 GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRII------AgletpDsGRIVLNGRDLFTNLPPRERR-VGFVFQHYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 472 LF-TGTVRENIRYG--RLDATDEEI-EVAARLA---NADEFIRRLPqgydtmltdngASLSQGQRQLIAIARAAVADPPV 544
Cdd:COG1118 86 LFpHMTVAENIAFGlrVRPPSKAEIrARVEELLelvQLEGLADRYP-----------SQLSGGQRQRVALARALAVEPEV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 545 MILDEATSSIDT--RTE------SLVQQgmdglmYGRT-VFV---------IAHRlstvrnsnaIMVLEHGRIIERGSHE 606
Cdd:COG1118 155 LLLDEPFGALDAkvRKElrrwlrRLHDE------LGGTtVFVthdqeealeLADR---------VVVMNQGRIEQVGTPD 219
|
..
gi 2541161597 607 EL 608
Cdd:COG1118 220 EV 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
400-620 |
6.79e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 77.82 E-value: 6.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 400 KPILHDITLYAKPGQKLAFVGSTGAGKTT----ITNLINrfydiADGKIRYDGI---NINKIKKSDLRHSLGIVLQDTNl 472
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQplhNLNRRQLLPVRHRIQVVFQDPN- 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 473 ftgtVRENIRYGRLDATDEEIEVAARLANADEFIRRLPQGYDTMLTDNG------ASLSQGQRQLIAIARAAVADPPVMI 546
Cdd:PRK15134 373 ----SSLNPRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDPEtrhrypAEFSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 547 LDEATSSIDtRTeslVQQGMDGLM------YGRTVFVIAHRLSTVRN-SNAIMVLEHGRIIERGSHEELIAQKGvyyQLY 619
Cdd:PRK15134 449 LDEPTSSLD-KT---VQAQILALLkslqqkHQLAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFAAPQ---QEY 521
|
.
gi 2541161597 620 T 620
Cdd:PRK15134 522 T 522
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
68-273 |
7.19e-15 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 75.43 E-value: 7.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 68 VPVFTGLV--------------HALMGMAVLYLAGLLATYLYNRI-MVTVSQRTLKgIRDTLFSHMQALPIRYFDTHPHG 132
Cdd:cd18784 15 IPYYTGQVidgivieksqdkfsRAIIIMGLLAIASSVAAGIRGGLfTLAMARLNIR-IRNLLFRSIVSQEIGFFDTVKTG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 133 DIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVMLVMVRVIarrsGTFF----IQQQT 208
Cdd:cd18784 94 DITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVY----GDYYkklsKAVQD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2541161597 209 DLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDF-DKLNDTLAGSARKANQYA-----NILMPAMNNVGNLQY 273
Cdd:cd18784 170 SLAKANEVAEETISSIRTVRSFANEDGEANRYsEKLKDTYKLKIKEALAYGgyvwsNELTELALTVSTLYY 240
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
274-581 |
1.33e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 76.77 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 274 VVIAIIGGAIALHGGGLTLGAI----AAFLQLSKSFTQPISQISQ--QMNAIVMALAGASRVFELMDEEPEQDEGyvtlv 347
Cdd:COG4178 280 VIFPILVAAPRYFAGEITLGGLmqaaSAFGQVQGALSWFVDNYQSlaEWRATVDRLAGFEEALEAADALPEAASR----- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 348 nakylpdgsltetsertgiwawKHPHENGTTTYTKLTgdvrffdvdfAYNPD-KPILHDITLYAKPGQKLAFVGSTGAGK 426
Cdd:COG4178 355 ----------------------IETSEDGALALEDLT----------LRTPDgRPLLEDLSLSLKPGERLLITGPSGSGK 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 427 TTITNLINRFYDIADGKIRydgininkikksdlRHSLGIVL---QDTNLFTGTVRENIRY--GRLDATDEEIEVAARLAN 501
Cdd:COG4178 403 STLLRAIAGLWPYGSGRIA--------------RPAGARVLflpQRPYLPLGTLREALLYpaTAEAFSDAELREALEAVG 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 502 ADEFIRRLPQGydtmlTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDTRTESLVQQGMDGLMYGRTVFVIAHR 581
Cdd:COG4178 469 LGHLAERLDEE-----ADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
386-608 |
1.66e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 73.79 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 386 DVRFFDVDFAynpDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDI-----ADGKIRYDGININKIKKSDLR 460
Cdd:PRK14247 5 EIRDLKVSFG---QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELypearVSGEVYLDGQDIFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 461 HSLGIVLQDTN-LFTGTVRENIRYG----RLDATDEEIEVAARLANA-----DEFIRRL--PQGydtmltdngaSLSQGQ 528
Cdd:PRK14247 82 RRVQMVFQIPNpIPNLSIFENVALGlklnRLVKSKKELQERVRWALEkaqlwDEVKDRLdaPAG----------KLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 529 RQLIAIARAAVADPPVMILDEATSSIDTRTESLVQQGMDGLMYGRTVFVIAH-RLSTVRNSNAIMVLEHGRIIERGSHEE 607
Cdd:PRK14247 152 QQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTRE 231
|
.
gi 2541161597 608 L 608
Cdd:PRK14247 232 V 232
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
400-610 |
2.25e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 77.13 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 400 KPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDgininkikksdlrHSLGIVLQDTNLFTGTVRE 479
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 480 NIRYgrldaTDEEieVAARLANA------DEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSS 553
Cdd:PTZ00243 740 NILF-----FDEE--DAARLADAvrvsqlEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2541161597 554 IDTRT-ESLVQQGMDGLMYGRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEELIA 610
Cdd:PTZ00243 813 LDAHVgERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR 870
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
81-329 |
2.72e-14 |
|
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: 73.73 E-value: 2.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 81 MAVLYLAGLLATYLYNRIMVTVSQRTLKGIRDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSV 160
Cdd:cd18574 48 LLGLYLLQSLLTFAYISLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 161 ITILAVFFSMLVMSWQLTIVVLVCVAVMLV-------MVRVIARRSgtffiQQQTdlGKLNGYIEEMIEGQKVVKVFCHE 233
Cdd:cd18574 128 TQTVGCVVSLYLISPKLTLLLLVIVPVVVLvgtlygsFLRKLSRRA-----QAQV--AKATGVADEALGNIRTVRAFAME 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 234 QKAKEDFDKLNDtlagSARKANQY-----------ANIlmpAMNNVgnlqyVVIAIIGGAIALHGGGLTLGAIAAFLQLS 302
Cdd:cd18574 201 DRELELYEEEVE----KAAKLNEKlglgigifqglSNL---ALNGI-----VLGVLYYGGSLVSRGELTAGDLMSFLVAT 268
|
250 260
....*....|....*....|....*..
gi 2541161597 303 KSFTQPISQISQQMNAIVMALAGASRV 329
Cdd:cd18574 269 QTIQRSLAQLSVLFGQYVKGKSAGARV 295
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
402-608 |
3.16e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 74.35 E-value: 3.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 402 ILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRhsLGIVLQDTNLFTG-TVREN 480
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK--VGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 481 IRYG--------RLDATDEEIEVA--------ARLANadefirRLPqgydtmltdngASLSQGQRQLIAIARAAVADPPV 544
Cdd:PRK10851 95 IAFGltvlprreRPNAAAIKAKVTqllemvqlAHLAD------RYP-----------AQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2541161597 545 MILDEATSSIDT--RTE--SLVQQGMDGLMYgRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEEL 608
Cdd:PRK10851 158 LLLDEPFGALDAqvRKElrRWLRQLHEELKF-TSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
70-319 |
4.83e-14 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 72.93 E-value: 4.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 70 VFTGLVHALMGmavlYLAGLLATYLYNRIMVTVSQRTlkgirdtlFSHMQALPIRYFDTHPHGDIMSvYTNDVDTLRQMI 149
Cdd:cd18783 49 VIALLFEGILG----YLRRYLLLVATTRIDARLALRT--------FDRLLSLPIDFFERTPAGVLTK-HMQQIERIRQFL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 150 SQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVM----LVMVRVIARRSGTFFIQQqtdlGKLNGYIEEMIEGQK 225
Cdd:cd18783 116 TGQLFGTLLDATSLLVFLPVLFFYSPTLALVVLAFSALIaliiLAFLPPFRRRLQALYRAE----GERQAFLVETVHGIR 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 226 VVKVFCHEQKAKEDFDKLNDTLAGSARKANQYANILMPAMNNVGNLQYVVIAIIGGAIALhGGGLTLGAIAAFLQLSKSF 305
Cdd:cd18783 192 TVKSLALEPRQRREWDERVARAIRARFAVGRLSNWPQTLTGPLEKLMTVGVIWVGAYLVF-AGSLTVGALIAFNMLAGRV 270
|
250
....*....|....
gi 2541161597 306 TQPISQISQQMNAI 319
Cdd:cd18783 271 AGPLVQLAGLVQEY 284
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
31-333 |
5.65e-14 |
|
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: 72.92 E-value: 5.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 31 LVVVLVAILISAAASVGASVFLESLIDDYIKPLLLQDVpvFTGLVHALMGMAVLYLAGLLATYLYNRIMVTVSQRtlkgI 110
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSG--YYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRR----L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 111 RDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVMLV 190
Cdd:cd18580 75 HDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 191 MVRviarrsgtFFIQQQTDLGKLNG--------YIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTlagsarkaNQYANILM 262
Cdd:cd18580 155 LQR--------YYLRTSRQLRRLESesrsplysHFSETLSGLSTIRAFGWQERFIEENLRLLDA--------SQRAFYLL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 263 PAMNN--------VGNLqyVVIAIIGGAIALHGG------GLtlgAIAAFLQLSKSFTQPISQISQ---QMNAIvmalag 325
Cdd:cd18580 219 LAVQRwlglrldlLGAL--LALVVALLAVLLRSSisaglvGL---ALTYALSLTGSLQWLVRQWTEletSMVSV------ 287
|
....*...
gi 2541161597 326 aSRVFELM 333
Cdd:cd18580 288 -ERILEYT 294
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
397-558 |
6.15e-14 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 71.53 E-value: 6.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 397 NPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLIN---RFYDIADGKIRYDGiniNKIKKSDLRHSLGIVLQDTNLF 473
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNG---QPRKPDQFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 474 TG-TVRENIRYGRLDATDEEIEVAARLANADEFirRLPQGYDTMLTDNG-ASLSQGQRQLIAIARAAVADPPVMILDEAT 551
Cdd:cd03234 94 PGlTVRETLTYTAILRLPRKSSDAIRKKRVEDV--LLRDLALTRIGGNLvKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
....*..
gi 2541161597 552 SSIDTRT 558
Cdd:cd03234 172 SGLDSFT 178
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
391-555 |
9.98e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 70.90 E-value: 9.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 391 DVDFAYNpDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQDT 470
Cdd:PRK10247 12 NVGYLAG-DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 471 NLFTGTVRENIRYG---RLDATDEeievAARLANADEFirRLPqgyDTMLTDNGASLSQGQRQLIAIARAAVADPPVMIL 547
Cdd:PRK10247 91 TLFGDTVYDNLIFPwqiRNQQPDP----AIFLDDLERF--ALP---DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLL 161
|
....*...
gi 2541161597 548 DEATSSID 555
Cdd:PRK10247 162 DEITSALD 169
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
400-621 |
1.26e-13 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 70.65 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 400 KPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKiKKSDLRHSLGIVL--QDTNLFTG-T 476
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITK-LPMHKRARLGIGYlpQEASIFRKlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 477 VRENIRygrldATDEEIEV--AARLANADEFIRRLpqGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDE----- 549
Cdd:cd03218 92 VEENIL-----AVLEIRGLskKEREEKLEELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEpfagv 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2541161597 550 ---ATSSIDTRTESLVQQGMdGLMYG----RTVFVIAHRlstvrnsnaIMVLEHGRIIERGSHEELIAQKGVyYQLYTG 621
Cdd:cd03218 165 dpiAVQDIQKIIKILKDRGI-GVLITdhnvRETLSITDR---------AYIIYEGKVLAEGTPEEIAANELV-RKVYLG 232
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
391-585 |
1.35e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 73.51 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 391 DVDFAYNpDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINrfydiAD------------GKIRYDGININKIKksd 458
Cdd:PRK10938 265 NGVVSYN-DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLIT-----GDhpqgysndltlfGRRRGSGETIWDIK--- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 459 lRHsLGIVLQDTNL---FTGTVRENIRYGRLDATDEEIEVAARLAN-ADEFIRRLpqGYDTMLTDNG-ASLSQGQRQLIA 533
Cdd:PRK10938 336 -KH-IGYVSSSLHLdyrVSTSVRNVILSGFFDSIGIYQAVSDRQQKlAQQWLDIL--GIDKRTADAPfHSLSWGQQRLAL 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2541161597 534 IARAAVADPPVMILDEATSSIDTRTESLVQQGMDGLM-YGRT--VFV----------IAHRLSTV 585
Cdd:PRK10938 412 IVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIsEGETqlLFVshhaedapacITHRLEFV 476
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
399-603 |
1.99e-13 |
|
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: 69.62 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 399 DKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGininKIKKSDLRHSLGIVLQDTNLFTG-TV 477
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG----KPLDIAARNRIGYLPEERGLYPKmKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 478 RENIRY-GRL-DATDEEIevaarLANADEFIRRLPqgydtmLTDNGAS----LSQGQRQLIAIARAAVADPPVMILDEAT 551
Cdd:cd03269 88 IDQLVYlAQLkGLKKEEA-----RRRIDEWLERLE------LSEYANKrveeLSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2541161597 552 SSIDTRTESLVQQGMDGLM-YGRTVFVIAHRLSTV-RNSNAIMVLEHGRIIERG 603
Cdd:cd03269 157 SGLDPVNVELLKDVIRELArAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
398-603 |
2.00e-13 |
|
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: 69.53 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 398 PDKPILHDITLYAKPGQkLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGINInKIKKSDLRHSLGIVLQDTNLFTG-T 476
Cdd:cd03264 11 GKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV-LKQPQKLRRRIGYLPQEFGVYPNfT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 477 VRENIRY----GRLDATDEEIEVAARLANADEFIRRlpqgydtmlTDNGASLSQGQRQLIAIARAAVADPPVMILDEATS 552
Cdd:cd03264 89 VREFLDYiawlKGIPSKEVKARVDEVLELVNLGDRA---------KKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2541161597 553 SID----TRTESLVQQgmdgLMYGRTVFVIAHRLSTVRNS-NAIMVLEHGRIIERG 603
Cdd:cd03264 160 GLDpeerIRFRNLLSE----LGEDRIVILSTHIVEDVESLcNQVAVLNKGKLVFEG 211
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
399-562 |
2.37e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.13 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 399 DKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGivLQD---TNLftg 475
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNamkPAL--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 476 TVRENIRYGR--LDATDEEIEVA-ARLANADefIRRLPQGYdtmltdngasLSQGQRQLIAIARAAVADPPVMILDEATS 552
Cdd:PRK13539 89 TVAENLEFWAafLGGEELDIAAAlEAVGLAP--LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170
....*....|
gi 2541161597 553 SIDTRTESLV 562
Cdd:PRK13539 157 ALDAAAVALF 166
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
391-600 |
3.96e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.02 E-value: 3.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 391 DVDFAYnPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGininkikksDLRhsLGIVLQDT 470
Cdd:COG0488 3 NLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK---------GLR--IGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 471 NLFTG-TVRENIRYG--RLDATDEEIEVA-ARLANADEFIRRLPQGYDTMLTDNG------------------------- 521
Cdd:COG0488 71 PLDDDlTVLDTVLDGdaELRALEAELEELeAKLAEPDEDLERLAELQEEFEALGGweaearaeeilsglgfpeedldrpv 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 522 ASLSQGQRQLIAIARAAVADPPVMILDEATSSIDTRT----ESLVQQgmdglmYGRTVFVIAH-R--LSTVrnSNAIMVL 594
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFLKN------YPGTVLVVSHdRyfLDRV--ATRILEL 222
|
....*.
gi 2541161597 595 EHGRII 600
Cdd:COG0488 223 DRGKLT 228
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
400-600 |
4.13e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 69.73 E-value: 4.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 400 KPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQDTNLFTG---T 476
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDPMMGTApsmT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 477 VRENI--------RYG---RLDATDEEiEVAARLAnadefirRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVM 545
Cdd:COG1101 99 IEENLalayrrgkRRGlrrGLTKKRRE-LFRELLA-------TLGLGLENRLDTKVGLLSGGQRQALSLLMATLTKPKLL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2541161597 546 ILDEATSSIDTR--------TESLVQQgmdglmYGRTVFVIAHRLS-TVRNSNAIMVLEHGRII 600
Cdd:COG1101 171 LLDEHTAALDPKtaalvlelTEKIVEE------NNLTTLMVTHNMEqALDYGNRLIMMHEGRII 228
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
405-608 |
4.26e-13 |
|
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: 68.94 E-value: 4.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 405 DITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKiKKSDLRHSLGIVLQDTNLFTG-TVRENIR- 482
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDElTGWENLYi 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 483 YGRL-----DATDEEIEVAARLANADEFIRRLPQGYdtmltdngaslSQGQRQLIAIARAAVADPPVMILDEATSSIDTR 557
Cdd:cd03265 97 HARLygvpgAERRERIDELLDFVGLLEAADRLVKTY-----------SGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQ 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2541161597 558 TESLVQQGMDGLM--YGRTVFVIAHRLSTVRN-SNAIMVLEHGRIIERGSHEEL 608
Cdd:cd03265 166 TRAHVWEYIEKLKeeFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
31-311 |
1.06e-12 |
|
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: 69.04 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 31 LVVVLVAILISAAASVgasvFLESLI----DDYIKPLLLqdvpvFTGLVhALMGMAVLYLAGLLATYLYNRIMVTVSQRt 106
Cdd:cd18569 12 LLLVIPGLVIPVFSRI----FIDDILvgglPDWLRPLLL-----GMALT-ALLQGLLTWLQQYYLLRLETKLALSSSSR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 107 lkgirdtLFSHMQALPIRYFDTHPHGDIMS-VYTNDvdTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCV 185
Cdd:cd18569 81 -------FFWHVLRLPVEFFSQRYAGDIASrVQSND--RVANLLSGQLATTVLNLVMAVFYALLMLQYDVPLTLIGIAIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 186 AVMLVMVRVIARRSGTFFIQQQTDLGKLNGYIE---EMIEGQKVvkvfcheQKAKEDF--------DKLNDTLAGSARKa 254
Cdd:cd18569 152 LLNLLVLRLVSRKRVDLNRRLLQDSGKLTGTTMsglQMIETLKA-------SGAESDFfsrwagyqAKVLNAQQELGRT- 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2541161597 255 NQYANILMPAMNNVGNlqyVVIAIIGGAIALHgGGLTLGAIAAFLQLSKSFTQPISQ 311
Cdd:cd18569 224 NQLLGALPTLLSALTN---AAILGLGGLLVMD-GALTIGMLVAFQSLMASFLAPVNS 276
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
391-603 |
1.11e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 69.34 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 391 DVDFAYNPDKPI----LHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRY------------------DG 448
Cdd:PRK13651 7 NIVKIFNKKLPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkktkekekvlEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 449 ININ-----KIKK-SDLRHSLGIVLQ--DTNLFTGTVRENIRYGRLDATDEEIEVAARlanADEFIRR--LPQGYdtmLT 518
Cdd:PRK13651 87 LVIQktrfkKIKKiKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKR---AAKYIELvgLDESY---LQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 519 DNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDTrteslvqQGMDGLM--------YGRTVFVIAHRLSTV-RNSN 589
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDP-------QGVKEILeifdnlnkQGKTIILVTHDLDNVlEWTK 233
|
250
....*....|....
gi 2541161597 590 AIMVLEHGRIIERG 603
Cdd:PRK13651 234 RTIFFKDGKIIKDG 247
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
396-608 |
1.26e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 68.33 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 396 YNPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDI-----ADGKIRYDGINI--NKIKKSDLRHSLGIVLQ 468
Cdd:PRK14267 13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELneearVEGEVRLFGRNIysPDVDPIEVRREVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 469 DTNLFTG-TVRENIRYG--------RLDATDEEIEVAARLANA-DEFIRRLpqgydtmlTDNGASLSQGQRQLIAIARAA 538
Cdd:PRK14267 93 YPNPFPHlTIYDNVAIGvklnglvkSKKELDERVEWALKKAALwDEVKDRL--------NDYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2541161597 539 VADPPVMILDEATSSIDTRTESLVQQGMDGLMYGRTVFVIAHR-LSTVRNSNAIMVLEHGRIIERGSHEEL 608
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
76-327 |
1.65e-12 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 68.27 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 76 HALMGMAVLYLAGLLATYLYNRIMVTVSQRTLKGIRDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQ 155
Cdd:cd18589 37 AAITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 156 AMSSVITILAVFFSMLVMSWQLTIVVLVCVAVMLvmvrVIARRSGTFF----IQQQTDLGKLNGYIEEMIEGQKVVKVFC 231
Cdd:cd18589 117 LMWYLARGLFLFIFMLWLSPKLALLTALGLPLLL----LVPKFVGKFQqslaVQVQKSLARANQVAVETFSAMKTVRSFA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 232 HEQKAKEDF-DKLNDT-----LAGSARKANQYANILMPAMNNVGNLQYvviaiigGAIALHGGGLTLGAIAAFLQLSKSF 305
Cdd:cd18589 193 NEEGEAQRYrQRLQKTyrlnkKEAAAYAVSMWTSSFSGLALKVGILYY-------GGQLVTAGTVSSGDLVTFVLYELQF 265
|
250 260
....*....|....*....|..
gi 2541161597 306 TQPIsQISQQMNAIVMALAGAS 327
Cdd:cd18589 266 TSAV-EVLLSYYPSVMKAVGSS 286
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
401-600 |
2.25e-12 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 65.14 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 401 PILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININkikksdlrhslgivlqdtnlfTGTVREN 480
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS---------------------FASPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 481 IRYGrldatdeeievaarlanadefIRRLPQgydtmltdngasLSQGQRQLIAIARAAVADPPVMILDEATSSIDTR-TE 559
Cdd:cd03216 73 RRAG---------------------IAMVYQ------------LSVGERQMVEIARALARNARLLILDEPTAALTPAeVE 119
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2541161597 560 SLVQQgMDGLM-YGRTVFVIAHRLSTVRN-SNAIMVLEHGRII 600
Cdd:cd03216 120 RLFKV-IRRLRaQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
402-583 |
2.38e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 67.15 E-value: 2.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 402 ILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIK---KSDLR-HSLGIVLQDTNLFTG-T 476
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaaKAELRnQKLGFIYQFHHLLPDfT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 477 VRENIRYGRLDATDEEIEVAARlanADEFIRRLpqGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDT 556
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEINSR---ALEMLAAV--GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDA 178
|
170 180
....*....|....*....|....*....
gi 2541161597 557 RTESLVQQGMDGL--MYGRTVFVIAHRLS 583
Cdd:PRK11629 179 RNADSIFQLLGELnrLQGTAFLVVTHDLQ 207
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
412-582 |
2.40e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.65 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 412 PGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININ-KIKKSDLRHSLGIVLQDTNLFTG-TVRENIRYGRldat 489
Cdd:PRK10762 29 PGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEAGIGIIHQELNLIPQlTIAENIFLGR---- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 490 deeiEVAARL---------ANADEFIRRL--PQGYDTMLTDngasLSQGQRQLIAIARAAVADPPVMILDEATSSI-DTR 557
Cdd:PRK10762 105 ----EFVNRFgridwkkmyAEADKLLARLnlRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTE 176
|
170 180 190
....*....|....*....|....*....|..
gi 2541161597 558 TESLVQ-------QGMdGLMYgrtvfvIAHRL 582
Cdd:PRK10762 177 TESLFRvirelksQGR-GIVY------ISHRL 201
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
405-610 |
2.91e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.31 E-value: 2.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 405 DITLYAkpGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSdLRHSLGIVL--QDTNLFTG-TVRENI 481
Cdd:PRK15439 31 DFTLHA--GEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGIYLvpQEPLLFPNlSVKENI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 482 RYGRLDATDEEIEVAARLANAdefirrlpqGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSID-TRTES 560
Cdd:PRK15439 108 LFGLPKRQASMQKMKQLLAAL---------GCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTpAETER 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2541161597 561 LVQQGMDGLMYGRTVFVIAHRLSTVRN-SNAIMVLEHGRIIERG-----SHEELIA 610
Cdd:PRK15439 179 LFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGktadlSTDDIIQ 234
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
413-568 |
4.04e-12 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 65.59 E-value: 4.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 413 GQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQDTNLFTGTVRENIRYGRLDATDEE 492
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWHADHSDEQ 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2541161597 493 IEVAarLANADEfirrlpQGYDTMLTdngASLSQGQRQLIAIARAAVADPPVMILDEATSSIDTRTESLVQQGMDG 568
Cdd:cd03231 106 VEEA--LARVGL------NGFEDRPV---AQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAG 170
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
406-608 |
4.38e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 66.55 E-value: 4.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 406 ITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGINI-----NKIKKsdlrhsLGIV--LQDTNLFTG-TV 477
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpgHQIAR------MGVVrtFQHVRLFREmTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 478 RENIrygrLDATDEEIEV----------AARLANAdEFIRRLPQGYDTM-LTD----NGASLSQGQRQLIAIARAAVADP 542
Cdd:PRK11300 98 IENL----LVAQHQQLKTglfsgllktpAFRRAES-EALDRAATWLERVgLLEhanrQAGNLAYGQQRRLEIARCMVTQP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2541161597 543 PVMILDEATSSIDTRTESLVQQGMDGLM--YGRTVFVIAHRLSTVRN-SNAIMVLEHGRIIERGSHEEL 608
Cdd:PRK11300 173 EILMLDEPAAGLNPKETKELDELIAELRneHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
35-313 |
5.09e-12 |
|
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: 66.92 E-value: 5.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 35 LVAILISAAASVGASVFLESLIDDYIkpLLLQDVPVFTGLVHALMGMAVLYLAGLlatYLYNRIMVTVSQRTLKGIRDTL 114
Cdd:cd18561 1 SVLLGLLITALYIAQAWLLARALARI--FAGGPWEDIMPPLAGIAGVIVLRAALL---WLRERVAHRAAQRVKQHLRRRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 115 FSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCVAVMLVMVRV 194
Cdd:cd18561 76 FAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 195 IARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAkedfdklNDTLagsARKANQYANILMPAMNNVGNLQYV 274
Cdd:cd18561 156 WDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRR-------GNEL---AARAEDLRQATMKVLAVSLLSSGI 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2541161597 275 VIAIIGGAIALH---------GGGLTLGAIAAFLQLSKSFTQPISQIS 313
Cdd:cd18561 226 MGLATALGTALAlgvgalrvlGGQLTLSSLLLILFLSREFFRPLRDLG 273
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
395-603 |
6.49e-12 |
|
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: 65.63 E-value: 6.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 395 AYNPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGininKIkKSDLRHSLGIvlqDTNLft 474
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG----RV-SSLLGLGGGF---NPEL-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 475 gTVRENIR-YGRL-DATDEEIEvaARLANADEFiRRLPQGYDT-MLTdngasLSQGQRQLIAIARAAVADPPVMILDEAT 551
Cdd:cd03220 100 -TGRENIYlNGRLlGLSRKEID--EKIDEIIEF-SELGDFIDLpVKT-----YSSGMKARLAFAIATALEPDILLIDEVL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2541161597 552 SSIDT--------RTESLVQQgmdglmyGRTVFVIAHRLSTVRN-SNAIMVLEHGRIIERG 603
Cdd:cd03220 171 AVGDAafqekcqrRLRELLKQ-------GKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
403-614 |
7.27e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 65.67 E-value: 7.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 403 LHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSD-LRHSLGIVLQDTNLFTG-TVREN 480
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAIVPEGRRVFSRmTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 481 IRYGRLDATDEEIEvaARLANADEFIRRLPQgydtMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSI------ 554
Cdd:PRK11614 101 LAMGGFFAERDQFQ--ERIKWVYELFPRLHE----RRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLapiiiq 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2541161597 555 ---DTrTESLVQQGMdglmygrTVFVIAHRLS-TVRNSNAIMVLEHGRIIERGSHEELIAQKGV 614
Cdd:PRK11614 175 qifDT-IEQLREQGM-------TIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLANEAV 230
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
399-556 |
1.22e-11 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 64.43 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 399 DKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYD---IADGKIRYDGININKIKkSDLRHsLGIVLQDTNLFTG 475
Cdd:COG4136 13 GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRLTALP-AEQRR-IGILFQDDLLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 476 -TVRENIRYG---RLDATDEEIEVAARLANA--DEFIRRLPqgydtmltdngASLSQGQRQLIAIARAAVADPPVMILDE 549
Cdd:COG4136 91 lSVGENLAFAlppTIGRAQRRARVEQALEEAglAGFADRDP-----------ATLSGGQRARVALLRALLAEPRALLLDE 159
|
....*..
gi 2541161597 550 ATSSIDT 556
Cdd:COG4136 160 PFSKLDA 166
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
399-613 |
1.33e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 64.09 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 399 DKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLI--NRFYDIADGKIRYDGININKIKKSDlRHSLGIVLqdtnlftgt 476
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEE-RARLGIFL--------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 477 vrenirygrldATDEEIEVAArLANADeFIRRLPQGydtmltdngasLSQGQRQLIAIARAAVADPPVMILDEATSSIDT 556
Cdd:cd03217 82 -----------AFQYPPEIPG-VKNAD-FLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2541161597 557 RTESLVQQGMDGLM-YGRTVFVIAH--RLSTVRNSNAIMVLEHGRIIERGSHE--ELIAQKG 613
Cdd:cd03217 138 DALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKElaLEIEKKG 199
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
388-611 |
1.62e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 64.72 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 388 RFFDVDFAYNPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGininkikksdlRHS----L 463
Cdd:COG1134 27 LLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-----------RVSalleL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 464 GivlqdtnlfTG-----TVRENIR-YGR-LDATDEEIEvaARLANADEF----------IRRlpqgYdtmltdngaslSQ 526
Cdd:COG1134 96 G---------AGfhpelTGRENIYlNGRlLGLSRKEID--EKFDEIVEFaelgdfidqpVKT----Y-----------SS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 527 GQRQLIAIARAAVADPPVMILDEATSSIDT--------RTESLVQQGmdglmygRTVFVIAHRLSTVRN-SNAIMVLEHG 597
Cdd:COG1134 150 GMRARLAFAVATAVDPDILLVDEVLAVGDAafqkkclaRIRELRESG-------RTVIFVSHSMGAVRRlCDRAIWLEKG 222
|
250
....*....|....
gi 2541161597 598 RIIERGSHEELIAQ 611
Cdd:COG1134 223 RLVMDGDPEEVIAA 236
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
391-610 |
1.72e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 65.03 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 391 DVDFAYNpDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKS--DLRHSLGIVLQ 468
Cdd:PRK13638 6 DLWFRYQ-DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGllALRQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 469 DTNlftgtvrENIRYgrldaTDEEIEVAARLAN----ADEFIRRLpqgyDTMLTDNGAS---------LSQGQRQLIAIA 535
Cdd:PRK13638 85 DPE-------QQIFY-----TDIDSDIAFSLRNlgvpEAEITRRV----DEALTLVDAQhfrhqpiqcLSHGQKKRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 536 RAAVADPPVMILDEATSSIDTRTES--------LVQQgmdglmyGRTVFVIAHRLSTVRN-SNAIMVLEHGRIIERGSHE 606
Cdd:PRK13638 149 GALVLQARYLLLDEPTAGLDPAGRTqmiaiirrIVAQ-------GNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPG 221
|
....
gi 2541161597 607 ELIA 610
Cdd:PRK13638 222 EVFA 225
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
399-585 |
2.13e-11 |
|
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: 63.42 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 399 DKPILHDITLYAKPGQKLAFVGSTGAGKTTITN-LINRFYD-IADGKIRYDGininKIKKSDLRHSLGIVLQ-DTNLFTG 475
Cdd:cd03232 19 KRQLLNNISGYVKPGTLTALMGESGAGKTTLLDvLAGRKTAgVITGEILING----RPLDKNFQRSTGYVEQqDVHSPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 476 TVRENIRYGRLdatdeeievaarlanadefIRrlpqgydtmltdngaSLSQGQRQLIAIARAAVADPPVMILDEATSSID 555
Cdd:cd03232 95 TVREALRFSAL-------------------LR---------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
170 180 190
....*....|....*....|....*....|.
gi 2541161597 556 TRTESLVQQGMDGL-MYGRTVFVIAHRLSTV 585
Cdd:cd03232 141 SQAAYNIVRFLKKLaDSGQAILCTIHQPSAS 171
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
398-558 |
2.35e-11 |
|
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: 63.44 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 398 PDKPILHDITLYAKPGQKLAFVGSTGAGKTT----ITNLINRFYDIaDGKIRYDGININKIKKSDLRHSLGIVLQDTNLF 473
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSV-EGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 474 TGTVRENIRYgrldatdeeievaARLANADEFIRrlpqgydtmltdngaSLSQGQRQLIAIARAAVADPPVMILDEATSS 553
Cdd:cd03233 97 TLTVRETLDF-------------ALRCKGNEFVR---------------GISGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
....*
gi 2541161597 554 IDTRT 558
Cdd:cd03233 149 LDSST 153
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
34-230 |
3.18e-11 |
|
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: 64.35 E-value: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 34 VLVAILISAAASVGASVFLESLIDDyikplLLQDVPVFTGLVHALMGMAVLYLAGLLATYLYNRIMVTVSQRTLKGIRDT 113
Cdd:cd18584 1 AVLLGLLAALLIIAQAWLLARIIAG-----VFLEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 114 LFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVC---VAVMLV 190
Cdd:cd18584 76 LLARLLALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALILLVTaplIPLFMI 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2541161597 191 MV----RVIARRsgtffiqQQTDLGKLNGYIEEMIEGQKVVKVF 230
Cdd:cd18584 156 LIgkaaQAASRR-------QWAALSRLSGHFLDRLRGLPTLKLF 192
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
403-611 |
4.13e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.70 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 403 LHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSD-LRHSLGIVLQDTNLFTG-TVREN 480
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAIIYQELHLVPEmTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 481 IRYGRLDATDEEIEVAARLANADEFIRRLPQGYD--TMLtdngASLSQGQRQLIAIARAAVADPPVMILDEATSSIDTR- 557
Cdd:PRK11288 100 LYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDpdTPL----KYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSARe 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2541161597 558 TE---SLVQQGMDGlmyGRTVFVIAHRLSTV-RNSNAIMVLEHGRIIE------RGSHEELIAQ 611
Cdd:PRK11288 176 IEqlfRVIRELRAE---GRVILYVSHRMEEIfALCDAITVFKDGRYVAtfddmaQVDRDQLVQA 236
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
401-555 |
5.66e-11 |
|
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: 61.99 E-value: 5.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 401 PILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQDTNLFTGTVREN 480
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALEN 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2541161597 481 IRYGR--LDATDEEIEVAARLANADEFIRRLpqgydtmltdnGASLSQGQRQLIAIARAAVADPPVMILDEATSSID 555
Cdd:TIGR01189 94 LHFWAaiHGGAQRTIEDALAAVGLTGFEDLP-----------AAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
399-616 |
7.46e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.52 E-value: 7.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 399 DKPILHDITLYAKPGQKLAFVGSTGAGKTTitnLINRFYDIADGKIRYDGI---NINKIKKSDLRhSLGIVLQ-DTNLFT 474
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTT---LLNVLAERVTTGVITGGDrlvNGRPLDSSFQR-SIGYVQQqDLHLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 475 GTVRENIRYGRLDATDEEIEVAARLANADEFIRRLP-QGY-DTMLTDNGASLSQGQRQLIAIARAAVADPPVMI-LDEAT 551
Cdd:TIGR00956 851 STVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEmESYaDAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPT 930
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2541161597 552 SSIDTRTESLVQQGMDGLM-YGRTVfviahrLSTVRNSNAIMVLEHGRIiergsheeLIAQKG---VYY 616
Cdd:TIGR00956 931 SGLDSQTAWSICKLMRKLAdHGQAI------LCTIHQPSAILFEEFDRL--------LLLQKGgqtVYF 985
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
401-562 |
8.32e-11 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 62.45 E-value: 8.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 401 PILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYD----GININKIKKSDL----RHSLGIVLQdtnl 472
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASPREIlalrRRTIGYVSQ---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 473 FtgtVRENIRYGRLD-----ATDEEIEVAARLANADEFIRRL----------PqgydtmltdngASLSQGQRQLIAIARA 537
Cdd:COG4778 101 F---LRVIPRVSALDvvaepLLERGVDREEARARARELLARLnlperlwdlpP-----------ATFSGGEQQRVNIARG 166
|
170 180
....*....|....*....|....*
gi 2541161597 538 AVADPPVMILDEATSSIDTRTESLV 562
Cdd:COG4778 167 FIADPPLLLLDEPTASLDAANRAVV 191
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
400-608 |
1.01e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 63.70 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 400 KPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKsdLRHSLGIVLQDTNLFTG-TVR 478
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP--YQRPINMMFQSYALFPHmTVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 479 ENIRYGRLDATDEEIEVAAR------LANADEFIRRLPQgydtmltdngaSLSQGQRQLIAIARAAVADPPVMILDEATS 552
Cdd:PRK11607 110 QNIAFGLKQDKLPKAEIASRvnemlgLVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2541161597 553 SIDTRTESLVQQGMDGLM--YGRTVFVIAH-RLSTVRNSNAIMVLEHGRIIERGSHEEL 608
Cdd:PRK11607 179 ALDKKLRDRMQLEVVDILerVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
403-618 |
1.51e-10 |
|
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: 61.71 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 403 LHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLrhslgIVLQDTNLFTG-TVRENI 481
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPWlTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 482 rYGRLDATDEEIEVAARLANADEFIRRLpqGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDTRTESL 561
Cdd:TIGR01184 76 -ALAVDRVLPDLSKSERRAIVEEHIALV--GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2541161597 562 VQqgmDGLM-----YGRTVFVIAH----------RLSTVRNSNAIMVlehGRIIE----RGSHEELIAQKGVYYQL 618
Cdd:TIGR01184 153 LQ---EELMqiweeHRVTVLMVTHdvdealllsdRVVMLTNGPAANI---GQILEvpfpRPRDRLEVVEDPSYYDL 222
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
411-610 |
1.74e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.11 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 411 KPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQDTnlfTGTVRENIRYGRLdatd 490
Cdd:PRK15112 37 REGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDP---STSLNPRQRISQI---- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 491 eeIEVAARLANADEFIRRLPQGYDT-----MLTDNGA----SLSQGQRQLIAIARAAVADPPVMILDEATSSIDTRTES- 560
Cdd:PRK15112 110 --LDFPLRLNTDLEPEQREKQIIETlrqvgLLPDHASyyphMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSq 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2541161597 561 -----LVQQGMDGLMYgrtVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHEELIA 610
Cdd:PRK15112 188 linlmLELQEKQGISY---IYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLA 239
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
402-611 |
1.74e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 62.81 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 402 ILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININK--IKKSDLrhslGIVLQDTNLFTG-TVR 478
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHrsIQQRDI----CMVFQSYALFPHmSLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 479 ENIRYG-RLDATDEEiEVAARLANADEFIRRlpQGYDTMLTDNgasLSQGQRQLIAIARAAVADPPVMILDEATSSIDT- 556
Cdd:PRK11432 97 ENVGYGlKMLGVPKE-ERKQRVKEALELVDL--AGFEDRYVDQ---ISGGQQQRVALARALILKPKVLLFDEPLSNLDAn 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2541161597 557 -------RTESLVQQgmdglmYGRTVFVIAHRLS-TVRNSNAIMVLEHGRIIERGSHEELIAQ 611
Cdd:PRK11432 171 lrrsmreKIRELQQQ------FNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
386-611 |
2.45e-10 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 63.16 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 386 DVRFFDVDFA-YNPDKPILHDITLYAKPGQKLAFVGSTGAGKT----TITNLINRFYDIADGKIRYDGININKIKKSDLR 460
Cdd:COG4172 8 SVEDLSVAFGqGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 461 H----SLGIVLQD--TNL---FT-GT-VRENIR----YGRLDATDEEIEVAAR--LANADEFIRRLP-Qgydtmltdnga 522
Cdd:COG4172 88 RirgnRIAMIFQEpmTSLnplHTiGKqIAEVLRlhrgLSGAAARARALELLERvgIPDPERRLDAYPhQ----------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 523 sLSQGQRQLIAIARAAVADPPVMILDEATSSIDTRT--------ESLVQQ-GMDGLMygrtvfvIAHRLSTVRN-SNAIM 592
Cdd:COG4172 157 -LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVqaqildllKDLQRElGMALLL-------ITHDLGVVRRfADRVA 228
|
250
....*....|....*....
gi 2541161597 593 VLEHGRIIERGSHEELIAQ 611
Cdd:COG4172 229 VMRQGEIVEQGPTAELFAA 247
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
399-625 |
2.64e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 63.36 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 399 DKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINrfydiadGKIRYDG------ININKIKKSDLRHSlGIVLQDTNL 472
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALA-------GRIQGNNftgtilANNRKPTKQILKRT-GFVTQDDIL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 473 FTG-TVRENIRYGRLDATDEEIEVAARLANADEFIRR--LPQGYDTMLTDNGA-SLSQGQRQLIAIARAAVADPPVMILD 548
Cdd:PLN03211 152 YPHlTVRETLVFCSLLRLPKSLTKQEKILVAESVISElgLTKCENTIIGNSFIrGISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 549 EATSSIDTRTESLVQQGMDGLMY-GRTVFVIAHRLST--VRNSNAIMVLEHGRIIERGSHEELIAqkgvYYQL--YTGAF 623
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSLAQkGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA----YFESvgFSPSF 307
|
..
gi 2541161597 624 EM 625
Cdd:PLN03211 308 PM 309
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
400-549 |
2.72e-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: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 400 KPILHDITLYAKPGQKLAFVGSTGAGKTTItnlinrFYDIA------DGKIRYDGINInkikkSDL----RHSLGI--VL 467
Cdd:COG1137 16 RTVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYMIVglvkpdSGRIFLDGEDI-----THLpmhkRARLGIgyLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 468 QDTNLFTG-TVRENIR----YGRLDATDEEIEVAARLanaDEF----IRRLPqgydtmltdnGASLSQGQRQLIAIARAA 538
Cdd:COG1137 85 QEASIFRKlTVEDNILavleLRKLSKKEREERLEELL---EEFgithLRKSK----------AYSLSGGERRRVEIARAL 151
|
170
....*....|.
gi 2541161597 539 VADPPVMILDE 549
Cdd:COG1137 152 ATNPKFILLDE 162
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
391-601 |
2.88e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 63.16 E-value: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 391 DVDFAYnPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYdGININkikksdlrhsLGIVLQDT 470
Cdd:COG0488 320 GLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IGYFDQHQ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 471 NLFTG--TVRENIRYGRLDATdeEIEVAARLAN-------ADEFIRrlpqgydtmltdngaSLSQGQRQLIAIARAAVAD 541
Cdd:COG0488 388 EELDPdkTVLDELRDGAPGGT--EQEVRGYLGRflfsgddAFKPVG---------------VLSGGEKARLALAKLLLSP 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2541161597 542 PPVMILDEATS--SIDTRtESLVqqgmDGLM-YGRTVFVIAH-R--LSTVRNSnaIMVLEHGRIIE 601
Cdd:COG0488 451 PNVLLLDEPTNhlDIETL-EALE----EALDdFPGTVLLVSHdRyfLDRVATR--ILEFEDGGVRE 509
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
412-603 |
3.69e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.95 E-value: 3.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 412 PGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDL---RHSLGIVLQDT-------NLFTGTVRENI 481
Cdd:PRK10261 349 PGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLqalRRDIQFIFQDPyasldprQTVGDSIMEPL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 482 R-YGRLDATDEEIEVA---ARLANADEFIRRLPQGYdtmltdngaslSQGQRQLIAIARAAVADPPVMILDEATSSIDTr 557
Cdd:PRK10261 429 RvHGLLPGKAAAARVAwllERVGLLPEHAWRYPHEF-----------SGGQRQRICIARALALNPKVIIADEAVSALDV- 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2541161597 558 teSLVQQGMDGLM-----YGRTVFVIAHRLSTV-RNSNAIMVLEHGRIIERG 603
Cdd:PRK10261 497 --SIRGQIINLLLdlqrdFGIAYLFISHDMAVVeRISHRVAVMYLGQIVEIG 546
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
391-581 |
3.82e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.96 E-value: 3.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 391 DVDFAYNpDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLR------HSLG 464
Cdd:PRK13540 6 ELDFDYH-DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKqlcfvgHRSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 465 IvlqDTNLftgTVRENIRYG-RLDATDEEIEVAARLANADEFIrRLPQGYdtmltdngasLSQGQRQLIAIARAAVADPP 543
Cdd:PRK13540 85 I---NPYL---TLRENCLYDiHFSPGAVGITELCRLFSLEHLI-DYPCGL----------LSSGQKRQVALLRLWMSKAK 147
|
170 180 190
....*....|....*....|....*....|....*....
gi 2541161597 544 VMILDEATSSIDTRT-ESLVQQGMDGLMYGRTVFVIAHR 581
Cdd:PRK13540 148 LWLLDEPLVALDELSlLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
400-608 |
3.90e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 62.34 E-value: 3.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 400 KPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDG--ININKIKKS----------DlRHSLGIVL 467
Cdd:COG1129 265 GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSPRDAiragiayvpeD-RKGEGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 468 QDTnlftgtVRENI---------RYGRLDATDEEievaarlANADEFIRRL---PQGYDTMLtdngASLSQGQRQLIAIA 535
Cdd:COG1129 344 DLS------IRENItlasldrlsRGGLLDRRRER-------ALAEEYIKRLrikTPSPEQPV----GNLSGGNQQKVVLA 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 536 RAAVADPPVMILDEATSSID--TRTE------SLVQQGMdglmygrTVFVIahrlST-----VRNSNAIMVLEHGRIIER 602
Cdd:COG1129 407 KWLATDPKVLILDEPTRGIDvgAKAEiyrlirELAAEGK-------AVIVI----SSelpelLGLSDRILVMREGRIVGE 475
|
....*.
gi 2541161597 603 GSHEEL 608
Cdd:COG1129 476 LDREEA 481
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
396-557 |
4.20e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 61.78 E-value: 4.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 396 YNPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDlRhslGI--VLQDTNLF 473
Cdd:PRK11650 13 YDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-R---DIamVFQNYALY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 474 TG-TVRENIRYGrL-------DATDEEIEVAARLANADEFIRRLPqgydtmltdngASLSQGQRQLIAIARAAVADPPVM 545
Cdd:PRK11650 89 PHmSVRENMAYG-LkirgmpkAEIEERVAEAARILELEPLLDRKP-----------RELSGGQRQRVAMGRAIVREPAVF 156
|
170
....*....|..
gi 2541161597 546 ILDEATSSIDTR 557
Cdd:PRK11650 157 LFDEPLSNLDAK 168
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
398-619 |
4.93e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 60.57 E-value: 4.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 398 PDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQDTNLFTG-T 476
Cdd:PRK10575 22 PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGmT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 477 VRENI---RY------GRLDATD-EEIEVAARLANADEFIRRLPQgydtmltdngaSLSQGQRQLIAIARAAVADPPVMI 546
Cdd:PRK10575 102 VRELVaigRYpwhgalGRFGAADrEKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWIAMLVAQDSRCLL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2541161597 547 LDEATSSIDTRTE----SLVQQGMDglMYGRTVFVIAHRLS-TVRNSNAIMVLEHGRIIERGSHEELIaQKGVYYQLY 619
Cdd:PRK10575 171 LDEPTSALDIAHQvdvlALVHRLSQ--ERGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELM-RGETLEQIY 245
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
63-316 |
5.21e-10 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 61.02 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 63 LLLQ----DVPVFTGLV----------HAL----MGMAVLYLAGLLATYLYNRIMVTVSQRTLKGIRDTLFSHMQALPIR 124
Cdd:cd18779 12 LLLQllglALPLLTGVLvdrviprgdrDLLgvlgLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLGFLEHLLRLPYR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 125 YFDTHPHGDIMsVYTNDVDTLRQMISQsipQAMSSVI--TILAVFFS-MLVMSWQLTIVVLVCVAVMLVMVRVIARRSGT 201
Cdd:cd18779 92 FFQQRSTGDLL-MRLSSNATIRELLTS---QTLSALLdgTLVLGYLAlLFAQSPLLGLVVLGLAALQVALLLATRRRVRE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 202 FFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKED-----FDKLNDTLAGSarkanQYANILMPAMNNVGNLQYVVI 276
Cdd:cd18779 168 LMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRwsnlfVDQLNASLRRG-----RLDALVDALLATLRLAAPLVL 242
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2541161597 277 AIIGgAIALHGGGLTLGAIAAFLQLSKSFTQPISQISQQM 316
Cdd:cd18779 243 LWVG-AWQVLDGQLSLGTMLALNALAGAFLAPLASLVGTA 281
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
377-609 |
5.98e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 60.39 E-value: 5.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 377 TTTYTKLTGDvrffDVDFAYNpDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKK 456
Cdd:PRK10253 2 TESVARLRGE----QLTLGYG-KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 457 SDLRHSLGIVLQD-TNLFTGTVRENIRYGRLDAT-------DEEIEVAARLANADEFIRRLPQGYDTmltdngasLSQGQ 528
Cdd:PRK10253 77 KEVARRIGLLAQNaTTPGDITVQELVARGRYPHQplftrwrKEDEEAVTKAMQATGITHLADQSVDT--------LSGGQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 529 RQLIAIARAAVADPPVMILDEATSSIDTRTESLVQQGMDGL--MYGRTVFVIAHRLS-TVRNSNAIMVLEHGRIIERGSH 605
Cdd:PRK10253 149 RQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAP 228
|
....
gi 2541161597 606 EELI 609
Cdd:PRK10253 229 KEIV 232
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
417-555 |
7.87e-10 |
|
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: 60.88 E-value: 7.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 417 AFVGSTGAGKTTITNLI---NRFydiADGKIRYDG---------INInkikKSDLRHsLGIVLQDTNLF-TGTVRENIRY 483
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIaglERP---DSGRIRLGGevlqdsargIFL----PPHRRR-IGYVFQEARLFpHLSVRGNLLY 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2541161597 484 GRLDAtdeeiEVAARLANADEFIRRLpqGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSID 555
Cdd:COG4148 101 GRKRA-----PRAERRISFDEVVELL--GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
399-608 |
7.91e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 60.51 E-value: 7.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 399 DKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGiniNKIKKSDLRHslgIvlqdtnlftG--- 475
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG---EPLDPEDRRR---I---------Gylp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 476 ---------TVRENIRY-GRL---DATDeeievaARlANADEFIRRLpqGYDTMLTDNGASLSQGQRQLIAIARAAVADP 542
Cdd:COG4152 78 eerglypkmKVGEQLVYlARLkglSKAE------AK-RRADEWLERL--GLGDRANKKVEELSKGNQQKVQLIAALLHDP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2541161597 543 PVMILDEATSSIDTRTESLVQQGMDGLMY-GRTVFVIAHRLSTV-RNSNAIMVLEHGRIIERGSHEEL 608
Cdd:COG4152 149 ELLILDEPFSGLDPVNVELLKDVIRELAAkGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEI 216
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
398-594 |
8.54e-10 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 58.40 E-value: 8.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 398 PDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGininkikksdlRHSLGIVLQDTNL---FT 474
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEVpdsLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 475 GTVRENIRYG---------RLDATDEEIEVAA--RLANADEFIRRLpqgydtmltdngASLSQGQRQLIAIARAAVADPP 543
Cdd:NF040873 72 LTVRDLVAMGrwarrglwrRLTRDDRAAVDDAleRVGLADLAGRQL------------GELSGGQRQRALLAQGLAQEAD 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2541161597 544 VMILDEATSSIDTRTESLVQQGMDGLMY-GRTVFVIAHRLSTVRNSNAIMVL 594
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
387-581 |
8.89e-10 |
|
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: 57.93 E-value: 8.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 387 VRFFDVDFAYNPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIrydgininkiKKSDLRHSLgIV 466
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI----------GMPEGEDLL-FL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 467 LQDTNLFTGTVRENIRYgrldATDEEievaarlanadefirrlpqgydtmltdngasLSQGQRQLIAIARAAVADPPVMI 546
Cdd:cd03223 70 PQRPYLPLGTLREQLIY----PWDDV-------------------------------LSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190
....*....|....*....|....*....|....*
gi 2541161597 547 LDEATSSIDTRTESLVQQGMDGLmyGRTVFVIAHR 581
Cdd:cd03223 115 LDEATSALDEESEDRLYQLLKEL--GITVISVGHR 147
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
402-558 |
1.05e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 59.02 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 402 ILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKI---KKSDLR-HSLGIVLQDTNLF-TGT 476
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARAKLRaKHVGFVFQSFMLIpTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 477 VRENIRYGRLDATDEEIEVAARlanADEFIRRLpqGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDT 556
Cdd:PRK10584 105 ALENVELPALLRGESSRQSRNG---AKALLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
|
..
gi 2541161597 557 RT 558
Cdd:PRK10584 180 QT 181
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
399-556 |
1.15e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 58.28 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 399 DKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLR------HSLGIvlqDTNL 472
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQdllylgHQPGI---KTEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 473 ftgTVRENIR-YGRL--DATDEEIEVAARLANADEFiRRLPQGYdtmltdngasLSQGQRQLIAIARAAVADPPVMILDE 549
Cdd:PRK13538 90 ---TALENLRfYQRLhgPGDDEALWEALAQVGLAGF-EDVPVRQ----------LSAGQQRRVALARLWLTRAPLWILDE 155
|
....*..
gi 2541161597 550 ATSSIDT 556
Cdd:PRK13538 156 PFTAIDK 162
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
403-608 |
1.46e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 60.81 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 403 LHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDiAD-GKIRYDGininkiKKSDLRHS-----LGI--VLQDTNLF- 473
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQ-PDsGEILIDG------KPVRIRSPrdaiaLGIgmVHQHFMLVp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 474 TGTVRENIRYGRLDATDEEIevaaRLANADEFIRRLPQGY------DTMLtdngASLSQGQRQLIAIARAAVADPPVMIL 547
Cdd:COG3845 94 NLTVAENIVLGLEPTKGGRL----DRKAARARIRELSERYgldvdpDAKV----EDLSVGEQQRVEILKALYRGARILIL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2541161597 548 DEATSsidtrteSLVQQGMDGLMY--------GRTVFVIAHRLSTVR-NSNAIMVLEHGRIIERG-----SHEEL 608
Cdd:COG3845 166 DEPTA-------VLTPQEADELFEilrrlaaeGKSIIFITHKLREVMaIADRVTVLRRGKVVGTVdtaetSEEEL 233
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
99-327 |
1.86e-09 |
|
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: 59.27 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 99 MVTVSQRTLKgIRDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLT 178
Cdd:cd18590 61 MCTLSRLNLR-LRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLT 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 179 IVVLVCVAVMLVMVRVIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDK-LNDTLAGSARKANQY 257
Cdd:cd18590 140 LLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEaLERTYNLKDRRDTVR 219
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 258 ANILMpaMNNVGNLQYVVIAIIGGAIALHGGGLTLGAIAAFLQLSKSFTQPISQISqQMNAIVMALAGAS 327
Cdd:cd18590 220 AVYLL--VRRVLQLGVQVLMLYCGRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLV-YIYGDMLSNVGAA 286
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
403-609 |
2.02e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.18 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 403 LHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIK-KSDLRHSLGIVLQDTNLFTG-TVREN 480
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhKLAAQLGIGIIYQELSVIDElTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 481 IRYGRLDATD----EEIEVAARLANADEFIRRLpqGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDT 556
Cdd:PRK09700 101 LYIGRHLTKKvcgvNIIDWREMRVRAAMMLLRV--GLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTN 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 557 RTESLVQQGMDGLMY-GRTVFVIAHRLSTVRN-SNAIMVLEHG-----RIIERGSHEELI 609
Cdd:PRK09700 179 KEVDYLFLIMNQLRKeGTAIVYISHKLAEIRRiCDRYTVMKDGssvcsGMVSDVSNDDIV 238
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
35-302 |
3.19e-09 |
|
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: 58.66 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 35 LVAILISAAASVGASVFLESLIDDyikpLLLQDVPVFTGLVHALMGMAVLYLAGLLATYLYNRIMVTVSQRTLKGIRDTL 114
Cdd:cd18582 2 LLLLVLAKLLNVAVPFLLKYAVDA----LSAPASALLAVPLLLLLAYGLARILSSLFNELRDALFARVSQRAVRRLALRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 115 FSHMQALPIRYFDTHPHGDIMSVY---TNDVDT-LRQMISQSIPQA--MSSVITILAVFFsmlvmSWQLTIVVLVCVAV- 187
Cdd:cd18582 78 FRHLHSLSLRFHLSRKTGALSRAIergTRGIEFlLRFLLFNILPTIleLLLVCGILWYLY-----GWSYALITLVTVALy 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 188 MLVMVRVIARRSGtfFIQQQTDL-GKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLndtLAGSARKANQYANILmpAMN 266
Cdd:cd18582 153 VAFTIKVTEWRTK--FRREMNEAdNEANAKAVDSLLNYETVKYFNNEEYEAERYDKA---LAKYEKAAVKSQTSL--ALL 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2541161597 267 NVGnlQYVVIAI------IGGAIALHGGGLTLGAIAA----FLQLS 302
Cdd:cd18582 226 NIG--QALIISLgltaimLLAAQGVVAGTLTVGDFVLvntyLLQLY 269
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
391-598 |
3.22e-09 |
|
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: 55.53 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 391 DVDFAYNpDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINrfydiadgkirydgininkikksdlrhslgivlqdt 470
Cdd:cd03221 5 NLSKTYG-GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIA------------------------------------ 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 471 nlftgtvreniryGRLDATDEEIEVAARLAnadefIRRLPQgydtmltdngasLSQGQRQLIAIARAAVADPPVMILDEA 550
Cdd:cd03221 48 -------------GELEPDEGIVTWGSTVK-----IGYFEQ------------LSGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2541161597 551 TSSIDTRTESLVQQGMDGlmYGRTVFVIAH-R--LSTVrnSNAIMVLEHGR 598
Cdd:cd03221 98 TNHLDLESIEALEEALKE--YPGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
399-605 |
3.50e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.88 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 399 DKPILHDITLYAKPGQKLAFVGSTGAGKTTIT-NLINRF-YDIADGKIRYDGININKIKKSDlRHSLGIVLQ-------- 468
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSaTLAGREdYEVTGGTVEFKGKDLLELSPED-RAGEGIFMAfqypveip 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 469 --DTNLFTGTVRENIRYGR----LDATDEE--IEVAARLAN--ADEFIRRLPQGYdtmltdngaslSQGQRQLIAIARAA 538
Cdd:PRK09580 92 gvSNQFFLQTALNAVRSYRgqepLDRFDFQdlMEEKIALLKmpEDLLTRSVNVGF-----------SGGEKKRNDILQMA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 539 VADPPVMILDEATSSIDTRTESLVQQGMDGLMYGRTVFVIA---HRLSTVRNSNAIMVLEHGRIIERGSH 605
Cdd:PRK09580 161 VLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVthyQRILDYIKPDYVHVLYQGRIVKSGDF 230
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
402-600 |
5.98e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 58.97 E-value: 5.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 402 ILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDL----RHSLGIVLQDTNLFTG-T 476
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLSHlT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 477 VRENIrygRLDATDEEIEVAARLANADEFIRRLpqGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDT 556
Cdd:PRK10535 103 AAQNV---EVPAVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDS 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2541161597 557 RTESLVQQGMDGLM-YGRTVFVIAHRLSTVRNSNAIMVLEHGRII 600
Cdd:PRK10535 178 HSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
406-611 |
7.35e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 58.66 E-value: 7.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 406 ITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRY----DGININKiKKSDLR----HSLGIVLQDTNLFT-GT 476
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTK-PGPDGRgrakRYIGILHQEYDLYPhRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 477 VRENIRygrlDATDEEI--EVAARLA------------NADEFIRRLPQgydtmltdngaSLSQGQRQLIAIARAAVADP 542
Cdd:TIGR03269 382 VLDNLT----EAIGLELpdELARMKAvitlkmvgfdeeKAEEILDKYPD-----------ELSEGERHRVALAQVLIKEP 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2541161597 543 PVMILDEATSSIDTRTESLVQqgmDGLMYGR-----TVFVIAHRLSTVRN-SNAIMVLEHGRIIERGSHEELIAQ 611
Cdd:TIGR03269 447 RIVILDEPTGTMDPITKVDVT---HSILKAReemeqTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
402-614 |
7.79e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 56.83 E-value: 7.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 402 ILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIK-KSDLRHSLGIVLQDTNLFTG-TVRE 479
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQEASIFRRlSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 480 NIRYG---RLDATDEEievaaRLANADEFIRRLpqgYDTMLTDN-GASLSQGQRQLIAIARAAVADPPVMILDEATSSID 555
Cdd:PRK10895 98 NLMAVlqiRDDLSAEQ-----REDRANELMEEF---HIEHLRDSmGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2541161597 556 TRTESLVQQGMDGLM-YGRTVFVIAHRL-STVRNSNAIMVLEHGRIIERGSHEELIAQKGV 614
Cdd:PRK10895 170 PISVIDIKRIIEHLRdSGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDEHV 230
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
405-604 |
7.96e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 59.26 E-value: 7.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 405 DITLYAKpgQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGINInKIKKSDLRHSLGIVLQDTNLFTG-TVRENIR- 482
Cdd:TIGR01257 950 NITFYEN--QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAEHILf 1026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 483 YGRLDATDEE---IEVAARLANADEFIRRLPQGYDtmltdngasLSQGQRQLIAIARAAVADPPVMILDEATSSIDTRTE 559
Cdd:TIGR01257 1027 YAQLKGRSWEeaqLEMEAMLEDTGLHHKRNEEAQD---------LSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR 1097
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2541161597 560 SLVQQGMDGLMYGRTVFVIAHRLSTVRN-SNAIMVLEHGRIIERGS 604
Cdd:TIGR01257 1098 RSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGT 1143
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
401-608 |
9.35e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.33 E-value: 9.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 401 PILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDG----------ININKIKKSDLRHSLG----IV 466
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRHVRGadmaMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 467 LQD--TNL---FT--GTVRENIRYGRLDATDEEIEVAARLANAdefiRRLPQGyDTMLTDNGASLSQGQRQLIAIARAAV 539
Cdd:PRK10261 110 FQEpmTSLnpvFTvgEQIAESIRLHQGASREEAMVEAKRMLDQ----VRIPEA-QTILSRYPHQLSGGMRQRVMIAMALS 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2541161597 540 ADPPVMILDEATSSIDTRTES-------LVQQGMDglmygRTVFVIAHRLSTVRN-SNAIMVLEHGRIIERGSHEEL 608
Cdd:PRK10261 185 CRPAVLIADEPTTALDVTIQAqilqlikVLQKEMS-----MGVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQI 256
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
403-600 |
1.02e-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: 57.91 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 403 LHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIA--DGKIRYDGiniNKIKKSDLRHS----LGIVLQDTNLFTG- 475
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSG---SPLKASNIRDTeragIVIIHQELTLVPEl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 476 TVRENIRYGrldatdEEIEVAARLANADEFIRR---------LPQGYDTMLTdngASLSQGQRQLIAIARAAVADPPVMI 546
Cdd:TIGR02633 94 SVAENIFLG------NEITLPGGRMAYNAMYLRaknllrelqLDADNVTRPV---GDYGGGQQQLVEIAKALNKQARLLI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2541161597 547 LDEATSSI-DTRTESLVQQGMDGLMYGRTVFVIAHRLSTVRN-SNAIMVLEHGRII 600
Cdd:TIGR02633 165 LDEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
391-606 |
1.47e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.43 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 391 DVDFAYNPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLrhsLGIVLQDT 470
Cdd:PRK15056 11 DVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 471 NL---FTGTVRENI---RYG------RLDATDEEIeVAARLANADEFIRRLPQGydtmltdngASLSQGQRQLIAIARAA 538
Cdd:PRK15056 88 EVdwsFPVLVEDVVmmgRYGhmgwlrRAKKRDRQI-VTAALARVDMVEFRHRQI---------GELSGGQKKRVFLARAI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2541161597 539 VADPPVMILDEATSSIDTRTE----SLVQQGMDglmYGRTVFVIAHRLSTVRNSNAIMVLEHGRIIERGSHE 606
Cdd:PRK15056 158 AQQGQVILLDEPFTGVDVKTEariiSLLRELRD---EGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
33-329 |
1.53e-08 |
|
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: 56.34 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 33 VVLVAILISAAASVGASVFLESLIDdYIKPLllQDVPVFTGLVHALmGMAVLYLAGLLATYLYNRIMVTVSQRTLKGIRD 112
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLIS-YLSSY--PDEPLSEGYLLAL-ALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 113 TLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMIsQSIPQAMSSVITILAVFFsmlVMSWQLTIVVLVCVAVMLVMV 192
Cdd:cd18579 77 LIYRKALRLSSSARQETSTGEIVNLMSVDVQRIEDFF-LFLHYLWSAPLQIIVALY---LLYRLLGWAALAGLGVLLLLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 193 ---RVIARRSGTFF--IQQQTD--LGKLNgyieEMIEGQKVVKVFCHEQKAKedfDKLNDtlagsAR-------KANQYA 258
Cdd:cd18579 153 plqAFLAKLISKLRkkLMKATDerVKLTN----EILSGIKVIKLYAWEKPFL---KRIEE-----LRkkelkalRKFGYL 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2541161597 259 NILMPAMNNVGNLqyVVIAIIGGAIALHGGGLTLG----AIAAFLQLSksftQPISQISQQMNAIVMALAGASRV 329
Cdd:cd18579 221 RALNSFLFFSTPV--LVSLATFATYVLLGNPLTAAkvftALSLFNLLR----FPLLMLPQAISSLIEALVSLKRI 289
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
403-600 |
1.77e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.25 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 403 LHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIA--DGKIRYDGiniNKIKKSDLRHS--LGIVL--QDTNLFTG- 475
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEG---EELQASNIRDTerAGIAIihQELALVKEl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 476 TVRENI-------RYGRLDatdeeieVAARLANADEFIRRLPQGYD--TMLTDNGAslsqGQRQLIAIARAAVADPPVMI 546
Cdd:PRK13549 98 SVLENIflgneitPGGIMD-------YDAMYLRAQKLLAQLKLDINpaTPVGNLGL----GQQQLVEIAKALNKQARLLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2541161597 547 LDEATSSIdtrTESLVQQGMDGLM----YGRTVFVIAHRLSTVRN-SNAIMVLEHGRII 600
Cdd:PRK13549 167 LDEPTASL---TESETAVLLDIIRdlkaHGIACIYISHKLNEVKAiSDTICVIRDGRHI 222
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
399-610 |
1.96e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 57.12 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 399 DKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRF--YDIADGKIRY------------------------------ 446
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYhvalcekcgyverpskvgepcpvcggtlep 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 447 ---DGININKIKKSDLRHSLGIVLQDTNLFTG--TVRENIrygrLDATdEEIEVAARLA--NADEFIRRLPQGYdtMLTD 519
Cdd:TIGR03269 92 eevDFWNLSDKLRRRIRKRIAIMLQRTFALYGddTVLDNV----LEAL-EEIGYEGKEAvgRAVDLIEMVQLSH--RITH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 520 NGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDTRTESLVQQGMDGLM--YGRTVFVIAHRLSTVRN-SNAIMVLEH 596
Cdd:TIGR03269 165 IARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWPEVIEDlSDKAIWLEN 244
|
250
....*....|....
gi 2541161597 597 GRIIERGSHEELIA 610
Cdd:TIGR03269 245 GEIKEEGTPDEVVA 258
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
417-555 |
2.52e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 56.04 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 417 AFVGSTGAGKTTITNLINRFYDIADGKIR------YD---GININKIKksdlRHsLGIVLQDTNLFTG-TVRENIRYGRL 486
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVlngrvlFDaekGICLPPEK----RR-IGYVFQDARLFPHyKVRGNLRYGMA 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2541161597 487 DATDEEIEVAARLANADEFIRRLPqgydtmltdngASLSQGQRQLIAIARAAVADPPVMILDEATSSID 555
Cdd:PRK11144 103 KSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
399-599 |
2.91e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 55.07 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 399 DKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKsDLRhslgIVLQDTNLFT-GTV 477
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARE-DTR----LMFQDARLLPwKKV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 478 RENIRYG-RLDATDEEIEVAARLANADEfirrlpqgydtmLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSID- 555
Cdd:PRK11247 99 IDNVGLGlKGQWRDAALQALAAVGLADR------------ANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDa 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2541161597 556 -TRTEslVQQGMDGL--MYGRTVFVIAHRLS-TVRNSNAIMVLEHGRI 599
Cdd:PRK11247 167 lTRIE--MQDLIESLwqQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
381-603 |
3.57e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.93 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 381 TKLTGDVR-FFDVDFaynpdkpilhdiTLYakPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDG-----ININKI 454
Cdd:PRK11701 13 TKLYGPRKgCRDVSF------------DLY--PGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 455 KKSDLRHSL----GIVLQDTnlftgtvRENIR--------------------YGRLDATD----EEIEVAArlanadefi 506
Cdd:PRK11701 79 SEAERRRLLrtewGFVHQHP-------RDGLRmqvsaggnigerlmavgarhYGDIRATAgdwlERVEIDA--------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 507 rrlpqgydTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDTRteslVQQGMDGLMYGRT------VFVIAH 580
Cdd:PRK11701 143 --------ARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVS----VQARLLDLLRGLVrelglaVVIVTH 210
|
250 260
....*....|....*....|....
gi 2541161597 581 RLSTVRN-SNAIMVLEHGRIIERG 603
Cdd:PRK11701 211 DLAVARLlAHRLLVMKQGRVVESG 234
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
399-608 |
4.88e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 54.77 E-value: 4.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 399 DKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDL---RHSLGIVLQDTNLFTG 475
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLFQSGALFTD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 476 -TVRENIRYgrldATDEEIEVAARLANADEFIRRLPQGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSI 554
Cdd:PRK11831 99 mNVFDNVAY----PLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2541161597 555 DTRTESLVQQGMDGLMY--GRTVFVIAHRLSTVRN--SNAIMVLEHgRIIERGSHEEL 608
Cdd:PRK11831 175 DPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiaDHAYIVADK-KIVAHGSAQAL 231
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
399-606 |
5.45e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.26 E-value: 5.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 399 DKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLI--NRFYDIADGKIRYDGININKiKKSDLRHSLGIVLQDTNLFTGT 476
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILD-LEPEERAHLGIFLAFQYPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 477 VRENIRYGRLDATDEEIEVAARLANADEFIRRLPQGYD------TMLTDN-GASLSQGQRQLIAIARAAVADPPVMILDE 549
Cdd:CHL00131 98 GVSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLKlvgmdpSFLSRNvNEGFSGGEKKRNEILQMALLDSELAILDE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 550 ATSSIDTRTESLVQQGMDGLM-YGRTVFVIAH--RLSTVRNSNAIMVLEHGRIIERGSHE 606
Cdd:CHL00131 178 TDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGDAE 237
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
412-596 |
7.89e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.99 E-value: 7.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 412 PGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYdgininkikksdlrhslgivlqdtnlftgtvrenirygrLDATDE 491
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY---------------------------------------IDGEDI 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 492 EIEVAARLANadefirrlpqgydTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDTRTESLVQQGMDGLM- 570
Cdd:smart00382 42 LEEVLDQLLL-------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLl 108
|
170 180 190
....*....|....*....|....*....|..
gi 2541161597 571 ------YGRTVFVIAHRLSTVRNSNAIMVLEH 596
Cdd:smart00382 109 lllkseKNLTVILTTNDEKDLGPALLRRRFDR 140
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
80-312 |
9.38e-08 |
|
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: 54.13 E-value: 9.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 80 GMAVLYLAGLLATYLYNRIMVTVSQRTLKGIRDTLFSHMQALPIRYFDTHPHGDIMSvYTNDVDTLRQMISQsipQAMSS 159
Cdd:cd18566 47 GVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLE-RLNSLEQIREFLTG---QALLA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 160 VITILAVFFSMLVM---SWQLTIVVLVCVAVMLVMVRVIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKA 236
Cdd:cd18566 123 LLDLPFVLIFLGLIwylGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQM 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2541161597 237 KEDFDKLNDTLAGSARKANQYANILMpamnNVGNL--QYVVIAIIG-GAIALHGGGLTLGAIAAFLQLSKSFTQPISQI 312
Cdd:cd18566 203 LRRYERLQANAAYAGFKVAKINAVAQ----TLGQLfsQVSMVAVVAfGALLVINGDLTVGALIACTMLSGRVLQPLQRA 277
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
32-199 |
1.05e-07 |
|
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: 54.01 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 32 VVVLVAILISAAASVGASVFLESLIDDYIKPLLLQDVPVftGLVHALMGMAVLYLAGLLATYLYNRIMVTVSQRTLKGI- 110
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSEV--SVLYYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLh 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 111 RDTLFSHMQAlPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTI--VVLVCVAVM 188
Cdd:cd18604 80 ERLLHSVLRA-PLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLpaVVLAALYVY 158
|
170
....*....|.
gi 2541161597 189 LVMVRVIARRS 199
Cdd:cd18604 159 IGRLYLRASRE 169
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
399-603 |
1.14e-07 |
|
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: 53.11 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 399 DKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKiKKSDLRHSLGIVL-QDTNLFTG-T 476
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWK-RRKKFLRRIGVVFgQKTQLWWDlP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 477 VRENIRygrLDATDEEIEVAARLANADEFIRRLPQGydTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSIDT 556
Cdd:cd03267 112 VIDSFY---LLAAIYDLPPARFKKRLDELSELLDLE--ELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2541161597 557 RTESLVQQGMDGLM--YGRTVFVIAHRLSTV-RNSNAIMVLEHGRIIERG 603
Cdd:cd03267 187 VAQENIRNFLKEYNreRGTTVLLTSHYMKDIeALARRVLVIDKGRLLYDG 236
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
83-264 |
1.38e-07 |
|
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: 53.82 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 83 VLYLAGLLATYLYNRIMVTVSQRTLKGIRDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVIT 162
Cdd:cd18558 67 IIGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIAT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 163 ILAVFFSMLVMSWQLTIVVLVCVAVMLVMVRVIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDK 242
Cdd:cd18558 147 FGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQ 226
|
170 180
....*....|....*....|...
gi 2541161597 243 -LNDTLAGSARKANQyANILMPA 264
Cdd:cd18558 227 nLEIAKRNGIKKAIT-FNISMGA 248
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
105-299 |
1.61e-07 |
|
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: 53.25 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 105 RTLKGIRDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQ----MISQSIpqamSSVITILAVFFSMLVMSWQLTIV 180
Cdd:cd18585 65 RLLSNLRVWFYRKLEPLAPARLQKYRSGDLLNRIVADIDTLDNlylrVLSPPV----VALLVILATILFLAFFSPALALI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 181 VLVCVAVMLVMVRVIARRSGTFFIQQQTDL-GKLNGYIEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANQyAN 259
Cdd:cd18585 141 LLAGLLLAGVVIPLLFYRLGKKIGQQLVQLrAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLAR-LS 219
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2541161597 260 ILMPAMNNVGNLQYVVIAIIGGAIALHGGGLTlGAIAAFL 299
Cdd:cd18585 220 GLSQALMILLSGLTVWLVLWLGAPLVQNGALD-GALLAML 258
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
403-601 |
1.62e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.03 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 403 LHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIA--DGKIRYDGiniNKIKKSDLRHS--LGIVL--QDTNLFTG- 475
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDG---EVCRFKDIRDSeaLGIVIihQELALIPYl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 476 TVRENIRYGRLDATDEEIEVAARLANADEFIRR--LPQGYDTMLTDNGAslsqGQRQLIAIARAAVADPPVMILDEATSS 553
Cdd:NF040905 94 SIAENIFLGNERAKRGVIDWNETNRRARELLAKvgLDESPDTLVTDIGV----GKQQLVEIAKALSKDVKLLILDEPTAA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2541161597 554 I-DTRTESLV-------QQGMdglmygrTVFVIAHRLSTVRN-SNAIMVLEHGRIIE 601
Cdd:NF040905 170 LnEEDSAALLdlllelkAQGI-------TSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
403-554 |
1.63e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.35 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 403 LHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININ-KIKKSDLRHSLGIVLQDTNLFTG-TVREN 480
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELNLVLQrSVMDN 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2541161597 481 IRYGRLDATDEEIEVAARLANADEFIRRLpqGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSI 554
Cdd:PRK10982 94 MWLGRYPTKGMFVDQDKMYRDTKAIFDEL--DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
31-193 |
1.82e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350047 [Multi-domain] Cd Length: 296 Bit Score: 53.25 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 31 LVVVLVAILISAAASVGASVFLESLIDDYIKPLLLQDVPVFTGL-VHALMGMAVLyLAGLLATYLYNRIMVTVSQRtlkg 109
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSDDPALNGTQDTEQRDYRLgVYGALGLGQA-IFVFLGSLALALGCVRASRN---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 110 IRDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFsMLVMSWQLTIVVLVCVAVML 189
Cdd:cd18603 76 LHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLV-VISISTPIFLVVIIPLAILY 154
|
....
gi 2541161597 190 VMVR 193
Cdd:cd18603 155 FFIQ 158
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
403-608 |
2.60e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 52.32 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 403 LHDITLYAKPGQKLAFVGSTGAGKTTI----TNLIN------RFYDIADGKIRYDGININKIKKSdlRHSLGIVLQDTNL 472
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLlrhlSGLITgdksagSHIELLGRTVQREGRLARDIRKS--RANTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 473 FTG-TVRENIRYGRLDAT---------------DEEIEVAARLANADEFIRRLpqgydtmltdngASLSQGQRQLIAIAR 536
Cdd:PRK09984 98 VNRlSVLENVLIGALGSTpfwrtcfswftreqkQRALQALTRVGMVHFAHQRV------------STLSGGQQQRVAIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2541161597 537 AAVADPPVMILDEATSSIDTRTESLVQQGMDGLMY--GRTVFVIAHRLS-TVRNSNAIMVLEHGRIIERGSHEEL 608
Cdd:PRK09984 166 ALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
395-580 |
5.35e-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: 52.63 E-value: 5.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 395 AYNPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRY-DGINInkikksdlrhslGIVLQDTNL- 472
Cdd:TIGR03719 13 VVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGIKV------------GYLPQEPQLd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 473 FTGTVRENIRYG---RLDATDEEIEVAARLANAD--------------EFI---------RRLPQGYDTM-LTDNGAS-- 523
Cdd:TIGR03719 81 PTKTVRENVEEGvaeIKDALDRFNEISAKYAEPDadfdklaaeqaelqEIIdaadawdldSQLEIAMDALrCPPWDADvt 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2541161597 524 -LSQGQRQLIAIARAAVADPPVMILDEATSSIDTRTESLVQQGMDGlmYGRTVFVIAH 580
Cdd:TIGR03719 161 kLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQE--YPGTVVAVTH 216
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
397-599 |
5.84e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.24 E-value: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 397 NPDKPILHDITLYAKPGQKLAFVGSTGAGKT-TITNLINRFYDIADGKIRYDG--ININKIKKSdLRHSLGIVLQDTNLF 473
Cdd:PRK13549 272 NPHIKRVDDVSFSLRRGEILGIAGLVGAGRTeLVQCLFGAYPGRWEGEIFIDGkpVKIRNPQQA-IAQGIAMVPEDRKRD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 474 tG-----TVRENIRYGRLD--ATDEEIEVAARLANADEFIRRLP-QGYDTMLTDngASLSQGQRQLIAIARAAVADPPVM 545
Cdd:PRK13549 351 -GivpvmGVGKNITLAALDrfTGGSRIDDAAELKTILESIQRLKvKTASPELAI--ARLSGGNQQKAVLAKCLLLNPKIL 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2541161597 546 ILDEATSSID--TRTE------SLVQQGMdglmygrTVFVIAHRLSTVRN-SNAIMVLEHGRI 599
Cdd:PRK13549 428 ILDEPTRGIDvgAKYEiyklinQLVQQGV-------AIIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
35-197 |
8.19e-07 |
|
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: 51.07 E-value: 8.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 35 LVAILISAAASVGASVFLESLIDDyikpLLLQDVPVFTGLVHALMGMAVLYLAGLLATYLYNRIMVTVSQRTLKGIRDTL 114
Cdd:cd18560 2 LLLLILGKACNVLAPLFLGRAVNA----LTLAKVKDLESAVTLILLYALLRFSSKLLKELRSLLYRRVQQNAYRELSLKT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 115 FSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQS----IPQAMSSVITILaVFFSMLvmSWQLTIVVLVCVAVMLV 190
Cdd:cd18560 78 FAHLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLvfylVPTLLELIVVSV-VFAFHF--GAWLALIVFLSVLLYGV 154
|
....*..
gi 2541161597 191 MVRVIAR 197
Cdd:cd18560 155 FTIKVTE 161
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
402-583 |
9.26e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.16 E-value: 9.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 402 ILHDITLYAKPGQKLAFVGSTGAGKTTITNLI--NRFYDIADGKIRYDGININK---------IKKSDLrHSLGIVLQDT 470
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGFPKKQetfarisgyCEQNDI-HSPQVTVRES 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 471 NLFTGTVR---ENIRYGRLDATDEEIEVAaRLANADEFIRRLPqgydtmltdNGASLSQGQRQLIAIARAAVADPPVMIL 547
Cdd:PLN03140 974 LIYSAFLRlpkEVSKEEKMMFVDEVMELV-ELDNLKDAIVGLP---------GVTGLSTEQRKRLTIAVELVANPSIIFM 1043
|
170 180 190
....*....|....*....|....*....|....*..
gi 2541161597 548 DEATSSIDTRTESLVQQGMDGLM-YGRTVFVIAHRLS 583
Cdd:PLN03140 1044 DEPTSGLDARAAAIVMRTVRNTVdTGRTVVCTIHQPS 1080
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
398-610 |
1.81e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 49.70 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 398 PDKPILHDITLYAKPGQKLAFVGSTGAGKT-TITNLInrfyDIA-------DGKIRYDGIninKIKKSDLR-HSLGIVLQ 468
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAAL----GILpagvrqtAGRVLLDGK---PVAPCALRgRKIATIMQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 469 D-------TNLFTGTVRENIR-YGRL--DATDEEIEVAARLANADEFIRRLPqgydtmltdngASLSQGQRQLIAIARAA 538
Cdd:PRK10418 87 NprsafnpLHTMHTHARETCLaLGKPadDATLTAALEAVGLENAARVLKLYP-----------FEMSGGMLQRMMIALAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2541161597 539 VADPPVMILDEATSSIDTRTESLVQQGMDGLMYGRT--VFVIAHRLSTV-RNSNAIMVLEHGRIIERGSHEELIA 610
Cdd:PRK10418 156 LCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETLFN 230
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
401-555 |
2.22e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.39 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 401 PILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSD-LRHSLGIVLQDTN---LFTG- 475
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGIVYISEDRKrdgLVLGm 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 476 TVREN-----IRY-----GRLDATDEEIEVaarlanaDEFIRRLPQGYDTMLTDNGaSLSQGQRQLIAIARAAVADPPVM 545
Cdd:PRK10762 346 SVKENmsltaLRYfsragGSLKHADEQQAV-------SDFIRLFNIKTPSMEQAIG-LLSGGNQQKVAIARGLMTRPKVL 417
|
170
....*....|
gi 2541161597 546 ILDEATSSID 555
Cdd:PRK10762 418 ILDEPTRGVD 427
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
403-599 |
2.84e-06 |
|
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: 48.20 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 403 LHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGINInKIKKSDLRHSLGIVL-----QDTNLFTG-T 476
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPV-TRRSPRDAIRAGIAYvpedrKREGLVLDlS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 477 VRENIrygrldatdeeievaarlanadeFIRRLpqgydtmltdngasLSQGQRQLIAIARAAVADPPVMILDEATSSIDT 556
Cdd:cd03215 95 VAENI-----------------------ALSSL--------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2541161597 557 RTESLVQQGMDGL-MYGRTVFVIAHRLSTV-RNSNAIMVLEHGRI 599
Cdd:cd03215 138 GAKAEIYRLIRELaDAGKAVLLISSELDELlGLCDRILVMYEGRI 182
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
387-580 |
2.94e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 50.36 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 387 VRFFDVDFAYnPD-----KPIlhDITLyaKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSDLRH 461
Cdd:PRK10522 323 LELRNVTFAY-QDngfsvGPI--NLTI--KRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRK 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 462 SLGIVLQDTNLFTGTvrenirygrLDATDEEIEVAArlanADEFIRRLPQGYDTMLTDNGAS---LSQGQRQLIAIARAA 538
Cdd:PRK10522 398 LFSAVFTDFHLFDQL---------LGPEGKPANPAL----VEKWLERLKMAHKLELEDGRISnlkLSKGQKKRLALLLAL 464
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2541161597 539 VADPPVMILDEATSSIDTRTESLVQQGMDGLM--YGRTVFVIAH 580
Cdd:PRK10522 465 AEERDILLLDEWAADQDPHFRREFYQVLLPLLqeMGKTIFAISH 508
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
31-167 |
3.71e-06 |
|
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: 49.01 E-value: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 31 LVVVLVAILISAAASVGASVFLESLIDDYikplllqdvpvFTGLVHALMGM-AVLYLAGLLATYLYNRIMVTVSQRTLKG 109
Cdd:cd18606 1 LPLLLLLLILSQFAQVFTNLWLSFWTEDF-----------FGLSQGFYIGIyAGLGVLQAIFLFLFGLLLAYLGIRASKR 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2541161597 110 IrdtlfsHMQAL------PIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVF 167
Cdd:cd18606 70 L------HNKALkrvlraPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTF 127
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
76-191 |
4.28e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 49.14 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 76 HALMGMAVLYLAGLLATYLYNRIMVTVSQRTLKGIRDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQ 155
Cdd:cd18602 51 YYISVYAGLSLGAVILSLVTNLAGELAGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLER 130
|
90 100 110
....*....|....*....|....*....|....*..
gi 2541161597 156 AMSSV-ITILAVFFSMLVMSWQLTIVVLVCVAVMLVM 191
Cdd:cd18602 131 LLRFLlLCLSAIIVNAIVTPYFLIALIPIIIVYYFLQ 167
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
76-322 |
4.92e-06 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 48.75 E-value: 4.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 76 HALMGMAVLYLAGLLATYLYNRIMVTVSQRTLKGIR---DTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQS 152
Cdd:cd18559 36 HGQVYLSVLGALAILQGITVFQYSMAVSIGGIFASRavhLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 153 IPQAMSSVITILAVFFSMLvmswQLTIVVLVCVAVMLVMV---RVIARRSGTFfiQQQTDLGKLNGY--IEEMIEGQKVV 227
Cdd:cd18559 116 IKMWMGPLQNVIGLYLLIL----LAGPMAAVGIPLGLLYVpvnRVYAASSRQL--KRLESVSKDPRYklFNETLLGISVI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 228 KVFCHEQKAKEDFDKLNDTLAGSARK--ANQYANILMPAMNNVgnlqYVVIAIIGGAIALH-GGGLTLGAIAAFLQLSKS 304
Cdd:cd18559 190 KAFEWEEAFIRQVDAKRDNELAYLPSivYLRALAVRLWCVGPC----IVLFASFFAYVSRHsLAGLVALKVFYSLALTTY 265
|
250
....*....|....*...
gi 2541161597 305 FTQPISQISQQMNAIVMA 322
Cdd:cd18559 266 LNWPLNMSPEVITNIVAA 283
|
|
| ABC_6TM_PglK_like |
cd18553 |
Six-transmembrane helical domain of the ABC transporter PglK and similar proteins; This group ... |
83-263 |
5.67e-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: 48.70 E-value: 5.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 83 VLYLAGLLATYLYNRIMVTVSQRTLKGIRDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMIsQSIPQAMSSVIT 162
Cdd:cd18553 62 GFYIFRSLYNIFYTYLLNRFSFGRYHSIAYRLFKNYLKLNYQDFTNKNSSDLSKSIINEASNLSQVI-QSFLFILSEIFV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 163 ILAVFFSMLVMSWQLTIVVLVCVAVM-LVMVRVIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDFD 241
Cdd:cd18553 141 ILFIYSLLLYVNWKITLVLTLFLGLNvFFITKIVSKKIKKQGKKREESQKKFYKILSETFGNFKIIKLKSNEKEILKNFS 220
|
170 180
....*....|....*....|..
gi 2541161597 242 KLNDTLAgsarKANQYANILMP 263
Cdd:cd18553 221 QASLKFA----KANIINQTLQT 238
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
402-558 |
6.31e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.72 E-value: 6.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 402 ILHDITLYAKPGQKLAFVGSTGAGKTT----ITNLINRFYDIADGKIRYDGININKIKKSDLRHSLGIVLQDTNLFTGTV 477
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHLTV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 478 RENIRYG--------RLDATDEEiEVAARLANADEFIRRLPQGYDTMLTDNGA-SLSQGQRQLIAIARAAVADPPVMILD 548
Cdd:TIGR00956 156 GETLDFAarcktpqnRPDGVSRE-EYAKHIADVYMATYGLSHTRNTKVGNDFVrGVSGGERKRVSIAEASLGGAKIQCWD 234
|
170
....*....|
gi 2541161597 549 EATSSIDTRT 558
Cdd:TIGR00956 235 NATRGLDSAT 244
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
401-582 |
9.19e-06 |
|
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: 49.24 E-value: 9.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 401 PILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGINInKIKKSDLRHSLGIVLQ-DT--NLFTGtv 477
Cdd:TIGR01257 1953 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISDVHQNMGYCPQfDAidDLLTG-- 2029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 478 RENIR-YGRLDAT-DEEIEvaaRLANADefIRRLpqGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATSSID 555
Cdd:TIGR01257 2030 REHLYlYARLRGVpAEEIE---KVANWS--IQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 2102
|
170 180
....*....|....*....|....*...
gi 2541161597 556 TRTESLVQQGMDGLMY-GRTVFVIAHRL 582
Cdd:TIGR01257 2103 PQARRMLWNTIVSIIReGRAVVLTSHSM 2130
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
390-601 |
1.09e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.24 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 390 FDVDFAYNPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKKSD-LRHSLGIVLQ 468
Cdd:PRK09700 266 FEVRNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDaVKKGMAYITE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 469 ---DTNLFTG-TVRENI------RYGRLDAT----DEEIEvaARLANADefiRRLPQGYDTMLTDNGASLSQGQRQLIAI 534
Cdd:PRK09700 346 srrDNGFFPNfSIAQNMaisrslKDGGYKGAmglfHEVDE--QRTAENQ---RELLALKCHSVNQNITELSGGNQQKVLI 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2541161597 535 ARAAVADPPVMILDEATSSIDTRTESLVQQGMDGLM-YGRTVFVIAHRLSTVRN-SNAIMVLEHGRIIE 601
Cdd:PRK09700 421 SKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELPEIITvCDRIAVFCEGRLTQ 489
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
411-582 |
1.34e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.27 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 411 KPGQKLAFVGSTGAGKTTI------------------------------TNLINRFYDIADGKIR------YdginINKI 454
Cdd:PRK13409 97 KEGKVTGILGPNGIGKTTAvkilsgelipnlgdyeeepswdevlkrfrgTELQNYFKKLYNGEIKvvhkpqY----VDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 455 KKsdlrhslgivlqdtnLFTGTVREnirygRLDATDEEievaarlANADEFIRRLpqGYDTMLTDNGASLSQGQRQLIAI 534
Cdd:PRK13409 173 PK---------------VFKGKVRE-----LLKKVDER-------GKLDEVVERL--GLENILDRDISELSGGELQRVAI 223
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2541161597 535 ARAAVADPPVMILDEATSSIDTRTESLVQQGMDGLMYGRTVFVIAHRL 582
Cdd:PRK13409 224 AAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
396-562 |
1.95e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.02 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 396 YNPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDGININKIKK---SDLRHSLGIVLQdtnl 472
Cdd:PRK13541 9 FNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKpycTYIGHNLGLKLE---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 473 ftGTVRENIRYGrldatdEEIEVAARLANADEFIRRLpqgyDTMLTDNGASLSQGQRQLIAIARAAVADPPVMILDEATS 552
Cdd:PRK13541 85 --MTVFENLKFW------SEIYNSAETLYAAIHYFKL----HDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVET 152
|
170
....*....|
gi 2541161597 553 SIDTRTESLV 562
Cdd:PRK13541 153 NLSKENRDLL 162
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
403-621 |
1.98e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.58 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 403 LHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDG----ININKIKKSDLRHSLGIVLQdtNLFTGTVR 478
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGsaalIAISSGLNGQLTGIENIELK--GLMMGLTK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 479 ENIRygrlDATDEEIEvaarLANADEFIRRLPQGYdtmltdngaslSQGQRQLIAIARAAVADPPVMILDEATSSID-TR 557
Cdd:PRK13545 118 EKIK----EIIPEIIE----FADIGKFIYQPVKTY-----------SSGMKSRLGFAISVHINPDILVIDEALSVGDqTF 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2541161597 558 TESLVQQGMDGLMYGRTVFVIAHRLSTVRN--SNAIMvLEHGRIIERGSHEELIAQKGVYYQLYTG 621
Cdd:PRK13545 179 TKKCLDKMNEFKEQGKTIFFISHSLSQVKSfcTKALW-LHYGQVKEYGDIKEVVDHYDEFLKKYNQ 243
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
397-599 |
2.15e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 47.51 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 397 NPDKPILHDITLYAKPGQKLAFVGSTGAGKT-TITNLINRFYDIADGKIRYDG--ININKIKKSdLRHSLGIVLQDTN-- 471
Cdd:TIGR02633 270 NPHRKRVDDVSFSLRRGEILGVAGLVGAGRTeLVQALFGAYPGKFEGNVFINGkpVDIRNPAQA-IRAGIAMVPEDRKrh 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 472 --LFTGTVRENIRYGRLD--ATDEEIEVAARLANADEFIRRLP-QGYDTMLTDngASLSQGQRQLIAIARAAVADPPVMI 546
Cdd:TIGR02633 349 giVPILGVGKNITLSVLKsfCFKMRIDAAAELQIIGSAIQRLKvKTASPFLPI--GRLSGGNQQKAVLAKMLLTNPRVLI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2541161597 547 LDEATSSIDTRTESLVQQGMDGLMY-GRTVFVIAHRLSTVRN-SNAIMVLEHGRI 599
Cdd:TIGR02633 427 LDEPTRGVDVGAKYEIYKLINQLAQeGVAIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
140-314 |
2.90e-05 |
|
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: 46.28 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 140 NDVDTLRQMISQSipqAMSSVITILAVFFSMLVM---SWQLTIVVLVCVAVMLVMVRVIARRSGTFFIQQQTDLGKLNGY 216
Cdd:cd18587 105 REFESVRDFFTSA---TLTALIDLPFVLLFLAVIaliGGPLALVPLVAIPLVLLYGLLLQKPLRRLVEESMRESAQKNAL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 217 IEEMIEGQKVVKVFCHEQKAKEDFDKLNDTLAGSARKANQYANILMPAMNNVGNLQYVVIaIIGGAIALHGGGLTLGAIA 296
Cdd:cd18587 182 LVESLSGLETIKALGAEGRMQRRWEEAVAALARSSLKSRLLSSSATNFAQFVQQLVTVAI-VIVGVYLISDGELTMGGLI 260
|
170
....*....|....*...
gi 2541161597 297 AFLQLSKSFTQPISQISQ 314
Cdd:cd18587 261 ACVILSGRALAPLGQIAG 278
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
411-584 |
3.37e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 46.70 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 411 KPGQKLAFVGSTGAGKTTI------------------------------TNLINRFYDIADGKIR------YdginINKI 454
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTAlkilsgelkpnlgdydeepswdevlkrfrgTELQDYFKKLANGEIKvahkpqY----VDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 455 KKSdlrhslgivlqdtnlFTGTVREnirygRLDATDEEievaarlANADEFIRRLpqGYDTMLTDNGASLSQGQRQLIAI 534
Cdd:COG1245 173 PKV---------------FKGTVRE-----LLEKVDER-------GKLDELAEKL--GLENILDRDISELSGGELQRVAI 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2541161597 535 ARAAVADPPVMILDEATSSIDTRTESLVQQGMDGLM-YGRTVFVIAHRLST 584
Cdd:COG1245 224 AAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAeEGKYVLVVEHDLAI 274
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
411-596 |
3.64e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 45.82 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 411 KPGQKLAFVGSTGAGKTT---------ITNLiNRFydiaDGKIRYDGInINKIKKSDLRHSLGIVLQDT----------- 470
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTalkilagklKPNL-GKF----DDPPDWDEI-LDEFRGSELQNYFTKLLEGDvkvivkpqyvd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 471 ---NLFTGTVRENirygrLDATDEeievaarLANADEFIRRLpqGYDTMLTDNGASLSQGQRQLIAIARAAVADPPVMIL 547
Cdd:cd03236 98 lipKAVKGKVGEL-----LKKKDE-------RGKLDELVDQL--ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2541161597 548 DEATSSIDtrteslVQQGMdglmygrTVFVIAHRLStvRNSNAIMVLEH 596
Cdd:cd03236 164 DEPSSYLD------IKQRL-------NAARLIRELA--EDDNYVLVVEH 197
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
78-199 |
4.68e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 45.63 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 78 LMGMAVLYLAGLLATYLYNRIMVTVSQRtlkgIRDTLFSHMQALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAM 157
Cdd:cd18599 65 GGSILVILLLSLIRGFVFVKVTLRASSR----LHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFL 140
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2541161597 158 SSVITILAVFFSMLVMSWQLTIVVLVCVAVMLVmVRVIARRS 199
Cdd:cd18599 141 QNVLLVVFSLIIIAIVFPWFLIALIPLAIIFVF-LSKIFRRA 181
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
399-611 |
4.94e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 46.24 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 399 DKPILHDITLYAKPGQKLAFVGSTGAGKTtITNL-INRF-------YdiADGKIRYDGININKIKKSDLRHSLG----IV 466
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKS-VTALsILRLlpsppvvY--PSGDIRFHGESLLHASEQTLRGVRGnkiaMI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 467 LQDT------------------NLFTGTVRENIRYGRLDATDEeieVAARLANadefiRRLpqgydtmlTDNGASLSQGQ 528
Cdd:PRK15134 98 FQEPmvslnplhtlekqlyevlSLHRGMRREAARGEILNCLDR---VGIRQAA-----KRL--------TDYPHQLSGGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 529 RQLIAIARAAVADPPVMILDEATSSIDTRTESLV-------QQGMD-GLMYgrtvfvIAHRLSTVRN-SNAIMVLEHGRI 599
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQIlqllrelQQELNmGLLF------ITHNLSIVRKlADRVAVMQNGRC 235
|
250
....*....|..
gi 2541161597 600 IERGSHEELIAQ 611
Cdd:PRK15134 236 VEQNRAATLFSA 247
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
395-555 |
1.10e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.11 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 395 AYNPDKPILHDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRY-DGINInkikksdlrhslGIVLQDTNL- 472
Cdd:PRK11819 15 VVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGIKV------------GYLPQEPQLd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 473 FTGTVRENIRYG---RLDATDEEIEVAARLAN--------ADEFIR------------------------RLPQGyDTML 517
Cdd:PRK11819 83 PEKTVRENVEEGvaeVKAALDRFNEIYAAYAEpdadfdalAAEQGElqeiidaadawdldsqleiamdalRCPPW-DAKV 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 2541161597 518 TdngaSLSQGQRQLIAIARAAVADPPVMILDEATSSID 555
Cdd:PRK11819 162 T----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
404-607 |
1.53e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.52 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 404 HDITLYAKPGQKLAFVGSTGAGKTTITNLINRFYDIADGKIRYDG--ININKIKKSdLRHslGIVL------QDTNLFTG 475
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRDA-IRA--GIMLcpedrkAEGIIPVH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 476 TVRENI---------RYGRLDATDEEIEvaarlaNADEFIRRL----PQGYDTMLTdngasLSQGQRQLIAIARAAVADP 542
Cdd:PRK11288 347 SVADNInisarrhhlRAGCLINNRWEAE------NADRFIRSLniktPSREQLIMN-----LSGGNQQKAILGRWLSEDM 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2541161597 543 PVMILDEATSSIDTRTESLVQQgmdgLMY-----GRTVFVIAHRLSTVRN-SNAIMVLEHGRIIERGSHEE 607
Cdd:PRK11288 416 KVILLDEPTRGIDVGAKHEIYN----VIYelaaqGVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQ 482
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
500-613 |
1.63e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 44.34 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 500 ANADEFIRRLPqgydtmLTDNG----ASLSQGQRQLIAIARAAVADPPVMILDEATSSIDTRTESLVQQGMDGLMY-GRT 574
Cdd:NF000106 123 ARADELLERFS------LTEAAgraaAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRdGAT 196
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2541161597 575 VFVIAHRLSTVRN-SNAIMVLEHGRIIERGSHEELIAQKG 613
Cdd:NF000106 197 VLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
397-555 |
1.86e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.31 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 397 NPDKPILHDITLYAKPGQKLAFVGSTGAGKTTIT-NLINRFY--DIAdGKIRYDG--ININKIKK---------SDLRHS 462
Cdd:NF040905 270 HPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAmSVFGRSYgrNIS-GTVFKDGkeVDVSTVSDaidaglayvTEDRKG 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 463 LGIVLQDTnlftgtVRENI---------RYGRLDAtDEEIEVAarlanaDEFIRRLPQGYDTMLTDNGaSLSQGQRQLIA 533
Cdd:NF040905 349 YGLNLIDD------IKRNItlanlgkvsRRGVIDE-NEEIKVA------EEYRKKMNIKTPSVFQKVG-NLSGGNQQKVV 414
|
170 180
....*....|....*....|..
gi 2541161597 534 IARAAVADPPVMILDEATSSID 555
Cdd:NF040905 415 LSKWLFTDPDVLILDEPTRGID 436
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
80-312 |
2.38e-03 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 40.28 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 80 GMAVLYLAGLLATYLYNRIMVTVSQRTLKGIRDTLFSHMQALPiryFDTHPHGDIMSVYtNDVDTLRQMISQSIPQA--- 156
Cdd:cd18586 47 GMVVLLAFDGLLRQVRSRILQRVGLRLDVELGRRVFRAVLELP---LESRPSGYWQQLL-RDLDTLRNFLTGPSLFAffd 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 157 MSSVITILAVFFsmLVMSWqLTIVVLVCVAVMLVMVRVIARRSGTFFIQQQTDLGKLNGYIEEMIEGQKVVKVFCHEQKA 236
Cdd:cd18586 123 LPWAPLFLAVIF--LIHPP-LGWVALVGAPVLVGLAWLNHRATRKPLGEANEAQAARDALAAETLRNAETIKALGMLGNL 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2541161597 237 KEDFDKLNDTLAGSARKANQYANILmpamNNVGN-LQYVVIAII--GGAIALHGGGLTLGAIAAFLQLSKSFTQPISQI 312
Cdd:cd18586 200 RRRWEARHAETLELQIRASDLAGAI----SAIGKtLRMALQSLIlgVGAYLVIDGELTIGALIAASILSGRALAPIDQL 274
|
|
| ABC_6TM_AarD_CydDC_like |
cd18781 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ... |
39-198 |
2.64e-03 |
|
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: 40.21 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 39 LISAAASVGASVFLESLIDDyikplLLQDVPVFTGLVHALMGMAVLYLAGLLATYLYNRIMVTVSQRTLKGIRDTLFSHM 118
Cdd:cd18781 6 WISLLANIAFVFSIANLLQK-----LLEGKLTTASLLIVLGILAIAIIVRFICTRLASRASYRASADVKKTLREKIYDKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 119 QALPIRYFDTHPHGDIMSVYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVCV---AVMLVMVRVI 195
Cdd:cd18781 81 LRLGPSYQEKVSTAEVVQLSVEGVEQLEIYFGRYLPQFFYSMLAPLTLFVVLAPINWKAALVLLICVpliPISIIAVQKI 160
|
...
gi 2541161597 196 ARR 198
Cdd:cd18781 161 AKK 163
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
31-184 |
3.07e-03 |
|
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: 40.12 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 31 LVVVLVAILISAAASVgASVFL-ESLIDDYIKpllLQDVPvFTGLVhaLMGMAVLYLAGLLATYLYNRIMVTVSQRT-LK 108
Cdd:cd18571 4 ILQLLLGLLLGSLLQL-IFPFLtQSIVDKGIN---NKDLN-FIYLI--LIAQLVLFLGSTSIEFIRSWILLHISSRInIS 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2541161597 109 GIRDTLFSHMQaLPIRYFDTHPHGDIMSvYTNDVDTLRQMISQSIPQAMSSVITILAVFFSMLVMSWQLTIVVLVC 184
Cdd:cd18571 77 IISDFLIKLMR-LPISFFDTKMTGDILQ-RINDHSRIESFLTSSSLSILFSLLNLIVFSIVLAYYNLTIFLIFLIG 150
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
35-324 |
3.46e-03 |
|
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: 39.82 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 35 LVAILISAAASVGASVFLESLIDDYIKPLLLQDVPVFTGLVHA-LMGMAVLYLAGLLATYLYNRIMVTVSQRTLKGIRDT 113
Cdd:cd18605 1 LILILLSLILMQASRNLIDFWLSYWVSHSNNSFFNFINDSFNFfLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 114 LFSHMQALPIRYFDTHPHGDIMSVYTNDVDTlrqmISQSIP--------QAMSSVITILAVFFSMlvmsWQLTIVVLVCV 185
Cdd:cd18605 81 LLSSILFAKMSFFDKTPVGRILNRFSSDVYT----IDDSLPfilnillaQLFGLLGYLVVICYQL----PWLLLLLLPLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2541161597 186 AVMlvmvrviarrsgtFFIQQQ-------------TDLGKLNGYIEEMIEGQKVVKVFCHEQKAKEDF-DKLND----TL 247
Cdd:cd18605 153 FIY-------------YRIQRYyratsrelkrlnsVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYlEKLENnqraQL 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2541161597 248 AGSArkANQYANILMPAMNNVgnlqyVVIAIIGGAIALHGGGLTlgAIAAFLQLSKSFTQPisqISQQMNAIVMALA 324
Cdd:cd18605 220 ASQA--ASQWLSIRLQLLGVL-----IVTFVALTAVVQHFFGLS--IDAGLIGLALSYALP---ITGLLSGLLNSFT 284
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
409-431 |
8.15e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 38.76 E-value: 8.15e-03
|
| |
