|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-517 |
0e+00 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 691.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 2 DQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQ 81
Cdd:TIGR00958 198 PALASAIFFMCLLSIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 82 NINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFA 161
Cdd:TIGR00958 278 NVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFA 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 162 NEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESV 241
Cdd:TIGR00958 358 AEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVL 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 242 GSVYSGLMQGVGAAEKVFEFIDRQPTMVHDGSLAPDHLEGRVDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSG 321
Cdd:TIGR00958 438 SYVYSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSG 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 322 SGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAH 401
Cdd:TIGR00958 518 SGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAH 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 402 GFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIhgNLQKHTVLIIAHRLS 481
Cdd:TIGR00958 598 DFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESR--SRASRTVLLIAHRLS 675
|
490 500 510
....*....|....*....|....*....|....*.
gi 2217288354 482 TVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLV 517
Cdd:TIGR00958 676 TVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-523 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 564.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 1 MDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVS 80
Cdd:COG1132 57 LSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 81 QNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSF 160
Cdd:COG1132 137 HGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAF 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 161 ANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMES 240
Cdd:COG1132 217 GREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQ 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 241 VGSVYSGLMQGVGAAEKVFEFIDRQPTMVH-DGSLAPDHLEGRVDFENVTFTYRtrPHTQVLQNVSFSLSPGKVTALVGP 319
Cdd:COG1132 297 LANVLNQLQRALASAERIFELLDEPPEIPDpPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGP 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 320 SGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKAN 399
Cdd:COG1132 375 SGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQ 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 400 AHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHR 479
Cdd:COG1132 455 AHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHR 534
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2217288354 480 LSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQMLG 523
Cdd:COG1132 535 LSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYRLQFGE 578
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
1-258 |
5.54e-166 |
|
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: 472.18 E-value: 5.54e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 1 MDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVS 80
Cdd:cd18784 32 QDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 81 QNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSF 160
Cdd:cd18784 112 LNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSF 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 161 ANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMES 240
Cdd:cd18784 192 ANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQISGGNLISFILYQLELGSCLES 271
|
250
....*....|....*...
gi 2217288354 241 VGSVYSGLMQGVGAAEKV 258
Cdd:cd18784 272 VGSVYTGLMQAVGAAEKV 289
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
272-497 |
5.12e-149 |
|
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: 426.50 E-value: 5.12e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 272 GSLAPDHLEGRVDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISA 351
Cdd:cd03248 1 GSLAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 352 YDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVA 431
Cdd:cd03248 81 YEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217288354 432 MARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRV 497
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
8-521 |
1.49e-148 |
|
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: 443.12 E-value: 1.49e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 8 VVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLtSDTTMVSDLVSQNINVFL 87
Cdd:COG2274 199 AIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTAL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 88 RNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEA 167
Cdd:COG2274 278 LDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFR 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 168 EVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYefvlgdcmesVGSVYSG 247
Cdd:COG2274 358 RRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNIL----------SGRFLAP 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 248 LMQGVG----------AAEKVFEFIDRQPTMVHDGS-LAPDHLEGRVDFENVTFTYRTRPhTQVLQNVSFSLSPGKVTAL 316
Cdd:COG2274 428 VAQLIGllqrfqdakiALERLDDILDLPPEREEGRSkLSLPRLKGDIELENVSFRYPGDS-PPVLDNISLTIKPGERVAI 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 317 VGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQ 396
Cdd:COG2274 507 VGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAAR 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 397 KANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLII 476
Cdd:COG2274 587 LAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIII 666
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2217288354 477 AHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQM 521
Cdd:COG2274 667 AHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
4-520 |
3.24e-148 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 437.98 E-value: 3.24e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 4 FSTAVVIVCLLAIGSSFaagiRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNI 83
Cdd:TIGR02204 61 FAFLLVVALVLALGTAA----RFYLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 84 NVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANE 163
Cdd:TIGR02204 137 SMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 164 EEEAEVYLRKLQQVYKLNRKE-------AAAYMYYVWGSgltllvvQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGD 236
Cdd:TIGR02204 217 DAERSRFGGAVEKAYEAARQRirtrallTAIVIVLVFGA-------IVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 237 CMESVGSVYSGLMQGVGAAEKVFEFIDRQPTM---VHDGSLaPDHLEGRVDFENVTFTYRTRPHTQVLQNVSFSLSPGKV 313
Cdd:TIGR02204 290 SIGTLSEVWGELQRAAGAAERLIELLQAEPDIkapAHPKTL-PVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGET 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 314 TALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVE 393
Cdd:TIGR02204 369 VALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEA 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 394 AAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTV 473
Cdd:TIGR02204 449 AARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTT 528
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2217288354 474 LIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQ 520
Cdd:TIGR02204 529 LIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
40-516 |
2.87e-139 |
|
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: 414.88 E-value: 2.87e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 40 LRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIM 119
Cdd:TIGR02203 89 IRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLS 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 120 MVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYvwgSGLTL 199
Cdd:TIGR02203 169 ILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSIS---SPITQ 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 200 LVVQVS---ILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKVFEFIDrQPTMVHDGSLAP 276
Cdd:TIGR02203 246 LIASLAlavVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLD-SPPEKDTGTRAI 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 277 DHLEGRVDFENVTFTYRTRpHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKY 356
Cdd:TIGR02203 325 ERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAS 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 357 LHRVISLVSQEPVLFARSITDNISYGLP-TVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARA 435
Cdd:TIGR02203 404 LRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARA 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 436 LVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAK 515
Cdd:TIGR02203 484 LLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQ 563
|
.
gi 2217288354 516 L 516
Cdd:TIGR02203 564 L 564
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
283-520 |
7.79e-121 |
|
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: 355.31 E-value: 7.79e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 362
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 LVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPV 442
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217288354 443 LILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQ 520
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
1-258 |
5.44e-118 |
|
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: 349.92 E-value: 5.44e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 1 MDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVS 80
Cdd:cd18572 32 REAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 81 QNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSF 160
Cdd:cd18572 112 TNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSF 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 161 ANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMES 240
Cdd:cd18572 192 ATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQS 271
|
250
....*....|....*...
gi 2217288354 241 VGSVYSGLMQGVGAAEKV 258
Cdd:cd18572 272 LGDVFSSLMQAVGAAEKV 289
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
36-520 |
2.79e-114 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 350.86 E-value: 2.79e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 36 LNIRLRncLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGF 115
Cdd:PRK11176 98 MTMRRR--LFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVIA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 116 PIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEvylrKLQQVYKLNRKEAaayMYYVWGS 195
Cdd:PRK11176 176 PIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETK----RFDKVSNRMRQQG---MKMVSAS 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 196 GLTLLVVQ-------VSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKVFEFIDRQPTm 268
Cdd:PRK11176 249 SISDPIIQliaslalAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQE- 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 269 VHDGSLAPDHLEGRVDFENVTFTYRTRpHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKP 348
Cdd:PRK11176 328 KDEGKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 349 ISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLP-TVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQK 427
Cdd:PRK11176 407 LRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTeQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQR 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 428 QRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQKH-TVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQL 506
Cdd:PRK11176 487 QRIAIARALLRDSPILILDEATSALDTESERAIQAALD-ELQKNrTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAEL 565
|
490
....*....|....
gi 2217288354 507 LAQGGLYAKLVQRQ 520
Cdd:PRK11176 566 LAQNGVYAQLHKMQ 579
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
156-520 |
6.68e-110 |
|
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: 340.26 E-value: 6.68e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 156 TVRSFANEEEEAEVYLRKLQqvyklnRKEAAAYMyyVWGSGLTLLVVQ--------VSILYYGGHLVISGQMTSGNLI-- 225
Cdd:COG5265 230 TVKYFGNEAREARRYDEALA------RYERAAVK--SQTSLALLNFGQaliialglTAMMLMAAQGVVAGTMTVGDFVlv 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 226 -AFIIYEFV-LGdcmeSVGSVYSGLMQGVGAAEKVFEFIDRQPTmVHDgslAPD--HL---EGRVDFENVTFTYRtrPHT 298
Cdd:COG5265 302 nAYLIQLYIpLN----FLGFVYREIRQALADMERMFDLLDQPPE-VAD---APDapPLvvgGGEVRFENVSFGYD--PER 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 299 QVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDN 378
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYN 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 379 ISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEY 458
Cdd:COG5265 452 IAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTER 531
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217288354 459 LIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQ 520
Cdd:COG5265 532 AIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQ 593
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
283-516 |
8.06e-104 |
|
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: 311.47 E-value: 8.06e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRPhTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 362
Cdd:cd03251 1 VEFKNVTFRYPGDG-PPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 LVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPV 442
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217288354 443 LILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKL 516
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
96-511 |
4.01e-102 |
|
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: 318.63 E-value: 4.01e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 96 VVVFMFSLSWQLSLVTFMGFPII---MMvsnIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEvylr 172
Cdd:COG4988 149 ILVAVFPLDWLSGLILLVTAPLIplfMI---LVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAE---- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 173 klqQVYKLNRKEAAAYMyyvwG-------SGLTL-LVVQVSI---LYYGGHLVISGQMT--SGNLIAFIIYEFVLGdcME 239
Cdd:COG4988 222 ---RIAEASEDFRKRTM----KvlrvaflSSAVLeFFASLSIalvAVYIGFRLLGGSLTlfAALFVLLLAPEFFLP--LR 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 240 SVGSVYSGLMQGVGAAEKVFEFIDRQPTMVHDGSL-APDHLEGRVDFENVTFTYRTRphTQVLQNVSFSLSPGKVTALVG 318
Cdd:COG4988 293 DLGSFYHARANGIAAAEKIFALLDAPEPAAPAGTApLPAAGPPSIELEDVSFSYPGG--RPALDGLSLTIPPGERVALVG 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 319 PSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKA 398
Cdd:COG4988 371 PSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAA 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 399 NAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAH 478
Cdd:COG4988 451 GLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITH 530
|
410 420 430
....*....|....*....|....*....|...
gi 2217288354 479 RLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGG 511
Cdd:COG4988 531 RLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
39-519 |
8.51e-99 |
|
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: 8.51e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 39 RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDttmVSDLVsqniNVFLR-------NTVKVTGVVVFMFSLSWQLSLVT 111
Cdd:COG4987 89 DLRVRLYRRLEPLAPAGLARLRSGDLLNRLVAD---VDALD----NLYLRvllpllvALLVILAAVAFLAFFSPALALVL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 112 FMGF-------PIIMMVSNiygkyyKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKE 184
Cdd:COG4987 162 ALGLllaglllPLLAARLG------RRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 185 AAAYMyyvWGSGLTLLVVQ---VSILYYGGHLVISGQMtSGNLIAFIIYeFVLGdCMESVGSVySGLMQGVG----AAEK 257
Cdd:COG4987 236 ARLSA---LAQALLQLAAGlavVAVLWLAAPLVAAGAL-SGPLLALLVL-AALA-LFEALAPL-PAAAQHLGrvraAARR 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 258 VFEFIDRQPTMVHDGSLAPDHLEGRVDFENVTFTYRTRPHTqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPL 337
Cdd:COG4987 309 LNELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRP-VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDP 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 338 EGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGE 417
Cdd:COG4987 388 QSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGE 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 418 KGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRV 497
Cdd:COG4987 468 GGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRI 547
|
490 500
....*....|....*....|..
gi 2217288354 498 VQQGTHQQLLAQGGLYAKLVQR 519
Cdd:COG4987 548 VEQGTHEELLAQNGRYRQLYQR 569
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
283-520 |
9.40e-98 |
|
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: 296.06 E-value: 9.40e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 362
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 LVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPV 442
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217288354 443 LILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQ 520
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
281-511 |
1.09e-96 |
|
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: 292.98 E-value: 1.09e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 281 GRVDFENVTFTYRtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV 360
Cdd:cd03254 1 GEIEFENVNFSYD--EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 361 ISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNP 440
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217288354 441 PVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGG 511
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
30-529 |
2.51e-92 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 294.32 E-value: 2.51e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 30 TLIFARLNI----RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSW 105
Cdd:PRK10790 86 SLLFNRAAVgvvqQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDW 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 106 QLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEvylrKLQQVyklNRKEA 185
Cdd:PRK10790 166 RMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGE----RMGEA---SRSHY 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 186 AAYMYYVWGSGLTL--LVVQVSILYYGGHLVI-----SGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 258
Cdd:PRK10790 239 MARMQTLRLDGFLLrpLLSLFSALILCGLLMLfgfsaSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERV 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 259 FEFID--RQPTMVHDGSLApdhlEGRVDFENVTFTYRTrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYP 336
Cdd:PRK10790 319 FELMDgpRQQYGNDDRPLQ----SGRIDIDNVSFAYRD--DNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYP 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 337 LEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPtVPFEMVVEAAQKANAHGFIMELQDGYSTETG 416
Cdd:PRK10790 393 LTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD-ISEEQVWQALETVQLAELARSLPDGLYTPLG 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 417 EKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGR 496
Cdd:PRK10790 472 EQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQ 551
|
490 500 510
....*....|....*....|....*....|...
gi 2217288354 497 VVQQGTHQQLLAQGGLYAKLVQRQMLGLQPAAD 529
Cdd:PRK10790 552 AVEQGTHQQLLAAQGRYWQMYQLQLAGEELAAS 584
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
283-520 |
1.55e-91 |
|
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: 280.14 E-value: 1.55e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 362
Cdd:cd03252 1 ITFEHVRFRYKP-DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 LVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPV 442
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217288354 443 LILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQ 520
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
101-522 |
2.14e-89 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 286.47 E-value: 2.14e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 101 FSLSWQLSLVTFmgfpIIMMVSNIYGKYYKRLSKEVQNAL--------ARASntaeETISAMKTVRSFANEEEEAEVyLR 172
Cdd:PRK13657 152 LFMNWRLSLVLV----VLGIVYTLITTLVMRKTKDGQAAVeehyhdlfAHVS----DAIGNVSVVQSYNRIEAETQA-LR 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 173 KLqqvykLNRKEAAAYMYYVW---GSGLTLL---VVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYS 246
Cdd:PRK13657 223 DI-----ADNLLAAQMPVLSWwalASVLNRAastITMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFIN 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 247 GLMQgvgAAEKVFEFIDRQPTM--VHDGSLAPD--HLEGRVDFENVTFTYRTRPhtQVLQNVSFSLSPGKVTALVGPSGS 322
Cdd:PRK13657 298 QVFM---AAPKLEEFFEVEDAVpdVRDPPGAIDlgRVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTGA 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 323 GKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHG 402
Cdd:PRK13657 373 GKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHD 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 403 FIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLST 482
Cdd:PRK13657 453 FIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLST 532
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2217288354 483 VEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQML 522
Cdd:PRK13657 533 VRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQGM 572
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
1-258 |
4.55e-87 |
|
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: 270.59 E-value: 4.55e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 1 MDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVS 80
Cdd:cd18557 32 LDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 81 QNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSF 160
Cdd:cd18557 112 DNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSF 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 161 ANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMES 240
Cdd:cd18557 192 SAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGG 271
|
250
....*....|....*...
gi 2217288354 241 VGSVYSGLMQGVGAAEKV 258
Cdd:cd18557 272 LSSLLADIMKALGASERV 289
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
2-258 |
5.15e-85 |
|
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: 265.36 E-value: 5.15e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 2 DQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQ 81
Cdd:cd18590 33 NAFTSAIGLMCLFSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVAL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 82 NINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFA 161
Cdd:cd18590 113 NANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 162 NEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESV 241
Cdd:cd18590 193 AEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGSLVSFILYQKNLGSYVRTL 272
|
250
....*....|....*..
gi 2217288354 242 GSVYSGLMQGVGAAEKV 258
Cdd:cd18590 273 VYIYGDMLSNVGAAAKV 289
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
54-518 |
3.43e-83 |
|
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: 273.36 E-value: 3.43e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 54 SFFDENRTGDLISRLTSDTTmVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLS 133
Cdd:TIGR03796 243 RFFAQRHAGDIASRVQLNDQ-VAEFLSGQLATTALDAVMLVFYALLMLLYDPVLTLIGIAFAAINVLALQLVSRRRVDAN 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 134 KEVQNALARASNTAEETISAMKTVRSFANEEEE----AEVYLRKLQQVYKLNRKEAaayMYYVWGSGLTLLVVqVSILYY 209
Cdd:TIGR03796 322 RRLQQDAGKLTGVAISGLQSIETLKASGLESDFfsrwAGYQAKLLNAQQELGVLTQ---ILGVLPTLLTSLNS-ALILVV 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 210 GGHLVISGQMTSGNLIAFiiyEFVLGDCMESVGSV--YSGLMQGVGAAEKVFEFIDRQPTMVHDGSLAPD--------HL 279
Cdd:TIGR03796 398 GGLRVMEGQLTIGMLVAF---QSLMSSFLEPVNNLvgFGGTLQELEGDLNRLDDVLRNPVDPLLEEPEGSaatsepprRL 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 280 EGRVDFENVTFTY-RTRPHtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLH 358
Cdd:TIGR03796 475 SGYVELRNITFGYsPLEPP--LIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLA 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 359 RVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVR 438
Cdd:TIGR03796 553 NSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVR 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 439 NPPVLILDEATSALDAESEYLIQQaihgNLQKH--TVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKL 516
Cdd:TIGR03796 633 NPSILILDEATSALDPETEKIIDD----NLRRRgcTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARL 708
|
..
gi 2217288354 517 VQ 518
Cdd:TIGR03796 709 IR 710
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
283-496 |
4.99e-80 |
|
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: 248.07 E-value: 4.99e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRPHtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 362
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 LVSQEPVLFARSITDNIsyglptvpfemvveaaqkanahgfimelqdgystetgekgaqLSGGQKQRVAMARALVRNPPV 442
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2217288354 443 LILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGR 496
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
2-258 |
1.14e-78 |
|
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: 248.93 E-value: 1.14e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 2 DQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQ 81
Cdd:cd18589 33 EAFTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 82 NINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFA 161
Cdd:cd18589 113 NLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 162 NEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESV 241
Cdd:cd18589 193 NEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGGQLVTAGTVSSGDLVTFVLYELQFTSAVEVL 272
|
250
....*....|....*..
gi 2217288354 242 GSVYSGLMQGVGAAEKV 258
Cdd:cd18589 273 LSYYPSVMKAVGSSEKI 289
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
1-258 |
9.62e-77 |
|
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: 244.08 E-value: 9.62e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 1 MDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVS 80
Cdd:cd18780 38 LRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 81 QNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSF 160
Cdd:cd18780 118 VNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSF 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 161 ANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYvwgSGLTLLVVQVSI---LYYGGHLVISGQMTSGNLIAFIIYEFVLGDC 237
Cdd:cd18780 198 AKETKEVSRYSEKINESYLLGKKLARASGGF---NGFMGAAAQLAIvlvLWYGGRLVIDGELTTGLLTSFLLYTLTVAMS 274
|
250 260
....*....|....*....|.
gi 2217288354 238 MESVGSVYSGLMQGVGAAEKV 258
Cdd:cd18780 275 FAFLSSLYGDFMQAVGASVRV 295
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
35-541 |
9.71e-77 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 252.71 E-value: 9.71e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 35 RLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFS-LSWQLSLVTFM 113
Cdd:PRK10789 66 QLAVELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMSTqISWQLTLLALL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 114 GFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANE-------EEEAEVYLRKLQQVYKLN-RKEA 185
Cdd:PRK10789 146 PMPVMAIMIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEdrqsalfAADAEDTGKKNMRVARIDaRFDP 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 186 AAYMyyvwGSGLT-LLVVQvsilyYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKVFEFIDR 264
Cdd:PRK10789 226 TIYI----AIGMAnLLAIG-----GGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 265 QPtMVHDGSLAPDHLEGRVDFENVTFTYrtrPHTQ--VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRV 342
Cdd:PRK10789 297 AP-VVKDGSEPVPEGRGELDVNIRQFTY---PQTDhpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 343 LLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQL 422
Cdd:PRK10789 373 RFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVML 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 423 SGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGT 502
Cdd:PRK10789 453 SGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGN 532
|
490 500 510
....*....|....*....|....*....|....*....
gi 2217288354 503 HQQLLAQGGLYAKLVQRQMlgLQPAADFTAGHNEPVANG 541
Cdd:PRK10789 533 HDQLAQQSGWYRDMYRYQQ--LEAALDDAPEIREEAVDA 569
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
1-258 |
1.30e-76 |
|
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: 243.58 E-value: 1.30e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 1 MDQFSTAVVIVCLLAIGSsFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVS 80
Cdd:cd18573 38 LSLKTFALALLGVFVVGA-AANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 81 QNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSF 160
Cdd:cd18573 117 QNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 161 ANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMES 240
Cdd:cd18573 197 AAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSG 276
|
250
....*....|....*...
gi 2217288354 241 VGSVYSGLMQGVGAAEKV 258
Cdd:cd18573 277 LSSFYSELMKGLGASSRL 294
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
96-492 |
1.13e-74 |
|
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: 246.04 E-value: 1.13e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 96 VVVFMFSLSWQ---LSLVTFMGFPIIMMVSniyGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVyLR 172
Cdd:TIGR02857 135 ILAAVFPQDWIsglILLLTAPLIPIFMILI---GWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAA-IR 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 173 KLQQVYklnRKEAAAYMYYVWGSGLTL-----LVVQVSILYYGGHLViSGQMT--SGNLIAFIIYEFVLGdcMESVGSVY 245
Cdd:TIGR02857 211 RSSEEY---RERTMRVLRIAFLSSAVLelfatLSVALVAVYIGFRLL-AGDLDlaTGLFVLLLAPEFYLP--LRQLGAQY 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 246 SGLMQGVGAAEKVFEFIDRQPTMVHDGSLAPDHLEGRVDFENVTFTYRTRphTQVLQNVSFSLSPGKVTALVGPSGSGKS 325
Cdd:TIGR02857 285 HARADGVAAAEALFAVLDAAPRPLAGKAPVTAAPASSLEFSGVSVAYPGR--RPALRPVSFTVPPGERVALVGPSGAGKS 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 326 SCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIM 405
Cdd:TIGR02857 363 TLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVA 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 406 ELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEH 485
Cdd:TIGR02857 443 ALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAAL 522
|
....*..
gi 2217288354 486 AHLIVVL 492
Cdd:TIGR02857 523 ADRIVVL 529
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
54-517 |
6.01e-69 |
|
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: 235.02 E-value: 6.01e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 54 SFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTgVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLS 133
Cdd:TIGR01193 245 SFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILVI-VGLFLVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKLN 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 134 KEVQNALARASNTAEETISAMKTVRSFANEEE-------EAEVYLRKlqqVYKLNRKEAAAYMYYVwgsgLTLLVVQVSI 206
Cdd:TIGR01193 324 HDAMQANAVLNSSIIEDLNGIETIKSLTSEAEryskidsEFGDYLNK---SFKYQKADQGQQAIKA----VTKLILNVVI 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 207 LYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKVFE--FIDRQPTMVHDGSlAPDHLEGRVD 284
Cdd:TIGR01193 397 LWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEvyLVDSEFINKKKRT-ELNNLNGDIV 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 285 FENVTFTYRTrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLV 364
Cdd:TIGR01193 476 INDVSYSYGY--GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYL 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 365 SQEPVLFARSITDNISYGL-PTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVL 443
Cdd:TIGR01193 554 PQEPYIFSGSILENLLLGAkENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVL 633
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217288354 444 ILDEATSALDAESEYLIQQAIHgNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLV 517
Cdd:TIGR01193 634 ILDESTSNLDTITEKKIVNNLL-NLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
53-521 |
3.75e-68 |
|
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: 232.54 E-value: 3.75e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 53 TSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVfMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRL 132
Cdd:TIGR03797 224 VSFFRQYSTGDLASRAMGISQIRRILSGSTLTTLLSGIFALLNLGL-MFYYSWKLALVAVALALVAIAVTLVLGLLQVRK 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 133 SKEVQNALARASNTAEETIS-------AMKTVRSFAneeEEAEVYLRKLQQVYKLNRkeaaaymyyvWGSGLT-----LL 200
Cdd:TIGR03797 303 ERRLLELSGKISGLTVQLINgisklrvAGAENRAFA---RWAKLFSRQRKLELSAQR----------IENLLTvfnavLP 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 201 VVQVSILYYgghLVISGQMTSG-NLIAFIIYEFVLGDCMESVGSVySGLMQGVGAAEKVFEFID---RQPTMVHDGSLAP 276
Cdd:TIGR03797 370 VLTSAALFA---AAISLLGGAGlSLGSFLAFNTAFGSFSGAVTQL-SNTLISILAVIPLWERAKpilEALPEVDEAKTDP 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 277 DHLEGRVDFENVTFTYRtRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKY 356
Cdd:TIGR03797 446 GKLSGAIEVDRVTFRYR-PDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQA 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 357 LHRVISLVSQEPVLFARSITDNISYGLPTVPfEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARAL 436
Cdd:TIGR03797 525 VRRQLGVVLQNGRLMSGSIFENIAGGAPLTL-DEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARAL 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 437 VRNPPVLILDEATSALDAESEYLIQQAIHGnlQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKL 516
Cdd:TIGR03797 604 VRKPRILLFDEATSALDNRTQAIVSESLER--LKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQL 681
|
....*
gi 2217288354 517 VQRQM 521
Cdd:TIGR03797 682 ARRQL 686
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
200-509 |
3.33e-67 |
|
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: 227.32 E-value: 3.33e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 200 LVVQVSILYYGGHLVISGQMTSGNLIAFIIyefVLGDCM---ESVGSVYSGLMQGVGAAEKVFEFIDRQPTmvHDGSLAP 276
Cdd:COG4618 250 LLLQSAVLGLGAYLVIQGEITPGAMIAASI---LMGRALapiEQAIGGWKQFVSARQAYRRLNELLAAVPA--EPERMPL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 277 DHLEGRVDFENVTFTY--RTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDH 354
Cdd:COG4618 325 PRPKGRLSVENLTVVPpgSKRP---ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDR 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 355 KYLHRVISLVSQEPVLFARSITDNISyGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMAR 434
Cdd:COG4618 402 EELGRHIGYLPQDVELFDGTIAENIA-RFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLAR 480
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217288354 435 ALVRNPPVLILDEATSALDAESEYLIQQAIhGNLQKH--TVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQ 509
Cdd:COG4618 481 ALYGDPRLVVLDEPNSNLDDEGEAALAAAI-RALKARgaTVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
7-258 |
3.79e-63 |
|
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: 208.49 E-value: 3.79e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 7 AVVIVCLLAIGSSFAAgIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVF 86
Cdd:cd18576 39 ALLLLGLFLLQAVFSF-FRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 87 LRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEE 166
Cdd:cd18576 118 LRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 167 AEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYS 246
Cdd:cd18576 198 IERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYG 277
|
250
....*....|..
gi 2217288354 247 GLMQGVGAAEKV 258
Cdd:cd18576 278 QLQKALGASERV 289
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
250-520 |
6.37e-63 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 216.25 E-value: 6.37e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 250 QGVGAAEKVFEFIDRQPTMVHDGSlAPDHLEGRVDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVN 329
Cdd:PRK11174 316 QAVGAAESLVTFLETPLAHPQQGE-KELASNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLN 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 330 ILENFYPLEGgRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQD 409
Cdd:PRK11174 395 ALLGFLPYQG-SLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQ 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 410 GYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLI 489
Cdd:PRK11174 474 GLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQI 553
|
250 260 270
....*....|....*....|....*....|.
gi 2217288354 490 VVLDKGRVVQQGTHQQLLAQGGLYAKLVQRQ 520
Cdd:PRK11174 554 WVMQDGQIVQQGDYAELSQAGGLFATLLAHR 584
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
281-502 |
8.43e-63 |
|
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: 205.03 E-value: 8.43e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 281 GRVDFENVTFTYRtrPHTQ-VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHR 359
Cdd:cd03244 1 GDIEFKNVSLRYR--PNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 360 VISLVSQEPVLFARSITDNISyglptvPF-----EMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMAR 434
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLD------PFgeysdEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217288354 435 ALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGT 502
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
281-501 |
1.02e-62 |
|
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: 204.75 E-value: 1.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 281 GRVDFENVTFTYRTRPHtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV 360
Cdd:cd03245 1 GRIEFRNVSFSYPNQEI-PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 361 ISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNP 440
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217288354 441 PVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQG 501
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
195-520 |
3.97e-61 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 211.22 E-value: 3.97e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 195 SGLTLLVvqvsILYYGGHLViSGQMTSGNLIAFIIyeFVLGDCMES---VGSVYSGLMQGVGAAEKVFEFIDRQPTMVHD 271
Cdd:PRK11160 255 NGLTVVL----MLWLAAGGV-GGNAQPGALIALFV--FAALAAFEAlmpVAGAFQHLGQVIASARRINEITEQKPEVTFP 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 272 GSLAPDHLEGRVDFENVTFTYRTRPHtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISA 351
Cdd:PRK11160 328 TTSTAAADQVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAD 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 352 YDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFImELQDGYSTETGEKGAQLSGGQKQRVA 431
Cdd:PRK11160 407 YSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLL-EDDKGLNAWLGEGGRQLSGGEQRRLG 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 432 MARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGG 511
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQG 565
|
....*....
gi 2217288354 512 LYAKLVQRQ 520
Cdd:PRK11160 566 RYYQLKQRL 574
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
200-509 |
2.38e-56 |
|
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: 197.57 E-value: 2.38e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 200 LVVQVSILYYGGHLVISGQMTSGNLIA-FIIYEFVLGDCMESVGsVYSGLMQGVGAAEKVFEFIDRQPtmvhdgsLAPDH 278
Cdd:TIGR01842 236 IVLQSLVLGLGAYLAIDGEITPGMMIAgSILVGRALAPIDGAIG-GWKQFSGARQAYKRLNELLANYP-------SRDPA 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 279 L-----EGRVDFENVTFTYrTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD 353
Cdd:TIGR01842 308 MplpepEGHLSVENVTIVP-PGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWD 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 354 HKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMA 433
Cdd:TIGR01842 387 RETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALA 466
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217288354 434 RALVRNPPVLILDEATSALDAESEYLIQQAI-HGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQ 509
Cdd:TIGR01842 467 RALYGDPKLVVLDEPNSNLDEEGEQALANAIkALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-480 |
2.83e-55 |
|
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: 194.50 E-value: 2.83e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 5 STAVVIVCLLAIGSSFAAGI-RGGIFTLIFARLNiRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNI 83
Cdd:TIGR02868 53 SVAAVAVRAFGIGRAVFRYLeRLVGHDAALRSLG-ALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVI 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 84 NVFLRNTVKVTGVVVFMFSLSWQLSLVT--------FMGFPIIMMVSNIYGKYYKRLSKEVQNALARA-SNTAEETIS-A 153
Cdd:TIGR02868 132 VPAGVALVVGAAAVAAIAVLSVPAALILaaglllagFVAPLVSLRAARAAEQALARLRGELAAQLTDAlDGAAELVASgA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 154 MKTVRSfanEEEEAEVYLRKLQQvyklNRKEAAAymyyvWGSGLTLLVVQVSI---LYYGGHLVISGQMTSGNLIAFIIY 230
Cdd:TIGR02868 212 LPAALA---QVEEADRELTRAER----RAAAATA-----LGAALTLLAAGLAVlgaLWAGGPAVADGRLAPVTLAVLVLL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 231 EFVLGDCMESVGSVYSGLMQGVGAAEKVFEFID---RQPTMVH--DGSLAPDHLegRVDFENVTFTYRTRPhtQVLQNVS 305
Cdd:TIGR02868 280 PLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDaagPVAEGSApaAGAVGLGKP--TLELRDLSAGYPGAP--PVLDGVS 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 306 FSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPT 385
Cdd:TIGR02868 356 LDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPD 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 386 VPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIH 465
Cdd:TIGR02868 436 ATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLL 515
|
490
....*....|....*
gi 2217288354 466 GNLQKHTVLIIAHRL 480
Cdd:TIGR02868 516 AALSGRTVVLITHHL 530
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
1-258 |
7.56e-55 |
|
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: 186.60 E-value: 7.56e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 1 MDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVS 80
Cdd:cd07346 35 LSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 81 QNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSF 160
Cdd:cd07346 115 SGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 161 ANEEEEAEVYLRKLQQVYKLNRKeAAAYMYYVWG-SGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCME 239
Cdd:cd07346 195 AAEEREIERFREANRDLRDANLR-AARLSALFSPlIGLLTALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQ 273
|
250
....*....|....*....
gi 2217288354 240 SVGSVYSGLMQGVGAAEKV 258
Cdd:cd07346 274 RLANLYNQLQQALASLERI 292
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
44-518 |
2.46e-54 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 198.71 E-value: 2.46e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 44 LFRSLVSQETSFFDE--NRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVK--VTGVVVFMFSlSWQLSLVTFMGFpIIM 119
Cdd:PTZ00265 905 LFENILYQEISFFDQdkHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLflVSMVMSFYFC-PIVAAVLTGTYF-IFM 982
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 120 MVSNIYGKYYKrlSKEVQNALARASNTA-----------------EETISAMKTVRSFANEE------EEAEVYLRKLQQ 176
Cdd:PTZ00265 983 RVFAIRARLTA--NKDVEKKEINQPGTVfaynsddeifkdpsfliQEAFYNMNTVIIYGLEDyfcnliEKAIDYSNKGQK 1060
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 177 vyklnRKEAAAYMyyVWG-SGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIiYEFVLgdcmesVGSVYSGLMQGVGAA 255
Cdd:PTZ00265 1061 -----RKTLVNSM--LWGfSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSL-FTFLF------TGSYAGKLMSLKGDS 1126
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 256 EKV-FEFIDRQPTMVH--------DGSLA---PDHLEGRVDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSG 323
Cdd:PTZ00265 1127 ENAkLSFEKYYPLIIRksnidvrdNGGIRiknKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSG 1206
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 324 KSSCVNILENFYPLE------------------------------------------------------GGRVLLDGKPI 349
Cdd:PTZ00265 1207 KSTVMSLLMRFYDLKndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfknSGKILLDGVDI 1286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 350 SAYDHKYLHRVISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQR 429
Cdd:PTZ00265 1287 CDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQR 1366
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 430 VAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQK--HTVLIIAHRLSTVEHAHLIVVLDK----GRVVQ-QGT 502
Cdd:PTZ00265 1367 IAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKadKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGT 1446
|
570
....*....|....*..
gi 2217288354 503 HQQLL-AQGGLYAKLVQ 518
Cdd:PTZ00265 1447 HEELLsVQDGVYKKYVK 1463
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
5-258 |
3.77e-54 |
|
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: 184.93 E-value: 3.77e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 5 STAVVIVCLLAIGSSFAAGI--RGGIFTLIFARLNI--RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVS 80
Cdd:cd18552 35 LEALLLVPLAIIGLFLLRGLasYLQTYLMAYVGQRVvrDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 81 QNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSF 160
Cdd:cd18552 115 SALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 161 ANEEEEAEVYLRKLQQVYKLNRKEAAAymyyvwgSGLTLLVVQV-------SILYYGGHLVISGQMTSGNLIAFIIYEFV 233
Cdd:cd18552 195 GAEDYEIKRFRKANERLRRLSMKIARA-------RALSSPLMELlgaiaiaLVLWYGGYQVISGELTPGEFISFITALLL 267
|
250 260
....*....|....*....|....*
gi 2217288354 234 LGDCMESVGSVYSGLMQGVGAAEKV 258
Cdd:cd18552 268 LYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
9-492 |
4.45e-53 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 194.86 E-value: 4.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 9 VIVCLLAIG---------SSFAAGIrggIFTLIFARLNIRLrnclFRSLVSQETSFFDENRTgdliSRLTSDTTMVSDLV 79
Cdd:PTZ00265 99 IIFSLVLIGifqfilsfiSSFCMDV---VTTKILKTLKLEF----LKSVFYQDGQFHDNNPG----SKLTSDLDFYLEQV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 80 SQNINV----FLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKrLSKevQNALARASNTA---EETIS 152
Cdd:PTZ00265 168 NAGIGTkfitIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKVK-INK--KTSLLYNNNTMsiiEEALV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 153 AMKTVRSFANEEEEAEVY--LRKLQQVY--KLNRKEA-----------AAYMYYVWgSGLTLLVVQVSILY----YGGHL 213
Cdd:PTZ00265 245 GIRTVVSYCGEKTILKKFnlSEKLYSKYilKANFMESlhigmingfilASYAFGFW-YGTRIIISDLSNQQpnndFHGGS 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 214 VISgqMTSGNLIAFIIYEFVLGDCMEsvgsvysgLMQGVGAAEKVFEFIDRQPTMVH--DGSLAPDhlEGRVDFENVTFT 291
Cdd:PTZ00265 324 VIS--ILLGVLISMFMLTIILPNITE--------YMKSLEATNSLYEIINRKPLVENndDGKKLKD--IKKIQFKNVRFH 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 292 YRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFY-PLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVL 370
Cdd:PTZ00265 392 YDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYdPTEGDIIINDSHNLKDINLKWWRSKIGVVSQDPLL 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 371 FARSITDNISYGL---------------------------------------------------------PTVPFEMVVE 393
Cdd:PTZ00265 472 FSNSIKNNIKYSLyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemrknyQTIKDSEVVD 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 394 AAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIH---GNLQK 470
Cdd:PTZ00265 552 VSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlkGNENR 631
|
570 580
....*....|....*....|..
gi 2217288354 471 HTVlIIAHRLSTVEHAHLIVVL 492
Cdd:PTZ00265 632 ITI-IIAHRLSTIRYANTIFVL 652
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
13-234 |
3.14e-52 |
|
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: 178.99 E-value: 3.14e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 13 LLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVK 92
Cdd:pfam00664 49 LLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLAT 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 93 VTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLR 172
Cdd:pfam00664 129 IVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDK 208
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217288354 173 KLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVL 234
Cdd:pfam00664 209 ALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQL 270
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
6-258 |
3.93e-52 |
|
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: 179.22 E-value: 3.93e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 6 TAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINV 85
Cdd:cd18575 37 RAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 86 FLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEE 165
Cdd:cd18575 117 ALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 166 EAEVYLRKLQQVYKLNRKEAAAYmyyvwgSGLTLLVVQ------VSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCME 239
Cdd:cd18575 197 ERQRFATAVEAAFAAALRRIRAR------ALLTALVIFlvfgaiVFVLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVG 270
|
250
....*....|....*....
gi 2217288354 240 SVGSVYSGLMQGVGAAEKV 258
Cdd:cd18575 271 ALSEVWGDLQRAAGAAERL 289
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
283-509 |
6.75e-48 |
|
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: 165.97 E-value: 6.75e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 362
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 LVSQEPV--LFARSITDNISYGlPT---VPFEMVVEAAQKA-NAHGfIMELQDgYSTetgekgAQLSGGQKQRVAMARAL 436
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFG-PEnlgLPREEIRERVEEAlELVG-LEHLAD-RPP------HELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217288354 437 VRNPPVLILDEATSALDAESEYLIQQAIHG-NLQKHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLAQ 509
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSD 224
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
2-258 |
1.72e-47 |
|
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: 167.22 E-value: 1.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 2 DQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARL--NI--RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSD 77
Cdd:cd18542 32 GGLRELLWLLALLILGVALLRGVFRYLQGYLAEKAsqKVayDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 78 LVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTV 157
Cdd:cd18542 112 FLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 158 RSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYV-WGSGLTLLVVqVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGD 236
Cdd:cd18542 192 KAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWpLMDFLSGLQI-VLVLWVGGYLVINGEITLGELVAFISYLWMLIW 270
|
250 260
....*....|....*....|..
gi 2217288354 237 CMESVGSVYSGLMQGVGAAEKV 258
Cdd:cd18542 271 PVRQLGRLINDMSRASASAERI 292
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
29-518 |
2.43e-47 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 177.86 E-value: 2.43e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 29 FTLIFARLNI--RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSwQ 106
Cdd:PLN03232 972 FWLISSSLHAakRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVS-T 1050
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 107 LSLVTFMgfPIIMMVSNIYgKYYKRLSKEVQ--NALARASNTAE--ETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNR 182
Cdd:PLN03232 1051 ISLWAIM--PLLILFYAAY-LYYQSTSREVRrlDSVTRSPIYAQfgEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTL 1127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 183 KEAAAYMYYV-----WGSGLTLLVVQVSILYYG---GHLVISGQMtsGNLIAFIIyefvlgdcmeSVGSVYSGLMQGVGA 254
Cdd:PLN03232 1128 ANTSSNRWLTirletLGGVMIWLTATFAVLRNGnaeNQAGFASTM--GLLLSYTL----------NITTLLSGVLRQASK 1195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 255 AEKVFEFIDRQPTMVHDGSLAPDHLE-----------GRVDFENVTFTYRtrPH-TQVLQNVSFSLSPGKVTALVGPSGS 322
Cdd:PLN03232 1196 AENSLNSVERVGNYIDLPSEATAIIEnnrpvsgwpsrGSIKFEDVHLRYR--PGlPPVLHGLSFFVSPSEKVGVVGRTGA 1273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 323 GKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISyglptvPFEM-----VVEAAQK 397
Cdd:PLN03232 1274 GKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNID------PFSEhndadLWEALER 1347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 398 ANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIA 477
Cdd:PLN03232 1348 AHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIA 1427
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2217288354 478 HRLSTVEHAHLIVVLDKGRVVQQGTHQQLLA-QGGLYAKLVQ 518
Cdd:PLN03232 1428 HRLNTIIDCDKILVLSSGQVLEYDSPQELLSrDTSAFFRMVH 1469
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
5-258 |
1.69e-46 |
|
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: 164.14 E-value: 1.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 5 STAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNIN 84
Cdd:cd18551 36 GGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 85 VFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEE 164
Cdd:cd18551 116 QLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 165 EEAEVYLRKLQQVYKLNRKEAAaymYYVWGSGLTLLVVQVS---ILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESV 241
Cdd:cd18551 196 RETKRGGEAAERLYRAGLKAAK---IEALIGPLMGLAVQLAllvVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQL 272
|
250
....*....|....*..
gi 2217288354 242 GSVYSGLMQGVGAAEKV 258
Cdd:cd18551 273 SSFFTQLQKALGALERI 289
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
285-478 |
3.70e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 160.75 E-value: 3.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 285 FENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRViSL 363
Cdd:COG4619 3 LEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPpPEWRRQV-AY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 364 VSQEPVLFARSITDNISYglptvPFEMVVEAAQKANAHGFIMELqdGYSTETGEKGA-QLSGGQKQRVAMARALVRNPPV 442
Cdd:COG4619 79 VPQEPALWGGTVRDNLPF-----PFQLRERKFDRERALELLERL--GLPPDILDKPVeRLSGGERQRLALIRALLLQPDV 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 2217288354 443 LILDEATSALDAESEYLIQQAIHGNLQKH--TVLIIAH 478
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEEgrAVLWVSH 189
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
13-513 |
4.92e-46 |
|
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: 173.98 E-value: 4.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 13 LLAIGSSFAAGIrGGIFTlifARlniRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVK 92
Cdd:TIGR00957 1020 FAVFGYSMAVSI-GGIQA---SR---VLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFN 1092
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 93 VTGVVVFMFsLSWQLSLVTFMGFPII-MMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFaNEEEEAEVyl 171
Cdd:TIGR00957 1093 VIGALIVIL-LATPIAAVIIPPLGLLyFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAF-EEQERFIH-- 1168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 172 rklQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVS---ILYYGGHLVISGQMTSGNLIAFII-YEFVLGDCMESVGSVYSG 247
Cdd:TIGR00957 1169 ---QSDLKVDENQKAYYPSIVANRWLAVRLECVGnciVLFAALFAVISRHSLSAGLVGLSVsYSLQVTFYLNWLVRMSSE 1245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 248 LMQGVGAAEKVFEF--IDRQPTMVHDGSLAPDHL--EGRVDFENvtFTYRTRPHTQ-VLQNVSFSLSPGKVTALVGPSGS 322
Cdd:TIGR00957 1246 METNIVAVERLKEYseTEKEAPWQIQETAPPSGWppRGRVEFRN--YCLRYREDLDlVLRHINVTIHGGEKVGIVGRTGA 1323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 323 GKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISyglptvPF-----EMVVEAAQK 397
Cdd:TIGR00957 1324 GKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLD------PFsqysdEEVWWALEL 1397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 398 ANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIA 477
Cdd:TIGR00957 1398 AHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIA 1477
|
490 500 510
....*....|....*....|....*....|....*.
gi 2217288354 478 HRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLY 513
Cdd:TIGR00957 1478 HRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
10-268 |
5.02e-46 |
|
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: 163.78 E-value: 5.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 10 IVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFD--ENRTGDLISRLTSDTTMVSDLVSQNINVFL 87
Cdd:cd18578 57 MFLVLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDdpENSTGALTSRLSTDASDVRGLVGDRLGLIL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 88 RNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEA 167
Cdd:cd18578 137 QAIVTLVAGLIIAFVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 168 EVYLRKLQQVYKLNRKEAAAYMyyvWGSGLT---LLVVQVSILYYGGHLVISGQMTSGNLiaFIIYEFVLGdCMESVGSV 244
Cdd:cd18578 217 EKYEEALEEPLKKGLRRALISG---LGFGLSqslTFFAYALAFWYGGRLVANGEYTFEQF--FIVFMALIF-GAQSAGQA 290
|
250 260
....*....|....*....|....*..
gi 2217288354 245 YSGL---MQGVGAAEKVFEFIDRQPTM 268
Cdd:cd18578 291 FSFApdiAKAKAAAARIFRLLDRKPEI 317
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
286-497 |
5.76e-46 |
|
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: 158.92 E-value: 5.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 286 ENVTFTY--RTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISL 363
Cdd:cd03246 4 ENVSFRYpgAEPP---VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 364 VSQEPVLFARSITDNIsyglptvpfemvveaaqkanahgfimelqdgystetgekgaqLSGGQKQRVAMARALVRNPPVL 443
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2217288354 444 ILDEATSALDAESEYLIQQAI-HGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRV 497
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIaALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
1-258 |
3.69e-45 |
|
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: 161.10 E-value: 3.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 1 MDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVS 80
Cdd:cd18577 43 LDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 81 QNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSF 160
Cdd:cd18577 123 EKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAF 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 161 ANEEEEAEVYLRKLQQVYKLNRKEAAAYMyyvWGSGLTLLVVQVSI---LYYGGHLVISGQMTSGNLIAFIIYEFVLGDC 237
Cdd:cd18577 203 GGEEKEIKRYSKALEKARKAGIKKGLVSG---LGLGLLFFIIFAMYalaFWYGSRLVRDGEISPGDVLTVFFAVLIGAFS 279
|
250 260
....*....|....*....|.
gi 2217288354 238 MESVGSVYSGLMQGVGAAEKV 258
Cdd:cd18577 280 LGQIAPNLQAFAKARAAAAKI 300
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
276-502 |
8.71e-45 |
|
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: 157.19 E-value: 8.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 276 PDHleGRVDFENVTFTYRtrPH-TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDH 354
Cdd:cd03369 2 PEH--GEIEVENLSVRYA--PDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 355 KYLHRVISLVSQEPVLFARSITDNISyglptvPFEMVVEAAqkanahgfIMElqdgySTETGEKGAQLSGGQKQRVAMAR 434
Cdd:cd03369 78 EDLRSSLTIIPQDPTLFSGTIRSNLD------PFDEYSDEE--------IYG-----ALRVSEGGLNLSQGQRQLLCLAR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217288354 435 ALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGT 502
Cdd:cd03369 139 ALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
225-509 |
2.31e-44 |
|
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: 164.31 E-value: 2.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 225 IAFIIYEFVLGDCMESVGSV---YSGLMQGVGAAEKVFEFIDR---QPTMVHDGSLAPDHLEGR---VDFENVTFTYRTR 295
Cdd:COG1123 194 TTVLLITHDLGVVAEIADRVvvmDDGRIVEDGPPEEILAAPQAlaaVPRLGAARGRAAPAAAAAeplLEVRNLSKRYPVR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 296 P--HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDH---KYLHRVISLVSQEPV- 369
Cdd:COG1123 274 GkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslRELRRRVQMVFQDPYs 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 370 -LFAR-SITDNISYGLptvpfeMVVEAAQKANAHGFIMELQD--GYSTETGEK-GAQLSGGQKQRVAMARALVRNPPVLI 444
Cdd:COG1123 354 sLNPRmTVGDIIAEPL------RLHGLLSRAERRERVAELLErvGLPPDLADRyPHELSGGQRQRVAIARALALEPKLLI 427
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217288354 445 LDEATSALDaeseYLIQQAIHGNLQK------HTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLAQ 509
Cdd:COG1123 428 LDEPTSALD----VSVQAQILNLLRDlqrelgLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
283-500 |
2.82e-44 |
|
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: 156.09 E-value: 2.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRT-RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAydhkyLHRVI 361
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 362 SLVSQEPVLFA-RSITDNISYGLptvpfEM--VVEAAQKANAHGFImelqdgysTETGEKGA------QLSGGQKQRVAM 432
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGL-----ELqgVPKAEARERAEELL--------ELVGLSGFenayphQLSGGMRQRVAL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217288354 433 ARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKH--TVLIIAHRLStvEHAHL---IVVLDK--GRVVQQ 500
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDID--EAVFLadrVVVLSArpGRIVAE 215
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
283-496 |
3.72e-44 |
|
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: 155.32 E-value: 3.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRPHTQ--VLQNVSFSLSPGKVTALVGPSGSGKSSCVN-ILENFYPLEGgrvlldgkpisaydHKYLHR 359
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEKLSG--------------SVSVPG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 360 VISLVSQEPVLFARSITDNISYGLPTVP--FEMVVEAAQ-KANahgfIMELQDGYSTETGEKGAQLSGGQKQRVAMARAL 436
Cdd:cd03250 67 SIAYVSQEPWIQNGTIRENILFGKPFDEerYEKVIKACAlEPD----LEILPDGDLTEIGEKGINLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217288354 437 VRNPPVLILDEATSALDAE-SEYLIQQAIHGNLQKH-TVLIIAHRLSTVEHAHLIVVLDKGR 496
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHvGRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
285-496 |
1.15e-43 |
|
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: 154.16 E-value: 1.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 285 FENVTFTYRTRPhTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLV 364
Cdd:cd03225 2 LKNLSFSYPDGA-RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 365 SQEP--VLFARSITDNISYGLP--TVPFEMVVEAAQKANAHGFIMELQDgYSTETgekgaqLSGGQKQRVAMARALVRNP 440
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGLEnlGLPEEEIEERVEEALELVGLEGLRD-RSPFT------LSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217288354 441 PVLILDEATSALDAESEYLIQQAIHG-NLQKHTVLIIAHRLSTV-EHAHLIVVLDKGR 496
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
283-509 |
1.25e-43 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 154.84 E-value: 1.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRtrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRvIS 362
Cdd:COG1131 1 IEVRGLTKRYG---DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR-IG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 LVSQEPVLFAR-SITDNIS-----YGLPTVPFEMVVEAAQKAnahgfiMELQDgystETGEKGAQLSGGQKQRVAMARAL 436
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRffarlYGLPRKEARERIDELLEL------FGLTD----AADRKVGTLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217288354 437 VRNPPVLILDEATSALDAESEYLIQQAIHG-NLQKHTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLAQ 509
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRElAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
35-229 |
1.41e-43 |
|
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: 156.55 E-value: 1.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 35 RLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDttmVSDLVS---QNINVFLRNTVKVTGVVVFMFSLSWQLSLVT 111
Cdd:cd18574 72 RVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTAD---VQEFKSsfkQCVSQGLRSVTQTVGCVVSLYLISPKLTLLL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 112 FMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYY 191
Cdd:cd18574 149 LVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEKLGLGIGIF 228
|
170 180 190
....*....|....*....|....*....|....*...
gi 2217288354 192 VWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFII 229
Cdd:cd18574 229 QGLSNLALNGIVLGVLYYGGSLVSRGELTAGDLMSFLV 266
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
29-518 |
5.05e-43 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 164.91 E-value: 5.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 29 FTLIFARLNI--RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSwQ 106
Cdd:PLN03130 975 YWLIMSSLYAakRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVS-T 1053
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 107 LSLVTFMgfPIIMMVSNIYgKYYKRLSKEVQ--NALARASNTAE--ETISAMKTVRSFANEEEEAEVYLRKLQQvyklNR 182
Cdd:PLN03130 1054 ISLWAIM--PLLVLFYGAY-LYYQSTAREVKrlDSITRSPVYAQfgEALNGLSTIRAYKAYDRMAEINGRSMDN----NI 1126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 183 KEAAAYMYYVWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKVFEFI 262
Cdd:PLN03130 1127 RFTLVNMSSNRWLAIRLETLGGLMIWLTASFAVMQNGRAENQAAFASTMGLLLSYALNITSLLTAVLRLASLAENSLNAV 1206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 263 DRQPTMVHDGSLAPDHLE-----------GRVDFENVTFTYRTR--PhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVN 329
Cdd:PLN03130 1207 ERVGTYIDLPSEAPLVIEnnrpppgwpssGSIKFEDVVLRYRPElpP---VLHGLSFEISPSEKVGIVGRTGAGKSSMLN 1283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 330 ILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISyglptvPFEM-----VVEAAQKANAHGFI 404
Cdd:PLN03130 1284 ALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLD------PFNEhndadLWESLERAHLKDVI 1357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 405 MELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVE 484
Cdd:PLN03130 1358 RRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTII 1437
|
490 500 510
....*....|....*....|....*....|....*
gi 2217288354 485 HAHLIVVLDKGRVVQQGTHQQLLA-QGGLYAKLVQ 518
Cdd:PLN03130 1438 DCDRILVLDAGRVVEFDTPENLLSnEGSAFSKMVQ 1472
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
283-506 |
2.06e-42 |
|
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: 151.18 E-value: 2.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENFYPLE--GGRVLLDGKPISAYDHK-- 355
Cdd:cd03260 1 IELRDLNVYYGDK---HALKDISLDIPKGEITALIGPSGCGKSTllrLLNRLNDLIPGApdEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 356 YLHRVISLVSQEPVLFARSITDNISYGLP-------TVPFEMVVEAAQKANAHGFIMELQDGYStetgekgaqLSGGQKQ 428
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGLRlhgiklkEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217288354 429 RVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQL 506
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
286-507 |
3.04e-42 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 151.73 E-value: 3.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 286 ENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVS 365
Cdd:COG1120 5 ENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 366 QEPVL-FARSITDNISYG-LPTVPF---------EMVVEAAQKANahgfIMELQDGYSTEtgekgaqLSGGQKQRVAMAR 434
Cdd:COG1120 82 QEPPApFGLTVRELVALGrYPHLGLfgrpsaedrEAVEEALERTG----LEHLADRPVDE-------LSGGERQRVLIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217288354 435 ALVRNPPVLILDEATSALDAESEYLIQQAIHG--NLQKHTVLIIAHRLS-TVEHAHLIVVLDKGRVVQQGTHQQLL 507
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
40-230 |
8.23e-42 |
|
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: 151.80 E-value: 8.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 40 LRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIM 119
Cdd:cd18541 75 LRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 120 MVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKeaaayMYYVWG----- 194
Cdd:cd18541 155 LLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLR-----LARVDAlffpl 229
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2217288354 195 ----SGLTLLVVqvsiLYYGGHLVISGQMTSGNLIAFIIY 230
Cdd:cd18541 230 igllIGLSFLIV----LWYGGRLVIRGTITLGDLVAFNSY 265
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
280-498 |
1.33e-41 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 150.24 E-value: 1.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 280 EGRVDFENVTFTYRTRP-HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylh 358
Cdd:COG1116 5 APALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 359 rvISLVSQEPVLFA-RSITDNISYGLptvpfEMVVEAAQKANAHgfIMELQDgystETGEKGA------QLSGGQKQRVA 431
Cdd:COG1116 82 --RGVVFQEPALLPwLTVLDNVALGL-----ELRGVPKAERRER--ARELLE----LVGLAGFedayphQLSGGMRQRVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217288354 432 MARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKH--TVLIIAH------RLSTVehahlIVVLDK--GRVV 498
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETgkTVLFVTHdvdeavFLADR-----VVVLSArpGRIV 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
283-501 |
5.12e-41 |
|
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: 147.65 E-value: 5.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRP-HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD---HKYLH 358
Cdd:cd03257 2 LEVKNLSVSFPTGGgSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 359 RVISLVSQEPVL---FARSITDNISYGLptVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARA 435
Cdd:cd03257 82 KEIQMVFQDPMSslnPRMTIGEQIAEPL--RIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 436 LVRNPPVLILDEATSALDAESEYLIQQAIHgNLQKH---TVLIIAHRLSTVEH-AHLIVVLDKGRVVQQG 501
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLK-KLQEElglTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
285-501 |
7.61e-41 |
|
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: 145.53 E-value: 7.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 285 FENVTFTYrtrPH--TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDhKYLHRVIS 362
Cdd:cd03247 3 INNVSFSY---PEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 LVSQEPVLFARSITDNIsyglptvpfemvveaaqkanahgfimelqdgystetgekGAQLSGGQKQRVAMARALVRNPPV 442
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217288354 443 LILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQG 501
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
301-450 |
2.04e-40 |
|
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: 143.17 E-value: 2.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 301 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFAR-SITDNI 379
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217288354 380 SYGLptvPFEMVVEAAQKANAHGFI--MELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATS 450
Cdd:pfam00005 81 RLGL---LLKGLSKREKDARAEEALekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
285-496 |
6.32e-40 |
|
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: 142.38 E-value: 6.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 285 FENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLV 364
Cdd:cd00267 2 IENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 365 SQepvlfarsitdnisyglptvpfemvveaaqkanahgfimelqdgystetgekgaqLSGGQKQRVAMARALVRNPPVLI 444
Cdd:cd00267 79 PQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2217288354 445 LDEATSALDAESEYLIQQAIHGNLQKH-TVLIIAHRLSTVEHA-HLIVVLDKGR 496
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEEGrTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
283-501 |
6.47e-40 |
|
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: 144.20 E-value: 6.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRtrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKylhRVI 361
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPpER---RNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 362 SLVSQEPVLFA-RSITDNISYGLPtvpfEMVVEAAQKANAHGFIMELQdGYSTETGEKGAQLSGGQKQRVAMARALVRNP 440
Cdd:cd03259 75 GMVFQDYALFPhLTVAENIAFGLK----LRGVPKAEIRARVRELLELV-GLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217288354 441 PVLILDEATSALDAESEYLIQ---QAIHGNLQKhTVLIIAHRLS-TVEHAHLIVVLDKGRVVQQG 501
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELReelKELQRELGI-TTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
283-509 |
1.28e-39 |
|
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: 143.88 E-value: 1.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRP-HTQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILEnfYPLEGgRVLLDGKPISAYDHKYL- 357
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTlirCINGLE--RPTSG-SVLVDGTDLTLLSGKELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 358 --HRVISLVSQEPVLF-ARSITDNISYglptvPFEmvVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAM 432
Cdd:cd03258 79 kaRRRIGMIFQHFNLLsSRTVFENVAL-----PLE--IAGVPKAEIEERVLELLElvGLEDKADAYPAQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 433 ARALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQKH---TVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLA 508
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLR-DINRElglTIVLITHEMEVVkRICDRVAVMEKGEVVEEGTVEEVFA 230
|
.
gi 2217288354 509 Q 509
Cdd:cd03258 231 N 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
283-509 |
1.69e-39 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 150.82 E-value: 1.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRPHTqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEG---GRVLLDGKPISAYDHKYLHR 359
Cdd:COG1123 5 LEVRDLSVRYPGGDVP-AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 360 VISLVSQEP--VLFARSITDNISYGL--PTVPFEMVVEAAQKANAHGFIMELQDGYStetgekgAQLSGGQKQRVAMARA 435
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEALenLGLSRAEARARVLELLEAVGLERRLDRYP-------HQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217288354 436 LVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKH--TVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLAQ 509
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
6-230 |
4.83e-39 |
|
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: 144.45 E-value: 4.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 6 TAVVIVCLLAIGSSFAAGIRGGIFTLIFARL--NI--RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQ 81
Cdd:cd18544 38 QGLLLLALLYLGLLLLSFLLQYLQTYLLQKLgqRIiyDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 82 NINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFA 161
Cdd:cd18544 118 GLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFN 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217288354 162 NEEEEAEVYLRKLQQVYKLNRKEaaAYMYYVWGSGLTLL--VVQVSILYYGGHLVISGQMTSGNLIAFIIY 230
Cdd:cd18544 198 REKREFEEFDEINQEYRKANLKS--IKLFALFRPLVELLssLALALVLWYGGGQVLSGAVTLGVLYAFIQY 266
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
286-511 |
5.60e-39 |
|
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: 142.69 E-value: 5.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 286 ENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRvISLVS 365
Cdd:COG4555 5 ENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ-IGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 366 QEPVLFAR-SITDNISY-----GLPTVPFEMVVEAAQKAnahgfiMELQDGYSTETGEkgaqLSGGQKQRVAMARALVRN 439
Cdd:COG4555 81 DERGLYDRlTVRENIRYfaelyGLFDEELKKRIEELIEL------LGLEEFLDRRVGE----LSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217288354 440 PPVLILDEATSALDAESEYLIQQAI--HGNlQKHTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLAQGG 511
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILraLKK-EGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
285-509 |
1.34e-38 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 141.05 E-value: 1.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 285 FENVTFTYRTRPhtqvlQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKylhRVISL 363
Cdd:COG3840 4 LDDLTYRYGDFP-----LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPpAE---RPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 364 VSQEPVLFAR-SITDNISYGL-----PTVP-FEMVVEAAQKANAHGFImelqdgystetGEKGAQLSGGQKQRVAMARAL 436
Cdd:COG3840 76 LFQENNLFPHlTVAQNIGLGLrpglkLTAEqRAQVEQALERVGLAGLL-----------DRLPGQLSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217288354 437 VRNPPVLILDEATSALD----AESEYLIQQaIHGNLQKhTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLAQ 509
Cdd:COG3840 145 VRKRPILLLDEPFSALDpalrQEMLDLVDE-LCRERGL-TVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDG 220
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
283-502 |
1.38e-38 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 144.47 E-value: 1.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPIS---AYdhkylHR 359
Cdd:COG3842 6 LELENVSKRYGD---VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTglpPE-----KR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 360 VISLVSQEPVLFA-RSITDNISYGLptvpfEM--VVEAAQKANAHGFI--MELqDGYStetGEKGAQLSGGQKQRVAMAR 434
Cdd:COG3842 78 NVGMVFQDYALFPhLTVAENVAFGL-----RMrgVPKAEIRARVAELLelVGL-EGLA---DRYPHQLSGGQQQRVALAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217288354 435 ALVRNPPVLILDEATSALDAESEYLIQQAIhGNLQKH---TVLIIAHRLS---TVehAHLIVVLDKGRVVQQGT 502
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAKLREEMREEL-RRLQRElgiTFIYVTHDQEealAL--ADRIAVMNDGRIEQVGT 219
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
13-230 |
2.48e-38 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 142.26 E-value: 2.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 13 LLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVK 92
Cdd:cd18563 51 GAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILM 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 93 VTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLR 172
Cdd:cd18563 131 IIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDE 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 173 KLQQVYKLNRKeaAAYMYYVWGSGLTLLVV--QVSILYYGGHLVISGQMTSGNLIAFIIY 230
Cdd:cd18563 211 ANQELLDANIR--AEKLWATFFPLLTFLTSlgTLIVWYFGGRQVLSGTMTLGTLVAFLSY 268
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
283-497 |
6.26e-38 |
|
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: 138.78 E-value: 6.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRT-RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHK----YL 357
Cdd:cd03255 1 IELKNLSKTYGGgGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaaFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 358 HRVISLVSQEPVLFAR-SITDNISygLPtvpfeMVVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAMAR 434
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVE--LP-----LLLAGVPKKERRERAEELLErvGLGDRLNHYPSELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217288354 435 ALVRNPPVLILDEATSALDAESEYLIQQAIHG--NLQKHTVLIIAHRLSTVEHAHLIVVLDKGRV 497
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
286-508 |
2.31e-37 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 138.40 E-value: 2.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 286 ENVTFTYRTRPH-TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLV 364
Cdd:COG1124 5 RNLSVSYGQGGRrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 365 SQEP--VLFAR-SITDNIS-----YGLPTVPfEMVVEAAQKanahgfiMELQDGYSTEtgeKGAQLSGGQKQRVAMARAL 436
Cdd:COG1124 85 FQDPyaSLHPRhTVDRILAeplriHGLPDRE-ERIAELLEQ-------VGLPPSFLDR---YPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 437 VRNPPVLILDEATSALDAeseylIQQAIHGNLQKH-------TVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLA 508
Cdd:COG1124 154 ILEPELLLLDEPTSALDV-----SVQAEILNLLKDlreerglTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
283-502 |
1.63e-36 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 138.67 E-value: 1.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRPHT-QVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENfyPLEGgRVLLDGKPISAYDHKYLH 358
Cdd:COG1135 2 IELENLSKTFPTKGGPvTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLER--PTSG-SVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 359 RV---ISLVSQEPVLF-ARSITDNISYglptvPFEMV----VEAAQKANahgfimELQD--GYStetgEKG----AQLSG 424
Cdd:COG1135 79 AArrkIGMIFQHFNLLsSRTVAENVAL-----PLEIAgvpkAEIRKRVA------ELLElvGLS----DKAdaypSQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 425 GQKQRVAMARALVRNPPVLILDEATSALDAESEY----LIQQaIHGNLQKhTVLIIAHRLSTVEH-AHLIVVLDKGRVVQ 499
Cdd:COG1135 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTRsildLLKD-INRELGL-TIVLITHEMDVVRRiCDRVAVLENGRIVE 221
|
...
gi 2217288354 500 QGT 502
Cdd:COG1135 222 QGP 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
286-497 |
4.82e-36 |
|
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: 132.14 E-value: 4.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 286 ENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRvISLVS 365
Cdd:cd03230 4 RNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR-IGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 366 QEPVLfarsitdnisyglptvpfemvveaaqkanahgfimelqdgYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLIL 445
Cdd:cd03230 80 EEPSL----------------------------------------YENLTVRENLKLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2217288354 446 DEATSALDAESEYLIQQAIHG-NLQKHTVLIIAHRLSTVEH-AHLIVVLDKGRV 497
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
286-501 |
8.12e-36 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 131.79 E-value: 8.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 286 ENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVS 365
Cdd:cd03214 3 ENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 366 QepvlfarsitdnisyglptvpfemVVEAAQKAN-AHGFIMElqdgystetgekgaqLSGGQKQRVAMARALVRNPPVLI 444
Cdd:cd03214 80 Q------------------------ALELLGLAHlADRPFNE---------------LSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217288354 445 LDEATSALDAESEYLIQQAIHgNLQKH---TVLIIAHRLS-TVEHAHLIVVLDKGRVVQQG 501
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLR-RLARErgkTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
6-230 |
1.12e-35 |
|
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: 134.90 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 6 TAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINV 85
Cdd:cd18545 41 IIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLIN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 86 FLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEE 165
Cdd:cd18545 121 LIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDE 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217288354 166 EAEVYLRKLQQVYKLNRKeAAAYMYYVWGS-GLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIY 230
Cdd:cd18545 201 NEEIFDELNRENRKANMR-AVRLNALFWPLvELISALGTALVYWYGGKLVLGGAITVGVLVAFIGY 265
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
283-496 |
1.43e-35 |
|
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: 131.16 E-value: 1.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD--HKYLHRV 360
Cdd:cd03229 1 LELKNVSKRY---GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 361 ISLVSQEPVLFAR-SITDNISYGLptvpfemvveaaqkanahgfimelqdgystetgekgaqlSGGQKQRVAMARALVRN 439
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALGL---------------------------------------SGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217288354 440 PPVLILDEATSALDAESEYLIQ---QAIHGNLQKhTVLIIAHRLSTVEH-AHLIVVLDKGR 496
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRallKSLQAQLGI-TVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
283-500 |
2.15e-35 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 132.09 E-value: 2.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRPH-TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILenfypleG-------GRVLLDGKPISAYDH 354
Cdd:COG1136 5 LELRNLTKSYGTGEGeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIL-------GgldrptsGEVLIDGQDISSLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 355 KYLHRV----ISLVSQEPVLFAR-SITDNISygLPtvpfeMVVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQK 427
Cdd:COG1136 78 RELARLrrrhIGFVFQFFNLLPElTALENVA--LP-----LLLAGVSRKERRERARELLErvGLGDRLDHRPSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217288354 428 QRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHG--NLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQ 500
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
283-509 |
5.06e-35 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 131.65 E-value: 5.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRtrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILEnfyPLEGGRVLLDGKPISAyDHKYLHR 359
Cdd:COG1126 2 IEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTllrCINLLE---EPDSGTITVDGEDLTD-SKKDINK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 360 V---ISLVSQEPVLFA-RSITDNISYGLptvpfeMVV------EAAQKAnahgfiMEL---------QDGYStetgekgA 420
Cdd:COG1126 75 LrrkVGMVFQQFNLFPhLTVLENVTLAP------IKVkkmskaEAEERA------MELlervgladkADAYP-------A 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 421 QLSGGQKQRVAMARALVRNPPVLILDEATSALDAE--SEYL--IQQAIHGNLqkhTVLIIAHRLS---TVehAHLIVVLD 493
Cdd:COG1126 136 QLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPElvGEVLdvMRDLAKEGM---TMVVVTHEMGfarEV--ADRVVFMD 210
|
250
....*....|....*.
gi 2217288354 494 KGRVVQQGTHQQLLAQ 509
Cdd:COG1126 211 GGRIVEEGPPEEFFEN 226
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
283-497 |
5.42e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 131.75 E-value: 5.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylhrvIS 362
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR-----IG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 LVSQEpVLFARS--IT--DNISYGL-PTVPF---------EMVVEAAQKANAHGF----ImelqdgystetgekgAQLSG 424
Cdd:COG1121 79 YVPQR-AEVDWDfpITvrDVVLMGRyGRRGLfrrpsradrEAVDEALERVGLEDLadrpI---------------GELSG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217288354 425 GQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQKH--TVLIIAHRLSTV-EHAHLIVVLDKGRV 497
Cdd:COG1121 143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLR-ELRREgkTILVVTHDLGAVrEYFDRVLLLNRGLV 217
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1-230 |
8.21e-35 |
|
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: 133.02 E-value: 8.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 1 MDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVS 80
Cdd:cd18564 50 LALLLLAAAALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 81 QNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSF 160
Cdd:cd18564 130 SGVLPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAF 209
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 161 ANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIY 230
Cdd:cd18564 210 GREEHEERRFARENRKSLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAY 279
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
1-258 |
4.58e-33 |
|
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: 127.90 E-value: 4.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 1 MDQFSTAVVIVCLLAIGSSfaagirggIFTLIFARLNI--------RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDT 72
Cdd:cd18547 41 FSGLLRILLLLLGLYLLSA--------LFSYLQNRLMArvsqrtvyDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 73 TMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETIS 152
Cdd:cd18547 113 DNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMIS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 153 AMKTVRSFANEEEEAEVYLRKLQQVYKLNRKeaaAYMYyvwgSGLTL-------LVVQVSILYYGGHLVISGQMTSGNLI 225
Cdd:cd18547 193 GQKVVKAFNREEEAIEEFDEINEELYKASFK---AQFY----SGLLMpimnfinNLGYVLVAVVGGLLVINGALTVGVIQ 265
|
250 260 270
....*....|....*....|....*....|...
gi 2217288354 226 AFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 258
Cdd:cd18547 266 AFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
283-508 |
4.80e-33 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 126.26 E-value: 4.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRPhtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 362
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 LVSQEPVLFA-RSITDNISyglpTVP-FEMVVEAAQKANAHGFI-------MELQDGYStetgekgAQLSGGQKQRVAMA 433
Cdd:cd03295 79 YVIQQIGLFPhMTVEENIA----LVPkLLKWPKEKIRERADELLalvgldpAEFADRYP-------HELSGGQQQRVGVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 434 RALVRNPPVLILDEATSALDA------ESEYL-IQQAIHgnlqkHTVLIIAHRL-STVEHAHLIVVLDKGRVVQQGTHQQ 505
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPitrdqlQEEFKrLQQELG-----KTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDE 222
|
...
gi 2217288354 506 LLA 508
Cdd:cd03295 223 ILR 225
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
283-508 |
5.09e-33 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 126.08 E-value: 5.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV-- 360
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 361 -ISLVSQEPVLF-ARSITDNISYGL---PTVPFEMVVE-AAQKANAHGfIMELQDGYStetgekgAQLSGGQKQRVAMAR 434
Cdd:cd03261 78 rMGMLFQSGALFdSLTVFENVAFPLrehTRLSEEEIREiVLEKLEAVG-LRGAEDLYP-------AELSGGMKKRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217288354 435 ALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQKH---TVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLA 508
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIASGVIDDLIR-SLKKElglTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
286-509 |
5.17e-33 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 129.11 E-value: 5.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 286 ENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILenfYPLE---GGRVLLDGKPISAyDHKYLHRVIS 362
Cdd:COG1118 6 RNISKRF---GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRII---AGLEtpdSGRIVLNGRDLFT-NLPPRERRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 LVSQEPVLFaR--SITDNISYGLPTVPfemVVEAAQKANAHGFIMELQ-DGYStetGEKGAQLSGGQKQRVAMARALVRN 439
Cdd:COG1118 79 FVFQHYALF-PhmTVAENIAFGLRVRP---PSKAEIRARVEELLELVQlEGLA---DRYPSQLSGGQRQRVALARALAVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217288354 440 PPVLILDEATSALDAESEYLIQQ---AIHGNLQkHTVLIIAH-RLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQ 509
Cdd:COG1118 152 PEVLLLDEPFGALDAKVRKELRRwlrRLHDELG-GTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
283-507 |
5.32e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 127.03 E-value: 5.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRpHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 362
Cdd:PRK13632 8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 LVSQEP--VLFARSITDNISYGLPTV---PFEM---VVEAAQKANAHGFImelqdgystetgEKGAQ-LSGGQKQRVAMA 433
Cdd:PRK13632 87 IIFQNPdnQFIGATVEDDIAFGLENKkvpPKKMkdiIDDLAKKVGMEDYL------------DKEPQnLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217288354 434 RALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQKH---TVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLL 507
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMV-DLRKTrkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
301-509 |
6.76e-33 |
|
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: 126.60 E-value: 6.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 301 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV----ISLVSQEPVLFA-RSI 375
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLPhRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 376 TDNISYGLPT--VP----FEMVVEAAQKANAHGFIMELQDgystetgekgaQLSGGQKQRVAMARALVRNPPVLILDEAT 449
Cdd:cd03294 120 LENVAFGLEVqgVPraerEERAAEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217288354 450 SALDA------ESEYLiqqAIHGNLQKhTVLIIAHRLS-TVEHAHLIVVLDKGRVVQQGTHQQLLAQ 509
Cdd:cd03294 189 SALDPlirremQDELL---RLQAELQK-TIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
11-230 |
1.74e-32 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 126.06 E-value: 1.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 11 VCLLAIGSsFAAGIRGGIFTLIFARLNIR--------LRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQN 82
Cdd:cd18550 38 LVLLALGM-VAVAVASALLGVVQTYLSARigqgvmydLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 83 INVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEET--ISAMKTVRSF 160
Cdd:cd18550 117 LTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETlsVSGALLVKLF 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 161 ANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIY 230
Cdd:cd18550 197 GREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPALVYWVGGLLVIGGGLTIGTLVAFTAL 266
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
283-510 |
1.86e-32 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 125.24 E-value: 1.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYrTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDG-KPISAYDHKYLHRVI 361
Cdd:TIGR04520 1 IEVENVSFSY-PESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 362 SLVSQEP--VLFARSITDNISYGLPT--VPFEMVVEAAQKANAhgfIMELQDGYSTETgekgAQLSGGQKQRVAMARALV 437
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLENlgVPREEMRKRVDEALK---LVGMEDFRDREP----HLLSGGQKQRVAIAGVLA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217288354 438 RNPPVLILDEATSALDAESEYLIQQAIHgNLQKH---TVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQG 510
Cdd:TIGR04520 153 MRPDIIILDEATSMLDPKGRKEVLETIR-KLNKEegiTVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQV 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
273-480 |
2.22e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 124.76 E-value: 2.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 273 SLAPDHLEGRVDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENFYP---LEgGRVLLDG 346
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDK---QALKDINLDIPENKVTALIGPSGCGKSTllrCLNRMNDLIPgarVE-GEILLDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 347 KPIsaYDHKY----LHRVISLVSQEPVLFARSITDNISYGL-------PTVPFEMVVEAAQKANahgfimeLQDgystET 415
Cdd:COG1117 78 EDI--YDPDVdvveLRRRVGMVFQKPNPFPKSIYDNVAYGLrlhgiksKSELDEIVEESLRKAA-------LWD----EV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217288354 416 ----GEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAES----EYLIQQaihgnL-QKHTVLIIAHRL 480
Cdd:COG1117 145 kdrlKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIStakiEELILE-----LkKDYTIVIVTHNM 213
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
6-258 |
3.68e-32 |
|
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: 125.29 E-value: 3.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 6 TAVVIVCLLAIGSSFAAGIR---GGIFTLifaRLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQn 82
Cdd:cd18543 40 PLVLLLLALGVAEAVLSFLRrylAGRLSL---GVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAF- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 83 INVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFAN 162
Cdd:cd18543 116 GPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 163 EEEEAEVYLRKLQQVYKLNRKeaAAYMYYVWGSGLTLL--VVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMES 240
Cdd:cd18543 196 ERRELDRFEAAARRLRATRLR--AARLRARFWPLLEALpeLGLAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRM 273
|
250
....*....|....*...
gi 2217288354 241 VGSVYSGLMQGVGAAEKV 258
Cdd:cd18543 274 LGWLLAMAQRARAAAERV 291
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
283-506 |
5.03e-32 |
|
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: 123.12 E-value: 5.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKylhRVI 361
Cdd:cd03300 1 IELENVSKFY---GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPpHK---RPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 362 SLVSQEPVLFAR-SITDNISYGLPTvpfEMVVEAAQKANAHGFIMELQ-DGYStetGEKGAQLSGGQKQRVAMARALVRN 439
Cdd:cd03300 75 NTVFQNYALFPHlTVFENIAFGLRL---KKLPKAEIKERVAEALDLVQlEGYA---NRKPSQLSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217288354 440 PPVLILDEATSALDAESEYLIQQAIHgNLQKH---TVLIIAHRLS---TVehAHLIVVLDKGRVVQQGTHQQL 506
Cdd:cd03300 149 PKVLLLDEPLGALDLKLRKDMQLELK-RLQKElgiTFVFVTHDQEealTM--SDRIAVMNKGKIQQIGTPEEI 218
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
281-506 |
6.63e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 125.96 E-value: 6.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 281 GRVDFENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylHRV 360
Cdd:COG3839 2 ASLELENVSKSYGG---VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 361 ISLVSQEPVLF-ARSITDNISYGLptvpfEM-----------VVEAAQkanahgfIMELQDgYStetGEKGAQLSGGQKQ 428
Cdd:COG3839 77 IAMVFQSYALYpHMTVYENIAFPL-----KLrkvpkaeidrrVREAAE-------LLGLED-LL---DRKPKQLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 429 RVAMARALVRNPPVLILDEATSALDAE------SEylIQQaIHGNLqKHTVLIiahrlstVEH--------AHLIVVLDK 494
Cdd:COG3839 141 RVALGRALVREPKVFLLDEPLSNLDAKlrvemrAE--IKR-LHRRL-GTTTIY-------VTHdqveamtlADRIAVMND 209
|
250
....*....|..
gi 2217288354 495 GRVVQQGTHQQL 506
Cdd:COG3839 210 GRIQQVGTPEEL 221
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
285-506 |
8.41e-32 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 122.86 E-value: 8.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 285 FENVTFTYRTrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILEnfyPLEGGRVLLDGKPISAYDHKYLHRV- 360
Cdd:COG3638 5 LRNLSKRYPG--GTPALDDVSLEIERGEFVALIGPSGAGKSTllrCLNGLV---EPTSGEILVDGQDVTALRGRALRRLr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 361 --ISLVSQEPVLFAR-SITDNISYG-LPTVPF----EMVVEAAQKANAHGFI--MELQDgystETGEKGAQLSGGQKQRV 430
Cdd:COG3638 80 rrIGMIFQQFNLVPRlSVLTNVLAGrLGRTSTwrslLGLFPPEDRERALEALerVGLAD----KAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 431 AMARALVRNPPVLILDEATSALDAES-----EYLIQQAIHGNLqkhTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQ 504
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTarqvmDLLRRIAREDGI---TVVVNLHQVDLArRYADRIIGLRDGRVVFDGPPA 232
|
..
gi 2217288354 505 QL 506
Cdd:COG3638 233 EL 234
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
40-230 |
1.27e-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: 123.71 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 40 LRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIM 119
Cdd:cd18549 77 MRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALLPLMI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 120 MVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQvYKLNRKEAAAYM-YYVWGSGLT 198
Cdd:cd18549 157 IFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDR-FLESKKKAYKAMaYFFSGMNFF 235
|
170 180 190
....*....|....*....|....*....|..
gi 2217288354 199 LLVVQVSILYYGGHLVISGQMTSGNLIAFIIY 230
Cdd:cd18549 236 TNLLNLVVLVAGGYFIIKGEITLGDLVAFLLY 267
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
285-501 |
1.36e-31 |
|
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: 121.49 E-value: 1.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 285 FENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylhrvISLV 364
Cdd:cd03235 2 VEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR-----IGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 365 SQEPVL---FARSITDNISYGL-PTVPFEMVVEAAQKANahgfIMELQDgySTETGEKG----AQLSGGQKQRVAMARAL 436
Cdd:cd03235 74 PQRRSIdrdFPISVRDVVLMGLyGHKGLFRRLSKADKAK----VDEALE--RVGLSELAdrqiGELSGGQQQRVLLARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217288354 437 VRNPPVLILDEATSALDAESeyliQQAIHGNLQK-----HTVLIIAHRLSTV-EHAHLIVVLDKgRVVQQG 501
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKT----QEDIYELLRElrregMTILVVTHDLGLVlEYFDRVLLLNR-TVVASG 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
298-508 |
1.54e-31 |
|
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: 121.39 E-value: 1.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 298 TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEPVLFAR-SI 375
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPpHERARAGIGYVPEGRRIFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 376 TDNIsyglptvpfEMVVEAAQKANAHgFIME--------LQDGYSTetgeKGAQLSGGQKQRVAMARALVRNPPVLILDE 447
Cdd:cd03224 93 EENL---------LLGAYARRRAKRK-ARLErvyelfprLKERRKQ----LAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217288354 448 ATSALdaeSEYLIQQ---AIHG-NLQKHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLA 508
Cdd:cd03224 159 PSEGL---APKIVEEifeAIRElRDEGVTILLVEQNARFAlEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
299-497 |
2.28e-31 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 120.71 E-value: 2.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 299 QVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENFyplEGGRVLLDGKPISAyDHKYLHRV---ISLVSQEPVLFA 372
Cdd:cd03262 14 HVLKGIDLTVKKGEVVVIIGPSGSGKSTllrCINLLEEP---DSGTIIIDGLKLTD-DKKNINELrqkVGMVFQQFNLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 373 -RSITDNISYGLPTVPFEMVVEAAQKAnahgfiMELQD--GYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEAT 449
Cdd:cd03262 90 hLTVLENITLAPIKVKGMSKAEAEERA------LELLEkvGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2217288354 450 SALDAE--SEYL--IQQAIHgnlQKHTVLIIAHRLSTVEH-AHLIVVLDKGRV 497
Cdd:cd03262 164 SALDPElvGEVLdvMKDLAE---EGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
286-478 |
2.46e-31 |
|
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: 120.44 E-value: 2.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 286 ENVTFTYRtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAydhKYLHRVISLVS 365
Cdd:cd03226 3 ENISFSYK--KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 366 QEP--VLFARSITDNISYGLPTVPfemvvEAAQKANAhgfIMELQDGYSTEtgEKGAQ-LSGGQKQRVAMARALVRNPPV 442
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKELD-----AGNEQAET---VLKDLDLYALK--ERHPLsLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 2217288354 443 LILDEATSALDAESEYLIQQAI-HGNLQKHTVLIIAH 478
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIrELAAQGKAVIVITH 184
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
282-493 |
2.83e-31 |
|
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: 120.28 E-value: 2.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 282 RVDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYlHRVI 361
Cdd:COG4133 2 MLEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 362 SLVSQEPVLFAR-SITDNIS-----YGLPtVPFEMVVEAAQKANahgfIMELQDgystetgEKGAQLSGGQKQRVAMARA 435
Cdd:COG4133 78 AYLGHADGLKPElTVRENLRfwaalYGLR-ADREAIDEALEAVG----LAGLAD-------LPVRQLSAGQKRRVALARL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217288354 436 LVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIA-HRLSTVEHAHLIVVLD 493
Cdd:COG4133 146 LLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDLGD 204
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
283-508 |
4.00e-31 |
|
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: 120.85 E-value: 4.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV-- 360
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 361 -ISLVSQEPVLFArSIT--DNISYGL---PTVPFEMVVEAAqkanahgfIMELQdgystETGEKGA------QLSGGQKQ 428
Cdd:COG1127 83 rIGMLFQGGALFD-SLTvfENVAFPLrehTDLSEAEIRELV--------LEKLE-----LVGLPGAadkmpsELSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 429 RVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQKH---TVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQ 504
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPITSAVIDELIR-ELRDElglTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPE 227
|
....
gi 2217288354 505 QLLA 508
Cdd:COG1127 228 ELLA 231
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
283-498 |
5.46e-31 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 119.77 E-value: 5.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRPhtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHK---YLHR 359
Cdd:COG2884 2 IRFENVSKRYPGGR--EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReipYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 360 VISLVSQE-PVLFARSITDNISygLPtvpfeMVVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAMARAL 436
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVA--LP-----LRVTGKSRKEIRRRVREVLDlvGLSDKAKALPHELSGGEQQRVAIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217288354 437 VRNPPVLILDEATSALDAESEYLIQQAIHG-NLQKHTVLIIAHRLSTVEHA-HLIVVLDKGRVV 498
Cdd:COG2884 153 VNRPELLLADEPTGNLDPETSWEIMELLEEiNRRGTTVLIATHDLELVDRMpKRVLELEDGRLV 216
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
300-502 |
1.03e-30 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 119.46 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 300 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEPVLFAR-SITD 377
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPpHEIARLGIGRTFQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 378 NI---------SYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEkgaqLSGGQKQRVAMARALVRNPPVLILDEA 448
Cdd:cd03219 95 NVmvaaqartgSGLLLARARREEREARERAEELLERVGLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217288354 449 TSAL-DAESEYLIQ--QAIhgNLQKHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGT 502
Cdd:cd03219 171 AAGLnPEETEELAEliREL--RERGITVLLVEHDMDVVmSLADRVTVLDQGRVIAEGT 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
303-501 |
2.44e-30 |
|
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: 117.78 E-value: 2.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 303 NVSFSLsPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDG-------KPISAYDHKylhRVISLVSQEPVLFAR-S 374
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKINLPPQQ---RKIGLVFQQYALFPHlN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 375 ITDNISYGLPTV-PFEMVVEAAQKANAHGfIMELQDGYStetgekgAQLSGGQKQRVAMARALVRNPPVLILDEATSALD 453
Cdd:cd03297 92 VRENLAFGLKRKrNREDRISVDELLDLLG-LDHLLNRYP-------AQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2217288354 454 AESEYLIQ---QAIHGNLQKHtVLIIAHRLSTVEH-AHLIVVLDKGRVVQQG 501
Cdd:cd03297 164 RALRLQLLpelKQIKKNLNIP-VIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
283-501 |
2.63e-30 |
|
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: 117.59 E-value: 2.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRPHTQVLQnvsfsLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylHRVIS 362
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLT-----FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 LVSQEPVLFAR-SITDNISYGL-PTVPFEMVVEAAQKANAHgfimelQDGYSTETGEKGAQLSGGQKQRVAMARALVRNP 440
Cdd:cd03298 74 MLFQENNLFAHlTVEQNVGLGLsPGLKLTAEDRQAIEVALA------RVGLAGLEKRLPGELSGGERQRVALARVLVRDK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217288354 441 PVLILDEATSALDAESEYLIQQAIHG--NLQKHTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQG 501
Cdd:cd03298 148 PVLLLDEPFAALDPALRAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
283-526 |
3.77e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 119.09 E-value: 3.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRT-RPHTqvLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVI 361
Cdd:PRK13648 8 IVFKNVSFQYQSdASFT--LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 362 SLVSQEPV-LFARSITD-NISYGLP--TVPFEMVVEAAQKAnahgfiMELQDGYSTETGEKGAqLSGGQKQRVAMARALV 437
Cdd:PRK13648 86 GIVFQNPDnQFVGSIVKyDVAFGLEnhAVPYDEMHRRVSEA------LKQVDMLERADYEPNA-LSGGQKQRVAIAGVLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 438 RNPPVLILDEATSALDAES-EYLIQQAIHGNLQKH-TVLIIAHRLSTVEHAHLIVVLDKGRVVQQGT------HQQLLAQ 509
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDArQNLLDLVRKVKSEHNiTIISITHDLSEAMEADHVIVMNKGTVYKEGTpteifdHAEELTR 238
|
250
....*....|....*....
gi 2217288354 510 GGLYAKLVQR--QMLGLQP 526
Cdd:PRK13648 239 IGLDLPFPIKinQMLGHQT 257
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
279-521 |
3.99e-30 |
|
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: 118.47 E-value: 3.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 279 LEGRVDFENVTFTYRT--RPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKY 356
Cdd:cd03288 16 LGGEIKIHDLCVRYENnlKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 357 LHRVISLVSQEPVLFARSITDNISyglP--TVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMAR 434
Cdd:cd03288 93 LRSRLSIILQDPILFSGSIRFNLD---PecKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLAR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 435 ALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQ-GGLY 513
Cdd:cd03288 170 AFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQeDGVF 249
|
....*...
gi 2217288354 514 AKLVQRQM 521
Cdd:cd03288 250 ASLVRTDK 257
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
283-498 |
4.01e-30 |
|
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: 115.60 E-value: 4.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAydhkylhrvis 362
Cdd:cd03216 1 LELRGITKRF---GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSF----------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 lvsqepvlfaRSITDNISYGLPTVPfemvveaaqkanahgfimelqdgystetgekgaQLSGGQKQRVAMARALVRNPPV 442
Cdd:cd03216 67 ----------ASPRDARRAGIAMVY---------------------------------QLSVGERQMVEIARALARNARL 103
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 443 LILDEATSAL-DAESEYLIqqAIHGNLQK--HTVLIIAHRLSTV-EHAHLIVVLDKGRVV 498
Cdd:cd03216 104 LILDEPTAALtPAEVERLF--KVIRRLRAqgVAVIFISHRLDEVfEIADRVTVLRDGRVV 161
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
283-507 |
4.15e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 117.89 E-value: 4.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILEnfyPLEGGRVLLDGkpISAYDHKYLHR 359
Cdd:PRK09493 2 IEFKNVSKHF---GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTllrCINKLE---EITSGDLIVDG--LKVNDPKVDER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 360 VI----SLVSQEPVLFAR-SITDNISYGlptvPFEmvVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAM 432
Cdd:PRK09493 74 LIrqeaGMVFQQFYLFPHlTALENVMFG----PLR--VRGASKEEAEKQARELLAkvGLAERAHHYPSELSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 433 ARALVRNPPVLILDEATSALDAE--SEYL--IQQ-AIHGnlqkHTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQL 506
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDPElrHEVLkvMQDlAEEG----MTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVL 223
|
.
gi 2217288354 507 L 507
Cdd:PRK09493 224 I 224
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
282-501 |
4.44e-30 |
|
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: 116.50 E-value: 4.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 282 RVDFENVTFT---YRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEG--GRVLLDGKPISAYDHKY 356
Cdd:cd03213 3 TLSFRNLTVTvksSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKRSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 357 LhrvISLVSQEPVLFARSitdnisyglpTVpFEMVVEAAqkanahgfimELQdgystetgekgaQLSGGQKQRVAMARAL 436
Cdd:cd03213 83 I---IGYVPQDDILHPTL----------TV-RETLMFAA----------KLR------------GLSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217288354 437 VRNPPVLILDEATSALDAESEYLIQQAIHG-NLQKHTVLIIAHRLST--VEHAHLIVVLDKGRVVQQG 501
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
283-510 |
5.66e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 118.96 E-value: 5.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYrtrPHTQ--VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV 360
Cdd:PRK13635 6 IRVEHISFRY---PDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 361 ISLVSQEP--VLFARSITDNISYGLPT--VPFEMVVEAAQKANAHgfiMELQDGYSTETgekgAQLSGGQKQRVAMARAL 436
Cdd:PRK13635 83 VGMVFQNPdnQFVGATVQDDVAFGLENigVPREEMVERVDQALRQ---VGMEDFLNREP----HRLSGGQKQRVAIAGVL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217288354 437 VRNPPVLILDEATSALDAESEYLIQQAIH-----GNLqkhTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQG 510
Cdd:PRK13635 156 ALQPDIIILDEATSMLDPRGRREVLETVRqlkeqKGI---TVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSG 231
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
300-507 |
8.33e-30 |
|
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: 117.05 E-value: 8.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 300 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISayDHKYLHRVISLVSQEPVLFAR-SITDN 378
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYVPQNYALFPHmTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 379 ISYGL-------PTVPfEMVVEAAQKANahgfIMELQDgystetgEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSA 451
Cdd:cd03299 92 IAYGLkkrkvdkKEIE-RKVLEIAEMLG----IDHLLN-------RKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217288354 452 LDAESE----YLIQQAIHGNlqKHTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLL 507
Cdd:cd03299 160 LDVRTKeklrEELKKIRKEF--GVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
6-258 |
9.64e-30 |
|
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: 118.36 E-value: 9.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 6 TAVVIVCLLAIGSSFAAGIRGGIFTLIFAR------LNIRLRncLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLV 79
Cdd:cd18546 36 GVLLLAAAAYLAVVLAGWVAQRAQTRLTGRtgerllYDLRLR--VFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 80 SQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRS 159
Cdd:cd18546 114 QTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 160 FANEEEEAEVYlRKLQQVYKLNRKEAAAYMyYVWGSGLTLL--VVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDC 237
Cdd:cd18546 194 FRRERRNAERF-AELSDDYRDARLRAQRLV-AIYFPGVELLgnLATAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAP 271
|
250 260
....*....|....*....|.
gi 2217288354 238 MESVGSVYSGLMQGVGAAEKV 258
Cdd:cd18546 272 IQQLSQVFDSYQQARAALEKI 292
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
286-540 |
1.86e-29 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 116.65 E-value: 1.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 286 ENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVS 365
Cdd:PRK11231 6 ENLTVGYGTKR---ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 366 QEPvLFARSIT--DNISYGL-PTVPF---------EMVVEAAQKANahgfIMELQDGYSTEtgekgaqLSGGQKQRVAMA 433
Cdd:PRK11231 83 QHH-LTPEGITvrELVAYGRsPWLSLwgrlsaednARVNQAMEQTR----INHLADRRLTD-------LSGGQRQRAFLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 434 RALVRNPPVLILDEATSALD----AESEYLIQQAihgNLQKHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLA 508
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDinhqVELMRLMREL---NTQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVMT 227
|
250 260 270
....*....|....*....|....*....|..
gi 2217288354 509 QGGLyaklvqRQMLGLQpaadfTAGHNEPVAN 540
Cdd:PRK11231 228 PGLL------RTVFDVE-----AEIHPEPVSG 248
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
285-506 |
2.34e-29 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 116.13 E-value: 2.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 285 FENVTFTYRTrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILEnfyPLEGGRVLLDGKPISAYDHKYLHRV- 360
Cdd:cd03256 3 VENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTllrCLNGLV---EPTSGSVLIDGTDINKLKGKALRQLr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 361 --ISLVSQEPVLFAR-SITDNISYG-LPTVP-----FEMVVEAA-QKANAhgfIMElQDGYSTETGEKGAQLSGGQKQRV 430
Cdd:cd03256 78 rqIGMIFQQFNLIERlSVLENVLSGrLGRRStwrslFGLFPKEEkQRALA---ALE-RVGLLDKAYQRADQLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 431 AMARALVRNPPVLILDEATSALDAES-----EYLIQQAIHGNLqkhTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQ 504
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASsrqvmDLLKRINREEGI---TVIVSLHQVDLArEYADRIVGLKDGRIVFDGPPA 230
|
..
gi 2217288354 505 QL 506
Cdd:cd03256 231 EL 232
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
299-502 |
2.56e-29 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 116.29 E-value: 2.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 299 QVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEPVLFAR-SIT 376
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPpHRIARLGIARTFQNPRLFPElTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 377 DNI--------SYGLPTVPFEMVVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILD 446
Cdd:COG0411 98 ENVlvaaharlGRGLLAALLRLPRARREEREARERAEELLErvGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 447 EATSAL-DAESEYLIQ--QAIHGNlQKHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGT 502
Cdd:COG0411 178 EPAAGLnPEETEELAEliRRLRDE-RGITILLIEHDMDLVmGLADRIVVLDFGRVIAEGT 236
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
283-502 |
8.35e-29 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 116.82 E-value: 8.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRPHT-QVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENfyPlEGGRVLLDGKPISAYDHKYL- 357
Cdd:PRK11153 2 IELKNISKVFPQGGRTiHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER--P-TSGRVLVDGQDLTALSEKELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 358 --HRVISLVSQE-PVLFARSITDNISYglptvPFEMVVEAAQKANAHgfIMELQD--GYSTETGEKGAQLSGGQKQRVAM 432
Cdd:PRK11153 79 kaRRQIGMIFQHfNLLSSRTVFDNVAL-----PLELAGTPKAEIKAR--VTELLElvGLSDKADRYPAQLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217288354 433 ARALVRNPPVLILDEATSALDAESeyliQQAIHGNLQK------HTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGT 502
Cdd:PRK11153 152 ARALASNPKVLLCDEATSALDPAT----TRSILELLKDinrelgLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
283-483 |
1.25e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 114.75 E-value: 1.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEG-----GRVLLDGKPIsaYDHKY- 356
Cdd:PRK14258 8 IKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNI--YERRVn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 357 ---LHRVISLVSQEPVLFARSITDNISYGL------PTVPFEMVVEAAQKAnahgfiMELQDGYSTETGEKGAQLSGGQK 427
Cdd:PRK14258 83 lnrLRRQVSMVHPKPNLFPMSVYDNVAYGVkivgwrPKLEIDDIVESALKD------ADLWDEIKHKIHKSALDLSGGQQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217288354 428 QRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKH--TVLIIAHRLSTV 483
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSelTMVIVSHNLHQV 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
283-497 |
1.33e-28 |
|
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: 112.89 E-value: 1.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYrtrPHTQV-LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHK---YLH 358
Cdd:cd03292 1 IEFINVTKTY---PNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 359 RVISLVSQE-PVLFARSITDNISyglptvpFEMVVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAMARA 435
Cdd:cd03292 78 RKIGVVFQDfRLLPDRNVYENVA-------FALEVTGVPPREIRKRVPAALElvGLSHKHRALPAELSGGEQQRVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217288354 436 LVRNPPVLILDEATSALDAESEYLIQQAIHG-NLQKHTVLIIAHRLSTVE-HAHLIVVLDKGRV 497
Cdd:cd03292 151 IVNSPTILIADEPTGNLDPDTTWEIMNLLKKiNKAGTTVVVATHAKELVDtTRHRVIALERGKL 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
283-501 |
1.44e-28 |
|
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: 112.73 E-value: 1.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylHRVIS 362
Cdd:cd03301 1 VELENVTKRFGNVT---ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 LVSQEPVLFAR-SITDNISYGLPT--VPFEMVVEAAQKANAHGFIMELQDgystetgEKGAQLSGGQKQRVAMARALVRN 439
Cdd:cd03301 76 MVFQNYALYPHmTVYDNIAFGLKLrkVPKDEIDERVREVAELLQIEHLLD-------RKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217288354 440 PPVLILDEATSALDAESEYLIQQAI---HGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQG 501
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELkrlQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
286-507 |
1.58e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 114.06 E-value: 1.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 286 ENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVS 365
Cdd:COG4559 5 ENLSVRLGGR---TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 366 Q-----------EPVLFARsitdnISYGLPTVPFEMVVEAAqkanahgfiMELqdgysTETGEKGA----QLSGGQKQRV 430
Cdd:COG4559 82 QhsslafpftveEVVALGR-----APHGSSAAQDRQIVREA---------LAL-----VGLAHLAGrsyqTLSGGEQQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 431 AMARAL------VRNPP-VLILDEATSALDaeseyLIQQaihgnlqkHTVLIIAHRLS-------TVEH--------AHL 488
Cdd:COG4559 143 QLARVLaqlwepVDGGPrWLFLDEPTSALD-----LAHQ--------HAVLRLARQLArrgggvvAVLHdlnlaaqyADR 209
|
250
....*....|....*....
gi 2217288354 489 IVVLDKGRVVQQGTHQQLL 507
Cdd:COG4559 210 ILLLHQGRLVAQGTPEEVL 228
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
286-509 |
2.41e-28 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 115.15 E-value: 2.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 286 ENVTFTYRTRPHT-QVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYP---LEGGRVLLDGKPISAYDHKYLHRV- 360
Cdd:COG0444 5 RNLKVYFPTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELRKIr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 361 ---ISLVSQE------PVLfarsitdnisyglpTVpFEMVVEAaqkanahgfiMELQDGYSTETGEKGA----------- 420
Cdd:COG0444 85 greIQMIFQDpmtslnPVM--------------TV-GDQIAEP----------LRIHGGLSKAEARERAiellervglpd 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 421 ----------QLSGGQKQRVAMARALVRNPPVLILDEATSALDAeseyLIQQAIHG---NLQKH---TVLIIAHRLSTVE 484
Cdd:COG0444 140 perrldryphELSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQAQILNllkDLQRElglAILFITHDLGVVA 215
|
250 260
....*....|....*....|....*.
gi 2217288354 485 H-AHLIVVLDKGRVVQQGTHQQLLAQ 509
Cdd:COG0444 216 EiADRVAVMYAGRIVEEGPVEELFEN 241
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
303-520 |
2.97e-28 |
|
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: 115.58 E-value: 2.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 303 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPIsaYD---------HKylhRVISLVSQEPVLFA- 372
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL--QDsargiflppHR---RRIGYVFQEARLFPh 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 373 RSITDNISYGL-------PTVPFEMVVEAAQkanahgfIMELQDGYStetgekgAQLSGGQKQRVAMARALVRNPPVLIL 445
Cdd:COG4148 92 LSVRGNLLYGRkrapraeRRISFDEVVELLG-------IGHLLDRRP-------ATLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 446 DEATSALDAES-----EYLIQqaihgnLQKHT---VLIIAHrlSTVEHAHL---IVVLDKGRVVQQGTHQQLLAQGGLYA 514
Cdd:COG4148 158 DEPLAALDLARkaeilPYLER------LRDELdipILYVSH--SLDEVARLadhVVLLEQGRVVASGPLAEVLSRPDLLP 229
|
....*.
gi 2217288354 515 KLVQRQ 520
Cdd:COG4148 230 LAGGEE 235
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
298-492 |
3.20e-28 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 112.50 E-value: 3.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 298 TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITD 377
Cdd:PRK10247 20 AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 378 NISYglptvPFEMvveAAQKANAHGFIMELQD-GYSTETGEKG-AQLSGGQKQRVAMARALVRNPPVLILDEATSALDAE 455
Cdd:PRK10247 100 NLIF-----PWQI---RNQQPDPAIFLDDLERfALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 2217288354 456 SEYLIQQAIHGNLQKH--TVLIIAHRLSTVEHAHLIVVL 492
Cdd:PRK10247 172 NKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKVITL 210
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
283-506 |
3.41e-28 |
|
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: 112.21 E-value: 3.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRPHTqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPIsAYDHKYLHRVIS 362
Cdd:cd03263 1 LQIRNLTKTYKKGTKP-AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 LVSQEPVLFAR-SITDNISY-----GLPTVPFEMVVEAAQKanahgfIMELQDGYSTETGekgaQLSGGQKQRVAMARAL 436
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkGLPKSEIKEEVELLLR------VLGLTDKANKRAR----TLSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217288354 437 VRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQL 506
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
283-501 |
4.03e-28 |
|
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: 111.52 E-value: 4.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYrtrPHTQVLQNVSFSLSPGkVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYlHRVIS 362
Cdd:cd03264 1 LQLENLTKRY---GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKL-RRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 LVSQEPVLFAR-SITDNISY-----GLP--TVPfEMVVEAAQKANAHGFimelqdgysteTGEKGAQLSGGQKQRVAMAR 434
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDYiawlkGIPskEVK-ARVDEVLELVNLGDR-----------AKKKIGSLSGGMRRRVGIAQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217288354 435 ALVRNPPVLILDEATSALDAES-----EYLIQQAihgnlQKHTVLIIAHRLSTVE-HAHLIVVLDKGRVVQQG 501
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDPEErirfrNLLSELG-----EDRIVILSTHIVEDVEsLCNQVAVLNKGKLVFEG 211
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
10-258 |
5.44e-28 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 113.40 E-value: 5.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 10 IVCLLAIGSSFAAGIRGGIFTLIFA------------RLNIR--------LRNCLFRSLVSQETSFFDENRTGDLISRLT 69
Cdd:cd18778 25 LVDLVTIGSKSLGLLLGLALLLLGAyllrallnflriYLNHVaeqkvvadLRSDLYDKLQRLSLRYFDDRQTGDLMSRVI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 70 SDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEE 149
Cdd:cd18778 105 NDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 150 TISAMKTVRSFANEEEEAEVYLRKLQQVYKLN---RKEAAAY---MYYVWGSGlTLLVvqvsiLYYGGHLVISGQMTSGN 223
Cdd:cd18778 185 NLSGIREIQAFGREEEEAKRFEALSRRYRKAQlraMKLWAIFhplMEFLTSLG-TVLV-----LGFGGRLVLAGELTIGD 258
|
250 260 270
....*....|....*....|....*....|....*
gi 2217288354 224 LIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKV 258
Cdd:cd18778 259 LVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
296-498 |
7.18e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 116.66 E-value: 7.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 296 PHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPIS------AYDHKylhrvISLVSQEPV 369
Cdd:COG1129 15 GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfrsprdAQAAG-----IAIIHQELN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 370 LFA-RSITDNISYG-LPTVPF-----EMVVEAAQKANAHGFIMELqdgySTETGEkgaqLSGGQKQRVAMARALVRNPPV 442
Cdd:COG1129 90 LVPnLSVAENIFLGrEPRRGGlidwrAMRRRARELLARLGLDIDP----DTPVGD----LSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 443 LILDEATSAL-DAESEYLIqqAIHGNLQKH--TVLIIAHRLSTV-EHAHLIVVLDKGRVV 498
Cdd:COG1129 162 LILDEPTASLtEREVERLF--RIIRRLKAQgvAIIYISHRLDEVfEIADRVTVLRDGRLV 219
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
283-511 |
8.18e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 112.52 E-value: 8.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 362
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 LVSQEP--VLFARSITDNISYGLPT--VPFEMVVEAAQKANAhgfIMELQDGYSTETgekgAQLSGGQKQRVAMARALVR 438
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENkgIPHEEMKERVNEALE---LVGMQDFKEREP----ARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217288354 439 NPPVLILDEATSALDAESEYLIQQAIHGNLQKH--TVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGG 511
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGN 232
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
293-506 |
1.34e-27 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 113.29 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 293 RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYL---HRVISLVSQEPv 369
Cdd:COG4608 26 RTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplRRRMQMVFQDP- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 370 lFA-----RSITDNISYGLptvpfeMVVEAAQKANAHGFIMELQD--GYSTETGEKGA-QLSGGQKQRVAMARALVRNPP 441
Cdd:COG4608 105 -YAslnprMTVGDIIAEPL------RIHGLASKAERRERVAELLElvGLRPEHADRYPhEFSGGQRQRIGIARALALNPK 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217288354 442 VLILDEATSALDAeSeylIQ-QAIhgN----LQK---HTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQL 506
Cdd:COG4608 178 LIVCDEPVSALDV-S---IQaQVL--NlledLQDelgLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
286-509 |
2.08e-27 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 110.06 E-value: 2.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 286 ENVTFTYRTRPhtqvlqnVSFSLS--PGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKpisayDHKYL---HRV 360
Cdd:PRK10771 5 TDITWLYHHLP-------MRFDLTveRGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ-----DHTTTppsRRP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 361 ISLVSQEPVLFAR-SITDNISYGL-PTVPF-----EMVVEAAQKANAHGFIMELQdgystetgekgAQLSGGQKQRVAMA 433
Cdd:PRK10771 73 VSMLFQENNLFSHlTVAQNIGLGLnPGLKLnaaqrEKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 434 RALVRNPPVLILDEATSALD----AESEYLIQQAIHGnlQKHTVLIIAHRLstvEHAHLI----VVLDKGRVVQQGTHQQ 505
Cdd:PRK10771 142 RCLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQE--RQLTLLMVSHSL---EDAARIaprsLVVADGRIAWDGPTDE 216
|
....
gi 2217288354 506 LLAQ 509
Cdd:PRK10771 217 LLSG 220
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
286-501 |
3.55e-27 |
|
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: 108.84 E-value: 3.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 286 ENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAyDHKYLHRVISLVS 365
Cdd:cd03268 4 NDLTKTYGKK---RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-NIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 366 qEPVLF-ARSITDNISYglptvpfemvveaaqKANAHGF----IMELQD--GYSTETGEKGAQLSGGQKQRVAMARALVR 438
Cdd:cd03268 80 -APGFYpNLTARENLRL---------------LARLLGIrkkrIDEVLDvvGLKDSAKKKVKGFSLGMKQRLGIALALLG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217288354 439 NPPVLILDEATSALDAESEYLIQQAIHgNLQK--HTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQG 501
Cdd:cd03268 144 NPDLLILDEPTNGLDPDGIKELRELIL-SLRDqgITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
283-506 |
4.32e-27 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 109.35 E-value: 4.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISayDHKYLHRVIS 362
Cdd:cd03296 3 IEVRNVSKRF---GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT--DVPVQERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 LVSQEPVLFAR-SITDNISYGLPTVP-FEMVVEAAQKANAHGFIMELQ-DGYSTETGekgAQLSGGQKQRVAMARALVRN 439
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVAFGLRVKPrSERPPEAEIRAKVHELLKLVQlDWLADRYP---AQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 440 PPVLILDEATSALDAESEYLIQ---QAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQL 506
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRrwlRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
291-507 |
4.79e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 109.86 E-value: 4.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 291 TYRtRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPVL 370
Cdd:PRK13548 9 SVR-LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 371 -FARSITDNISYGL-----PTVPFEMVVEAAqkanahgfiMELQD--GYStetGEKGAQLSGGQKQRVAMARALVR---- 438
Cdd:PRK13548 88 sFPFTVEEVVAMGRaphglSRAEDDALVAAA---------LAQVDlaHLA---GRDYPQLSGGEQQRVQLARVLAQlwep 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 439 --NPPVLILDEATSALDaeseyLIQQaihgnlqkHTVLIIAHRLST--------VEH--------AHLIVVLDKGRVVQQ 500
Cdd:PRK13548 156 dgPPRWLLLDEPTSALD-----LAHQ--------HHVLRLARQLAHerglavivVLHdlnlaaryADRIVLLHQGRLVAD 222
|
....*..
gi 2217288354 501 GTHQQLL 507
Cdd:PRK13548 223 GTPAEVL 229
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
281-506 |
2.61e-26 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 114.11 E-value: 2.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 281 GRVDFENVTFTYRT-RPhtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHR 359
Cdd:PTZ00243 1307 GSLVFEGVQMRYREgLP--LVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRR 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 360 VISLVSQEPVLFARSITDNISYGLPTVPFEmVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRN 439
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTVRQNVDPFLEASSAE-VWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKK 1463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217288354 440 PPVLIL-DEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQL 506
Cdd:PTZ00243 1464 GSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
293-509 |
3.75e-26 |
|
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: 112.09 E-value: 3.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 293 RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSC----VNILENfypleGGRVLLDGKPISAYDHKYLHRV---ISLVS 365
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIPS-----EGEIRFDGQDLDGLSRRALRPLrrrMQVVF 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 366 QEPvlFA-----RSITDNISYGLpTVPF---------EMVVEAAQKAnahGFIMELQDGYSTEtgekgaqLSGGQKQRVA 431
Cdd:COG4172 369 QDP--FGslsprMTVGQIIAEGL-RVHGpglsaaerrARVAEALEEV---GLDPAARHRYPHE-------FSGGQRQRIA 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 432 MARALVRNPPVLILDEATSALDAeseyLIQQAIHG---NLQKH---TVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQ 504
Cdd:COG4172 436 IARALILEPKLLVLDEPTSALDV----SVQAQILDllrDLQREhglAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTE 511
|
....*
gi 2217288354 505 QLLAQ 509
Cdd:COG4172 512 QVFDA 516
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
283-508 |
3.94e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 107.87 E-value: 3.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 362
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 LVSQEP--VLFARSITDNISYGLPT--VPFEMVVEAAQKANAHGFIMELQDgystetgEKGAQLSGGQKQRVAMARALVR 438
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENqgIPREEMIKRVDEALLAVNMLDFKT-------REPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217288354 439 NPPVLILDEATSALDAESEYLIQQAIHGNLQKH--TVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLA 508
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
286-523 |
4.36e-26 |
|
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: 106.47 E-value: 4.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 286 ENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLV 364
Cdd:cd03218 4 ENLSKRYGKR---KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 365 SQEPVLFAR-SITDNISYGLPTVPFEmvvEAAQKANAHGFIMELQdgYSTETGEKGAQLSGGQKQRVAMARALVRNPPVL 443
Cdd:cd03218 81 PQEASIFRKlTVEENILAVLEIRGLS---KKEREEKLEELLEEFH--ITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 444 ILDEATSALDAESEYLIQQAIHgNLQKHT--VLIIAHR----LSTVEHAHLIVvldKGRVVQQGTHQQLLAQgglyaKLV 517
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIK-ILKDRGigVLITDHNvretLSITDRAYIIY---EGKVLAEGTPEEIAAN-----ELV 226
|
....*.
gi 2217288354 518 QRQMLG 523
Cdd:cd03218 227 RKVYLG 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
297-506 |
4.65e-26 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 109.40 E-value: 4.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 297 HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISaydhkYLH---RVISLVSQEPVLFaR 373
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS-----RLHardRKVGFVFQHYALF-R 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 374 SIT--DNISYGLPTVPfemvveAAQKANAHGF---IMELQDGYSTE--TGEKGAQLSGGQKQRVAMARALVRNPPVLILD 446
Cdd:PRK10851 88 HMTvfDNIAFGLTVLP------RRERPNAAAIkakVTQLLEMVQLAhlADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217288354 447 EATSALDAE-----SEYLIQqaIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQL 506
Cdd:PRK10851 162 EPFGALDAQvrkelRRWLRQ--LHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
244-517 |
4.88e-26 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 113.50 E-value: 4.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 244 VYSGLMQGVGAAEKVFEFIDRQptmvhdgSLAPDHLEGR---------VDFENVTFTY-RTRPHTqvLQNVSFSLSPGKV 313
Cdd:TIGR00957 596 VISSIVQASVSLKRLRIFLSHE-------ELEPDSIERRtikpgegnsITVHNATFTWaRDLPPT--LNGITFSIPEGAL 666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 314 TALVGPSGSGKSSCVN-ILENFYPLEGgrvlldgkpisaydHKYLHRVISLVSQEPVLFARSITDNISYGLPTVP--FEM 390
Cdd:TIGR00957 667 VAVVGQVGCGKSSLLSaLLAEMDKVEG--------------HVHMKGSVAYVPQQAWIQNDSLRENILFGKALNEkyYQQ 732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 391 VVEAAqkanahGFIMELQ---DGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAE-SEYLIQQAI-- 464
Cdd:TIGR00957 733 VLEAC------ALLPDLEilpSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFEHVIgp 806
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2217288354 465 HGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLV 517
Cdd:TIGR00957 807 EGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFL 859
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
286-541 |
6.58e-26 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 112.91 E-value: 6.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 286 ENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVN-ILENFYPLEGGRVLLDGKpisaydhkylhrvISLV 364
Cdd:PLN03130 618 KNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT-------------VAYV 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 365 SQEPVLFARSITDNISYGLPTVP--FEMVVEAAqkANAHGFIMeLQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPV 442
Cdd:PLN03130 685 PQVSWIFNATVRDNILFGSPFDPerYERAIDVT--ALQHDLDL-LPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDV 761
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 443 LILDEATSALDAE-SEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGLYAKLVQR-- 519
Cdd:PLN03130 762 YIFDDPLSALDAHvGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMENag 841
|
250 260
....*....|....*....|....*
gi 2217288354 520 QMLGLQPAADFTAGHNE---PVANG 541
Cdd:PLN03130 842 KMEEYVEENGEEEDDQTsskPVANG 866
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
293-528 |
7.04e-26 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 107.08 E-value: 7.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 293 RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD---HKYLHRVISLVSQEP- 368
Cdd:PRK10419 20 GKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQDSi 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 369 --VLFARSITDNIsyGLPTVPFEMVVEAAQKANAHGFI--MELQDGYSTEtgeKGAQLSGGQKQRVAMARALVRNPPVLI 444
Cdd:PRK10419 100 saVNPRKTVREII--REPLRHLLSLDKAERLARASEMLraVDLDDSVLDK---RPPQLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 445 LDEATSALDaeseyLIQQA----IHGNLQKHT---VLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLAQGGLYAKL 516
Cdd:PRK10419 175 LDEAVSNLD-----LVLQAgvirLLKKLQQQFgtaCLFITHDLRLVERfCQRVMVMDNGQIVETQPVGDKLTFSSPAGRV 249
|
250
....*....|..
gi 2217288354 517 VQRQMLGLQPAA 528
Cdd:PRK10419 250 LQNAVLPAFPVR 261
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
283-524 |
8.18e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 107.19 E-value: 8.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRPHTqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFY---PLEGGRVLLDGKPISAYDHKYLHR 359
Cdd:PRK13640 6 VEFKHVSFTYPDSKKP-ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 360 VISLVSQEP--VLFARSITDNISYGLPT--VPFEMVVEAAQKANAHGFIMELQDGystetgeKGAQLSGGQKQRVAMARA 435
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENraVPRPEMIKIVRDVLADVGMLDYIDS-------EPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 436 LVRNPPVLILDEATSALDAESEYLIQQAIHgNLQKH---TVLIIAHRLSTVEHAHLIVVLDKGRVVQQGT------HQQL 506
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIR-KLKKKnnlTVISITHDIDEANMADQVLVLDDGKLLAQGSpveifsKVEM 236
|
250
....*....|....*...
gi 2217288354 507 LAQGGLYAKLVQRQMLGL 524
Cdd:PRK13640 237 LKEIGLDIPFVYKLKNKL 254
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
8-228 |
9.96e-26 |
|
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: 107.15 E-value: 9.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 8 VVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLtSDTTMVSDLVSQN-INVF 86
Cdd:cd18570 45 SIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISSTtISLF 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 87 LrNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEE 166
Cdd:cd18570 124 L-DLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQF 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217288354 167 AEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFI 228
Cdd:cd18570 203 LKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSYLVIKGQLSLGQLIAFN 264
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
9-230 |
1.44e-25 |
|
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: 106.71 E-value: 1.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 9 VIVCLLAIGSSFAAGIRGGIFTLIFARlniRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLR 88
Cdd:cd18548 46 LLLALLGLIAGILAGYFAAKASQGFGR---DLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 89 NTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAE 168
Cdd:cd18548 123 APIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217288354 169 VYLRKLQQVYKLNRKeaaAYMYYVWGSGLTLLVVQVS---ILYYGGHLVISGQMTSGNLIAFIIY 230
Cdd:cd18548 203 RFDKANDDLTDTSLK---AGRLMALLNPLMMLIMNLAivaILWFGGHLINAGSLQVGDLVAFINY 264
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
304-512 |
3.03e-25 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 107.12 E-value: 3.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 304 VSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDG-------KPISAYDHKylhRVISLVSQEPVLFAR-SI 375
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrKGIFLPPEK---RRIGYVFQEARLFPHlSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 376 TDNISYGL--PTVPFEMVVEAAqkanahgfIMELQdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD 453
Cdd:TIGR02142 93 RGNLRYGMkrARPSERRISFER--------VIELL-GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217288354 454 AESEYLIQQAIHgNLQKHT---VLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLAQGGL 512
Cdd:TIGR02142 164 DPRKYEILPYLE-RLHAEFgipILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASPDL 225
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
283-525 |
3.46e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 105.20 E-value: 3.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 362
Cdd:PRK13647 5 IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 LVSQEP--VLFARSITDNISYG-----LPTVPFEMVVEAAQKANAhgfIMELQDgystetgEKGAQLSGGQKQRVAMARA 435
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGpvnmgLDKDEVERRVEEALKAVR---MWDFRD-------KPPYHLSYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 436 LVRNPPVLILDEATSALDAESEYLIQQAIHG-NLQKHTVLIIAHRLS-TVEHAHLIVVLDKGRVVQQG-----THQQLLA 508
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGdksllTDEDIVE 232
|
250
....*....|....*..
gi 2217288354 509 QGGLYAKLVQRQMLGLQ 525
Cdd:PRK13647 233 QAGLRLPLVAQIFEDLP 249
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
299-508 |
4.81e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 104.06 E-value: 4.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 299 QVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENfyPLEG----GRVLLDG-KPISAYDH--KYLHRVISLVSQEP 368
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTllrCINLLEQ--PEAGtirvGDITIDTaRSLSQQKGliRQLRQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 369 VLFA-RSITDNISYGlptvPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDE 447
Cdd:PRK11264 95 NLFPhRTVLENIIEG----PVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217288354 448 ATSALDAESEYLIQQAIHGNLQ-KHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLA 508
Cdd:PRK11264 171 PTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKALFA 233
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
301-480 |
5.97e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 104.09 E-value: 5.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 301 LQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENFYP---LEGgRVLLDGKPISA--YDHKYLHRVISLVSQEPVLFA 372
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTilrCFNRLNDLIPgfrVEG-KVTFHGKNLYApdVDPVEVRRRIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 373 RSITDNISYGlPTV-----PFEMVVEAAQKANAhgfimeLQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDE 447
Cdd:PRK14243 105 KSIYDNIAYG-ARIngykgDMDELVERSLRQAA------LWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190
....*....|....*....|....*....|...
gi 2217288354 448 ATSALDAESEYLIQQAIHGNLQKHTVLIIAHRL 480
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
8-258 |
6.32e-25 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 104.87 E-value: 6.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 8 VVIVCLLAIGSSFAAGIrggiftlIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFL 87
Cdd:cd18540 52 ILIQALSVFLFIRLAGK-------IEMGVSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 88 RNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIygkYYKRLSKevQNALARASN---TA--EETISAMKTVRSFAN 162
Cdd:cd18540 125 WGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSIY---FQKKILK--AYRKVRKINsriTGafNEGITGAKTTKTLVR 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 163 EEEEAEVYLRKLQQVYKLNRKeaAAYMyyvwgSGLTLLVVQV-------SILYYGGHLVISGQMTSGNLIAFIIYEFVLG 235
Cdd:cd18540 200 EEKNLREFKELTEEMRRASVR--AARL-----SALFLPIVLFlgsiataLVLWYGGILVLAGAITIGTLVAFISYATQFF 272
|
250 260
....*....|....*....|...
gi 2217288354 236 DCMESVGSVYSGLMQGVGAAEKV 258
Cdd:cd18540 273 EPIQQLARVLAELQSAQASAERV 295
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
297-524 |
7.47e-25 |
|
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: 103.14 E-value: 7.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 297 HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEPVLFAR-S 374
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPpHRIARLGIGYVPEGRRIFPSlT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 375 ITDNISYGLPTVPFEMVVEAAQKanahgFIMEL---------QdgystetgeKGAQLSGGQKQRVAMARALVRNPPVLIL 445
Cdd:COG0410 95 VEENLLLGAYARRDRAEVRADLE-----RVYELfprlkerrrQ---------RAGTLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 446 DEATSALDAeseyLIQQAIHGNLQK-----HTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLAQGGlyaklVQR 519
Cdd:COG0410 161 DEPSLGLAP----LIVEEIFEIIRRlnregVTILLVEQNARFAlEIADRAYVLERGRIVLEGTAAELLADPE-----VRE 231
|
....*
gi 2217288354 520 QMLGL 524
Cdd:COG0410 232 AYLGV 236
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
35-518 |
8.92e-25 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 109.30 E-value: 8.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 35 RLNIRLRNCLFRSLVSQETSFFDENR----TGDLISRLTSDTTMVSdLVSQNINVFLRNTVKVTgvvVFMFSLSWQLSLV 110
Cdd:PLN03232 367 RVGFRLRSTLVAAIFHKSLRLTHEARknfaSGKVTNMITTDANALQ-QIAEQLHGLWSAPFRII---VSMVLLYQQLGVA 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 111 TFMGFPIIMMV---SNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEE----------EAEVYLRKLQQV 177
Cdd:PLN03232 443 SLFGSLILFLLiplQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSfesriqgirnEELSWFRKAQLL 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 178 YKLNrkeaaAYMyyvwgsgLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEK 257
Cdd:PLN03232 523 SAFN-----SFI-------LNSIPVVVTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQR 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 258 VFE-FIDRQPTMVHDGSLAPDhlEGRVDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVN-ILENFY 335
Cdd:PLN03232 591 IEElLLSEERILAQNPPLQPG--APAISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELS 668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 336 PLEGGRVLLDGKpisaydhkylhrvISLVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGfiMELQDGYS-TE 414
Cdd:PLN03232 669 HAETSSVVIRGS-------------VAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHD--LDLLPGRDlTE 733
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 415 TGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAE-SEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLD 493
Cdd:PLN03232 734 IGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVS 813
|
490 500
....*....|....*....|....*
gi 2217288354 494 KGRVVQQGTHQQLLAQGGLYAKLVQ 518
Cdd:PLN03232 814 EGMIKEEGTFAELSKSGSLFKKLME 838
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
286-500 |
1.03e-24 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 103.40 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 286 ENVTFTY-RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylhRviSLV 364
Cdd:COG4525 7 RHVSVRYpGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD---R--GVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 365 SQEPVLFA-RSITDNISYGLPtvpFEMVVEAAQKANAHGFI--MELQDgysteTGEKG-AQLSGGQKQRVAMARALVRNP 440
Cdd:COG4525 82 FQKDALLPwLNVLDNVAFGLR---LRGVPKAERRARAEELLalVGLAD-----FARRRiWQLSGGMRQRVGIARALAADP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217288354 441 PVLILDEATSALDAESEYLIQQAIHG--NLQKHTVLIIAHrlsTVEHAHL----IVVLDK--GRVVQQ 500
Cdd:COG4525 154 RFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH---SVEEALFlatrLVVMSPgpGRIVER 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
293-508 |
1.17e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 107.48 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 293 RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGgRVLLDGKPISAYDHKYL---HRVISLVSQEP- 368
Cdd:PRK15134 294 RTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQG-EIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPn 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 369 -VLFAR-SITDNISYGLPTvpFEMVVEAAQKANAHGFIMElQDGYSTETGEK-GAQLSGGQKQRVAMARALVRNPPVLIL 445
Cdd:PRK15134 373 sSLNPRlNVLQIIEEGLRV--HQPTLSAAQREQQVIAVME-EVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIIL 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217288354 446 DEATSALDAESEYLIQQAIHGNLQKHTV--LIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLA 508
Cdd:PRK15134 450 DEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
301-498 |
1.19e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 107.42 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 301 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPIS------AYDHKylhrvISLVSQEPVLFAR- 373
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirsprdAIALG-----IGMVHQHFMLVPNl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 374 SITDNISYGLPTVPFEMV--VEAAQKanahgfIMELQDGYstetG------EKGAQLSGGQKQRVAMARALVRNPPVLIL 445
Cdd:COG3845 96 TVAENIVLGLEPTKGGRLdrKAARAR------IRELSERY----GldvdpdAKVEDLSVGEQQRVEILKALYRGARILIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217288354 446 DEATSAL-DAESEYLIqqAIHGNL--QKHTVLIIAHRLSTV-EHAHLIVVLDKGRVV 498
Cdd:COG3845 166 DEPTAVLtPQEADELF--EILRRLaaEGKSIIFITHKLREVmAIADRVTVLRRGKVV 220
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
296-495 |
2.05e-24 |
|
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: 101.25 E-value: 2.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 296 PHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCV-NILENFYPLEG----GRVLLDGKPISAYDHKYLHRViSLVSQEPVL 370
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGkvhwSNKNESEPSFEATRSRNRYSV-AYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 371 FARSITDNISYGLP--TVPFEMVVEAAqkaNAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEA 448
Cdd:cd03290 91 LNATVEENITFGSPfnKQRYKAVTDAC---SLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2217288354 449 TSALDAE-SEYLIQQAIHGNLQ--KHTVLIIAHRLSTVEHAHLIVVLDKG 495
Cdd:cd03290 168 FSALDIHlSDHLMQEGILKFLQddKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
290-515 |
2.18e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 103.78 E-value: 2.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 290 FTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVN-------------ILENFY---PLEGGRVLLDGKPISAYD 353
Cdd:PRK13631 31 FDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglikskygtiQVGDIYigdKKNNHELITNPYSKKIKN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 354 HKYLHRVISLVSQEP--VLFARSITDNISYGlPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGekgAQLSGGQKQRVA 431
Cdd:PRK13631 111 FKELRRRVSMVFQFPeyQLFKDTIEKDIMFG-PVALGVKKSEAKKLAKFYLNKMGLDDSYLERSP---FGLSGGQKRRVA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 432 MARALVRNPPVLILDEATSALDAESEYLIQQAI-HGNLQKHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLAQ 509
Cdd:PRK13631 187 IAGILAIQPEILIFDEPTAGLDPKGEHEMMQLIlDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEIFTD 266
|
....*.
gi 2217288354 510 GGLYAK 515
Cdd:PRK13631 267 QHIINS 272
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
286-501 |
3.42e-24 |
|
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: 100.52 E-value: 3.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 286 ENVTFTYR-TRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDG-----KPISAydhkylHR 359
Cdd:cd03266 5 DALTKRFRdVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkEPAEA------RR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 360 VISLVSQEPVLFAR-SITDNISY-----GLptvpfemvveaaQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVA 431
Cdd:cd03266 79 RLGFVSDSTGLYDRlTARENLEYfaglyGL------------KGDELTARLEELADrlGMEELLDRRVGGFSTGMRQKVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217288354 432 MARALVRNPPVLILDEATSALDAESEYLIQQAI-HGNLQKHTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQG 501
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDVMATRALREFIrQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
299-480 |
3.59e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 101.78 E-value: 3.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 299 QVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENFYP--LEGGRVLLDGKPISA--YDHKYLHRVISLVSQEPVLF 371
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTllrSINRMNDLNPevTITGSIVYNGHNIYSprTDTVDLRKEIGMVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 372 ARSITDNISYGL------PTVPFEMVVEAAQKANAhgfimeLQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLIL 445
Cdd:PRK14239 99 PMSIYENVVYGLrlkgikDKQVLDEAVEKSLKGAS------IWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190
....*....|....*....|....*....|....*
gi 2217288354 446 DEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRL 480
Cdd:PRK14239 173 DEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
285-506 |
3.74e-24 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 101.22 E-value: 3.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 285 FENVTFTYRTrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENfypLEGGRVLLDGKPISAYDHKYLHRV- 360
Cdd:TIGR02315 4 VENLSKVYPN--GKQALKNINLNINPGEFVAIIGPSGAGKSTllrCINRLVE---PSSGSILLEGTDITKLRGKKLRKLr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 361 --ISLVSQEPVLFAR-SITDNISYG----LPTVP--FEMVVEAaQKANAhgfiMELQD--GYSTETGEKGAQLSGGQKQR 429
Cdd:TIGR02315 79 rrIGMIFQHYNLIERlTVLENVLHGrlgyKPTWRslLGRFSEE-DKERA----LSALErvGLADKAYQRADQLSGGQQQR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 430 VAMARALVRNPPVLILDEATSALDAES-----EYLIQQAIHGNLqkhTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTH 503
Cdd:TIGR02315 154 VAIARALAQQPDLILADEPIASLDPKTskqvmDYLKRINKEDGI---TVIINLHQVDLAkKYADRIVGLKAGEIVFDGAP 230
|
...
gi 2217288354 504 QQL 506
Cdd:TIGR02315 231 SEL 233
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
14-241 |
3.87e-24 |
|
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: 103.13 E-value: 3.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 14 LAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKV 93
Cdd:cd18558 68 IGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 94 TGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRK 173
Cdd:cd18558 148 GTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQN 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217288354 174 LQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLI----AFIIYEFVLGDCMESV 241
Cdd:cd18558 228 LEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLtvffSVLIGAFSAGQQVPSI 299
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
286-455 |
9.53e-24 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 99.09 E-value: 9.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 286 ENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLE---GGRVLLDGKPISAYdhKYLHRVIS 362
Cdd:COG4136 5 ENLTITLGGRP---LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTAL--PAEQRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 LVSQEPVLFAR-SITDNISYGLP-TVPFE----MVVEAAQKANAHGFimelqdgystetGEKG-AQLSGGQKQRVAMARA 435
Cdd:COG4136 80 ILFQDDLLFPHlSVGENLAFALPpTIGRAqrraRVEQALEEAGLAGF------------ADRDpATLSGGQRARVALLRA 147
|
170 180
....*....|....*....|
gi 2217288354 436 LVRNPPVLILDEATSALDAE 455
Cdd:COG4136 148 LLAEPRALLLDEPFSKLDAA 167
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
286-509 |
1.00e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.92 E-value: 1.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 286 ENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISaYDHKYLHRV---IS 362
Cdd:PRK13639 3 ETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLLEVrktVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 LVSQEP--VLFARSITDNISYG-----LPTVPFEMVVEAAQKANAhgfiMElqdGYstetgEKGA--QLSGGQKQRVAMA 433
Cdd:PRK13639 82 IVFQNPddQLFAPTVEEDVAFGplnlgLSKEEVEKRVKEALKAVG----ME---GF-----ENKPphHLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217288354 434 RALVRNPPVLILDEATSALDAESEYLIQQAIHG-NLQKHTVLIIAHRLSTVE-HAHLIVVLDKGRVVQQGTHQQLLAQ 509
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDlNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
287-526 |
1.07e-23 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 100.65 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 287 NVTFTYRT------RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD---HKYL 357
Cdd:TIGR02769 7 DVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkqRRAF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 358 HRVISLVSQE-PVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGfIMELQDGYSTETGEKGAQLSGGQKQRVAMARAL 436
Cdd:TIGR02769 87 RRDVQLVFQDsPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAE-LLDMVGLRSEDADKLPRQLSGGQLQRINIARAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 437 VRNPPVLILDEATSALDAESEYLIQQAIHgNLQKH---TVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLAQGGL 512
Cdd:TIGR02769 166 AVKPKLIVLDEAVSNLDMVLQAVILELLR-KLQQAfgtAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLLSFKHP 244
|
250
....*....|....
gi 2217288354 513 YAKLVQRQMLGLQP 526
Cdd:TIGR02769 245 AGRNLQSAVLPEHP 258
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
283-508 |
1.73e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 100.67 E-value: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYR--TRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSScvnILENFYPL---EGGRVLLDGKPISAYDH--- 354
Cdd:PRK13641 3 IKFENVDYIYSpgTPMEKKGLDNISFELEEGSFVALVGHTGSGKST---LMQHFNALlkpSSGTITIAGYHITPETGnkn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 355 -KYLHRVISLVSQ--EPVLFARSITDNISYGLPTVPFEmvvEAAQKANAHGFIMELqdGYSTETGEKGA-QLSGGQKQRV 430
Cdd:PRK13641 80 lKKLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFS---EDEAKEKALKWLKKV--GLSEDLISKSPfELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 431 AMARALVRNPPVLILDEATSALDAESEYLIQQaIHGNLQK--HTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLL 507
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQ-LFKDYQKagHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIF 233
|
.
gi 2217288354 508 A 508
Cdd:PRK13641 234 S 234
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
289-509 |
1.75e-23 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 99.91 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 289 TFTYRT----RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLV 364
Cdd:COG4167 13 TFKYRTglfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 365 SQEPvlfarsitdNISYGlPTVPFEMVVEAAQKANAH-----------------GFIMELQDGYSTEtgekgaqLSGGQK 427
Cdd:COG4167 93 FQDP---------NTSLN-PRLNIGQILEEPLRLNTDltaeereerifatlrlvGLLPEHANFYPHM-------LSSGQK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 428 QRVAMARALVRNPPVLILDEATSALDAEseyLIQQAIhgNL-----QKHTV--LIIAHRLSTVEH-AHLIVVLDKGRVVQ 499
Cdd:COG4167 156 QRVALARALILQPKIIIADEALAALDMS---VRSQII--NLmlelqEKLGIsyIYVSQHLGIVKHiSDKVLVMHQGEVVE 230
|
250
....*....|
gi 2217288354 500 QGTHQQLLAQ 509
Cdd:COG4167 231 YGKTAEVFAN 240
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
300-516 |
1.75e-23 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 105.25 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 300 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDgkpisaydhkylhRVISLVSQEPVLFARSITDNI 379
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 380 SYGLPTVPFEM--VVEAAQ-KANahgfIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAE- 455
Cdd:PTZ00243 742 LFFDEEDAARLadAVRVSQlEAD----LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHv 817
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217288354 456 SEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQlLAQGGLYAKL 516
Cdd:PTZ00243 818 GERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSAD-FMRTSLYATL 877
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
284-509 |
2.74e-23 |
|
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: 103.23 E-value: 2.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 284 DFENVTFTYRTRPH-TQVLQNVSFSLSPGKVTALVGPSGSGKS----SCVNILENFYPLEGGRVLLDGKPISAYDHKYLH 358
Cdd:COG4172 8 SVEDLSVAFGQGGGtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 359 RV----ISLVSQEPV-----LFarSITDNISYGLptvpfeMVVEAAQKANAHGFIMELQDgystETGEKGA--------- 420
Cdd:COG4172 88 RIrgnrIAMIFQEPMtslnpLH--TIGKQIAEVL------RLHRGLSGAAARARALELLE----RVGIPDPerrldayph 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 421 QLSGGQKQRVAMARALVRNPPVLILDEATSALDAeseyLIQQAIHG---NLQKHT---VLIIAHRLSTVEH-AHLIVVLD 493
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADEPTTALDV----TVQAQILDllkDLQRELgmaLLLITHDLGVVRRfADRVAVMR 231
|
250
....*....|....*.
gi 2217288354 494 KGRVVQQGTHQQLLAQ 509
Cdd:COG4172 232 QGEIVEQGPTAELFAA 247
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
283-501 |
4.25e-23 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 98.23 E-value: 4.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNIL--ENfYPLEGGRVLLDGKPISAYDHKYLHRV 360
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLItgDL-PPTYGNDVRLFGERRGGEDVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 361 ISLVSQEpvlFARSITDNIsyglpTVpFEMV-------------VEAAQKANAHGFIMELqdGYSTETGEKGAQLSGGQK 427
Cdd:COG1119 80 IGLVSPA---LQLRFPRDE-----TV-LDVVlsgffdsiglyrePTDEQRERARELLELL--GLAHLADRPFGTLSQGEQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 428 QRVAMARALVRNPPVLILDEATSALDAES-EYLIQ--QAIHGNLQKHTVLiIAHRL----STVEHAhliVVLDKGRVVQQ 500
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDLGArELLLAllDKLAAEGAPTLVL-VTHHVeeipPGITHV---LLLKDGRVVAA 224
|
.
gi 2217288354 501 G 501
Cdd:COG1119 225 G 225
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
280-495 |
5.02e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 102.96 E-value: 5.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 280 EGRVDFENVTFTyrtRPHTQVL-QNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLL-DGKPISaydhkyl 357
Cdd:COG4178 360 DGALALEDLTLR---TPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVL------- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 358 hrvisLVSQEPVLFARSITDNISYGLPTVPF--EMVVEAAQKANAHGFIMELQdgystETGEKGAQLSGGQKQRVAMARA 435
Cdd:COG4178 430 -----FLPQRPYLPLGTLREALLYPATAEAFsdAELREALEAVGLGHLAERLD-----EEADWDQVLSLGEQQRLAFARL 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 436 LVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKG 495
Cdd:COG4178 500 LLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
298-501 |
5.83e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 98.06 E-value: 5.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 298 TQVLQNVSFSLSPGKVTALVGPSGSGKSSCV---NILENFYPLE--GGRVLLDGKPISAYDHKYLHRVISLVSQEPVLFA 372
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLrvfNRLIELYPEArvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 373 R-SITDNISYGLP--------TVPFEMVVEAAQKAnahgfimELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVL 443
Cdd:PRK14247 96 NlSIFENVALGLKlnrlvkskKELQERVRWALEKA-------QLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217288354 444 ILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAH------RLSTvehahLIVVLDKGRVVQQG 501
Cdd:PRK14247 169 LADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRISD-----YVAFLYKGQIVEWG 227
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
300-509 |
1.87e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 98.64 E-value: 1.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 300 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNI---LENfyPLEGgRVLLDGKPISayDHKYLHRVISLVSQEPVLFAR-SI 375
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLvagLEK--PTEG-QIFIDGEDVT--HRSIQQRDICMVFQSYALFPHmSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 376 TDNISYGLPT--VPFE----MVVEAAQKANAHGFimelQDGYSTetgekgaQLSGGQKQRVAMARALVRNPPVLILDEAT 449
Cdd:PRK11432 96 GENVGYGLKMlgVPKEerkqRVKEALELVDLAGF----EDRYVD-------QISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217288354 450 SALDAESEYLIQQAIHgNLQKH---TVLIIAHRLS---TVEHAhlIVVLDKGRVVQQGTHQQLLAQ 509
Cdd:PRK11432 165 SNLDANLRRSMREKIR-ELQQQfniTSLYVTHDQSeafAVSDT--VIVMNKGKIMQIGSPQELYRQ 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
285-478 |
1.92e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.52 E-value: 1.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 285 FENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGkpisaydhkylHRVISLV 364
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 365 SQEPVLFA-RSITDNISYGLPTV-------------PFEMVVEAAQKANAHGfIMELQDGYSTET--------------- 415
Cdd:COG0488 67 PQEPPLDDdLTVLDTVLDGDAELraleaeleeleakLAEPDEDLERLAELQE-EFEALGGWEAEAraeeilsglgfpeed 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217288354 416 -GEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAES-----EYLIQqaihgnlQKHTVLIIAH 478
Cdd:COG0488 146 lDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewleEFLKN-------YPGTVLVVSH 207
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
285-487 |
2.37e-22 |
|
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: 93.76 E-value: 2.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 285 FENVTFtyRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVlldgkpisaydHKYLHRVISLV 364
Cdd:cd03223 3 LENLSL--ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 365 SQEPVLFARSITDNISYglptvPFEMVveaaqkanahgfimelqdgystetgekgaqLSGGQKQRVAMARALVRNPPVLI 444
Cdd:cd03223 70 PQRPYLPLGTLREQLIY-----PWDDV------------------------------LSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2217288354 445 LDEATSALDAESEyliqQAIHGNLQKH--TVLIIAHRlSTVEHAH 487
Cdd:cd03223 115 LDEATSALDEESE----DRLYQLLKELgiTVISVGHR-PSLWKFH 154
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
286-508 |
3.07e-22 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 95.48 E-value: 3.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 286 ENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLV 364
Cdd:COG1137 7 ENLVKSYGKR---TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPmHKRARLGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 365 SQEPVLFAR-SITDNIsyglptvpfEMVVE------AAQKANAHGFIMELQDGYSTETgeKGAQLSGGQKQRVAMARALV 437
Cdd:COG1137 84 PQEASIFRKlTVEDNI---------LAVLElrklskKEREERLEELLEEFGITHLRKS--KAYSLSGGERRRVEIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217288354 438 RNPPVLILDEATSALD--AESEylIQQAIHgNLQKH--TVLIIAHR----LSTVEHAHLIvvlDKGRVVQQGTHQQLLA 508
Cdd:COG1137 153 TNPKFILLDEPFAGVDpiAVAD--IQKIIR-HLKERgiGVLITDHNvretLGICDRAYII---SEGKVLAEGTPEEILN 225
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
297-502 |
3.35e-22 |
|
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: 95.28 E-value: 3.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 297 HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEPVLFAR-S 374
Cdd:TIGR03410 12 QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPpHERARAGIAYVPQGREIFPRlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 375 ITDNISYGLPTVPfemvveaAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDA 454
Cdd:TIGR03410 92 VEENLLTGLAALP-------RRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2217288354 455 ESEYLIQQAIhGNLQKH---TVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGT 502
Cdd:TIGR03410 165 SIIKDIGRVI-RRLRAEggmAILLVEQYLDFARElADRYYVMERGRVVASGA 215
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
283-510 |
4.53e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 96.39 E-value: 4.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYR--TRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISA-YDHKYLHR 359
Cdd:PRK13646 3 IRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHkTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 360 V---ISLVSQ--EPVLFARSITDNISYGLPTvpFEMVVEAAqKANAHGFIMELqdGYSTETGEKGA-QLSGGQKQRVAMA 433
Cdd:PRK13646 83 VrkrIGMVFQfpESQLFEDTVEREIIFGPKN--FKMNLDEV-KNYAHRLLMDL--GFSRDVMSQSPfQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 434 RALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQ---KHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLAQ 509
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLK-SLQtdeNKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKD 236
|
.
gi 2217288354 510 G 510
Cdd:PRK13646 237 K 237
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
286-499 |
5.47e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 95.54 E-value: 5.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 286 ENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylhRVIsLVS 365
Cdd:PRK11248 5 SHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE---RGV-VFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 366 QEPVLFARSITDNISYGLPT--VPFEMVVEAAQKANAhgfimelqdgystETGEKGA------QLSGGQKQRVAMARALV 437
Cdd:PRK11248 78 NEGLLPWRNVQDNVAFGLQLagVEKMQRLEIAHQMLK-------------KVGLEGAekryiwQLSGGQRQRVGIARALA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217288354 438 RNPPVLILDEATSALDA----ESEYLIQQAIHGNLQKhtVLIIAHRL-STVEHAHLIVVL--DKGRVVQ 499
Cdd:PRK11248 145 ANPQLLLLDEPFGALDAftreQMQTLLLKLWQETGKQ--VLLITHDIeEAVFMATELVLLspGPGRVVE 211
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1-230 |
6.64e-22 |
|
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: 96.48 E-value: 6.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 1 MDQFSTAVVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVS 80
Cdd:cd18565 50 RGQLWLLGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 81 QNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSF 160
Cdd:cd18565 130 DGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAF 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 161 ANEEEEAEvYLRKLQQVYKLNRKEA----AAY---MYYVWGSGLtllvvqVSILYYGGHLVISG------QMTSGNLIAF 227
Cdd:cd18565 210 TAEDFERE-RVADASEEYRDANWRAirlrAAFfpvIRLVAGAGF------VATFVVGGYWVLDGpplftgTLTVGTLVTF 282
|
...
gi 2217288354 228 IIY 230
Cdd:cd18565 283 LFY 285
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
286-497 |
6.67e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 95.13 E-value: 6.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 286 ENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAydhkyLHRVISLVS 365
Cdd:PRK11247 16 NAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE-----AREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 366 QEPVLFA-RSITDNISYGLptvpfemvvEAAQKANAHGFIMELqdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLI 444
Cdd:PRK11247 88 QDARLLPwKKVIDNVGLGL---------KGQWRDAALQALAAV--GLADRANEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217288354 445 LDEATSALDAESEYLIQQAIHGNLQKH--TVLIIAHRLS-TVEHAHLIVVLDKGRV 497
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
292-509 |
8.53e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 95.68 E-value: 8.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 292 YRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISaYDHK---YLHRVISLVSQEP 368
Cdd:PRK13636 13 YNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKglmKLRESVGMVFQDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 369 --VLFARSITDNISYGLPT--VPFEMVVEAAQKANAHGFIMELQDgystetgEKGAQLSGGQKQRVAMARALVRNPPVLI 444
Cdd:PRK13636 92 dnQLFSASVYQDVSFGAVNlkLPEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217288354 445 LDEATSALDAESEYLIQQAIHgNLQKH---TVLIIAHRLSTVE-HAHLIVVLDKGRVVQQGTHQQLLAQ 509
Cdd:PRK13636 165 LDEPTAGLDPMGVSEIMKLLV-EMQKElglTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
300-477 |
8.77e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 93.40 E-value: 8.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 300 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHK----YL-HRVislvSQEPVLfarS 374
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAeachYLgHRN----AMKPAL---T 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 375 ITDNIS-----YGlptvPFEMVVEAAQKANAHGFIMELQDGYstetgekgaqLSGGQKQRVAMARALVRNPPVLILDEAT 449
Cdd:PRK13539 90 VAENLEfwaafLG----GEELDIAAALEAVGLAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPT 155
|
170 180
....*....|....*....|....*...
gi 2217288354 450 SALDAESEYLIQQAIHGNLQKHTVLIIA 477
Cdd:PRK13539 156 AALDAAAVALFAELIRAHLAQGGIVIAA 183
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
295-509 |
2.00e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 95.42 E-value: 2.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 295 RPHTQV--LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDH---KYLHRVISLVSQ--- 366
Cdd:PRK11308 23 KPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeaqKLLRQKIQIVFQnpy 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 367 --------------EPVLfarsITDNISyglptvpfemVVEAAQKANAhgfiMELQDGYSTE-TGEKGAQLSGGQKQRVA 431
Cdd:PRK11308 103 gslnprkkvgqileEPLL----INTSLS----------AAERREKALA----MMAKVGLRPEhYDRYPHMFSGGQRQRIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 432 MARALVRNPPVLILDEATSALDAEseylIQQAIHG---NLQKH---TVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQ 504
Cdd:PRK11308 165 IARALMLDPDVVVADEPVSALDVS----VQAQVLNlmmDLQQElglSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKE 240
|
....*
gi 2217288354 505 QLLAQ 509
Cdd:PRK11308 241 QIFNN 245
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
283-502 |
2.56e-21 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 95.78 E-value: 2.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylHRVIS 362
Cdd:PRK09452 15 VELRGISKSFDG---KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 LVSQEPVLFAR-SITDNISYGL--PTVPFE----MVVEAAQKANAHGFImelqdgystetGEKGAQLSGGQKQRVAMARA 435
Cdd:PRK09452 90 TVFQSYALFPHmTVFENVAFGLrmQKTPAAeitpRVMEALRMVQLEEFA-----------QRKPHQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217288354 436 LVRNPPVLILDEATSALDAESEYLIQQAIHGnLQKH---TVLIIAH----RLSTVEHahlIVVLDKGRVVQQGT 502
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELKA-LQRKlgiTFVFVTHdqeeALTMSDR---IVVMRDGRIEQDGT 228
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
286-502 |
2.92e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 93.22 E-value: 2.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 286 ENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVS 365
Cdd:COG4604 5 KNVSKRYGG---KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 366 QEPVLFAR-SITDNISYG-------LPTVPFEMVVEAAqkanahgfI-----MELQDGYSTEtgekgaqLSGGQKQR--V 430
Cdd:COG4604 82 QENHINSRlTVRELVAFGrfpyskgRLTAEDREIIDEA--------IayldlEDLADRYLDE-------LSGGQRQRafI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217288354 431 AMarALVRNPPVLILDEATSALD----AESEYLIQQAIHgNLQKhTVLIIAHRL---STveHAHLIVVLDKGRVVQQGT 502
Cdd:COG4604 147 AM--VLAQDTDYVLLDEPLNNLDmkhsVQMMKLLRRLAD-ELGK-TVVIVLHDInfaSC--YADHIVAMKDGRVVAQGT 219
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
300-508 |
4.51e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 93.24 E-value: 4.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 300 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFY-PLEG----GRVLLDGKPISAY-DHKYLHRVISLVSQEPVLFAR 373
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdKVSGyrysGDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 374 SITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD 453
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217288354 454 AESEYLIQQAIHGNLQKHTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLA 508
Cdd:PRK14271 196 PTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFS 251
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
283-526 |
5.41e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 93.13 E-value: 5.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYrtrPH-TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGkpISAYDHKYLH--- 358
Cdd:PRK13644 2 IRLENVSYSY---PDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKLQgir 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 359 RVISLVSQEP--VLFARSITDNISYG-----LPTVPFEMVVEAAqkanahgfIMELQDGYSTETGEKgaQLSGGQKQRVA 431
Cdd:PRK13644 77 KLVGIVFQNPetQFVGRTVEEDLAFGpenlcLPPIEIRKRVDRA--------LAEIGLEKYRHRSPK--TLSGGQGQCVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 432 MARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQK-HTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQG 510
Cdd:PRK13644 147 LAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
250
....*....|....*.
gi 2217288354 511 GLyaklvqrQMLGLQP 526
Cdd:PRK13644 227 SL-------QTLGLTP 235
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
283-502 |
7.57e-21 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 94.14 E-value: 7.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylHRVIS 362
Cdd:PRK11650 4 LKLQAVRKSYDGK--TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA--DRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 LVSQEPVLFAR-SITDNISYGLPT--VP----FEMVVEAAQkanahgfIMELQ---DgystetgEKGAQLSGGQKQRVAM 432
Cdd:PRK11650 80 MVFQNYALYPHmSVRENMAYGLKIrgMPkaeiEERVAEAAR-------ILELEpllD-------RKPRELSGGQRQRVAM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 433 ARALVRNPPVLILDEATSALDA--------EseylIQQaihgnLQKhtvliiahRLST----VEH--------AHLIVVL 492
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLDAklrvqmrlE----IQR-----LHR--------RLKTtslyVTHdqveamtlADRVVVM 208
|
250
....*....|
gi 2217288354 493 DKGRVVQQGT 502
Cdd:PRK11650 209 NGGVAEQIGT 218
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
4-227 |
9.26e-21 |
|
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: 92.56 E-value: 9.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 4 FSTAVVIVCLLAIGSSFAA---GIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISR----------LTS 70
Cdd:cd18588 38 LSTLDVLAIGLLVVALFEAvlsGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFESRQVGDTVARvrelesirqfLTG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 71 DT-TMVSDLVSqnINVFLrntvkvtgvvVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEE 149
Cdd:cd18588 118 SAlTLVLDLVF--SVVFL----------AVMFYYSPTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVE 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217288354 150 TISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAF 227
Cdd:cd18588 186 TVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLVMDGELTIGQLIAF 263
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
286-499 |
1.00e-20 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 90.96 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 286 ENVTFTYRTRPHT-QVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENfypLE---GGRVLLDGKPISAYDHKYLHRV- 360
Cdd:COG4181 12 RGLTKTVGTGAGElTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAG---LDrptSGTVRLAGQDLFALDEDARARLr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 361 ---ISLVSQE----PVLFARsitDNIsyglpTVPFEM--VVEAAQKANAhgfimELQD-GYSTETGEKGAQLSGGQKQRV 430
Cdd:COG4181 89 arhVGFVFQSfqllPTLTAL---ENV-----MLPLELagRRDARARARA-----LLERvGLGHRLDHYPAQLSGGEQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217288354 431 AMARALVRNPPVLILDEATSALDAESEYLIQQAIHG-NLQKHTVLIIA-HRLSTVEHAHLIVVLDKGRVVQ 499
Cdd:COG4181 156 ALARAFATEPAILFADEPTGNLDAATGEQIIDLLFElNRERGTTLVLVtHDPALAARCDRVLRLRAGRLVE 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
286-502 |
1.02e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 92.42 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 286 ENVTFTY--RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKY--LHRVI 361
Cdd:PRK13637 6 ENLTHIYmeGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLsdIRKKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 362 SLVSQEP--VLFARSITDNISYGlptvPFEMVVEAAQKANAHGFIMELQdGYSTET-GEKGA-QLSGGQKQRVAMARALV 437
Cdd:PRK13637 86 GLVFQYPeyQLFEETIEKDIAFG----PINLGLSEEEIENRVKRAMNIV-GLDYEDyKDKSPfELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217288354 438 RNPPVLILDEATSALD--AESEYLIQ-QAIHGNlQKHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGT 502
Cdd:PRK13637 161 MEPKILILDEPTAGLDpkGRDEILNKiKELHKE-YNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGT 228
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
286-463 |
1.28e-20 |
|
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: 90.57 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 286 ENV--TFTYRTRPHTQ--VLQNVSFSLSPGKVTALVGPSGSGKSS---CvnILENFYPlEGGRVLL--DGKPI---SAYD 353
Cdd:COG4778 8 ENLskTFTLHLQGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTllkC--IYGNYLP-DSGSILVrhDGGWVdlaQASP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 354 HKYLH---RVISLVSQepvlFARSItdnisyglPTVP-FEMVVEAAqkanahgfimeLQDGYSTETG-EKGAQL------ 422
Cdd:COG4778 85 REILAlrrRTIGYVSQ----FLRVI--------PRVSaLDVVAEPL-----------LERGVDREEArARARELlarlnl 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217288354 423 ------------SGGQKQRVAMARALVRNPPVLILDEATSALDAESE----YLIQQA 463
Cdd:COG4778 142 perlwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRavvvELIEEA 198
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
300-501 |
1.46e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 94.73 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 300 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV-ISLVSQEPVLFAR-SITD 377
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgIYLVPQEPLLFPNlSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 378 NISYGLPTVPfemvvEAAQKANAhgFIMELqdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD-AES 456
Cdd:PRK15439 106 NILFGLPKRQ-----ASMQKMKQ--LLAAL--GCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTpAET 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2217288354 457 EYLIQQaIHGNLQK-HTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQG 501
Cdd:PRK15439 177 ERLFSR-IRELLAQgVGIVFISHKLPEIrQLADRISVMRDGTIALSG 222
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
283-501 |
1.85e-20 |
|
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: 89.65 E-value: 1.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHkylHRvIS 362
Cdd:cd03269 1 LEVENVTKRFGR---VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAAR---NR-IG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 LVSQEPVLF-ARSITDNISY-----GLPTvpfemvvEAAQKANAHGF----IMELQDgystetgEKGAQLSGGQKQRVAM 432
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVYlaqlkGLKK-------EEARRRIDEWLerleLSEYAN-------KRVEELSKGNQQKVQF 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217288354 433 ARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQK-HTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQG 501
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
293-513 |
2.56e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 94.73 E-value: 2.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 293 RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYP---LEGGRVLLDGKPIsayDHKYLHRVISLVSQepv 369
Cdd:TIGR00955 33 RERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPI---DAKEMRAISAYVQQ--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 370 lfarsitDNISYGLPTVPFEMVVEAAQKANAHGFI-------------MELQDGYSTETGEKGAQ--LSGGQKQRVAMAR 434
Cdd:TIGR00955 107 -------DDLFIPTLTVREHLMFQAHLRMPRRVTKkekrervdevlqaLGLRKCANTRIGVPGRVkgLSGGERKRLAFAS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 435 ALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQK-HTVLIIAHRLST--VEHAHLIVVLDKGRVVQQGTHQQL---LA 508
Cdd:TIGR00955 180 ELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKgKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAvpfFS 259
|
....*
gi 2217288354 509 QGGLY 513
Cdd:TIGR00955 260 DLGHP 264
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
283-511 |
3.07e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 91.32 E-value: 3.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISaYDHKylhRVIS 362
Cdd:COG4152 2 LELKGLTKRFGDK---TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-PEDR---RRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 LVSQEPVLFAR-SITDNISY-----GLPtvpfemvvEAAQKANAHGFI--MELQDgYSTETGEKgaqLSGGQKQRVAMAR 434
Cdd:COG4152 75 YLPEERGLYPKmKVGEQLVYlarlkGLS--------KAEAKRRADEWLerLGLGD-RANKKVEE---LSKGNQQKVQLIA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 435 ALVRNPPVLILDEATSALDAESEYLIQQAIhgnLQKH----TVLIIAHRLSTVE----HahlIVVLDKGRVVQQGTHQQL 506
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDPVNVELLKDVI---RELAakgtTVIFSSHQMELVEelcdR---IVIINKGRKVLSGSVDEI 216
|
....*
gi 2217288354 507 LAQGG 511
Cdd:COG4152 217 RRQFG 221
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
300-477 |
4.34e-20 |
|
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: 88.32 E-value: 4.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 300 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPIsAYDHKYLHRVISLVSQEPVLFAR-SITDN 378
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-DFQRDSIARGLLYLGHAPGIKTTlSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 379 ISYGLPTVPFEMVVEAAQKANAHGFimelqdgysteTGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEY 458
Cdd:cd03231 94 LRFWHADHSDEQVEEALARVGLNGF-----------EDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170
....*....|....*....
gi 2217288354 459 LIQQAIHGNLQKHTVLIIA 477
Cdd:cd03231 163 RFAEAMAGHCARGGMVVLT 181
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
12-230 |
4.97e-20 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 90.60 E-value: 4.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 12 CLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFdENR-TGDLISRLTSDTTMVSDLVSQNINVFLrNT 90
Cdd:cd18567 49 GLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYF-EKRhLGDIVSRFGSLDEIQQTLTTGFVEALL-DG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 91 VKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVY 170
Cdd:cd18567 127 LMAILTLVMMFLYSPKLALIVLAAVALYALLRLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARW 206
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 171 LRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIY 230
Cdd:cd18567 207 LNLLVDAINADIRLQRLQILFSAANGLLFGLENILVIYLGALLVLDGEFTVGMLFAFLAY 266
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
289-508 |
6.12e-20 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 89.85 E-value: 6.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 289 TFTYRT----RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLV 364
Cdd:PRK15112 13 TFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 365 SQEPvlfARSITDNISYG-LPTVPFEMVVEAAQKANAHGFIMEL-QDGYSTE-TGEKGAQLSGGQKQRVAMARALVRNPP 441
Cdd:PRK15112 93 FQDP---STSLNPRQRISqILDFPLRLNTDLEPEQREKQIIETLrQVGLLPDhASYYPHMLAPGQKQRLGLARALILRPK 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217288354 442 VLILDEATSALDAEseyLIQQAIHGNL---QKHTV--LIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLA 508
Cdd:PRK15112 170 VIIADEALASLDMS---MRSQLINLMLelqEKQGIsyIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLA 239
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
295-477 |
6.36e-20 |
|
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: 87.80 E-value: 6.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 295 RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYlHRVISLVSQEPVLFAR- 373
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP-HENILYLGHLPGLKPEl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 374 SITDNISYGLPTVPFE--MVVEAAQKANAHGFimelqdgysteTGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSA 451
Cdd:TIGR01189 89 SALENLHFWAAIHGGAqrTIEDALAAVGLTGF-----------EDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180
....*....|....*....|....*.
gi 2217288354 452 LDAESEYLIQQAIHGNLQKHTVLIIA 477
Cdd:TIGR01189 158 LDKAGVALLAGLLRAHLARGGIVLLT 183
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
8-229 |
6.46e-20 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 90.31 E-value: 6.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 8 VVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFL 87
Cdd:cd18568 45 LIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRFQENQKIRRFLTRSALTTIL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 88 rNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEE-- 165
Cdd:cd18568 125 -DLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPir 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217288354 166 ---EAEvYLRKLQQVYKLNRKEAAAYMyyvwGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFII 229
Cdd:cd18568 204 wrwENK-FAKALNTRFRGQKLSIVLQL----ISSLINHLGTIAVLWYGAYLVISGQLTIGQLVAFNM 265
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
284-507 |
7.69e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 89.34 E-value: 7.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 284 DFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEG------GRVLLDGKPISAYDHKYL 357
Cdd:PRK14246 9 DVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDskikvdGKVLYFGKDIFQIDAIKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 358 HRVISLVSQEPVLFAR-SITDNISYGLPTVPFE-------MVVEAAQKAnahGFIMELQDGYSTetgeKGAQLSGGQKQR 429
Cdd:PRK14246 89 RKEVGMVFQQPNPFPHlSIYDNIAYPLKSHGIKekreikkIVEECLRKV---GLWKEVYDRLNS----PASQLSGGQQQR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217288354 430 VAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLL 507
Cdd:PRK14246 162 LTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
283-515 |
9.15e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 89.48 E-value: 9.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRPHtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 362
Cdd:PRK13652 4 IETRDLCYSYSGSKE--ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 LVSQEP--VLFARSITDNISYG-----LPTVPFEMVVEAAQKANAhgfIMELQDgystetgEKGAQLSGGQKQRVAMARA 435
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGpinlgLDEETVAHRVSSALHMLG---LEELRD-------RVPHHLSGGEKKRVAIAGV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 436 LVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKH--TVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLAQGGL 512
Cdd:PRK13652 152 IAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYgmTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQPDL 231
|
...
gi 2217288354 513 YAK 515
Cdd:PRK13652 232 LAR 234
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
9-447 |
1.68e-19 |
|
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: 91.78 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 9 VIVCLLAIGSSFAAGIRggiFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSqNINVFLR 88
Cdd:COG4615 55 AGLLVLLLLSRLASQLL---LTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFV-RLPELLQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 89 NTVKVTGVVVFMFSLSWQLSLVTFmgfpiIMMVSNIYGkyYKRLSKEVQNALARASNTAEETISAMKTV----------- 157
Cdd:COG4615 131 SVALVLGCLAYLAWLSPPLFLLTL-----VLLGLGVAG--YRLLVRRARRHLRRAREAEDRLFKHFRALlegfkelklnr 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 158 ---RSFANEEeeaevYLRKLQQVYKLNRKEAAAYMYYV-WGSgLTLLVVQVSILYYGGHLV-ISGQMTSGnlIAFIIYeF 232
Cdd:COG4615 204 rrrRAFFDED-----LQPTAERYRDLRIRADTIFALANnWGN-LLFFALIGLILFLLPALGwADPAVLSG--FVLVLL-F 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 233 VLGDcMESVGSVYSGLMQGVGAAEKVFEF---IDRQPTMVHDGSLAPDHLE-GRVDFENVTFTYRTRPHTQ--VLQNVSF 306
Cdd:COG4615 275 LRGP-LSQLVGALPTLSRANVALRKIEELelaLAAAEPAAADAAAPPAPADfQTLELRGVTYRYPGEDGDEgfTLGPIDL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 307 SLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISA--YDHkYLHRvISLVSQEPVLFARsitdniSYGLP 384
Cdd:COG4615 354 TIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTAdnREA-YRQL-FSAVFSDFHLFDR------LLGLD 425
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217288354 385 TVPfemvveAAQKANAHGFIMELQ------DGYSTETgekgaQLSGGQKQRVAMARALVRNPPVLILDE 447
Cdd:COG4615 426 GEA------DPARARELLERLELDhkvsveDGRFSTT-----DLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
283-502 |
2.56e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 88.26 E-value: 2.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYR--TRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAY----DHKY 356
Cdd:PRK13649 3 INLQNVSYTYQagTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 357 LHRVISLVSQ--EPVLFARSITDNISYGLPTvpFEMVVEAAQKANAHGFIMElqdGYSTETGEKGA-QLSGGQKQRVAMA 433
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQN--FGVSQEEAEALAREKLALV---GISESLFEKNPfELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217288354 434 RALVRNPPVLILDEATSALDA----ESEYLIQQAIHGNLqkhTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGT 502
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPkgrkELMTLFKKLHQSGM---TIVLVTHLMDDVaNYADFVYVLEKGKLVLSGK 228
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
300-506 |
3.20e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 89.51 E-value: 3.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 300 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISayDHKYLHRVISLVSQEPVLFAR-SITDN 378
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPINMMFQSYALFPHmTVEQN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 379 ISYGLPTVPFEMVvEAAQKANAHGFIMELQDgystETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEY 458
Cdd:PRK11607 112 IAFGLKQDKLPKA-EIASRVNEMLGLVHMQE----FAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRD 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2217288354 459 LIQQAIHGNLQK--HTVLIIAH-RLSTVEHAHLIVVLDKGRVVQQGTHQQL 506
Cdd:PRK11607 187 RMQLEVVDILERvgVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
301-507 |
3.68e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 86.82 E-value: 3.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 301 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGgRVLLDGKPISAYDHKYLHRVIS-LVSQEPVLFARSITDNI 379
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQG-EILLNGRPLSDWSAAELARHRAyLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 380 SYGLPTVPFEMVVEA--AQKANAhgfiMELQDGYSTETGekgaQLSGGQKQRVAMARALVR-----NPP--VLILDEATS 450
Cdd:COG4138 91 ALHQPAGASSEAVEQllAQLAEA----LGLEDKLSRPLT----QLSGGEWQRVRLAAVLLQvwptiNPEgqLLLLDEPMN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217288354 451 ALDaeseyLIQQAIHGNL------QKHTVLIIAHRLS-TVEHAHLIVVLDKGRVVQQGTHQQLL 507
Cdd:COG4138 163 SLD-----VAQQAALDRLlrelcqQGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
283-503 |
5.21e-19 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 86.61 E-value: 5.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCV---NILEnfYPLEGGRVLLDGK-----PISAYDH 354
Cdd:COG4161 3 IQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLrvlNLLE--TPDSGQLNIAGHQfdfsqKPSEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 355 KYLHRVISLVSQEPVLFA-RSITDNISYGlPTVPFEMVVEAAQ-KANAHGFIMELQDgystETGEKGAQLSGGQKQRVAM 432
Cdd:COG4161 78 RLLRQKVGMVFQQYNLWPhLTVMENLIEA-PCKVLGLSKEQAReKAMKLLARLRLTD----KADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217288354 433 ARALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQKH--TVLIIAHRlstVEHAHLI----VVLDKGRVVQQGTH 503
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDPEITAQVVEIIR-ELSQTgiTQVIVTHE---VEFARKVasqvVYMEKGRIIEQGDA 225
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
283-506 |
5.23e-19 |
|
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: 85.88 E-value: 5.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAyDHKYLHRVIS 362
Cdd:cd03265 1 IEVENLVKKYGD---FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 LVSQEPVLfARSIT--DNIS-----YGLPTvpfemvVEAAQKanahgfIMELQDGYstETGEKGAQL----SGGQKQRVA 431
Cdd:cd03265 77 IVFQDLSV-DDELTgwENLYiharlYGVPG------AERRER------IDELLDFV--GLLEAADRLvktySGGMRRRLE 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217288354 432 MARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKH--TVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQL 506
Cdd:cd03265 142 IARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
299-501 |
5.49e-19 |
|
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: 85.79 E-value: 5.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 299 QVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILEN---FYPLEGGRVLLDGKPISAYDHKYlhrVISLVSQEPVlFARSI 375
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPRKPDQFQK---CVAYVRQDDI-LLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 376 T--DNISYglpTVPFEMVVEA--AQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSA 451
Cdd:cd03234 97 TvrETLTY---TAILRLPRKSsdAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217288354 452 LDAESEYLI----QQAIHGNlqkHTVLIIAH--RLSTVEHAHLIVVLDKGRVVQQG 501
Cdd:cd03234 174 LDSFTALNLvstlSQLARRN---RIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
286-523 |
6.71e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 86.10 E-value: 6.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 286 ENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLV 364
Cdd:PRK10895 7 KNLAKAYKGR---RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 365 SQEPVLFAR-SITDNISYGLPT---VPFEMVVEAAQKANAHGFIMELQDGYstetgekGAQLSGGQKQRVAMARALVRNP 440
Cdd:PRK10895 84 PQEASIFRRlSVYDNLMAVLQIrddLSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARALAANP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 441 PVLILDEATSALDAESEYLIQQAI-HGNLQKHTVLIIAHR----LSTVEHAHLIvvlDKGRVVQQGTHQQLLAQgglyaK 515
Cdd:PRK10895 157 KFILLDEPFAGVDPISVIDIKRIIeHLRDSGLGVLITDHNvretLAVCERAYIV---SQGHLIAHGTPTEILQD-----E 228
|
....*...
gi 2217288354 516 LVQRQMLG 523
Cdd:PRK10895 229 HVKRVYLG 236
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
283-507 |
1.45e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 87.19 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAydHKYLHRV-I 361
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA--RARLARArI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 362 SLVSQ----EPVLFARsitDNI-----SYGLPTVPFEMVV----EAAQ---KANAhgfimelqdgystetgeKGAQLSGG 425
Cdd:PRK13536 117 GVVPQfdnlDLEFTVR---ENLlvfgrYFGMSTREIEAVIpsllEFARlesKADA-----------------RVSDLSGG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 426 QKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQK-HTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTH 503
Cdd:PRK13536 177 MKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARgKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRP 256
|
....
gi 2217288354 504 QQLL 507
Cdd:PRK13536 257 HALI 260
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
297-502 |
1.60e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 84.87 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 297 HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPI----SAYDHKYLHRVISLVSQepvlFA 372
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklsSAAKAELRNQKLGFIYQ----FH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 373 RSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSAL 452
Cdd:PRK11629 97 HLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2217288354 453 DAESEYLIQQAIhGNL---QKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGT 502
Cdd:PRK11629 177 DARNADSIFQLL-GELnrlQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
283-508 |
1.79e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 86.40 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 362
Cdd:PRK13537 8 IDFRNVEKRYGDK---LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 L-----------VSQEPVLFARSitdnisYGLPT------VPfeMVVEAA---QKANAhgfimelqdgystetgeKGAQL 422
Cdd:PRK13537 85 VpqfdnldpdftVRENLLVFGRY------FGLSAaaaralVP--PLLEFAkleNKADA-----------------KVGEL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 423 SGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQK-HTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQ 500
Cdd:PRK13537 140 SGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARgKTILLTTHFMEEAERlCDRLCVIEEGRKIAE 219
|
....*...
gi 2217288354 501 GTHQQLLA 508
Cdd:PRK13537 220 GAPHALIE 227
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
301-507 |
1.81e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 87.40 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 301 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV----ISLVSQEPVLFAR-SI 375
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 376 TDNISYG--LPTVPFEMVVEAAQKANAHGFIMELQDGYSTEtgekgaqLSGGQKQRVAMARALVRNPPVLILDEATSALD 453
Cdd:PRK10070 124 LDNTAFGmeLAGINAEERREKALDALRQVGLENYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217288354 454 A------ESEYLIQQAIHgnlqKHTVLIIAHRL-STVEHAHLIVVLDKGRVVQQGTHQQLL 507
Cdd:PRK10070 197 PlirtemQDELVKLQAKH----QRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
281-516 |
1.88e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 85.83 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 281 GRVDFENVTFTY--RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISA-----YD 353
Cdd:PRK13645 5 KDIILDNVSYTYakKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkiKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 354 HKYLHRVISLVSQEP--VLFARSITDNISYGlptvPFEMvveAAQKANAHGFIMELQDGYS--TETGEKGA-QLSGGQKQ 428
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIAFG----PVNL---GENKQEAYKKVPELLKLVQlpEDYVKRSPfELSGGQKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 429 RVAMARALVRNPPVLILDEATSALD--AESEYL-IQQAIHGNlQKHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQ 504
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDpkGEEDFInLFERLNKE-YKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSPF 236
|
250
....*....|..
gi 2217288354 505 QLLAQGGLYAKL 516
Cdd:PRK13645 237 EIFSNQELLTKI 248
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
286-504 |
2.53e-18 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 84.30 E-value: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 286 ENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCV---NILEnfYPLEG-----GRVLLDGKPISAYDHKYL 357
Cdd:PRK11124 6 NGINCFYGA---HQALFDITLDCPQGETLVLLGPSGAGKSSLLrvlNLLE--MPRSGtlniaGNHFDFSKTPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 358 HRVISLVSQEPVLFAR-SITDNisygLPTVPfeMVVEAAQKANAHGFIMELQDGYS-TETGEK-GAQLSGGQKQRVAMAR 434
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHlTVQQN----LIEAP--CRVLGLSKDQALARAEKLLERLRlKPYADRfPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217288354 435 ALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKH-TVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQ 504
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGiTQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
283-530 |
2.90e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 85.17 E-value: 2.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRP--HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFY-PLEGGRVLLDGKPISAYDHKYLHR 359
Cdd:PRK13643 2 IKFEKVNYTYQPNSpfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLqPTEGKVTVGDIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 360 V---ISLVSQEP--VLFARSITDNISYGLPTvpFEMVVEAAQKANAHGFIMElqdGYSTETGEKGA-QLSGGQKQRVAMA 433
Cdd:PRK13643 82 VrkkVGVVFQFPesQLFEETVLKDVAFGPQN--FGIPKEKAEKIAAEKLEMV---GLADEFWEKSPfELSGGQMRRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 434 RALVRNPPVLILDEATSALDAESEYLIQ---QAIHGNLQkhTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLAQ 509
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKARIEMMqlfESIHQSGQ--TVVLVTHLMDDVaDYADYVYLLEKGHIISCGTPSDVFQE 234
|
250 260
....*....|....*....|.
gi 2217288354 510 gglyAKLVQRQMLGLQPAADF 530
Cdd:PRK13643 235 ----VDFLKAHELGVPKATHF 251
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
286-507 |
2.96e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 84.84 E-value: 2.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 286 ENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHR-VISLV 364
Cdd:PRK10575 15 RNVSFRV---PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARkVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 365 SQEPVLFARSITDNISYGlpTVPF------------EMVVEAAQKANAHGFIMELQDgystetgekgaQLSGGQKQRVAM 432
Cdd:PRK10575 92 QQLPAAEGMTVRELVAIG--RYPWhgalgrfgaadrEKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217288354 433 ARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKH--TVLIIAHRLS-TVEHAHLIVVLDKGRVVQQGTHQQLL 507
Cdd:PRK10575 159 AMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELM 236
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
4-227 |
3.90e-18 |
|
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: 84.87 E-value: 3.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 4 FSTAVVIVCLLAIGSSFaagIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSdTTMVSDLVSQNI 83
Cdd:cd18555 44 LGIGILILFLLYGLFSF---LRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFENRSSGDLLFRANS-NVYIRQILSNQV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 84 NVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANE 163
Cdd:cd18555 120 ISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSE 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217288354 164 EEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAF 227
Cdd:cd18555 200 KNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLILWIGAYLVINGELTLGELIAF 263
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
301-478 |
5.86e-18 |
|
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: 82.90 E-value: 5.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 301 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLhrvisLVSQEPVLFA-RSITDNI 379
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 380 SYGLPTVPFEMVVEAAQKANAHGFIMElqdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYL 459
Cdd:TIGR01184 76 ALAVDRVLPDLSKSERRAIVEEHIALV---GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180
....*....|....*....|.
gi 2217288354 460 IQQAIHGNLQKH--TVLIIAH 478
Cdd:TIGR01184 153 LQEELMQIWEEHrvTVLMVTH 173
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
40-230 |
6.59e-18 |
|
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: 84.39 E-value: 6.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 40 LRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIM 119
Cdd:cd18554 81 IRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 120 MVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAaymyyvWgSGLTL 199
Cdd:cd18554 161 LAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTR------W-NAKTF 233
|
170 180 190
....*....|....*....|....*....|....*...
gi 2217288354 200 LVVQVS-------ILYYGGHLVISGQMTSGNLIAFIIY 230
Cdd:cd18554 234 SAVNTItdlapllVIGFAAYLVIEGNLTVGTLVAFVGY 271
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
301-526 |
8.45e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 86.14 E-value: 8.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 301 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLE--GGRVLLDGKPISAYDHKYLHRV-ISLVSQEPVLFAR-SIT 376
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIRDTERAgIAIIHQELALVKElSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 377 DNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETgeKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALdAES 456
Cdd:PRK13549 101 ENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPAT--PVGNLGLGQQQLVEIAKALNKQARLLILDEPTASL-TES 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217288354 457 EYLIQQAIHGNLQKHTV--LIIAHRLSTVEH-AHLIVVLDKGRVVqqGTH-QQLLAQGGLYAKLVQRQMLGLQP 526
Cdd:PRK13549 178 ETAVLLDIIRDLKAHGIacIYISHKLNEVKAiSDTICVIRDGRHI--GTRpAAGMTEDDIITMMVGRELTALYP 249
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
282-501 |
9.70e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 82.83 E-value: 9.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 282 RVDFENVTFTyrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKS-SCVNILENFYP---LEGGRVLLDGKPISAYDHKyl 357
Cdd:PRK10418 4 QIELRNIALQ----AAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPAgvrQTAGRVLLDGKPVAPCALR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 358 HRVISLVSQEPvlfaRSITDNI----SYGLPTvpfemvVEAAQKANAHGFIMELQDGYSTETGEKGAQL-----SGGQKQ 428
Cdd:PRK10418 78 GRKIATIMQNP----RSAFNPLhtmhTHARET------CLALGKPADDATLTAALEAVGLENAARVLKLypfemSGGMLQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217288354 429 RVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHT--VLIIAHRLSTVEH-AHLIVVLDKGRVVQQG 501
Cdd:PRK10418 148 RMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARlADDVAVMSHGRIVEQG 223
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
283-502 |
1.14e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 85.99 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV-I 361
Cdd:PRK09700 6 ISMAGIGKSF---GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 362 SLVSQE-PVLFARSITDNISYG-LPT-----VPF----EMVVEAAqkanahgfIMELQDGYSTETGEKGAQLSGGQKQRV 430
Cdd:PRK09700 83 GIIYQElSVIDELTVLENLYIGrHLTkkvcgVNIidwrEMRVRAA--------MMLLRVGLKVDLDEKVANLSISHKQML 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217288354 431 AMARALVRNPPVLILDEATSAL-DAESEYLIqqAIHGNLQKH--TVLIIAHRLstvehAHLIVVLDKGRVVQQGT 502
Cdd:PRK09700 155 EIAKTLMLDAKVIIMDEPTSSLtNKEVDYLF--LIMNQLRKEgtAIVYISHKL-----AEIRRICDRYTVMKDGS 222
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
285-495 |
1.67e-17 |
|
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: 80.75 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 285 FENVTFTYRT-RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILEN--FYPLEGGRVLLDGKPISaydhKYLHRVI 361
Cdd:cd03232 6 WKNLNYTVPVkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLD----KNFQRST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 362 SLVSQEPVLFarsitdnisyglptvPFEMVVEAAQ-KANAHGfimelqdgystetgekgaqLSGGQKQRVAMARALVRNP 440
Cdd:cd03232 82 GYVEQQDVHS---------------PNLTVREALRfSALLRG-------------------LSVEQRKRLTIGVELAAKP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217288354 441 PVLILDEATSALDAESEYLIQQAIHgNLQKH--TVLIIAHRLSTV--EHAHLIVVLDKG 495
Cdd:cd03232 128 SILFLDEPTSGLDSQAAYNIVRFLK-KLADSgqAILCTIHQPSASifEKFDRLLLLKRG 185
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
285-510 |
1.90e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 82.76 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 285 FENVTFTY--RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISA----YDHKYLH 358
Cdd:PRK13634 5 FQKVEHRYqyKTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkknKKLKPLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 359 RVISLVSQ--EPVLFARSITDNISYGlPT---VPFEmvvEAAQKANAhgfIMELQdGYSTETGEKGA-QLSGGQKQRVAM 432
Cdd:PRK13634 85 KKVGIVFQfpEHQLFEETVEKDICFG-PMnfgVSEE---DAKQKARE---MIELV-GLPEELLARSPfELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 433 ARALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQKH---TVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLA 508
Cdd:PRK13634 157 AGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFY-KLHKEkglTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFA 235
|
..
gi 2217288354 509 QG 510
Cdd:PRK13634 236 DP 237
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
11-532 |
3.97e-17 |
|
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: 85.35 E-value: 3.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 11 VCLLAIGSSFAagIRGGIFTL--IFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISrltsdttmvsdLVSQNINVF-- 86
Cdd:TIGR01271 128 LCLLFIVRTLL--LHPAIFGLhhLGMQMRIALFSLIYKKTLKLSSRVLDKISTGQLVS-----------LLSNNLNKFde 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 87 ---LRNTVKVTGV-VVFMFSLSWQL---SLVTFMGFPIIMMV-----SNIYGKYYKRLSKEVQNALARASntaeETISAM 154
Cdd:TIGR01271 195 glaLAHFVWIAPLqVILLMGLIWELlevNGFCGLGFLILLALfqaclGQKMMPYRDKRAGKISERLAITS----EIIENI 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 155 KTVRSFAnEEEEAEVYLRKLQQV-YKLNRKeaAAYMYYVWGSGL---TLLVVQVSILYYGghlvISGQMTSGNLIAFIIY 230
Cdd:TIGR01271 271 QSVKAYC-WEEAMEKIIKNIRQDeLKLTRK--IAYLRYFYSSAFffsGFFVVFLSVVPYA----LIKGIILRRIFTTISY 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 231 EFVLgdcMESVGSVYSGLMQ----GVGAAEKVFEFIDRQPTMVHDGSLAPDHLEgrvdFENVT----------------- 289
Cdd:TIGR01271 344 CIVL---RMTVTRQFPGAIQtwydSLGAITKIQDFLCKEEYKTLEYNLTTTEVE----MVNVTaswdegigelfekikqn 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 290 --------------FTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVN-ILENFYPLEGgRVLLDGKpisaydh 354
Cdd:TIGR01271 417 nkarkqpngddglfFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMmIMGELEPSEG-KIKHSGR------- 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 355 kylhrvISLVSQEPVLFARSITDNISYGLPTVPFEM--VVEAAQKANAhgfIMELQDGYSTETGEKGAQLSGGQKQRVAM 432
Cdd:TIGR01271 489 ------ISFSPQTSWIMPGTIKDNIIFGLSYDEYRYtsVIKACQLEED---IALFPEKDKTVLGEGGITLSGGQRARISL 559
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 433 ARALVRNPPVLILDEATSALDAESEYLI-QQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQGG 511
Cdd:TIGR01271 560 ARAVYKDADLYLLDSPFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRP 639
|
570 580
....*....|....*....|.
gi 2217288354 512 LYAKlvqrQMLGLQPAADFTA 532
Cdd:TIGR01271 640 DFSS----LLLGLEAFDNFSA 656
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
294-529 |
4.46e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 83.35 E-value: 4.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 294 TRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVISLVSQEPvlfar 373
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDT----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 374 sitdnisyglpTVPFEMVVEAAQKANAHGFIMELqdGYSTETGEKGAQ------------------LSGGQKQRVAMARA 435
Cdd:PRK09536 87 -----------SLSFEFDVRQVVEMGRTPHRSRF--DTWTETDRAAVEramertgvaqfadrpvtsLSGGERQRVLLARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 436 LVRNPPVLILDEATSALD--------------AESEYLIQQAIHGnlqkhtvLIIAHRlstveHAHLIVVLDKGRVVQQG 501
Cdd:PRK09536 154 LAQATPVLLLDEPTASLDinhqvrtlelvrrlVDDGKTAVAAIHD-------LDLAAR-----YCDELVLLADGRVRAAG 221
|
250 260
....*....|....*....|....*...
gi 2217288354 502 THQQLLAQGGLYAKLVQRQMLGLQPAAD 529
Cdd:PRK09536 222 PPADVLTADTLRAAFDARTAVGTDPATG 249
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
283-498 |
8.55e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 79.53 E-value: 8.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTrpHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHK---YLHR 359
Cdd:PRK10908 2 IRFEHVSKAYLG--GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 360 VISLVSQEP-VLFARSITDNISygLPtvpfeMVVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAMARAL 436
Cdd:PRK10908 80 QIGMIFQDHhLLMDRTVYDNVA--IP-----LIIAGASGDDIRRRVSAALDkvGLLDKAKNFPIQLSGGEQQRVGIARAV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217288354 437 VRNPPVLILDEATSALD-AESEYLIQQAIHGNLQKHTVLIIAHRLSTVE-HAHLIVVLDKGRVV 498
Cdd:PRK10908 153 VNKPAVLLADEPTGNLDdALSEGILRLFEEFNRVGVTVLMATHDIGLISrRSYRMLTLSDGHLH 216
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
8-229 |
9.21e-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: 80.71 E-value: 9.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 8 VVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFL 87
Cdd:cd18782 45 GVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRISELDTIRGFLTGTALTTLL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 88 rNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEE--- 164
Cdd:cd18782 125 -DVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELkar 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217288354 165 -EEAEVYLRKLQQVYKLNRKEAAAYMYyvwgSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFII 229
Cdd:cd18782 204 wRWQNRYARSLGEGFKLTVLGTTSGSL----SQFLNKLSSLLVLWVGAYLVLRGELTLGQLIAFRI 265
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
1-229 |
9.54e-17 |
|
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: 80.70 E-value: 9.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 1 MDQFSTAVVIVCLLaigSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVS 80
Cdd:cd18566 41 LQVLVIGVVIAILL---ESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERLNSLEQIREFLTG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 81 QNINVFLrntvKVTGVVVF---MFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTV 157
Cdd:cd18566 118 QALLALL----DLPFVLIFlglIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTI 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217288354 158 RSFANEEEEAEVYLRKLQQ----VYKLNRKEAAAYMyyvwGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFII 229
Cdd:cd18566 194 KAMAMEPQMLRRYERLQANaayaGFKVAKINAVAQT----LGQLFSQVSMVAVVAFGALLVINGDLTVGALIACTM 265
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
301-526 |
1.08e-16 |
|
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: 82.95 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 301 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYP--LEGGRVLLDGKPISAYDHKYLHRV-ISLVSQEPVLFAR-SIT 376
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVPElSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 377 DNISYGLP-TVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGaQLSGGQKQRVAMARALVRNPPVLILDEATSAL-DA 454
Cdd:TIGR02633 97 ENIFLGNEiTLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVG-DYGGGQQQLVEIAKALNKQARLLILDEPSSSLtEK 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217288354 455 ESEYLIQqaIHGNLQKHTV--LIIAHRLSTVEhahliVVLDKGRVVQQGTH-----QQLLAQGGLYAKLVQRQMLGLQP 526
Cdd:TIGR02633 176 ETEILLD--IIRDLKAHGVacVYISHKLNEVK-----AVCDTICVIRDGQHvatkdMSTMSEDDIITMMVGREITSLYP 247
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
285-509 |
1.33e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 82.65 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 285 FENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPI---SAYDHkyLHRVI 361
Cdd:PRK11288 7 FDGIGKTF---PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAA--LAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 362 SLVSQE----PVLfarSITDNISYG-LPTvPFEMVVEAAQKANAHGFIMELQDGYSTETgeKGAQLSGGQKQRVAMARAL 436
Cdd:PRK11288 82 AIIYQElhlvPEM---TVAENLYLGqLPH-KGGIVNRRLLNYEAREQLEHLGVDIDPDT--PLKYLSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 437 VRNPPVLILDEATSALDA-ESEYLIqqAIHGNL--QKHTVLIIAHRLSTV-EHAHLIVVLDKGRVV------QQGTHQQL 506
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSArEIEQLF--RVIRELraEGRVILYVSHRMEEIfALCDAITVFKDGRYVatfddmAQVDRDQL 233
|
...
gi 2217288354 507 LAQ 509
Cdd:PRK11288 234 VQA 236
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
287-509 |
1.61e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 79.63 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 287 NVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENfyPLEGGrVLLDGKPIS----------AYD 353
Cdd:PRK10619 7 NVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTflrCINFLEK--PSEGS-IVVNGQTINlvrdkdgqlkVAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 354 HKYLHRV---ISLVSQEPVLFAR-SITDNISYGLPTVPFEMVVEAAQKA----NAHGFIMELQDGYStetgekgAQLSGG 425
Cdd:PRK10619 84 KNQLRLLrtrLTMVFQHFNLWSHmTVLENVMEAPIQVLGLSKQEARERAvkylAKVGIDERAQGKYP-------VHLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 426 QKQRVAMARALVRNPPVLILDEATSALDAE--SEYL-IQQAIHGnlQKHTVLIIAHRLSTVEH--AHLIvVLDKGRVVQQ 500
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALDPElvGEVLrIMQQLAE--EGKTMVVVTHEMGFARHvsSHVI-FLHQGKIEEE 233
|
....*....
gi 2217288354 501 GTHQQLLAQ 509
Cdd:PRK10619 234 GAPEQLFGN 242
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
293-501 |
2.06e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 82.21 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 293 RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPI---SAYDHKYLHRVISLVSQEPV 369
Cdd:PRK10261 332 RVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDPY 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 370 --LFAR-SITDNISYGLpTVPFEMVVEAAQKANAH-----GFIMELQDGYSTEtgekgaqLSGGQKQRVAMARALVRNPP 441
Cdd:PRK10261 412 asLDPRqTVGDSIMEPL-RVHGLLPGKAAAARVAWllervGLLPEHAWRYPHE-------FSGGQRQRICIARALALNPK 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217288354 442 VLILDEATSALDAESEYLIQQAIHgNLQKH---TVLIIAHRLSTVEH-AHLIVVLDKGRVVQQG 501
Cdd:PRK10261 484 VIIADEAVSALDVSIRGQIINLLL-DLQRDfgiAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
283-478 |
2.38e-16 |
|
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: 75.95 E-value: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVlldgkpisaydhkylhrvis 362
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV-------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 lvsqepvlfARSITDNISYglptvpFEmvveaaqkanahgfimelqdgystetgekgaQLSGGQKQRVAMARALVRNPPV 442
Cdd:cd03221 58 ---------TWGSTVKIGY------FE-------------------------------QLSGGEKMRLALAKLLLENPNL 91
|
170 180 190
....*....|....*....|....*....|....*.
gi 2217288354 443 LILDEATSALDAESEYLIQQAIHGnlQKHTVLIIAH 478
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKE--YPGTVILVSH 125
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
39-513 |
2.74e-16 |
|
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: 82.65 E-value: 2.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 39 RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVvFMFSLSWQLSLVTFMGFPII 118
Cdd:TIGR01271 959 RLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAI-FVVSVLQPYIFIAAIPVAVI 1037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 119 MMVSNIYgkyYKRLSKEVQNALARA-SNTAEETISAMK---TVRSFANEEeeaevYLRKLqqVYK-LNRKEAAAYMYYVW 193
Cdd:TIGR01271 1038 FIMLRAY---FLRTSQQLKQLESEArSPIFSHLITSLKglwTIRAFGRQS-----YFETL--FHKaLNLHTANWFLYLST 1107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 194 GSGLTLLVVQVSILYYGGHLVIS---GQMTSGNL-IAFIIYEFVLGDCMESVGSVYS--GLMQGVgaaEKVFEFIDRQP- 266
Cdd:TIGR01271 1108 LRWFQMRIDIIFVFFFIAVTFIAigtNQDGEGEVgIILTLAMNILSTLQWAVNSSIDvdGLMRSV---SRVFKFIDLPQe 1184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 267 ---------------TMVHDGSLAPDHL--EGRVDFENVTFTYrTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVN 329
Cdd:TIGR01271 1185 eprpsggggkyqlstVLVIENPHAQKCWpsGGQMDVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLS 1263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 330 ILENFYPLEGgRVLLDGKPISAYDHKYLHRVISLVSQEPVLFARSITDNISyglptvPFEM-----VVEAAQKANAHGFI 404
Cdd:TIGR01271 1264 ALLRLLSTEG-EIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD------PYEQwsdeeIWKVAEEVGLKSVI 1336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 405 MELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVE 484
Cdd:TIGR01271 1337 EQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALL 1416
|
490 500
....*....|....*....|....*....
gi 2217288354 485 HAHLIVVLDKGRVVQQGTHQQLLAQGGLY 513
Cdd:TIGR01271 1417 ECQQFLVIEGSSVKQYDSIQKLLNETSLF 1445
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
283-501 |
4.04e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 80.07 E-value: 4.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISayDHKYLHRVIS 362
Cdd:PRK11000 4 VTLRNVTKAYGD---VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN--DVPPAERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 LVSQEPVLFAR-SITDNISYGLPTVPFEMVvEAAQKANAHGFImeLQDGYSTETGEKGaqLSGGQKQRVAMARALVRNPP 441
Cdd:PRK11000 79 MVFQSYALYPHlSVAENMSFGLKLAGAKKE-EINQRVNQVAEV--LQLAHLLDRKPKA--LSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217288354 442 VLILDEATSALDAESEylIQQAI-----HGNLQKhTVLIIAHrlSTVEH---AHLIVVLDKGRVVQQG 501
Cdd:PRK11000 154 VFLLDEPLSNLDAALR--VQMRIeisrlHKRLGR-TMIYVTH--DQVEAmtlADKIVVLDAGRVAQVG 216
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
299-519 |
4.39e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 77.80 E-value: 4.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 299 QVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENF--YPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEPV------ 369
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSpDERARAGIFLAFQYPVeipgvs 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 370 --LFARSITDNISYGLPTVPfEMVVEAAQKANAHGFIMELQDGYSTETgekgaqLSGGQKQRVAMARALVRNPPVLILDE 447
Cdd:COG0396 94 vsNFLRTALNARRGEELSAR-EFLKLLKEKMKELGLDEDFLDRYVNEG------FSGGEKKRNEILQMLLLEPKLAILDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 448 ATSALDAE-----SEYLiqQAIHGnlQKHTVLIIAH--RLSTVEHAHLIVVLDKGRVVQQGTH---QQLLAQGglYAKLV 517
Cdd:COG0396 167 TDSGLDIDalrivAEGV--NKLRS--PDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGKelaLELEEEG--YDWLK 240
|
..
gi 2217288354 518 QR 519
Cdd:COG0396 241 EE 242
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
292-492 |
6.25e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 76.12 E-value: 6.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 292 YRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGkpisaydhkylHRVISLVSQ---EP 368
Cdd:NF040873 2 YGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQrseVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 369 VLFARSITDNISYGL---------PTVPFEMVVEAAQKAnahgfiMELQDGYSTETGEkgaqLSGGQKQRVAMARALVRN 439
Cdd:NF040873 68 DSLPLTVRDLVAMGRwarrglwrrLTRDDRAAVDDALER------VGLADLAGRQLGE----LSGGQRQRALLAQGLAQE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217288354 440 PPVLILDEATSALDAESEYLIQQAI---HGnlQKHTVLIIAHRLSTVEHAHLIVVL 492
Cdd:NF040873 138 ADLLLLDEPTTGLDAESRERIIALLaeeHA--RGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
298-498 |
8.44e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 80.54 E-value: 8.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 298 TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV----ISLVSQEPVLFAR 373
Cdd:PRK10535 21 VEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLrrehFGFIFQRYHLLSH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 374 -SITDNISygLPTVpFEMVVEAAQKANAHGFIMELqdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSAL 452
Cdd:PRK10535 101 lTAAQNVE--VPAV-YAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGAL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2217288354 453 DAESEYLIQQAIHG-NLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVV 498
Cdd:PRK10535 176 DSHSGEEVMAILHQlRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
284-529 |
1.02e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 79.75 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 284 DFENVTFTYRTRPHT-QVLQNVSFSLSPGKVTALVGPSGSGKS----SCVNILEN---FYPleGGRVLLDGKPISAYDHK 355
Cdd:PRK15134 7 AIENLSVAFRQQQTVrTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppvVYP--SGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 356 YLHRV----ISLVSQEPVlfarsITDNISYGLPTVPFEMVV--EAAQKANAHGFIMELQDgystETGEKGA--------- 420
Cdd:PRK15134 85 TLRGVrgnkIAMIFQEPM-----VSLNPLHTLEKQLYEVLSlhRGMRREAARGEILNCLD----RVGIRQAakrltdyph 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 421 QLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQKH---TVLIIAHRLSTVEH-AHLIVVLDKGR 496
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLR-ELQQElnmGLLFITHNLSIVRKlADRVAVMQNGR 234
|
250 260 270
....*....|....*....|....*....|...
gi 2217288354 497 VVQQGTHQQLLAQGglyAKLVQRQMLGLQPAAD 529
Cdd:PRK15134 235 CVEQNRAATLFSAP---THPYTQKLLNSEPSGD 264
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
287-498 |
1.24e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 77.05 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 287 NVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAY-DHKYlHRVISLVS 365
Cdd:COG1101 8 SKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLpEYKR-AKYIGRVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 366 QEPVLfarsitdnisyGlpTVPfEMVVE-----AAQKANAHGFI-------------------MELQDGYSTETGekgaQ 421
Cdd:COG1101 87 QDPMM-----------G--TAP-SMTIEenlalAYRRGKRRGLRrgltkkrrelfrellatlgLGLENRLDTKVG----L 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 422 LSGGQKQRVAMARALVRNPPVLILDEATSALD---AE-----SEYLIQQaihgnlQKHTVLIIAHRLS-TVEHAHLIVVL 492
Cdd:COG1101 149 LSGGQRQALSLLMATLTKPKLLLLDEHTAALDpktAAlvlelTEKIVEE------NNLTTLMVTHNMEqALDYGNRLIMM 222
|
....*.
gi 2217288354 493 DKGRVV 498
Cdd:COG1101 223 HEGRII 228
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
300-497 |
1.29e-15 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 75.16 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 300 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV-ISLVSQEP----VLFARS 374
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDRkregLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 375 ITDNISYGlptvpfemvveaaqkanahgfimelqdgystetgekgAQLSGGQKQRVAMARALVRNPPVLILDEATSALDA 454
Cdd:cd03215 95 VAENIALS-------------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2217288354 455 ESeyliQQAIHGNLQK-----HTVLIIAHRLSTVEH-AHLIVVLDKGRV 497
Cdd:cd03215 138 GA----KAEIYRLIREladagKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
295-502 |
1.88e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 76.79 E-value: 1.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 295 RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEG--------GRVLLDGKPISAYDHKYLHRVISLVSQ 366
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 367 --EPVlFARSITDNISYGLptvpFEMVVEAAQKANAHGFI----MELQDGySTETGEKGAQLSGGQKQRVAMARAL---- 436
Cdd:PRK13547 91 aaQPA-FAFSAREIVLLGR----YPHARRAGALTHRDGEIawqaLALAGA-TALVGRDVTTLSGGELARVQFARVLaqlw 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217288354 437 -----VRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHT--VLIIAHRLS-TVEHAHLIVVLDKGRVVQQGT 502
Cdd:PRK13547 165 pphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNlgVLAIVHDPNlAARHADRIAMLADGAIVAHGA 238
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
302-516 |
2.01e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 74.84 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 302 QNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVI----------SLVSQEPVLF 371
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLylghqpgiktELTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 372 ARSITDNISYglptvpfEMVVEAAQKANAHGFiMELqdgystetgeKGAQLSGGQKQRVAMARALVRNPPVLILDEATSA 451
Cdd:PRK13538 98 YQRLHGPGDD-------EALWEALAQVGLAGF-EDV----------PVRQLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217288354 452 LDaeseyliqqaihgnlqKHTVLIIAHRLStvEHAhlivvlDKGRVVQQGTHQQLLAQGGLYAKL 516
Cdd:PRK13538 160 ID----------------KQGVARLEALLA--QHA------EQGGMVILTTHQDLPVASDKVRKL 200
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
282-519 |
2.36e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 76.18 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 282 RVDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVI 361
Cdd:PRK10253 7 RLRGEQLTLGYGKY---TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 362 SLVSQEPVLFAR-SITDNISYG-LPTVPF--------EMVVEAAQKANAhgfIMELQDgYSTETgekgaqLSGGQKQRVA 431
Cdd:PRK10253 84 GLLAQNATTPGDiTVQELVARGrYPHQPLftrwrkedEEAVTKAMQATG---ITHLAD-QSVDT------LSGGQRQRAW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 432 MARALVRNPPVLILDEATSALDAESEY-LIQQAIHGNLQK-HTVLIIAHRLS-TVEHAHLIVVLDKGRVVQQGTHQQLLA 508
Cdd:PRK10253 154 IAMVLAQETAIMLLDEPTTWLDISHQIdLLELLSELNREKgYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVT 233
|
250
....*....|.
gi 2217288354 509 qgglyAKLVQR 519
Cdd:PRK10253 234 -----AELIER 239
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
281-509 |
2.90e-15 |
|
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: 76.05 E-value: 2.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 281 GRVDFENVTFTYrTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGgRVLLDGKPISAYDHKYLHRV 360
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEG-DIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 361 ISLVSQEPVLFARSITDNIS-YGLPTVpfEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRN 439
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLDpYGKWSD--EEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 440 PPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQ 509
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
293-506 |
3.40e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 75.82 E-value: 3.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 293 RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFY---PLEGGRVLLDGKPIS-----AYDHKYLHRVISLV 364
Cdd:PRK09984 12 KTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQregrlARDIRKSRANTGYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 365 SQEPVLFAR-SITDNISYG-LPTVPFEMVV----EAAQKANAHGFIMELqdGYSTETGEKGAQLSGGQKQRVAMARALVR 438
Cdd:PRK09984 92 FQQFNLVNRlSVLENVLIGaLGSTPFWRTCfswfTREQKQRALQALTRV--GMVHFAHQRVSTLSGGQQQRVAIARALMQ 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217288354 439 NPPVLILDEATSALDAESEYLIQQAIHGNLQKH--TVLIIAHRLS-TVEHAHLIVVLDKGRVVQQGTHQQL 506
Cdd:PRK09984 170 QAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
283-509 |
3.80e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 75.89 E-value: 3.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRPHTQ---VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKY-LH 358
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 359 RVISLVSQEP--VLFARSITDNISYG---LPTVPFEM---VVEAAQKANAHGFimelqdgystetgEKGAQ--LSGGQKQ 428
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGpenLGIPPEEIrerVDESLKKVGMYEY-------------RRHAPhlLSGGQKQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 429 RVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKH--TVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQL 506
Cdd:PRK13633 152 RVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
...
gi 2217288354 507 LAQ 509
Cdd:PRK13633 232 FKE 234
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
304-506 |
6.29e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 75.90 E-value: 6.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 304 VSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV---ISLVSQEPV--LFAR-SITD 377
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdIQMIFQDPLasLNPRmTIGE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 378 NISYGL----PTVPFEMVVEAAQKANAH-GFIMELQDGYSTEtgekgaqLSGGQKQRVAMARALVRNPPVLILDEATSAL 452
Cdd:PRK15079 120 IIAEPLrtyhPKLSRQEVKDRVKAMMLKvGLLPNLINRYPHE-------FSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217288354 453 D----AESEYLIQQaihgnLQKH---TVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQL 506
Cdd:PRK15079 193 DvsiqAQVVNLLQQ-----LQREmglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
283-508 |
7.18e-15 |
|
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: 77.15 E-value: 7.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNIL---ENFYPLEG---------------GRVLL 344
Cdd:TIGR03269 1 IEVKNLTKKFDGK---EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgmDQYEPTSGriiyhvalcekcgyvERPSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 345 DGKPISAYDHKYLHRVISLVSQEPVLFARsITDNIS---------YGLPTVpFEMVVEAAQKAnahgfimelqdGYSTET 415
Cdd:TIGR03269 78 VGEPCPVCGGTLEPEEVDFWNLSDKLRRR-IRKRIAimlqrtfalYGDDTV-LDNVLEALEEI-----------GYEGKE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 416 GEKGA------------------QLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKH--TVLI 475
Cdd:TIGR03269 145 AVGRAvdliemvqlshrithiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVL 224
|
250 260 270
....*....|....*....|....*....|....
gi 2217288354 476 IAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLA 508
Cdd:TIGR03269 225 TSHWPEVIEDlSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
303-506 |
1.55e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 73.49 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 303 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISA--------------YDHKYLHRVISLVsqEP 368
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGlpghqiarmgvvrtFQHVRLFREMTVI--EN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 369 VLFA--RSITDNISYGLPTVPFEMVVEAAQKANAHGFI--MELQDGYSTETGekgaQLSGGQKQRVAMARALVRNPPVLI 444
Cdd:PRK11300 101 LLVAqhQQLKTGLFSGLLKTPAFRRAESEALDRAATWLerVGLLEHANRQAG----NLAYGQQRRLEIARCMVTQPEILM 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217288354 445 LDEATSALDAESEYLIQQAIhGNLQKH---TVLIIAHRLSTV----EHahlIVVLDKGRVVQQGTHQQL 506
Cdd:PRK11300 177 LDEPAAGLNPKETKELDELI-AELRNEhnvTVLLIEHDMKLVmgisDR---IYVVNQGTPLANGTPEEI 241
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
280-489 |
2.96e-14 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 75.56 E-value: 2.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 280 EGRVDFENVTFTyrtRPHTQVL-QNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYdhkylh 358
Cdd:TIGR00954 449 DNGIKFENIPLV---TPNGDVLiESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFY------ 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 359 rvislVSQEPVLFARSITDNISYglPTVPFEMVVEAAQKANAHGFIMELQDGY--STETGEKGAQ-----LSGGQKQRVA 431
Cdd:TIGR00954 520 -----VPQRPYMTLGTLRDQIIY--PDSSEDMKRRGLSDKDLEQILDNVQLTHilEREGGWSAVQdwmdvLSGGEKQRIA 592
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217288354 432 MARALVRNPPVLILDEATSALDAESEyliqQAIHGNLQKH--TVLIIAHRLSTVE-HAHLI 489
Cdd:TIGR00954 593 MARLFYHKPQFAILDECTSAVSVDVE----GYMYRLCREFgiTLFSVSHRKSLWKyHEYLL 649
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
286-501 |
4.24e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 71.98 E-value: 4.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 286 ENVTFTYRT----------------RPHTQV--LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGK 347
Cdd:cd03267 4 SNLSKSYRVyskepgligslkslfkRKYREVeaLKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 348 PISAYDHKYLHRVISLVSQE-------PVLFARSITDNIsYGLPTVPFemvveaaqKANAHGF--IMELQDGYSTETgek 418
Cdd:cd03267 84 VPWKRRKKFLRRIGVVFGQKtqlwwdlPVIDSFYLLAAI-YDLPPARF--------KKRLDELseLLDLEELLDTPV--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 419 gAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESeyliQQAIHGNLQ------KHTVLIIAHRLSTVEH-AHLIVV 491
Cdd:cd03267 152 -RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA----QENIRNFLKeynrerGTTVLLTSHYMKDIEAlARRVLV 226
|
250
....*....|
gi 2217288354 492 LDKGRVVQQG 501
Cdd:cd03267 227 IDKGRLLYDG 236
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
290-512 |
5.28e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 72.35 E-value: 5.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 290 FTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISaYDHK---YLHRVISLVSQ 366
Cdd:PRK13638 9 FRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRgllALRQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 367 EP--VLFARSITDNISYGLPT--VPFEMVV----EAAQKANAHGFIME-LQdgystetgekgaQLSGGQKQRVAMARALV 437
Cdd:PRK13638 85 DPeqQIFYTDIDSDIAFSLRNlgVPEAEITrrvdEALTLVDAQHFRHQpIQ------------CLSHGQKKRVAIAGALV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 438 RNPPVLILDEATSALD----AESEYLIQQAIHgnlQKHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLAQGGL 512
Cdd:PRK13638 153 LQARYLLLDEPTAGLDpagrTQMIAIIRRIVA---QGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFACTEA 229
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
283-498 |
6.28e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 74.33 E-value: 6.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLdGKPIS-AY---DHKYLH 358
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKiGYfdqHQEELD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 359 RvislvsqepvlfARSITDNISYGLPTvpfemvveaAQKANAHGFimeLQD-GYSTETGEKG-AQLSGGQKQRVAMARAL 436
Cdd:COG0488 392 P------------DKTVLDELRDGAPG---------GTEQEVRGY---LGRfLFSGDDAFKPvGVLSGGEKARLALAKLL 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217288354 437 VRNPPVLILDEATSALDAESEYLIQQAihgnLQKH--TVLIIAH-R--LSTVehAHLIVVLDKGRVV 498
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDIETLEALEEA----LDDFpgTVLLVSHdRyfLDRV--ATRILEFEDGGVR 508
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
283-506 |
6.49e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 72.11 E-value: 6.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV-- 360
Cdd:PRK11831 8 VDMRGVSFTRGNRC---IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVrk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 361 -ISLVSQEPVLFAR-SITDNISY------GLPTVPFEMVVeaaqkanahgfIMELQdgystETGEKGA------QLSGGQ 426
Cdd:PRK11831 85 rMSMLFQSGALFTDmNVFDNVAYplrehtQLPAPLLHSTV-----------MMKLE-----AVGLRGAaklmpsELSGGM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 427 KQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIhGNLQKH---TVLIIAHR----LSTVEHAHliVVLDKgRVVQ 499
Cdd:PRK11831 149 ARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLI-SELNSAlgvTCVVVSHDvpevLSIADHAY--IVADK-KIVA 224
|
....*..
gi 2217288354 500 QGTHQQL 506
Cdd:PRK11831 225 HGSAQAL 231
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
8-262 |
7.41e-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: 72.15 E-value: 7.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 8 VVIVCLLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFL 87
Cdd:cd18580 42 GVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 88 RNTVKVTGVVVFMFSLSWQLSLVtfmgFPIIMMVSNIYGKYYKRLSKEVQ--NALARAS--NTAEETISAMKTVRSFANE 163
Cdd:cd18580 122 QSLFSVLGSLIVIAIVSPYFLIV----LPPLLVVYYLLQRYYLRTSRQLRrlESESRSPlySHFSETLSGLSTIRAFGWQ 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 164 EEEAEVYLRKLQQVYKlnrkeaAAYMYYV---W--------GSGLTLLVVqvsILyygghLVISGQMTSGNLIAFII-YE 231
Cdd:cd18580 198 ERFIEENLRLLDASQR------AFYLLLAvqrWlglrldllGALLALVVA---LL-----AVLLRSSISAGLVGLALtYA 263
|
250 260 270
....*....|....*....|....*....|.
gi 2217288354 232 FVLGDCMESVGSVYSGLMQGVGAAEKVFEFI 262
Cdd:cd18580 264 LSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
300-498 |
1.33e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 73.13 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 300 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPIS------AYDHKylhrvISLVS----QEPV 369
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirsprdAIRAG-----IAYVPedrkGEGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 370 LFARSITDNISygLPTVP----FEMVVEAAQKANAHGFIMELQ---DGYSTETGekgaQLSGGQKQRVAMARALVRNPPV 442
Cdd:COG1129 342 VLDLSIRENIT--LASLDrlsrGGLLDRRRERALAEEYIKRLRiktPSPEQPVG----NLSGGNQQKVVLAKWLATDPKV 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217288354 443 LILDEATSALDAESEYLIQQAIHgNL--QKHTVLII----------AHRlstvehahlIVVLDKGRVV 498
Cdd:COG1129 416 LILDEPTRGIDVGAKAEIYRLIR-ELaaEGKAVIVIsselpellglSDR---------ILVMREGRIV 473
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
304-526 |
1.35e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 70.73 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 304 VSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGgRVLLDGKPISAYDHKYLHRVIS-LVSQEPVLF--------ARS 374
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSG-SIQFAGQPLEAWSAAELARHRAyLSQQQTPPFampvfqylTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 375 ITDNISYGLPTVPFEMVVEAAQkanahgfimeLQDGYSTETGekgaQLSGGQKQRVAMARALVR-----NP--PVLILDE 447
Cdd:PRK03695 94 QPDKTRTEAVASALNEVAEALG----------LDDKLGRSVN----QLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 448 ATSALDAESEYLIQQAIHGNLQKH-TVLIIAHRLS-TVEHAHLIVVLDKGRVVQQGTHQQLLAQGGL---YAKLVQRQML 522
Cdd:PRK03695 160 PMNSLDVAQQAALDRLLSELCQQGiAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPENLaqvFGVNFRRLDV 239
|
....
gi 2217288354 523 GLQP 526
Cdd:PRK03695 240 EGHP 243
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
287-506 |
1.49e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 71.66 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 287 NVTFTY--RTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRV---LLDGKPISAYDH------- 354
Cdd:PRK13651 7 NIVKIFnkKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEkekvlek 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 355 --------------KYLHRVISLVSQ--EPVLFARSITDNISYGlptvPFEMVV---EAAQKANAHGFIMELQDGYStet 415
Cdd:PRK13651 87 lviqktrfkkikkiKEIRRRVGVVFQfaEYQLFEQTIEKDIIFG----PVSMGVskeEAKKRAAKYIELVGLDESYL--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 416 gEKGA-QLSGGQKQRVAMARALVRNPPVLILDEATSALDAES--EYLiqqAIHGNLQKH--TVLIIAHRLSTV-EHAHLI 489
Cdd:PRK13651 160 -QRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGvkEIL---EIFDNLNKQgkTIILVTHDLDNVlEWTKRT 235
|
250
....*....|....*...
gi 2217288354 490 VVLDKGRVVQQG-THQQL 506
Cdd:PRK13651 236 IFFKDGKIIKDGdTYDIL 253
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
299-478 |
1.57e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 70.64 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 299 QVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEG-----GRVLLDGKPISAYDHKYLH--RVISLVSQEPVLF 371
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSPDVDPIEvrREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 372 AR-SITDNISYGL-------PTVPFEMVVEAAQKANAhgfimeLQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVL 443
Cdd:PRK14267 98 PHlTIYDNVAIGVklnglvkSKKELDERVEWALKKAA------LWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190
....*....|....*....|....*....|....*
gi 2217288354 444 ILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAH 478
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
296-480 |
2.23e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.34 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 296 PHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV-ISLVSQEPVLFAR- 373
Cdd:PRK10762 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgIGIIHQELNLIPQl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 374 SITDNISYGL-PTVPFEMVVEAAQKANAHGFIMELQDGYSTETgeKGAQLSGGQKQRVAMARALVRNPPVLILDEATSAL 452
Cdd:PRK10762 95 TIAENIFLGReFVNRFGRIDWKKMYAEADKLLARLNLRFSSDK--LVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
170 180
....*....|....*....|....*....
gi 2217288354 453 -DAESEYLIQQAIHGNLQKHTVLIIAHRL 480
Cdd:PRK10762 173 tDTETESLFRVIRELKSQGRGIVYISHRL 201
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
284-509 |
2.36e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 71.09 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 284 DFENVTFTYRTrPH--TQVLQNVSFSLSPGKVTALVGPSGSGKS----SCVNILENFYPLEGGRVLLDGK---PISAYD- 353
Cdd:COG4170 5 DIRNLTIEIDT-PQgrVKAVDRVSLTLNEGEIRGLVGESGSGKSliakAICGITKDNWHVTADRFRWNGIdllKLSPREr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 354 HKYLHRVISLVSQEPVLF---ARSITDNISYGLPTVPFE---MVVEAAQKANA-----------HGFIMelqDGYSTEtg 416
Cdd:COG4170 84 RKIIGREIAMIFQEPSSCldpSAKIGDQLIEAIPSWTFKgkwWQRFKWRKKRAiellhrvgikdHKDIM---NSYPHE-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 417 ekgaqLSGGQKQRVAMARALVRNPPVLILDEATSALDAESeyliQQAIH------GNLQKHTVLIIAHRLSTVEH-AHLI 489
Cdd:COG4170 159 -----LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTT----QAQIFrllarlNQLQGTSILLISHDLESISQwADTI 229
|
250 260
....*....|....*....|
gi 2217288354 490 VVLDKGRVVQQGTHQQLLAQ 509
Cdd:COG4170 230 TVLYCGQTVESGPTEQILKS 249
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
287-509 |
2.67e-13 |
|
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: 70.27 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 287 NVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCV-NILENFYPLEGgRVLLDGKpisaydhkylhrvISLVS 365
Cdd:cd03291 39 NLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLmLILGELEPSEG-KIKHSGR-------------ISFSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 366 QEPVLFARSITDNISYGLP--TVPFEMVVEAAQKANAhgfIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVL 443
Cdd:cd03291 105 QFSWIMPGTIKENIIFGVSydEYRYKSVVKACQLEED---ITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLY 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217288354 444 ILDEATSALDAESEYLIQQAIHGNLQKH-TVLIIAHRLSTVEHAHLIVVLDKGRVVQQGTHQQLLAQ 509
Cdd:cd03291 182 LLDSPFGYLDVFTEKEIFESCVCKLMANkTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSL 248
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
1-174 |
2.92e-13 |
|
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: 70.64 E-value: 2.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 1 MDQFSTAVVIVCLLAIGSSFAAGIRGGIF---TLIFARlniRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSD 77
Cdd:cd18605 38 NDSFNFFLTVYGFLAGLNSLFTLLRAFLFaygGLRAAR---RLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 78 LVSQNINVFLRNTVKVTG-VVVFMFSLSWQLSLVtfmgFPIIMMVSNIYgKYYKRLSKEVQ--NALARAS--NTAEETIS 152
Cdd:cd18605 115 SLPFILNILLAQLFGLLGyLVVICYQLPWLLLLL----LPLAFIYYRIQ-RYYRATSRELKrlNSVNLSPlyTHFSETLK 189
|
170 180
....*....|....*....|..
gi 2217288354 153 AMKTVRSFANEEEEAEVYLRKL 174
Cdd:cd18605 190 GLVTIRAFRKQERFLKEYLEKL 211
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
7-227 |
4.33e-13 |
|
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: 69.85 E-value: 4.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 7 AVVIVCLLAIGSSFAAgIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLtSDTTMVSDLVSQNinvF 86
Cdd:cd18783 45 TIGVVIALLFEGILGY-LRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAGVLTKHM-QQIERIRQFLTGQ---L 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 87 LRNTVKVTGVVVF---MFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANE 163
Cdd:cd18783 120 FGTLLDATSLLVFlpvLFFYSPTLALVVLAFSALIALIILAFLPPFRRRLQALYRAEGERQAFLVETVHGIRTVKSLALE 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217288354 164 EEEAEVYLRKLQQVYKLNRKEAAAYMyyvWGSGLTLL---VVQVSILYYGGHLVISGQMTSGNLIAF 227
Cdd:cd18783 200 PRQRREWDERVARAIRARFAVGRLSN---WPQTLTGPlekLMTVGVIWVGAYLVFAGSLTVGALIAF 263
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
299-501 |
5.70e-13 |
|
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: 67.94 E-value: 5.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 299 QVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENF--YPLEGGRVLLDGKPI---SAYDhkylhRV---ISLVSQEPVL 370
Cdd:cd03217 14 EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDItdlPPEE-----RArlgIFLAFQYPPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 371 FarsitdnisyglPTVPFEMvveaaqkanahgFIMELQDGystetgekgaqLSGGQKQRVAMARALVRNPPVLILDEATS 450
Cdd:cd03217 89 I------------PGVKNAD------------FLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2217288354 451 ALDAESEYLIQQAIHGNLQKHT-VLIIAH--RLSTVEHAHLIVVLDKGRVVQQG 501
Cdd:cd03217 134 GLDIDALRLVAEVINKLREEGKsVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
286-522 |
6.34e-13 |
|
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: 71.01 E-value: 6.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 286 ENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLE-GGRVLLDGKPISAYD-HKYLHRVISL 363
Cdd:TIGR02633 261 RNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNpAQAIRAGIAM 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 364 VSQE-------PVLfarSITDNISYG-LPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARA 435
Cdd:TIGR02633 341 VPEDrkrhgivPIL---GVGKNITLSvLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKM 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 436 LVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIAhrlsTVEHAHLIVVLDKGRVVQQGTHQQLLAQGGlyak 515
Cdd:TIGR02633 418 LLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVV----SSELAEVLGLSDRVLVIGEGKLKGDFVNHA---- 489
|
....*..
gi 2217288354 516 LVQRQML 522
Cdd:TIGR02633 490 LTQEQVL 496
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
300-453 |
9.61e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 67.88 E-value: 9.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 300 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDH----KYLHRVISLVSQE----PVLF 371
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearaKLRAKHVGFVFQSfmliPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 372 ARsitDNISygLPTVpfeMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSA 451
Cdd:PRK10584 105 AL---ENVE--LPAL---LRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
..
gi 2217288354 452 LD 453
Cdd:PRK10584 177 LD 178
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
283-501 |
2.04e-12 |
|
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: 66.13 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYR-TRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSS----CVNILENFYPLEGgRVLLDGKPISAYDHKYl 357
Cdd:cd03233 4 LSWRNISFTTGkGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSVEG-DIHYNGIPYKEFAEKY- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 358 HRVISLVSQEPVLFarsitdnisyglPTVPFEMVVEAAQKANAHGFImelqdgystetgeKGaqLSGGQKQRVAMARALV 437
Cdd:cd03233 82 PGEIIYVSEEDVHF------------PTLTVRETLDFALRCKGNEFV-------------RG--ISGGERKRVSIAEALV 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217288354 438 RNPPVLILDEATSALDAESEYLIQQAIH--GNLQKHTVLIIAHRLStVEHAHL---IVVLDKGRVVQQG 501
Cdd:cd03233 135 SRASVLCWDNSTRGLDSSTALEILKCIRtmADVLKTTTFVSLYQAS-DEIYDLfdkVLVLYEGRQIYYG 202
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
286-501 |
2.66e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.22 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 286 ENVTFTYRTrPHTqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLhrvISLVS 365
Cdd:PRK15056 10 NDVTVTWRN-GHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 366 QE-------PVLfarsITDNISYG---------LPTVPFEMVVEAAQKAnahgfiMELQDGYSTETGEkgaqLSGGQKQR 429
Cdd:PRK15056 85 QSeevdwsfPVL----VEDVVMMGryghmgwlrRAKKRDRQIVTAALAR------VDMVEFRHRQIGE----LSGGQKKR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217288354 430 VAMARALVRNPPVLILDEATSALDAESEYLIqQAIHGNLQKH--TVLIIAHRLSTVEHAHLIVVLDKGRVVQQG 501
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEARI-ISLLRELRDEgkTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
300-508 |
3.67e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 69.14 E-value: 3.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 300 VLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEG--GRVLLDGKPISaydhKYLHRVISLVSQEPVLFAR-SIT 376
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPT----KQILKRTGFVTQDDILYPHlTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 377 DNISY-GLPTVPFEMVVEAAQKAnAHGFIMEL--QDGYSTETGEKGAQ-LSGGQKQRVAMARALVRNPPVLILDEATSAL 452
Cdd:PLN03211 159 ETLVFcSLLRLPKSLTKQEKILV-AESVISELglTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGL 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2217288354 453 DAESEYLIQQAIHGNLQK-HTVLIIAHRLST--VEHAHLIVVLDKGRVVQQGTHQQLLA 508
Cdd:PLN03211 238 DATAAYRLVLTLGSLAQKgKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
310-494 |
4.98e-12 |
|
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: 63.93 E-value: 4.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 310 PGKVTALVGPSGSGKSSCVNILENFYPLEGGRVL-LDGKPISAYDHKYLHRVIslvsqepvlfarsitdnisyglptvpf 388
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 389 emvveaaqkanahgfimelqdgysteTGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNL 468
Cdd:smart00382 54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRL 107
|
170 180 190
....*....|....*....|....*....|...
gi 2217288354 469 QKH-------TVLIIAHRLSTVEHAHLIVVLDK 494
Cdd:smart00382 108 LLLlkseknlTVILTTNDEKDLGPALLRRRFDR 140
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
278-476 |
6.16e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.03 E-value: 6.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 278 HLEGRVDFE--NVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPleG---GRVLLDGKPIS-- 350
Cdd:PRK13549 253 HTIGEVILEvrNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYP--GrweGEIFIDGKPVKir 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 351 ----AYDHKylhrvISLVSQE-------PVLfarSITDNISYG-LPTVPFEMVV-EAAQKANAHGFIMELQdgYSTETGE 417
Cdd:PRK13549 331 npqqAIAQG-----IAMVPEDrkrdgivPVM---GVGKNITLAaLDRFTGGSRIdDAAELKTILESIQRLK--VKTASPE 400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 418 -KGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIhGNLQKHTVLII 476
Cdd:PRK13549 401 lAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLI-NQLVQQGVAII 459
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
283-483 |
6.31e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 65.91 E-value: 6.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 362
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 LvsqePVLFARSITDNisyglPTVPFEMVVEAAQKANA-HGFIMELQdgystetgekgaQLSGGQKQRVAMARALVRNPP 441
Cdd:PRK09544 82 L----PLTVNRFLRLR-----PGTKKEDILPALKRVQAgHLIDAPMQ------------KLSGGETQRVLLARALLNRPQ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2217288354 442 VLILDEATSALDAESEYLIQQAIHgNLQKH---TVLIIAHRLSTV 483
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALYDLID-QLRREldcAVLMVSHDLHLV 184
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
313-501 |
6.32e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 67.21 E-value: 6.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 313 VTALVGPSGSGKSSCVNILENF-YPLEG-----GRVLLD-GKPISAYDHKylhRVISLVSQEPVLFAR-SITDNISYGLp 384
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLtRPQKGrivlnGRVLFDaEKGICLPPEK---RRIGYVFQDARLFPHyKVRGNLRYGM- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 385 tvpfemvveaAQKANAHgF--------IMELQDGYStetgekgAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAES 456
Cdd:PRK11144 102 ----------AKSMVAQ-FdkivallgIEPLLDRYP-------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2217288354 457 E-----YLIQQAIHGNLqkhTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQG 501
Cdd:PRK11144 164 KrellpYLERLAREINI---PILYVSHSLDEILRlADRVVVLEQGKVKAFG 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
303-509 |
8.29e-12 |
|
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: 67.52 E-value: 8.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 303 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGR--VLLDGKPISAYDHKYLHR-----VISLVSQEPVLFA-RS 374
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDMTKPGPDGRgrakrYIGILHQEYDLYPhRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 375 ITDNI--SYGLpTVPFEM-VVEAAQKANAHGFimelQDGYSTETGEK-GAQLSGGQKQRVAMARALVRNPPVLILDEATS 450
Cdd:TIGR03269 382 VLDNLteAIGL-ELPDELaRMKAVITLKMVGF----DEEKAEEILDKyPDELSEGERHRVALAQVLIKEPRIVILDEPTG 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217288354 451 ALDAESEYLIQQAIHGNLQK--HTVLIIAHRLSTVehahlIVVLDK------GRVVQQGTHQQLLAQ 509
Cdd:TIGR03269 457 TMDPITKVDVTHSILKAREEmeQTFIIVSHDMDFV-----LDVCDRaalmrdGKIVKIGDPEEIVEE 518
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
286-507 |
9.32e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 65.33 E-value: 9.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 286 ENVTFTYRTRphtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKpisaydHKYLHRVISLVS 365
Cdd:PRK11701 10 RGLTKLYGPR---KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR------DGQLRDLYALSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 366 QEPVLFARS----ITDNISYGLptvpfEMVVEA---------AQKANAHGFI----------MELQdgySTETGEKGAQL 422
Cdd:PRK11701 81 AERRRLLRTewgfVHQHPRDGL-----RMQVSAggnigerlmAVGARHYGDIratagdwlerVEID---AARIDDLPTTF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 423 SGGQKQRVAMARALVRNPPVLILDEATSALD----AESEYLIQQAIHgNLQKhTVLIIAHRLSTVEH-AHLIVVLDKGRV 497
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsvqARLLDLLRGLVR-ELGL-AVVIVTHDLAVARLlAHRLLVMKQGRV 230
|
250
....*....|
gi 2217288354 498 VQQGTHQQLL 507
Cdd:PRK11701 231 VESGLTDQVL 240
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
287-506 |
1.59e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.80 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 287 NVTFtYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGK----------PISAYDHKY 356
Cdd:PRK10261 19 NIAF-MQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEQSAAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 357 LHRV----ISLVSQEPVL-----------FARSItdNISYGLPTvpfEMVVEAAQKANAHGFIMELQdgysTETGEKGAQ 421
Cdd:PRK10261 98 MRHVrgadMAMIFQEPMTslnpvftvgeqIAESI--RLHQGASR---EEAMVEAKRMLDQVRIPEAQ----TILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 422 LSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHgNLQKHT---VLIIAHRLSTV-EHAHLIVVLDKGRV 497
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIK-VLQKEMsmgVIFITHDMGVVaEIADRVLVMYQGEA 247
|
....*....
gi 2217288354 498 VQQGTHQQL 506
Cdd:PRK10261 248 VETGSVEQI 256
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
298-516 |
6.48e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 64.65 E-value: 6.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 298 TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRvisLVSQEpvlFARSITD 377
Cdd:PRK10938 16 TKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQK---LVSDE---WQRNNTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 378 NIS-----YGLPTVpfEMVVEAAqKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSAL 452
Cdd:PRK10938 90 MLSpgeddTGRTTA--EIIQDEV-KDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217288354 453 DAESEYLIQQAIHG-NLQKHTVLIIAHRLSTV-EHAHLIVVLDKGRVVQQGTHQQLLAQgGLYAKL 516
Cdd:PRK10938 167 DVASRQQLAELLASlHQSGITLVLVLNRFDEIpDFVQFAGVLADCTLAETGEREEILQQ-ALVAQL 231
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
296-496 |
8.01e-11 |
|
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: 64.57 E-value: 8.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 296 PHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNIL----ENFypleggrvllDGKPISAYDHKylhrvISLVSQEPVL- 370
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMagvdKDF----------NGEARPQPGIK-----VGYLPQEPQLd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 371 FARSITDNI-------------------SYGLPTVPFEMVVEAAQKANAhgfIMELQDGYSTET-------------GE- 417
Cdd:TIGR03719 81 PTKTVRENVeegvaeikdaldrfneisaKYAEPDADFDKLAAEQAELQE---IIDAADAWDLDSqleiamdalrcppWDa 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 418 KGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGnlQKHTVLIIAH-R--LSTVehAHLIVVLDK 494
Cdd:TIGR03719 158 DVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQE--YPGTVVAVTHdRyfLDNV--AGWILELDR 233
|
..
gi 2217288354 495 GR 496
Cdd:TIGR03719 234 GR 235
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
283-502 |
8.83e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 63.22 E-value: 8.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRPHTQVlQNVSFSLSPGKVTALVGPSGSGKS-SCVNILENF-YPlegGRVL-----LDGKPISAYDHK 355
Cdd:PRK11022 6 VDKLSVHFGDESAPFRAV-DRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIdYP---GRVMaekleFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 356 YLHRVI----SLVSQEPVlfarsITDNISYglpTVPFEM-----VVEAAQKANAHGFIMEL--QDGYSTETGEKGA---Q 421
Cdd:PRK11022 82 ERRNLVgaevAMIFQDPM-----TSLNPCY---TVGFQImeaikVHQGGNKKTRRQRAIDLlnQVGIPDPASRLDVyphQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 422 LSGGQKQRVAMARALVRNPPVLILDEATSALDAEseylIQQAIHG---NLQKH---TVLIIAHRLSTV-EHAHLIVVLDK 494
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVT----IQAQIIElllELQQKenmALVLITHDLALVaEAAHKIIVMYA 229
|
....*...
gi 2217288354 495 GRVVQQGT 502
Cdd:PRK11022 230 GQVVETGK 237
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
295-517 |
9.42e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 63.18 E-value: 9.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 295 RPHTQV--LQNVSFSLSPGKVTALVGPSGSGKSSCVNILEN-FYPlEGGRVLLDGKPISAYDHKYLHRvISLV----SQ- 366
Cdd:COG4586 30 REYREVeaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGiLVP-TSGEVRVLGYVPFKRRKEFARR-IGVVfgqrSQl 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 367 ---EPVL--FA--RSItdnisYGLPTVPF----EMVVEaaqkanahgfIMELQDGYSTETgekgAQLSGGQKQRVAMARA 435
Cdd:COG4586 108 wwdLPAIdsFRllKAI-----YRIPDAEYkkrlDELVE----------LLDLGELLDTPV----RQLSLGQRMRCELAAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 436 LVRNPPVLILDEATSALDAESeyliQQAIHGNL----QKH--TVLIIAHRLSTVEhaHL---IVVLDKGRVVQQGTHQQL 506
Cdd:COG4586 169 LLHRPKILFLDEPTIGLDVVS----KEAIREFLkeynRERgtTILLTSHDMDDIE--ALcdrVIVIDHGRIIYDGSLEEL 242
|
250
....*....|.
gi 2217288354 507 LAQGGLYAKLV 517
Cdd:COG4586 243 KERFGPYKTIV 253
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
283-502 |
9.57e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 62.02 E-value: 9.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRT-------------------RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVL 343
Cdd:COG1134 5 IEVENVSKSYRLyhepsrslkelllrrrrtrREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 344 LDGkpisaydhkylhRVISLVSqepvL---FARSIT--DNIS-----YGLPTVP----FEMVVEAAqkanahgfimELQD 409
Cdd:COG1134 85 VNG------------RVSALLE----LgagFHPELTgrENIYlngrlLGLSRKEidekFDEIVEFA----------ELGD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 410 -------GYSTetgekgaqlsgGQKQRVAMARALVRNPPVLILDEATSALDAE----SEYLIQQaihgnLQKH--TVLII 476
Cdd:COG1134 139 fidqpvkTYSS-----------GMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRE-----LRESgrTVIFV 202
|
250 260
....*....|....*....|....*..
gi 2217288354 477 AHRLSTV-EHAHLIVVLDKGRVVQQGT 502
Cdd:COG1134 203 SHSMGAVrRLCDRAIWLEKGRLVMDGD 229
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
282-496 |
1.06e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 64.22 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 282 RVDFENVTFTYrtrphtqvlQNVSFSLSP-------GKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDH 354
Cdd:PRK10522 322 TLELRNVTFAY---------QDNGFSVGPinltikrGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 355 KYLHRVISLVSQEPVLFARSITDNisyglptvPFEMVVEAAQKANAH---GFIMELQDGYSTETgekgaQLSGGQKQRVA 431
Cdd:PRK10522 393 EDYRKLFSAVFTDFHLFDQLLGPE--------GKPANPALVEKWLERlkmAHKLELEDGRISNL-----KLSKGQKKRLA 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217288354 432 MARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQK--HTVLIIAHRLSTVEHAHLIVVLDKGR 496
Cdd:PRK10522 460 LLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEmgKTIFAISHDDHYFIHADRLLEMRNGQ 526
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
296-459 |
1.42e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.60 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 296 PHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKY-LHRVISLVSQE-PVLFAR 373
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQElNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 374 SITDNISYG-LPTVPFeMVVEAAQKANAHGFIMELqdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSAL 452
Cdd:PRK10982 89 SVMDNMWLGrYPTKGM-FVDQDKMYRDTKAIFDEL--DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
....*...
gi 2217288354 453 -DAESEYL 459
Cdd:PRK10982 166 tEKEVNHL 173
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
283-501 |
1.85e-10 |
|
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: 61.01 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRT-------------------RPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVL 343
Cdd:cd03220 1 IELENVSKSYPTykggssslkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 344 LDGKPISaydhkylhrVISL-VSQEPVLFARsitDNIS-----YGLPTvpfemvVEAAQKANahgFIMELqdgysTETGE 417
Cdd:cd03220 81 VRGRVSS---------LLGLgGGFNPELTGR---ENIYlngrlLGLSR------KEIDEKID---EIIEF-----SELGD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 418 KGAQ----LSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKHTVLIIA-HRLSTV-EHAHLIVV 491
Cdd:cd03220 135 FIDLpvktYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIkRLCDRALV 214
|
250
....*....|
gi 2217288354 492 LDKGRVVQQG 501
Cdd:cd03220 215 LEKGKIRFDG 224
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
297-499 |
1.91e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 60.74 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 297 HTQVLQNVSFSLSPGKVTALVGPSGSGKSS---CVNILENFYPLEGGRVLLDGKpisaydhkylhrvislVSQEpvlfaR 373
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTllrLLAGALKGTPVAGCVDVPDNQ----------------FGRE-----A 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 374 SITDNIsygLPTVPFEMVVEAaqkANAHGfimeLQDGYSTETgeKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD 453
Cdd:COG2401 101 SLIDAI---GRKGDFKDAVEL---LNAVG----LSDAVLWLR--RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2217288354 454 AESEYLIQQAIHGNLQKH--TVLIIAHRlSTVEHA---HLIVVLDKGRVVQ 499
Cdd:COG2401 169 RQTAKRVARNLQKLARRAgiTLVVATHH-YDVIDDlqpDLLIFVGYGGVPE 218
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
301-498 |
2.56e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.05 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 301 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILenfypleGGRVLLD-GKPISAYDhkylhRVISLVSQEPvlfARSITDN- 378
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDdGRIIYEQD-----LIVARLQQDP---PRNVEGTv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 379 --------------------ISYGLPTVPFEMVVEAAQKANAhgfIMELQDGYSTET-------------GEKGAQLSGG 425
Cdd:PRK11147 84 ydfvaegieeqaeylkryhdISHLVETDPSEKNLNELAKLQE---QLDHHNLWQLENrinevlaqlgldpDAALSSLSGG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217288354 426 QKQRVAMARALVRNPPVLILDEATSALDAES-EYLiqqaiHGNLQ--KHTVLIIAHRLSTVEH-AHLIVVLDKGRVV 498
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIETiEWL-----EGFLKtfQGSIIFISHDRSFIRNmATRIVDLDRGKLV 232
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
301-499 |
2.96e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.50 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 301 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPlEG---GRVLLDGKP-----ISAYDHkylhRVISLVSQE----P 368
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP-HGsyeGEILFDGEVcrfkdIRDSEA----LGIVIIHQElaliP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 369 VLfarSITDNISYGLPTVPF------EMVVEAAQKANAHGfimeLQDGYSTETGEKGAqlsgGQKQRVAMARALVRNPPV 442
Cdd:NF040905 92 YL---SIAENIFLGNERAKRgvidwnETNRRARELLAKVG----LDESPDTLVTDIGV----GKQQLVEIAKALSKDVKL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217288354 443 LILDEATSAL-DAESEYLIQQAIHgnLQKH--TVLIIAHRLSTVEH-AHLIVVLDKGRVVQ 499
Cdd:NF040905 161 LILDEPTAALnEEDSAALLDLLLE--LKAQgiTSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
2-252 |
4.75e-10 |
|
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: 60.59 E-value: 4.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 2 DQFSTAVVIVCLLA-----IGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDL---ISRLTSDTT 73
Cdd:cd18582 30 ASALLAVPLLLLLAyglarILSSLFNELRDALFARVSQRAVRRLALRVFRHLHSLSLRFHLSRKTGALsraIERGTRGIE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 74 MVSDLVSQNInvfLRNTVKVTGVVVFMFSL-SWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETIS 152
Cdd:cd18582 110 FLLRFLLFNI---LPTILELLLVCGILWYLyGWSYALITLVTVALYVAFTIKVTEWRTKFRREMNEADNEANAKAVDSLL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 153 AMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEF 232
Cdd:cd18582 187 NYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQALIISLGLTAIMLLAAQGVVAGTLTVGDFVLVNTYLL 266
|
250 260
....*....|....*....|
gi 2217288354 233 VLGDCMESVGSVYSGLMQGV 252
Cdd:cd18582 267 QLYQPLNFLGFVYREIRQSL 286
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
301-495 |
5.07e-10 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 58.49 E-value: 5.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 301 LQNVSFSLSPGKVTALVGPSGSGKSSCVNilENFYplEGGRVLLDGKPiSAYDHKYLHRVISLvsqepvlfaRSITDNis 380
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLY--ASGKARLISFL-PKFSRNKLIFIDQL---------QFLIDV-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 381 yGLptvpfemvveaaqkanahgfimelqdGYSTeTGEKGAQLSGGQKQRVAMARALVRNPP--VLILDEATSALDAESEY 458
Cdd:cd03238 75 -GL--------------------------GYLT-LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180 190
....*....|....*....|....*....|....*...
gi 2217288354 459 LIQQAIHGNL-QKHTVLIIAHRLSTVEHAHLIVVLDKG 495
Cdd:cd03238 127 QLLEVIKGLIdLGNTVILIEHNLDVLSSADWIIDFGPG 164
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
295-525 |
9.45e-10 |
|
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: 61.57 E-value: 9.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 295 RPHTQVLqNVSFSLSpgKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAyDHKYLHRVISLVSQEPVLFARS 374
Cdd:TIGR01257 943 RPAVDRL-NITFYEN--QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHL 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 375 itdnisyglpTVPFEMVVEAAQKANAH---GFIME--LQD-GYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEA 448
Cdd:TIGR01257 1019 ----------TVAEHILFYAQLKGRSWeeaQLEMEamLEDtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 449 TSALDAESEYLIQQAIHGNLQKHTVLIIAHRLSTVE-HAHLIVVLDKGRVVQQGTHQQL--LAQGGLYAKLVqRQMLGLQ 525
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGTPLFLknCFGTGFYLTLV-RKMKNIQ 1167
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
283-508 |
1.12e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 58.74 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHR-VI 361
Cdd:PRK11614 6 LSFDKVSAHY---GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMReAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 362 SLVSQEPVLFAR-SITDNISYGlptvpfEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNP 440
Cdd:PRK11614 83 AIVPEGRRVFSRmTVEENLAMG------GFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217288354 441 PVLILDEATSALdaeSEYLIQQaIHGNLQK-----HTVLIIAHRLS-TVEHAHLIVVLDKGRVVQQGTHQQLLA 508
Cdd:PRK11614 157 RLLLLDEPSLGL---APIIIQQ-IFDTIEQlreqgMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLA 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
303-464 |
1.76e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.02 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 303 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEP----VLFARSITD 377
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpQDGLANGIVYISEDRkrdgLVLGMSVKE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 378 NISY-GLPTVPFEMVV--EAAQKANAHGFImelqDGYSTETGEKGAQ---LSGGQKQRVAMARALVRNPPVLILDEATSA 451
Cdd:PRK10762 350 NMSLtALRYFSRAGGSlkHADEQQAVSDFI----RLFNIKTPSMEQAiglLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
|
170
....*....|...
gi 2217288354 452 LDAESEYLIQQAI 464
Cdd:PRK10762 426 VDVGAKKEIYQLI 438
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
298-502 |
2.10e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.11 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 298 TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENF--YPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEPVL---- 370
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEpEERAHLGIFLAFQYPIEipgv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 371 ----FARSI--TDNISYGLPTV-PFEMVVEAAQKANahgfIMELQDGYSTETGEKGaqLSGGQKQRVAMARALVRNPPVL 443
Cdd:CHL00131 100 snadFLRLAynSKRKFQGLPELdPLEFLEIINEKLK----LVGMDPSFLSRNVNEG--FSGGEKKRNEILQMALLDSELA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217288354 444 ILDEATSALDAESEYLIQQAIHgNL--QKHTVLIIAH--RLSTVEHAHLIVVLDKGRVVQQGT 502
Cdd:CHL00131 174 ILDETDSGLDIDALKIIAEGIN-KLmtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
301-502 |
2.62e-09 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 58.01 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 301 LQNVSFSLSPGKVTALVGPSGSGKSSCVNilENFYPLEGGRVLLDGKPISAYD----HKYLHRVIsLVSQEPV------- 369
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIN--DTLYPALARRLHLKKEQPGNHDriegLEHIDKVI-VIDQSPIgrtprsn 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 370 -------------LF------AR--SITDNISYGLPTVP--FEMVVEAAQK-----ANAHGFIMELQD---GYSTeTGEK 418
Cdd:cd03271 88 patytgvfdeireLFcevckgKRynRETLEVRYKGKSIAdvLDMTVEEALEffeniPKIARKLQTLCDvglGYIK-LGQP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 419 GAQLSGGQKQRVAMARALVR---NPPVLILDEATSALDAESeylIQQAIHGnLQK-----HTVLIIAHRLSTVEHAHLIV 490
Cdd:cd03271 167 ATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHD---VKKLLEV-LQRlvdkgNTVVVIEHNLDVIKCADWII 242
|
250
....*....|....*...
gi 2217288354 491 VL-----DK-GRVVQQGT 502
Cdd:cd03271 243 DLgpeggDGgGQVVASGT 260
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
296-496 |
3.47e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.36 E-value: 3.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 296 PHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNIL----ENFyplEGGRVLLDGKPISaydhkYLhrvislvSQEPVL- 370
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMagvdKEF---EGEARPAPGIKVG-----YL-------PQEPQLd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 371 FARSITDNISYGLPTVpfemvVEAAQKANAHGFIMELQDGYSTETGEKGAQ----------------------------- 421
Cdd:PRK11819 83 PEKTVRENVEEGVAEV-----KAALDRFNEIYAAYAEPDADFDALAAEQGElqeiidaadawdldsqleiamdalrcppw 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 422 ------LSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQaiHgnLQKH--TVLIIAH-R--LSTVehAHLIV 490
Cdd:PRK11819 158 dakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQ--F--LHDYpgTVVAVTHdRyfLDNV--AGWIL 231
|
....*.
gi 2217288354 491 VLDKGR 496
Cdd:PRK11819 232 ELDRGR 237
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
297-483 |
2.18e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.04 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 297 HTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILE---NFYPLEGGRVLLDGKPISAydhkYLHRVISLVSQEPVLFAR 373
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAervTTGVITGGDRLVNGRPLDS----SFQRSIGYVQQQDLHLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 374 S-ITDNISYG----LP-TVPFE---MVVEAAQKanahgfIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLI 444
Cdd:TIGR00956 851 StVRESLRFSaylrQPkSVSKSekmEYVEEVIK------LLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLL 924
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2217288354 445 -LDEATSALDAESEYLIQQAIHgNLQKH--TVLIIAHRLSTV 483
Cdd:TIGR00956 925 fLDEPTSGLDSQTAWSICKLMR-KLADHgqAILCTIHQPSAI 965
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
294-469 |
2.29e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.47 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 294 TRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKylhRVISLVSQEPVLFAR 373
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS---RFMAYLGHLPGLKAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 374 -SITDNISY--GLPTVpfemvvEAAQKANAHGFIMELQDGYSTETgekgAQLSGGQKQRVAMARALVRNPPVLILDEATS 450
Cdd:PRK13543 97 lSTLENLHFlcGLHGR------RAKQMPGSALAIVGLAGYEDTLV----RQLSAGQKKRLALARLWLSPAPLWLLDEPYA 166
|
170
....*....|....*....
gi 2217288354 451 ALDAESEYLIQQAIHGNLQ 469
Cdd:PRK13543 167 NLDLEGITLVNRMISAHLR 185
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
292-507 |
3.46e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.07 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 292 YRTRPHTQVL------------QNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLH 358
Cdd:PRK11288 248 YRPRPLGEVRlrldglkgpglrEPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSpRDAIR 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 359 RVISLV----SQEPVLFARSITDN--ISYGLPTVPFEMVVEAAQKA-NAHGFIMELQdgYSTETGE-KGAQLSGGQKQRV 430
Cdd:PRK11288 328 AGIMLCpedrKAEGIIPVHSVADNinISARRHHLRAGCLINNRWEAeNADRFIRSLN--IKTPSREqLIMNLSGGNQQKA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 431 AMARALVRNPPVLILDEATSALD--AESEylIQQAIHgNL--QKHTVLIIAHRLSTVEH-AHLIVVLDKGRVV-----QQ 500
Cdd:PRK11288 406 ILGRWLSEDMKVILLDEPTRGIDvgAKHE--IYNVIY-ELaaQGVAVLFVSSDLPEVLGvADRIVVMREGRIAgelarEQ 482
|
....*..
gi 2217288354 501 GTHQQLL 507
Cdd:PRK11288 483 ATERQAL 489
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
4-160 |
3.57e-08 |
|
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: 55.30 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 4 FSTAVVIVCLLAIGSSFAAGIRGgiftlifARlniRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNI 83
Cdd:cd18602 59 LSLGAVILSLVTNLAGELAGLRA-------AR---RLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 84 NVFLRNTVKV-TGVVVFMFSLSWQLslvtFMGFPIImMVSNIYGKYYKRLSKEVQ--NALARA---SNTAeETISAMKTV 157
Cdd:cd18602 129 ERLLRFLLLClSAIIVNAIVTPYFL----IALIPII-IVYYFLQKFYRASSRELQrlDNITKSpvfSHFS-ETLGGLTTI 202
|
...
gi 2217288354 158 RSF 160
Cdd:cd18602 203 RAF 205
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
303-497 |
3.79e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.83 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 303 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHK-YLHRVISLVS---QEPVLFARS-ITD 377
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAqRLARGLVYLPedrQSSGLYLDApLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 378 NI-SYGLPTVPFeMVVEAAQKANAHGFIMELqdGYSTETGEKGAQ-LSGGQKQRVAMARALVRNPPVLILDEATSALDAE 455
Cdd:PRK15439 361 NVcALTHNRRGF-WIKPARENAVLERYRRAL--NIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2217288354 456 SEYLIQQAIHGNLQKHT-VLIIAHRLSTVEH-AHLIVVLDKGRV 497
Cdd:PRK15439 438 ARNDIYQLIRSIAAQNVaVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
243-507 |
4.27e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.95 E-value: 4.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 243 SVYSGLMQGVGAAEKVF-----EFIDRQPTMVHdgslAPDHLEGRVDFE--NVTFTYRTRphtqvLQNVSFSLSPGKVTA 315
Cdd:PRK09700 223 SVCSGMVSDVSNDDIVRlmvgrELQNRFNAMKE----NVSNLAHETVFEvrNVTSRDRKK-----VRDISFSVCRGEILG 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 316 LVGPSGSGKSSCVNILENFYPLEGGRVLLDGK---PISAYDHkyLHRVISLVSQ---EPVLFAR-SITDN--ISYGLPTV 386
Cdd:PRK09700 294 FAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisPRSPLDA--VKKGMAYITEsrrDNGFFPNfSIAQNmaISRSLKDG 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 387 PFEMVV------EAAQKANAHGFIMELQdgySTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD--AESE- 457
Cdd:PRK09700 372 GYKGAMglfhevDEQRTAENQRELLALK---CHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDvgAKAEi 448
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2217288354 458 YLIQQAIHGnlQKHTVLIIAHRLstvehAHLIVVLDKGRVVQQGTHQQLL 507
Cdd:PRK09700 449 YKVMRQLAD--DGKVILMVSSEL-----PEIITVCDRIAVFCEGRLTQIL 491
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
406-540 |
4.38e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.13 E-value: 4.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 406 ELQDGYS-TET-GEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQK-HTVLIIAHRLST 482
Cdd:NF000106 127 ELLERFSlTEAaGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEE 206
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217288354 483 VEH-AHLIVVLDKGRVVQQGTHQQLLAQGG--------LYAKLVQRQM-----LGLQPAADFTAGHNEPVAN 540
Cdd:NF000106 207 AEQlAHELTVIDRGRVIADGKVDELKTKVGgrtlqirpAHAAELDRMVgaiaqAGLDGIAGATADHEDGVVN 278
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
287-509 |
5.02e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 54.73 E-value: 5.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 287 NVTFTYRTRPHTQVlQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEG---GRVLLDGKPISAYDHKYLHRV--- 360
Cdd:PRK09473 19 RVTFSTPDGDVTAV-NDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPEKELNKLrae 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 361 -ISLVSQEPVlfaRSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQL-----SGGQKQRVAMAR 434
Cdd:PRK09473 98 qISMIFQDPM---TSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMyphefSGGMRQRVMIAM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 435 ALVRNPPVLILDEATSALDAESEYLIQQAIhgNLQKH----TVLIIAHRLSTVehAHL---IVVLDKGRVVQQGTHQQLL 507
Cdd:PRK09473 175 ALLCRPKLLIADEPTTALDVTVQAQIMTLL--NELKRefntAIIMITHDLGVV--AGIcdkVLVMYAGRTMEYGNARDVF 250
|
..
gi 2217288354 508 AQ 509
Cdd:PRK09473 251 YQ 252
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
305-481 |
7.40e-08 |
|
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: 53.52 E-value: 7.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 305 SFSL------SPGKVTALVGPSGSGKSSCVNILENFYPLEGGRvlLDGKP-----ISAYD----HKYLHRVIS------- 362
Cdd:cd03236 14 SFKLhrlpvpREGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPdwdeiLDEFRgselQNYFTKLLEgdvkviv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 ---LVSQEPVLFARSITDNISYGLPTVPFEMVVEAaqkanahgfiMELQDGYSTETgekgAQLSGGQKQRVAMARALVRN 439
Cdd:cd03236 92 kpqYVDLIPKAVKGKVGELLKKKDERGKLDELVDQ----------LELRHVLDRNI----DQLSGGELQRVAIAAALARD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2217288354 440 PPVLILDEATSALDAESEYLIQQAIHGnLQKHT--VLIIAHRLS 481
Cdd:cd03236 158 ADFYFFDEPSSYLDIKQRLNAARLIRE-LAEDDnyVLVVEHDLA 200
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
307-478 |
9.10e-08 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 53.18 E-value: 9.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 307 SLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISaYDHKYLHRVISLVSQEpvlFARSITDnisyGLPTV 386
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-YKPQYIKADYEGTVRD---LLSSITK----DFYTH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 387 PFeMVVEAAQKanahgfiMELQDGYSTETGEkgaqLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHG 466
Cdd:cd03237 93 PY-FKTEIAKP-------LQIEQILDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
|
170
....*....|....
gi 2217288354 467 NLQKH--TVLIIAH 478
Cdd:cd03237 161 FAENNekTAFVVEH 174
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
283-501 |
1.12e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.87 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRPhtQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGK-PISAYDHkylHRVI 361
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKvRMAVFSQ---HHVD 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 362 SL-VSQEPVLFarsitdnISYGLPTVPfemvveaAQKANAH----GFI--MELQDGYStetgekgaqLSGGQKQRVAMAR 434
Cdd:PLN03073 584 GLdLSSNPLLY-------MMRCFPGVP-------EQKLRAHlgsfGVTgnLALQPMYT---------LSGGQKSRVAFAK 640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217288354 435 ALVRNPPVLILDEATSALDAES-EYLIQQAIhgnLQKHTVLIIAHrlstveHAHLIV-VLDKGRVVQQG 501
Cdd:PLN03073 641 ITFKKPHILLLDEPSNHLDLDAvEALIQGLV---LFQGGVLMVSH------DEHLISgSVDELWVVSEG 700
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
291-498 |
1.25e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 54.26 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 291 TYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEP- 368
Cdd:COG3845 264 SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSpRERRRLGVAYIPEDRl 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 369 ----VLfARSITDNI----SYGLPTVPFEMVVEAAQKANAHGFIMELQ---DGYSTETGekgaQLSGGQKQRVAMARALV 437
Cdd:COG3845 344 grglVP-DMSVAENLilgrYRRPPFSRGGFLDRKAIRAFAEELIEEFDvrtPGPDTPAR----SLSGGNQQKVILARELS 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217288354 438 RNPPVLILDEATSALDAESeyliQQAIHGNLQKH-----TVLIIAHRLSTV-EHAHLIVVLDKGRVV 498
Cdd:COG3845 419 RDPKLLIAAQPTRGLDVGA----IEFIHQRLLELrdagaAVLLISEDLDEIlALSDRIAVMYEGRIV 481
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
301-506 |
1.33e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 54.63 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 301 LQNVSFSLSPGKVTALVGPSGSGKSSCVN-----ILENFypLEGGRVLLD-GKPISAYDHkyLHRVISlVSQEPV----- 369
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINdtlypALANR--LNGAKTVPGrYTSIEGLEH--LDKVIH-IDQSPIgrtpr 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 370 ---------------LFARS--------------------------------ITDNIsygLPT--VP------------- 387
Cdd:TIGR00630 699 snpatytgvfdeireLFAETpeakvrgytpgrfsfnvkggrceacqgdgvikIEMHF---LPDvyVPcevckgkrynret 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 388 -------------FEMVVEAAQK-----ANAHGFIMELQD---GYSTeTGEKGAQLSGGQKQRVAMARALVR---NPPVL 443
Cdd:TIGR00630 776 levkykgkniadvLDMTVEEAYEffeavPSISRKLQTLCDvglGYIR-LGQPATTLSGGEAQRIKLAKELSKrstGRTLY 854
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217288354 444 ILDEATSALDAES----EYLIQQAIHgnlQKHTVLIIAHRLSTVEHAHLIVVL-----DK-GRVVQQGTHQQL 506
Cdd:TIGR00630 855 ILDEPTTGLHFDDikklLEVLQRLVD---KGNTVVVIEHNLDVIKTADYIIDLgpeggDGgGTVVASGTPEEV 924
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
8-228 |
1.46e-07 |
|
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: 53.32 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 8 VVIVCLLAIGSSFAAG-IRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVF 86
Cdd:cd18779 44 LGLGLAALVLTQLLAGlLRSHLLLRLRTRLDTQLTLGFLEHLLRLPYRFFQQRSTGDLLMRLSSNATIRELLTSQTLSAL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 87 LrNTVKVTGVVVFMFSLSWQLSLVTfMGFPII----MMVSNiygKYYKRLSKEVQNALARASNTAEETISAMKTVRSFAN 162
Cdd:cd18779 124 L-DGTLVLGYLALLFAQSPLLGLVV-LGLAALqvalLLATR---RRVRELMARELAAQAEAQSYLVEALSGIETLKASGA 198
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 163 EEEEAEVYLRKL--QQVYKLNRKEAAAYMyyvwGSGLTLL--VVQVSILYYGGHLVISGQMTSGNLIAFI 228
Cdd:cd18779 199 EDRALDRWSNLFvdQLNASLRRGRLDALV----DALLATLrlAAPLVLLWVGAWQVLDGQLSLGTMLALN 264
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
274-478 |
1.48e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.87 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 274 LAPDhlEGRVDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPlEG--------GRVLLD 345
Cdd:PRK10938 254 LPAN--EPRIVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHP-QGysndltlfGRRRGS 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 346 GKPIsaYDHKylhRVISLVSQEPVLFAR---SITDNI------SYGLptvpFEMVVEAAQKanahgFIMELQD--GYSTE 414
Cdd:PRK10938 328 GETI--WDIK---KHIGYVSSSLHLDYRvstSVRNVIlsgffdSIGI----YQAVSDRQQK-----LAQQWLDilGIDKR 393
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 415 TGEKGAQ-LSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAI-----HGNLQkhtVLIIAH 478
Cdd:PRK10938 394 TADAPFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVdvlisEGETQ---LLFVSH 460
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
96-226 |
2.29e-07 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 52.61 E-value: 2.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 96 VVVFMFSlSWqLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQ 175
Cdd:cd18586 131 AVIFLIH-PP-LGWVALVGAPVLVGLAWLNHRATRKPLGEANEAQAARDALAAETLRNAETIKALGMLGNLRRRWEARHA 208
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2217288354 176 QVYKL-NRKEAAAYMYYVWGSGLTlLVVQVSILYYGGHLVISGQMTSGNLIA 226
Cdd:cd18586 209 ETLELqIRASDLAGAISAIGKTLR-MALQSLILGVGAYLVIDGELTIGALIA 259
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
283-479 |
2.32e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 51.49 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRVIS 362
Cdd:PRK13540 2 LDVIELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 LVSQEPVLFARSITDNISYGLPTVPFEMVVEAAQKANAHGFIMELQDGYstetgekgaqLSGGQKQRVAMARALVRNPPV 442
Cdd:PRK13540 79 VGHRSGINPYLTLRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGL----------LSSGQKRQVALLRLWMSKAKL 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 2217288354 443 LILDEATSALDAESEYLIQQAIHGNLQK-HTVLIIAHR 479
Cdd:PRK13540 149 WLLDEPLVALDELSLLTIITKIQEHRAKgGAVLLTSHQ 186
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
308-480 |
3.26e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 308 LSPGKVTALVGPSGSGKSSCVNILE-----NFyplegGRVllDGKP-----ISAYDHKYLHRVISLVSQEPVLFARSI-- 375
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSgelipNL-----GDY--EEEPswdevLKRFRGTELQNYFKKLYNGEIKVVHKPqy 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 376 TDNIsyglPTVPFEMVVEAAQKANAHGFIMELQD--GYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALD 453
Cdd:PRK13409 169 VDLI----PKVFKGKVRELLKKVDERGKLDEVVErlGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
170 180
....*....|....*....|....*..
gi 2217288354 454 AESEYLIQQAIHGNLQKHTVLIIAHRL 480
Cdd:PRK13409 245 IRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
6-252 |
3.83e-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: 51.84 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 6 TAVVIVCLLAIGSSFAAGIRggifTLIFARLN----IRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSq 81
Cdd:cd18560 39 TLILLYALLRFSSKLLKELR----SLLYRRVQqnayRELSLKTFAHLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLS- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 82 ninVFLRNTVK-----VTGVVVFMFSLSWQLSLVTFMGFpIIMMVSNIYG-KYYKRLSKEVQNALARASNTAEETISAMK 155
Cdd:cd18560 114 ---YLVFYLVPtllelIVVSVVFAFHFGAWLALIVFLSV-LLYGVFTIKVtEWRTKFRRAANKKDNEAHDIAVDSLLNFE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 156 TVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLG 235
Cdd:cd18560 190 TVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQLGLTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLF 269
|
250
....*....|....*..
gi 2217288354 236 DCMESVGSVYSGLMQGV 252
Cdd:cd18560 270 QPLNFLGTIYRMIIQSL 286
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
13-201 |
5.75e-07 |
|
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: 51.32 E-value: 5.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 13 LLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVK 92
Cdd:cd18606 43 GLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 93 VTGVVVfmfslswqLSLVTF----MGFPIIMMVSNIYGKYYKRLSKEVQ--NALARAS--NTAEETISAMKTVRSFANEe 164
Cdd:cd18606 123 IIGTFI--------LIIIYLpwfaIALPPLLVLYYFIANYYRASSRELKrlESILRSFvyANFSESLSGLSTIRAYGAQ- 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2217288354 165 eeaEVYLRKLQqvYKLNRKEAAAYMYYV---W--------GSGLTLLV 201
Cdd:cd18606 194 ---DRFIKKNE--KLIDNMNRAYFLTIAnqrWlairldllGSLLVLIV 236
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
301-476 |
5.93e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.04 E-value: 5.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 301 LQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQE----------PV 369
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAINHGFALVTEErrstgiyaylDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 370 LFARSITDNISYglpTVPFEMVVEAAQKANAHGFI--MELQD-GYSTETGekgaQLSGGQKQRVAMARALVRNPPVLILD 446
Cdd:PRK10982 344 GFNSLISNIRNY---KNKVGLLDNSRMKSDTQWVIdsMRVKTpGHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLD 416
|
170 180 190
....*....|....*....|....*....|
gi 2217288354 447 EATSALDAESEYLIQQAIHGNLQKHTVLII 476
Cdd:PRK10982 417 EPTRGIDVGAKFEIYQLIAELAKKDKGIII 446
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
39-258 |
9.59e-07 |
|
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: 50.74 E-value: 9.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 39 RLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPII 118
Cdd:cd18561 70 HLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 119 MMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRKLQQVYKLNRKEAAAymyYVWGSGLT 198
Cdd:cd18561 150 PLSPALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAV---SLLSSGIM 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217288354 199 LLVVQVSI---LYYGGHLVISGQMTSGNLIAFIiyeFVLGDC---MESVGSVYSGLMQGVGAAEKV 258
Cdd:cd18561 227 GLATALGTalaLGVGALRVLGGQLTLSSLLLIL---FLSREFfrpLRDLGAYWHAGYQGISAADSI 289
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
307-484 |
1.35e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 48.51 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 307 SLSPGKVTALVGPSGSGKSscvNILenfypleggrvlldgkpisaydhkylhRVISLVsqepVLFARSITDNISYGLPTV 386
Cdd:cd03227 17 TFGEGSLTIITGPNGSGKS---TIL---------------------------DAIGLA----LGGAQSATRRRSGVKAGC 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 387 PfemvvEAAQKANAHGFIMelqdgystetgekgaQLSGGQKQRVAMARAL----VRNPPVLILDEATSALDAESEYLIQQ 462
Cdd:cd03227 63 I-----VAAVSAELIFTRL---------------QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAE 122
|
170 180
....*....|....*....|...
gi 2217288354 463 AIHGNLQKH-TVLIIAHRLSTVE 484
Cdd:cd03227 123 AILEHLVKGaQVIVITHLPELAE 145
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
284-478 |
1.57e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.10 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 284 DFENVTFTYrtrPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNI-LENFYPlEGGRVLLDGKPISAY-DHkylHRVI 361
Cdd:PRK11147 321 EMENVNYQI---DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQLQA-DSGRIHCGTKLEVAYfDQ---HRAE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 362 slvsQEPvlfARSITDNISYGLPTVpfeMVveAAQKANAHGFimeLQD----GYSTETGEKGaqLSGGQKQRVAMARALV 437
Cdd:PRK11147 394 ----LDP---EKTVMDNLAEGKQEV---MV--NGRPRHVLGY---LQDflfhPKRAMTPVKA--LSGGERNRLLLARLFL 456
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2217288354 438 RNPPVLILDEATSALDAESEYLIQQAIHGnlQKHTVLIIAH 478
Cdd:PRK11147 457 KPSNLLILDEPTNDLDVETLELLEELLDS--YQGTVLLVSH 495
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
8-192 |
1.59e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 50.16 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 8 VVIVCLLAIGSSFAAGIRGGIFTL--------IFARLnirlrnclFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLV 79
Cdd:cd18604 46 LGIYALISLLSVLLGTLRYLLFFFgslrasrkLHERL--------LHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSEL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 80 SQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFmgfpIIMMVSNIYGKYYKRLSKEVQ--NALARAS--NTAEETISAMK 155
Cdd:cd18604 118 ADSLSSLLESTLSLLVILIAIVVVSPAFLLPAV----VLAALYVYIGRLYLRASRELKrlESVARSPilSHFGETLAGLV 193
|
170 180 190
....*....|....*....|....*....|....*..
gi 2217288354 156 TVRSFANEeeeaEVYLRKLQQvyKLNRKEAAAYMYYV 192
Cdd:cd18604 194 TIRAFGAE----ERFIEEMLR--RIDRYSRAFRYLWN 224
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
305-453 |
2.01e-06 |
|
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: 50.55 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 305 SFSL------SPGKVTALVGPSGSGKSSCVNILE-----NFyplegGRVllDGKP-----ISAYD----HKYLHRVIS-- 362
Cdd:COG1245 87 GFRLyglpvpKKGKVTGILGPNGIGKSTALKILSgelkpNL-----GDY--DEEPswdevLKRFRgtelQDYFKKLANge 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 363 -LVSQEP--VlfarsitDNIsyglPTVPFEMVVEAAQKANAHGFIMELQDGYSTET--GEKGAQLSGGQKQRVAMARALV 437
Cdd:COG1245 160 iKVAHKPqyV-------DLI----PKVFKGTVRELLEKVDERGKLDELAEKLGLENilDRDISELSGGELQRVAIAAALL 228
|
170
....*....|....*.
gi 2217288354 438 RNPPVLILDEATSALD 453
Cdd:COG1245 229 RDADFYFFDEPSSYLD 244
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
298-520 |
3.70e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 48.63 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 298 TQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNIL--ENFYPLEGGRVLLDGKPISAYD-HKYLHRVISLVSQEPV----- 369
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSpEDRAGEGIFMAFQYPVeipgv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 370 ---LFARSITDNI-SY----GLPTVPFEMVVEAAQKanahgfIMELQDGYSTETGEKGaqLSGGQKQRVAMARALVRNPP 441
Cdd:PRK09580 94 snqFFLQTALNAVrSYrgqePLDRFDFQDLMEEKIA------LLKMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 442 VLILDEATSALDAESEYLIQQAIHgNLQ--KHTVLIIAH--RLSTVEHAHLIVVLDKGRVVQQGTH---QQLLAQGglYA 514
Cdd:PRK09580 166 LCILDESDSGLDIDALKIVADGVN-SLRdgKRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFtlvKQLEEQG--YG 242
|
....*.
gi 2217288354 515 KLVQRQ 520
Cdd:PRK09580 243 WLTEQQ 248
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
286-511 |
4.30e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.74 E-value: 4.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 286 ENVTFTYRTrphTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISayDHKylHRvislvs 365
Cdd:NF033858 5 EGVSHRYGK---TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA--DAR--HR------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 366 qepvlfaRSITDNISY---GL-----PTVPfemVVEAAQ---------KANAHGFIMELQDGysteTG-----EKGA-QL 422
Cdd:NF033858 72 -------RAVCPRIAYmpqGLgknlyPTLS---VFENLDffgrlfgqdAAERRRRIDELLRA----TGlapfaDRPAgKL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 423 SGGQKQRVAMARALVRNPPVLILDEATSALDAES-----EyLIQQaIHGNLQKHTVLIiahrlST--VEHA----HLiVV 491
Cdd:NF033858 138 SGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSrrqfwE-LIDR-IRAERPGMSVLV-----ATayMEEAerfdWL-VA 209
|
250 260
....*....|....*....|
gi 2217288354 492 LDKGRVVQQGTHQQLLAQGG 511
Cdd:NF033858 210 MDAGRVLATGTPAELLARTG 229
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
283-508 |
4.83e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 48.65 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRPH-TQVLQNVSFSLSPGKVTALVGPSGSGKS----SCVNILENFYPLEGGRVLLDGKPISAYDHKYL 357
Cdd:PRK15093 4 LDIRNLTIEFKTSDGwVKAVDRVSMTLTEGEIRGLVGESGSGKSliakAICGVTKDNWRVTADRMRFDDIDLLRLSPRER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 358 HRVI----SLVSQEP---VLFARSITDNISYGLP----------------TVPFEMVVEAAQKAnaHGFIMElqdGYSTE 414
Cdd:PRK15093 84 RKLVghnvSMIFQEPqscLDPSERVGRQLMQNIPgwtykgrwwqrfgwrkRRAIELLHRVGIKD--HKDAMR---SFPYE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 415 tgekgaqLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQKH--TVLIIAHRLSTVEH-AHLIVV 491
Cdd:PRK15093 159 -------LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLSQwADKINV 231
|
250
....*....|....*..
gi 2217288354 492 LDKGRVVQQGTHQQLLA 508
Cdd:PRK15093 232 LYCGQTVETAPSKELVT 248
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
290-501 |
6.08e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.34 E-value: 6.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 290 FTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNIL----ENFYPLEGGRVLLDGKPISAYDHKYLHRVI---- 361
Cdd:TIGR00956 66 KKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEIKKHYRGDVVynae 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 362 ------SLVSQEPVLF-ARSITDNISYGLPTvpfeMVVEAAQKANAHGFIMELQDGYSTETGE---KGaqLSGGQKQRVA 431
Cdd:TIGR00956 146 tdvhfpHLTVGETLDFaARCKTPQNRPDGVS----REEYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVS 219
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217288354 432 MARALVRNPPVLILDEATSALDAESEYLIQQAIH--GNLQKHTVLIIAHRLS--TVEHAHLIVVLDKGRVVQQG 501
Cdd:TIGR00956 220 IAEASLGGAKIQCWDNATRGLDSATALEFIRALKtsANILDTTPLVAIYQCSqdAYELFDKVIVLYEGYQIYFG 293
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
305-478 |
1.11e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.27 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 305 SFSLS-------PGKVTALVGPSGSGKSSCVNILE-NFYPLEGGrvlLDGKPISAYDHKYlhrvISLVSQEPV-LFARSI 375
Cdd:PRK13409 352 DFSLEveggeiyEGEVIGIVGPNGIGKTTFAKLLAgVLKPDEGE---VDPELKISYKPQY----IKPDYDGTVeDLLRSI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 376 TDNISyglpTVPFEmvVEAAQKANahgfIMELQDGYSTEtgekgaqLSGGQKQRVAMARALVRNPPVLILDEATSALDAE 455
Cdd:PRK13409 425 TDDLG----SSYYK--SEIIKPLQ----LERLLDKNVKD-------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 487
|
170 180
....*....|....*....|....*
gi 2217288354 456 SEYLIQQAI--HGNLQKHTVLIIAH 478
Cdd:PRK13409 488 QRLAVAKAIrrIAEEREATALVVDH 512
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
97-229 |
1.34e-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: 47.05 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 97 VVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSFAneeeeAE-VYLRKLQ 175
Cdd:cd18587 132 LAVIALIGGPLALVPLVAIPLVLLYGLLLQKPLRRLVEESMRESAQKNALLVESLSGLETIKALG-----AEgRMQRRWE 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2217288354 176 Q-VYKLNRKEAAAYMYYVWGSGLTLLVVQ---VSILYYGGHLVISGQMTSGNLIAFII 229
Cdd:cd18587 207 EaVAALARSSLKSRLLSSSATNFAQFVQQlvtVAIVIVGVYLISDGELTMGGLIACVI 264
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
299-481 |
3.14e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.15 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 299 QVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENfyPLEGGRVLLDGKpISAYDHKylhrvislvsQEPvlFAR----- 373
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGDIR-ISGFPKK----------QET--FARisgyc 958
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 374 ----------SITDNISY-GLPTVPFEmvVEAAQKANAHGFIMEL------QDGYSTETGEKGaqLSGGQKQRVAMARAL 436
Cdd:PLN03140 959 eqndihspqvTVRESLIYsAFLRLPKE--VSKEEKMMFVDEVMELveldnlKDAIVGLPGVTG--LSTEQRKRLTIAVEL 1034
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2217288354 437 VRNPPVLILDEATSALDAESEYLIQQAIHGNLQK-HTVLIIAHRLS 481
Cdd:PLN03140 1035 VANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTgRTVVCTIHQPS 1080
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
303-453 |
5.90e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.89 E-value: 5.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 303 NVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAYDHKYLHRV------ISL-----VSQEPVLF 371
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVgymsqaFSLygeltVRQNLELH 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 372 ARSitdnisYGLP--TVPfEMVVEAAQKanahgFimELQDgystETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEAT 449
Cdd:NF033858 364 ARL------FHLPaaEIA-ARVAEMLER-----F--DLAD----VADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
....
gi 2217288354 450 SALD 453
Cdd:NF033858 426 SGVD 429
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
310-511 |
6.59e-05 |
|
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: 46.16 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 310 PGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGKPISAyDHKYLHRVISLVSQ------------EPVLFARsitd 377
Cdd:TIGR01257 1964 PGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQfdaiddlltgreHLYLYAR---- 2038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 378 nisygLPTVPFEMVVEAAQKAnahgfIMELqdGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSALDAESE 457
Cdd:TIGR01257 2039 -----LRGVPAEEIEKVANWS-----IQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR 2106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2217288354 458 YLIQQAIHGNLQK-HTVLIIAHRLSTVEH-AHLIVVLDKGRVVQQGTHQQLLAQGG 511
Cdd:TIGR01257 2107 RMLWNTIVSIIREgRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
24-164 |
6.68e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 45.00 E-value: 6.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 24 IRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSL 103
Cdd:cd18601 78 LRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVV 157
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217288354 104 S-WqlslvTFMGFPIIMMVSNIYGKYYKRLSKEVQ--NALARAS--NTAEETISAMKTVRSFANEE 164
Cdd:cd18601 158 NpW-----VLIPVIPLVILFLFLRRYYLKTSREVKriEGTTRSPvfSHLSSTLQGLWTIRAYSAQE 218
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
422-495 |
7.58e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 43.71 E-value: 7.58e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217288354 422 LSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIHGNLQ--KHTVLIIAHRLSTVEHAHLIVVLDKG 495
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
283-455 |
8.02e-05 |
|
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: 45.31 E-value: 8.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLL-DGKPISAYDHkylhrvi 361
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKLAYVDQ------- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 362 slvSQEPVLFARSITDNISYGLPTVpfeMV--VEAAQKANAHGFIMELQDgysteTGEKGAQLSGGQKQRVAMARALVRN 439
Cdd:TIGR03719 393 ---SRDALDPNKTVWEEISGGLDII---KLgkREIPSRAYVGRFNFKGSD-----QQKKVGQLSGGERNRVHLAKTLKSG 461
|
170
....*....|....*.
gi 2217288354 440 PPVLILDEATSALDAE 455
Cdd:TIGR03719 462 GNVLLLDEPTNDLDVE 477
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
296-460 |
8.84e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.17 E-value: 8.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 296 PHTQVLQNVSFSLSPGKVTALVGPSGSG----------KSSCVNIlenfypleGGRVLLDGKPIS------AYDHKylhr 359
Cdd:NF040905 271 PERKVVDDVSLNVRRGEIVGIAGLMGAGrtelamsvfgRSYGRNI--------SGTVFKDGKEVDvstvsdAIDAG---- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 360 vISLVSQepvlfarsitDNISYGL---PTVPFEMVVEAAQKANAHGFI---MELQ--DGY-------STETGEKGAQLSG 424
Cdd:NF040905 339 -LAYVTE----------DRKGYGLnliDDIKRNITLANLGKVSRRGVIdenEEIKvaEEYrkkmnikTPSVFQKVGNLSG 407
|
170 180 190
....*....|....*....|....*....|....*.
gi 2217288354 425 GQKQRVAMARALVRNPPVLILDEATSALDAESEYLI 460
Cdd:NF040905 408 GNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEI 443
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
279-478 |
9.40e-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: 45.16 E-value: 9.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 279 LEGRVDFENVTF-----TYRTRPHTQVLQNV-------------SFSLS-------PGKVTALVGPSGSGKSSCVNILEN 333
Cdd:COG1245 309 LDGYLPEENVRIrdepiEFEVHAPRREKEEEtlveypdltksygGFSLEveggeirEGEVLGIVGPNGIGKTTFAKILAG 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 334 FYPLEGGRVLLDGKpISaYDHKYlhrvISLVSQEPV--LFARSITDNIsyglPTVPFEmvVEAAQKANahgfIMELQDGY 411
Cdd:COG1245 389 VLKPDEGEVDEDLK-IS-YKPQY----ISPDYDGTVeeFLRSANTDDF----GSSYYK--TEIIKPLG----LEKLLDKN 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217288354 412 STEtgekgaqLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAI--HGNLQKHTVLIIAH 478
Cdd:COG1245 453 VKD-------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIrrFAENRGKTAMVVDH 514
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
5-191 |
9.76e-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: 44.48 E-value: 9.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 5 STAVVIVCLLAIgssfaagiRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNIN 84
Cdd:cd18599 66 GSILVILLLSLI--------RGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 85 VFLRNTVKVTGVVVF-MFSLSWQLslvtfMGFPIIMMVSNIYGKYYKRLSKEvqnaLARASNTAE--------ETISAMK 155
Cdd:cd18599 138 NFLQNVLLVVFSLIIiAIVFPWFL-----IALIPLAIIFVFLSKIFRRAIRE----LKRLENISRsplfshltATIQGLS 208
|
170 180 190
....*....|....*....|....*....|....*.
gi 2217288354 156 TVRSFANEEEeaevYLRKLQQVykLNRKEAAAYMYY 191
Cdd:cd18599 209 TIHAFNKEKE----FLSKFKKL--LDQNSSAFFLFN 238
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
13-229 |
1.24e-04 |
|
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: 43.97 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 13 LLAIGSSFAAGIRGGIFTLIFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISR----------LTSDT--TMVSDLvs 80
Cdd:cd18571 50 VLFLGSTSIEFIRSWILLHISSRINISIISDFLIKLMRLPISFFDTKMTGDILQRindhsriesfLTSSSlsILFSLL-- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 81 qNINVFlrntvkvtGVVVFMFSlsWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQNALARASNTAEETISAMKTVRSF 160
Cdd:cd18571 128 -NLIVF--------SIVLAYYN--LTIFLIFLIGSVLYILWILLFLKKRKKLDYKRFDLSSENQSKLIELINGMQEIKLN 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217288354 161 AneeeeAEVYLR----KLQ-QVYKLNRKEAAAYMYYVWGSGLTLLVVQVSILYYGGHLVISGQMTSGNLIA--FII 229
Cdd:cd18571 197 N-----SERQKRweweRIQaKLFKINIKSLKLDQYQQIGALFINQLKNILITFLAAKLVIDGEITLGMMLAiqYII 267
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
422-508 |
1.39e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.84 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 422 LSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLI----QQAIHgnLQKHTVLI--IAHRLSTVEHAHLIVVLDKG 495
Cdd:PLN03140 337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIvkclQQIVH--LTEATVLMslLQPAPETFDLFDDIILLSEG 414
|
90
....*....|...
gi 2217288354 496 RVVQQGTHQQLLA 508
Cdd:PLN03140 415 QIVYQGPRDHILE 427
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
422-492 |
1.81e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 1.81e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217288354 422 LSGGQKQRVAMARAL---VRNPPVLILDEATSALDAESeylIQQAIHGNL----QKHTVLIIAHRLSTVEHAHLIVVL 492
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHD---IKALIYVLQslthQGHTVVIIEHNMHVVKVADYVLEL 884
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
287-478 |
2.01e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.11 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 287 NVTFTYRTRPhtqVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENfyPLE--GGRVLLD-----GKpIS----AYDHk 355
Cdd:PRK15064 6 NITMQFGAKP---LFENISVKFGGGNRYGLIGANGCGKSTFMKILGG--DLEpsAGNVSLDpnerlGK-LRqdqfAFEE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 356 ylHRVISLV--SQEPVLFARSITDNIsYGLPtvpfEMVVEAAQKAnahgfiMELQ------DGYSTET--GE--KGA--- 420
Cdd:PRK15064 79 --FTVLDTVimGHTELWEVKQERDRI-YALP----EMSEEDGMKV------ADLEvkfaemDGYTAEAraGEllLGVgip 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217288354 421 ---------QLSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAIhgNLQKHTVLIIAH 478
Cdd:PRK15064 146 eeqhyglmsEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVL--NERNSTMIIISH 210
|
|
| ABC_6TM_McjD_like |
cd18556 |
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ... |
35-252 |
1.46e-03 |
|
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter McjD and similar proteins; This group represents the 6-TM subunit of the ABC transporter McjD that exports the antibacterial peptide microcin J25, which is an antimicrobial peptide produced by Enterobacteriaceae against other microorganisms for survival under nutrient starvation. Thus, the ABC exporter McjD provides self-immunity of the producing bacteria through export of the toxic peptide out of the cell. 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: 350000 Cd Length: 298 Bit Score: 40.70 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 35 RLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNINVFLRNTVKVTGVVVFMFSLSWQLSLVTFMG 114
Cdd:cd18556 74 ELIISISSSYFRYLYEQPKTFFVKENSGDITQRLNQASNDLYTLVRNLSTNILPPLLQLIIAIVVILSSGDYFVAALFLL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 115 FPIIMMVSNIY----------------GKYYKRLSKEVQNALARASNTAEETIsaMKTVRSFANEEEEAevylrklQQVY 178
Cdd:cd18556 154 YAVLFVINNTIftkkivslrndlmdagRKSYSLLTDSVKNIVAAKQNNAFDFL--FKRYEATLTNDRNS-------QKRY 224
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217288354 179 -KLNRKEAAAymyyvwgSGLTLLVVQVSILYYGGHLVISGQMTSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGV 252
Cdd:cd18556 225 wKLTFKMLIL-------NSLLNVILFGLSFFYSLYGVVNGQVSIGHFVLITSYILLLSTPIESLGNMLSELRQSV 292
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
60-229 |
1.61e-03 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 40.54 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 60 RTGDLISRLTSDttmvsdlVSQNINVFLR-------NTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMV-SNIYGKYYKR 131
Cdd:cd18585 90 RSGDLLNRIVAD-------IDTLDNLYLRvlsppvvALLVILATILFLAFFSPALALILLAGLLLAGVViPLLFYRLGKK 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 132 LSKEVQNALARASNTAEETISAMKTVRSFANEEeeaevylRKLQQVYKLNRkeaaAYMYY--------VWGSGLTLLVVQ 203
Cdd:cd18585 163 IGQQLVQLRAELRTELVDGLQGMAELLIFGALE-------RQRQQLEQLSD----ALIKEqrrlarlsGLSQALMILLSG 231
|
170 180
....*....|....*....|....*....
gi 2217288354 204 VS---ILYYGGHLVISGQMTsGNLIAFII 229
Cdd:cd18585 232 LTvwlVLWLGAPLVQNGALD-GALLAMLV 259
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
421-490 |
1.84e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.11 E-value: 1.84e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217288354 421 QLSGGQKQRVAMarALV-----RNP-PVLILDEATSALDAESEYLIQQAIHgNLQKHT-VLIIAHRLSTVEHAHLIV 490
Cdd:pfam02463 1077 LLSGGEKTLVAL--ALIfaiqkYKPaPFYLLDEIDAALDDQNVSRVANLLK-ELSKNAqFIVISLREEMLEKADKLV 1150
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
421-453 |
1.87e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 1.87e-03
10 20 30
....*....|....*....|....*....|...
gi 2217288354 421 QLSGGQKQRVAMARALVRNPPVLILDEATSALD 453
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
2-209 |
2.23e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) 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: 350040 [Multi-domain] Cd Length: 309 Bit Score: 40.17 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 2 DQFSTAVVIVCLLAIGSSFAAGIrGGIFTLIFARLNIRLRNCLF---------RSLVSQETSFFDE-------------- 58
Cdd:cd18596 33 DATVRPWVWVLLLFLGPLLSSLL-DQQYLWIGRRLSVRLRAILTqlifekalrRRDKSGSSKSSESkkkdkeededekss 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 59 NRTGDLISRLTSDTTMVSDLVSqNINVFLRNTVKVTGVVVFMFSLSWQLSLV----TFMGFPIIMMVSNIYGKYYKRLSK 134
Cdd:cd18596 112 ASVGKINNLMSVDANRISEFAA-FLHLLVSAPLQIVIAIVFLYRLLGWSALVglavMVLLLPLNGYLAKRYSRAQKELMK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 135 evqnalARAS--NTAEETISAMKTVRSFANEEE---------EAEvyLRKLQQVYKLNrkeaaAYMYYVWgSGLTLLVVQ 203
Cdd:cd18596 191 ------ARDArvQLVTEVLQGIRMIKFFAWERKweerilearEEE--LKWLRKRFLLD-----LLLSLLW-FLIPILVTV 256
|
....*.
gi 2217288354 204 VSILYY 209
Cdd:cd18596 257 VTFATY 262
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
26-230 |
3.50e-03 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 39.43 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 26 GGIFTLIFARLNIRLRNCLFRSLV--------SQETSFFDENRTGDL---ISRLTSDTTMVSDLVSQNINVFLRNTVkvt 94
Cdd:cd18583 50 GGGLGLLRSWLWIPVEQYSYRALStaafnhvmNLSMDFHDSKKSGEVlkaIEQGSSINDLLEQILFQIVPMIIDLVI--- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 95 GVVVFMFSLSWQLSLVTFMgFPIIMMVSNIY-GKYYKRLSKEVQNALARASNTAEETISAMKTVRSFANEEEEAEVYLRK 173
Cdd:cd18583 127 AIVYLYYLFDPYMGLIVAV-VMVLYVWSTIKlTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREA 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217288354 174 LQqvyklnRKEAAAYMYYVWGSGLTLlvVQVSILYYG--------GHLVISGQMTSGNLIAFIIY 230
Cdd:cd18583 206 VK------NYQKAERKYLFSLNLLNA--VQSLILTLGllagcflaAYQVSQGQATVGDFVTLLTY 262
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
421-456 |
3.98e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 38.74 E-value: 3.98e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2217288354 421 QLSGGQKQ------RVAMARALVRNPPVLILDEATSALDAES 456
Cdd:cd03240 115 RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEN 156
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
283-455 |
4.91e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 39.72 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 283 VDFENVTFTYRTRphtqVL-QNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLdGKPISaydhkylhrvI 361
Cdd:PRK11819 325 IEAENLSKSFGDR----LLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK----------L 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 362 SLVSQ-----EPvlfARSITDNISYGLPTVP---FEMVVEAaqkanahgfimelqdgYSTETGEKGA-------QLSGGQ 426
Cdd:PRK11819 390 AYVDQsrdalDP---NKTVWEEISGGLDIIKvgnREIPSRA----------------YVGRFNFKGGdqqkkvgVLSGGE 450
|
170 180
....*....|....*....|....*....
gi 2217288354 427 KQRVAMARALVRNPPVLILDEATSALDAE 455
Cdd:PRK11819 451 RNRLHLAKTLKQGGNVLLLDEPTNDLDVE 479
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
299-493 |
5.97e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 38.31 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 299 QVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDG-------KPISAYDHKYLHRVISLVSQEPVLF 371
Cdd:PRK13541 14 KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNcninniaKPYCTYIGHNLGLKLEMTVFENLKF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 372 ARSITDNISyglpTVPfemvveaaqkANAHGFimELQDGYStetgEKGAQLSGGQKQRVAMARALVRNPPVLILDEATSA 451
Cdd:PRK13541 94 WSEIYNSAE----TLY----------AAIHYF--KLHDLLD----EKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETN 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2217288354 452 LDAESEYLIQQ--AIHGNlQKHTVLIIAHRLSTVEHAhLIVVLD 493
Cdd:PRK13541 154 LSKENRDLLNNliVMKAN-SGGIVLLSSHLESSIKSA-QILQLD 195
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
297-331 |
6.99e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 38.76 E-value: 6.99e-03
10 20 30
....*....|....*....|....*....|....*
gi 2217288354 297 HTQVLQNVsfsLSPGKVTALVGPSGSGKSSCVNIL 331
Cdd:PRK01889 184 GLDVLAAW---LSGGKTVALLGSSGVGKSTLVNAL 215
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
422-512 |
9.66e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 38.72 E-value: 9.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217288354 422 LSGGQKQRVAMARALVRNPPVLILDEATSALDAESEYLIQQAihgnLQKH--TVLIIAH------RLSTvehaHLIVVLD 493
Cdd:PRK15064 439 LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMA----LEKYegTLIFVSHdrefvsSLAT----RIIEITP 510
|
90
....*....|....*....
gi 2217288354 494 KGRVVQQGTHQQLLAQGGL 512
Cdd:PRK15064 511 DGVVDFSGTYEEYLRSQGI 529
|
|
| |
