|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
87-664 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 587.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 87 LWNLIKPFFGWFFAAVVCAILSAYINIQIPLCLGDLVNGIVkiikdesnnLRSHFEQLKPSALHLMTLYVAQSALTFLYI 166
Cdd:COG1132 12 LLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALL---------AGGDLSALLLLLLLLLGLALLRALLSYLQR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 167 TFLTVLGERMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFKLCVSQGLRTFAQTIGCIGSLYFLSPT 246
Cdd:COG1132 83 YLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 247 MTMYTVAVVPGIILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFDNELDKARAMQEQLGV 326
Cdd:COG1132 163 LALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAAR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 327 GIGLFQAGTNLFLNGMILSVLYGGSNLISKGEMTPGALMSFLVSAQTIQRSLSQLSIIFGTAIKGWTAGGRVLQFSRLEP 406
Cdd:COG1132 243 LSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 407 SIPmDTGVCIPYHSLWGDIKFEDVSFSYPtrPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTL 486
Cdd:COG1132 323 EIP-DPPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 487 DGRDLRELNVEWLRGQvIGLISQEPVLFATSVEENIRYGRPDATDEEVREAARAAHVDEFVSRFPSGYSTVVGERGAQLS 566
Cdd:COG1132 400 DGVDIRDLTLESLRRQ-IGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLS 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 567 GGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRLSTIRSAQMIYVIKDKKALESGTH 646
Cdd:COG1132 479 GGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTH 558
|
570
....*....|....*...
gi 115533592 647 EQLMAKKGsLYRKLVEAH 664
Cdd:COG1132 559 EELLARGG-LYARLYRLQ 575
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
101-398 |
4.76e-166 |
|
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: 477.04 E-value: 4.76e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 101 AVVCAILSAYINIQIPLCLGDLVNGIVKIIKDesnNLRSHFEQLKPSALHLMTLYVAQSALTFLYITFLTVLGERMATKM 180
Cdd:cd18574 1 AVLSALAAALVNIQIPLLLGDLVNVISRSLKE---TNGDFIEDLKKPALKLLGLYLLQSLLTFAYISLLSVVGERVAARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 181 RSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFKLCVSQGLRTFAQTIGCIGSLYFLSPTMTMYTVAVVPGIIL 260
Cdd:cd18574 78 RNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 261 AGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFDNELDKARAMQEQLGVGIGLFQAGTNLFLN 340
Cdd:cd18574 158 VGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEKLGLGIGIFQGLSNLALN 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 115533592 341 GMILSVLYGGSNLISKGEMTPGALMSFLVSAQTIQRSLSQLSIIFGTAIKGWTAGGRV 398
Cdd:cd18574 238 GIVLGVLYYGGSLVSRGELTAGDLMSFLVATQTIQRSLAQLSVLFGQYVKGKSAGARV 295
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
87-662 |
3.36e-156 |
|
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: 462.63 E-value: 3.36e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 87 LWNLIKPFFGWFFAAVVCAILSAYINIQIPLCLGDLV-NGIvkiIKDESNNLRSHFEqlkpsalhLMTLYVAQSAL-TFL 164
Cdd:TIGR02204 9 LWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIdHGF---SKDSSGLLNRYFA--------FLLVVALVLALgTAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 165 YITFLTVLGERMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFKLCVSQGLRTFAQTIGCIGSLYFLS 244
Cdd:TIGR02204 78 RFYLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 245 PTMTMYTVAVVPGIILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFDNELDKARAMQEQL 324
Cdd:TIGR02204 158 PKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 325 GVGIGLFQAGTNLFLNGMILSVLYGGSNLISKGEMTPGALMSFLVSAQTIQRSLSQLSIIFGTAIKGWTAGGRVLQFSRL 404
Cdd:TIGR02204 238 IRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 405 EPSIPMDTGVCIPYHSLWGDIKFEDVSFSYPTRPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRV 484
Cdd:TIGR02204 318 EPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 485 TLDGRDLRELNVEWLRgQVIGLISQEPVLFATSVEENIRYGRPDATDEEVREAARAAHVDEFVSRFPSGYSTVVGERGAQ 564
Cdd:TIGR02204 398 LLDGVDLRQLDPAELR-ARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVT 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 565 LSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRLSTIRSAQMIYVIKDKKALESG 644
Cdd:TIGR02204 477 LSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQG 556
|
570
....*....|....*...
gi 115533592 645 THEQLMAkKGSLYRKLVE 662
Cdd:TIGR02204 557 THAELIA-KGGLYARLAR 573
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
87-662 |
1.91e-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: 447.36 E-value: 1.91e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 87 LWNLIKPFFGWFFAAVVCAILSAYINIQIPLCLGDLVNgivKIIKDESnnlrshFEQLKPSALHLMTLYVAQSALTFLYI 166
Cdd:COG2274 147 FLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVID---RVLPNQD------LSTLWVLAIGLLLALLFEGLLRLLRS 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 167 TFLTVLGERMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNaDVQEFKSSFklcVSQGLRTFA---QTIGCIGSLYFL 243
Cdd:COG2274 218 YLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFL---TGSLLTALLdllFVLIFLIVLFFY 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 244 SPTMTMYTVAVVPGIILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFDNELDKARAMQEQ 323
Cdd:COG2274 294 SPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFK 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 324 LGVgIGLFQAGTNLFLNGMI-LSVLYGGSNLISKGEMTPGALMSF-LVSAQTIQrSLSQLSIIFGTAIKGWTAGGRVLQF 401
Cdd:COG2274 374 LRR-LSNLLSTLSGLLQQLAtVALLWLGAYLVIDGQLTLGQLIAFnILSGRFLA-PVAQLIGLLQRFQDAKIALERLDDI 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 402 SRLEPSIPMDTGVcIPYHSLWGDIKFEDVSFSYPTRpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKS 481
Cdd:COG2274 452 LDLPPEREEGRSK-LSLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTS 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 482 GRVTLDGRDLRELNVEWLRGQvIGLISQEPVLFATSVEENIRYGRPDATDEEVREAARAAHVDEFVSRFPSGYSTVVGER 561
Cdd:COG2274 530 GRILIDGIDLRQIDPASLRRQ-IGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEG 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 562 GAQLSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRLSTIRSAQMIYVIKDKKAL 641
Cdd:COG2274 609 GSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIV 688
|
570 580
....*....|....*....|.
gi 115533592 642 ESGTHEQLMAKKGsLYRKLVE 662
Cdd:COG2274 689 EDGTHEELLARKG-LYAELVQ 708
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
32-661 |
7.92e-147 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 443.39 E-value: 7.92e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 32 PISRTTILKTWRICGFGAGLGAVTLRKAACAPKLSKRIDHlrtTEDQNASMTAGELWNLIKPFFGWFFAAVVCAILSAYI 111
Cdd:TIGR00958 100 AVRVALGLWSWFVWSYGAALPAAALWAVLSSAGASEKEAE---QGQSETADLLFRLLGLSGRDWPWLISAFVFLTLSSLG 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 112 NIQIPLCLGDLVNGIVKiikdesnnlRSHFEQLKpSALHLMTLYVAQSALT-FLYITFLTVLGERMATKMRSDLFQKLLH 190
Cdd:TIGR00958 177 EMFIPFYTGRVIDTLGG---------DKGPPALA-SAIFFMCLLSIASSVSaGLRGGSFNYTMARINLRIREDLFRSLLR 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 191 HDMAFFDSHKSGELSARLNADVQEFKSSFKLCVSQGLRTFAQTIGCIGSLYFLSPTMTMYTVAVVPGIILAGSAIGAGLR 270
Cdd:TIGR00958 247 QDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQ 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 271 QLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFDNELDKARAMQEQLGVGIGLFQAGTNLFLNGMILSVLYGG 350
Cdd:TIGR00958 327 LLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYG 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 351 SNLISKGEMTPGALMSFLVSAQTIQRSLSQLSIIFGTAIKGWTAGGRVLQFSRLEPSIPMdTGVCIPYHsLWGDIKFEDV 430
Cdd:TIGR00958 407 GQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPL-TGTLAPLN-LEGLIEFQDV 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 431 SFSYPTRPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQViGLISQE 510
Cdd:TIGR00958 485 SFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQV-ALVGQE 563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 511 PVLFATSVEENIRYGRPDATDEEVREAARAAHVDEFVSRFPSGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILILDE 590
Cdd:TIGR00958 564 PVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDE 643
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115533592 591 ATSALDSHSEHMVQEALNnvMKGRTVLIIAHRLSTIRSAQMIYVIKDKKALESGTHEQLMAKKGsLYRKLV 661
Cdd:TIGR00958 644 ATSALDAECEQLLQESRS--RASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQG-CYKHLV 711
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
425-663 |
1.04e-138 |
|
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: 405.00 E-value: 1.04e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQvI 504
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQ-I 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEPVLFATSVEENIRYGRPDATDEEVREAARAAHVDEFVSRFPSGYSTVVGERGAQLSGGQKQRIAIARAILKNPP 584
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115533592 585 ILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRLSTIRSAQMIYVIKDKKALESGTHEQLMAKKGsLYRKLVEA 663
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKG-VYAKLVKA 237
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
87-660 |
1.54e-123 |
|
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: 378.68 E-value: 1.54e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 87 LWNLIKPFFGWFFAAVVCAILSAYINIQIPlclgdlvnGIVKIIKDESNNLRS-HFEQLKPsaLHLMTLYVAQSALTFLY 165
Cdd:TIGR02203 5 LWSYVRPYKAGLVLAGVAMILVAATESTLA--------ALLKPLLDDGFGGRDrSVLWWVP--LVVIGLAVLRGICSFVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 166 ITFLTVLGERMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSS----FKLCVSQGLrtfaQTIGCIGSLY 241
Cdd:TIGR02203 75 TYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAatdaFIVLVRETL----TVIGLFIVLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 242 FLSPTMTMYTVAVVPGIILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFDNELDKARAMQ 321
Cdd:TIGR02203 151 YYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 322 EQLGVGIGLFQAGTNLFLNGMILSVLYGGSNLISKGEMTPGALMSFLVSAQTIQRSLSQLSIIFGTAIKGWTAGGRVlqF 401
Cdd:TIGR02203 231 MKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESL--F 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 402 SRLEPSIPMDTGVcIPYHSLWGDIKFEDVSFSYPTRpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKS 481
Cdd:TIGR02203 309 TLLDSPPEKDTGT-RAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 482 GRVTLDGRDLRELNVEWLRGQvIGLISQEPVLFATSVEENIRYGRP-DATDEEVREAARAAHVDEFVSRFPSGYSTVVGE 560
Cdd:TIGR02203 387 GQILLDGHDLADYTLASLRRQ-VALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 561 RGAQLSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRLSTIRSAQMIYVIKDKKA 640
Cdd:TIGR02203 466 NGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRI 545
|
570 580
....*....|....*....|
gi 115533592 641 LESGTHEQLMAKKGsLYRKL 660
Cdd:TIGR02203 546 VERGTHNELLARNG-LYAQL 564
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
274-660 |
4.37e-119 |
|
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: 367.99 E-value: 4.37e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 274 RRAQGQSAT-ASAVSDEALTNIRTIRAFAMEKLESRLFDNELDKARAMQEQLGVGIGLFQAGTNLFLN-GMILSVLYGGS 351
Cdd:COG5265 207 RREMNEADSeANTRAVDSLLNYETVKYFGNEAREARRYDEALARYERAAVKSQTSLALLNFGQALIIAlGLTAMMLMAAQ 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 352 NlISKGEMTPGALMsfLVSAQTIQ--RSLSQLSIIFGTaIK-GWTAGGRVLQFSRLEPSIPmDTGVCIPYHSLWGDIKFE 428
Cdd:COG5265 287 G-VVAGTMTVGDFV--LVNAYLIQlyIPLNFLGFVYRE-IRqALADMERMFDLLDQPPEVA-DAPDAPPLVVGGGEVRFE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 429 DVSFSYptRPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRgQVIGLIS 508
Cdd:COG5265 362 NVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLR-AAIGIVP 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 509 QEPVLFATSVEENIRYGRPDATDEEVREAARAAHVDEFVSRFPSGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILIL 588
Cdd:COG5265 439 QDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIF 518
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115533592 589 DEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRLSTIRSAQMIYVIKDKKALESGTHEQLMAKKGsLYRKL 660
Cdd:COG5265 519 DEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGG-LYAQM 589
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
425-660 |
1.39e-117 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 350.76 E-value: 1.39e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQvI 504
Cdd:cd03251 1 VEFKNVTFRYPGD-GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQ-I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEPVLFATSVEENIRYGRPDATDEEVREAARAAHVDEFVSRFPSGYSTVVGERGAQLSGGQKQRIAIARAILKNPP 584
Cdd:cd03251 79 GLVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115533592 585 ILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRLSTIRSAQMIYVIKDKKALESGTHEQLMAKKGsLYRKL 660
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGG-VYAKL 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
425-660 |
2.44e-116 |
|
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: 347.68 E-value: 2.44e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPtrPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRgQVI 504
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLR-RAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEPVLFATSVEENIRYGRPDATDEEVREAARAAHVDEFVSRFPSGYSTVVGERGAQLSGGQKQRIAIARAILKNPP 584
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115533592 585 ILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRLSTIRSAQMIYVIKDKKALESGTHEQLMAKKGsLYRKL 660
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGG-LYAEM 232
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
87-654 |
3.94e-108 |
|
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: 338.27 E-value: 3.94e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 87 LWNLIKPFFGWFFAAVVCAILSAYINIQIPLCLGDLVNGIVkiikdesnNLRSHFEQLKPSALHLMTLYVAQSALTFLYI 166
Cdd:COG4988 8 LKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLI--------IGGAPLSALLPLLGLLLAVLLLRALLAWLRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 167 TFLTVLGERMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFKLCVSQGLRTFAQTIGCIGSLYFLSPT 246
Cdd:COG4988 80 RAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 247 MTMYTVAVVPGIILAGSAIGAGLRQLSRRaqgQSATASAVSD---EALTNIRTIRAFAMEKLESRLFDNELDK--ARAMq 321
Cdd:COG4988 160 SGLILLVTAPLIPLFMILVGKGAAKASRR---QWRALARLSGhflDRLRGLTTLKLFGRAKAEAERIAEASEDfrKRTM- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 322 EQLGVGiglfqagtnlFLNGMIL------SV----LYGGSNLISkGEMTPGALMSFLVSAQTIQRSLSQLSIIFGTAIKG 391
Cdd:COG4988 236 KVLRVA----------FLSSAVLeffaslSIalvaVYIGFRLLG-GSLTLFAALFVLLLAPEFFLPLRDLGSFYHARANG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 392 WTAGGRVLQFSRLEPSIPMDTGVCIPYHSLWgDIKFEDVSFSYPtrPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITH 471
Cdd:COG4988 305 IAAAEKIFALLDAPEPAAPAGTAPLPAAGPP-SIELEDVSFSYP--GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 472 LLERFYEPKSGRVTLDGRDLRELNVEWLRGQvIGLISQEPVLFATSVEENIRYGRPDATDEEVREAARAAHVDEFVSRFP 551
Cdd:COG4988 382 LLLGFLPPYSGSILINGVDLSDLDPASWRRQ-IAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALP 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 552 SGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRLSTIRSAQM 631
Cdd:COG4988 461 DGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADR 540
|
570 580
....*....|....*....|...
gi 115533592 632 IYVIKDKKALESGTHEQLMAKKG 654
Cdd:COG4988 541 ILVLDDGRIVEQGTHEELLAKNG 563
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
175-662 |
4.47e-105 |
|
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: 330.58 E-value: 4.47e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 175 RMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFklcvsqgLRTFAQTI-------GCIGSLYFLSPT- 246
Cdd:COG4987 85 RLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLY-------LRVLLPLLvallvilAAVAFLAFFSPAl 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 247 -MTMYTVAVVPGIILAGSAIGAGLRQLSRRAQGQSATASAVSDeALTNIRTIRAF-AMEKLESRLFDNELDKARAmQEQL 324
Cdd:COG4987 158 aLVLALGLLLAGLLLPLLAARLGRRAGRRLAAARAALRARLTD-LLQGAAELAAYgALDRALARLDAAEARLAAA-QRRL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 325 GVGIGLFQAGTNLFLNGMILSVLYGGSNLISKGEMTPG--ALMSFLV-----SAQTIQRSLSQLsiifGTAIkgwTAGGR 397
Cdd:COG4987 236 ARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPllALLVLAAlalfeALAPLPAAAQHL----GRVR---AAARR 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 398 VLQFSRLEPSIPMDTGVCIPYHSlwGDIKFEDVSFSYPTRPgHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFY 477
Cdd:COG4987 309 LNELLDAPPAVTEPAEPAPAPGG--PSLELEDVSFRYPGAG-RPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFL 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 478 EPKSGRVTLDGRDLRELNVEWLRgQVIGLISQEPVLFATSVEENIRYGRPDATDEEVREAARAAHVDEFVSRFPSGYSTV 557
Cdd:COG4987 386 DPQSGSITLGGVDLRDLDEDDLR-RRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTW 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 558 VGERGAQLSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRLSTIRSAQMIYVIKD 637
Cdd:COG4987 465 LGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLED 544
|
490 500
....*....|....*....|....*
gi 115533592 638 KKALESGTHEQLMAKKGSlYRKLVE 662
Cdd:COG4987 545 GRIVEQGTHEELLAQNGR-YRQLYQ 568
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
423-654 |
1.48e-103 |
|
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: 314.55 E-value: 1.48e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 423 GDIKFEDVSFSYptRPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQ 502
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 503 vIGLISQEPVLFATSVEENIRYGRPDATDEEVREAARAAHVDEFVSRFPSGYSTVVGERGAQLSGGQKQRIAIARAILKN 582
Cdd:cd03254 79 -IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115533592 583 PPILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRLSTIRSAQMIYVIKDKKALESGTHEQLMAKKG 654
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
343-658 |
1.01e-98 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 314.59 E-value: 1.01e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 343 ILSVLYGGSNLISKGEMTPGALMSFLVSAQT-IQRsLSQLSIIFGTAIkgwTAGGRVLQFSRLEPSIPM--DTGVCIPYH 419
Cdd:PRK13657 254 MLAILVLGAALVQKGQLRVGEVVAFVGFATLlIGR-LDQVVAFINQVF---MAAPKLEEFFEVEDAVPDvrDPPGAIDLG 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 420 SLWGDIKFEDVSFSYP-TRPGhtvFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEW 498
Cdd:PRK13657 330 RVKGAVEFDDVSFSYDnSRQG---VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAS 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 499 LRgQVIGLISQEPVLFATSVEENIRYGRPDATDEEVREAARAAHVDEFVSRFPSGYSTVVGERGAQLSGGQKQRIAIARA 578
Cdd:PRK13657 407 LR-RNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARA 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 579 ILKNPPILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRLSTIRSAQMIYVIKDKKALESGTHEQLMAKKGSLYR 658
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAA 565
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
148-660 |
3.41e-97 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 313.60 E-value: 3.41e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 148 ALHLMTLYVAQSALTFLYITFLTVLGERMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLN--ADVQEFKSSFKLCVSQ 225
Cdd:TIGR01846 182 ALAMLAVAIFEPALGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFESRRVGDTVARVRelEQIRNFLTGSALTVVL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 226 GLrTFAQTIgcIGSLYFLSPTMTMYTVAVVPGIILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKL 305
Cdd:TIGR01846 262 DL-LFVVVF--LAVMFFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 306 ESRLFDNELDKARAMQEQL-------GVGIGLFQAGTNLFLngmilsvLYGGSNLISKGEMTPGALMSFLVSAQTIQR-- 376
Cdd:TIGR01846 339 FQNRWDRQLAAYVAASFRVtnlgniaGQAIELIQKLTFAIL-------LWFGAHLVIGGALSPGQLVAFNMLAGRVTQpv 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 377 -SLSQLSIIFGTAIKGWTAGGRVLQfsrlEPSIPMDTG-VCIPyhSLWGDIKFEDVSFSY-PTRPghTVFENLTLSIPAG 453
Cdd:TIGR01846 412 lRLAQLWQDFQQTGIALERLGDILN----SPTEPRSAGlAALP--ELRGAITFENIRFRYaPDSP--EVLSNLNLDIKPG 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 454 QVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQViGLISQEPVLFATSVEENIRYGRPDATDEE 533
Cdd:TIGR01846 484 EFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQM-GVVLQENVLFSRSIRDNIALCNPGAPFEH 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 534 VREAARAAHVDEFVSRFPSGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMKG 613
Cdd:TIGR01846 563 VIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRG 642
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 115533592 614 RTVLIIAHRLSTIRSAQMIYVIKDKKALESGTHEQLMAKKGsLYRKL 660
Cdd:TIGR01846 643 RTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQG-LYARL 688
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
87-658 |
1.28e-96 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 308.87 E-value: 1.28e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 87 LWNLIKPFFGWFFAAVVCAILSAyiniqiplcLGD-LVNGIVKIIKDESnnlrshFEQLKPSALHLMTLYVAqsALTFL- 164
Cdd:PRK11176 16 LWPTIAPFKAGLIVAGVALILNA---------ASDtFMLSLLKPLLDDG------FGKADRSVLKWMPLVVI--GLMILr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 165 ----YIT--FLTVLGERMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSfklcVSQGL----RTFAQTI 234
Cdd:PRK11176 79 gitsFISsyCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASS----SSGALitvvREGASII 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 235 GCIGSLYFLSPTMTMYTVAVVPGIILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFDNEL 314
Cdd:PRK11176 155 GLFIMMFYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 315 DKARamqeQLGVGIGLFQAGTNLFLNgMILS-----VLYGGSNLISKGEMTPGALMSFLVSAQTIQRSLSQLSIIFGTAI 389
Cdd:PRK11176 235 NRMR----QQGMKMVSASSISDPIIQ-LIASlalafVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 390 KGWTAGGRVLQFSRLEPSipMDTGVCIPYHSLwGDIKFEDVSFSYPTRPgHTVFENLTLSIPAGQVVALCGPSGEGKSTI 469
Cdd:PRK11176 310 RGMAACQTLFAILDLEQE--KDEGKRVIERAK-GDIEFRNVTFTYPGKE-VPALRNINFKIPAGKTVALVGRSGSGKSTI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 470 THLLERFYEPKSGRVTLDGRDLRELNVEWLRGQViGLISQEPVLFATSVEENIRYGRPDA-TDEEVREAARAAHVDEFVS 548
Cdd:PRK11176 386 ANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQV-ALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFIN 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 549 RFPSGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRLSTIRS 628
Cdd:PRK11176 465 KMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEK 544
|
570 580 590
....*....|....*....|....*....|...
gi 115533592 629 AQMIYVIKDKKALESGTHEQLMAKKGS---LYR 658
Cdd:PRK11176 545 ADEILVVEDGEIVERGTHAELLAQNGVyaqLHK 577
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
413-635 |
8.33e-90 |
|
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: 278.97 E-value: 8.33e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 413 GVCIPYHsLWGDIKFEDVSFSYPTRPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLR 492
Cdd:cd03248 1 GSLAPDH-LKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 493 ELNVEWLRGQViGLISQEPVLFATSVEENIRYGRPDATDEEVREAARAAHVDEFVSRFPSGYSTVVGERGAQLSGGQKQR 572
Cdd:cd03248 80 QYEHKYLHSKV-SLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115533592 573 IAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRLSTIRSAQMIYVI 635
Cdd:cd03248 159 VAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVL 221
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
425-662 |
2.62e-84 |
|
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: 265.12 E-value: 2.62e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYptRP-GHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQV 503
Cdd:cd03252 1 ITFEHVRFRY--KPdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 504 iGLISQEPVLFATSVEENIRYGRPDATDEEVREAARAAHVDEFVSRFPSGYSTVVGERGAQLSGGQKQRIAIARAILKNP 583
Cdd:cd03252 79 -GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115533592 584 PILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRLSTIRSAQMIYVIKDKKALESGTHEQLMAKKGsLYRKLVE 662
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENG-LYAYLYQ 235
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
425-639 |
3.97e-82 |
|
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: 256.54 E-value: 3.97e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPgHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQvI 504
Cdd:cd03228 1 IEFKNVSFSYPGRP-KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEPVLFATSVEENIrygrpdatdeevreaaraahvdefvsrfpsgystvvgergaqLSGGQKQRIAIARAILKNPP 584
Cdd:cd03228 79 AYVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 115533592 585 ILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRLSTIRSAQMIYVIKDKK 639
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
144-662 |
1.95e-81 |
|
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: 272.20 E-value: 1.95e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 144 LKPSALHLMTLYVAQSALTFLYITFLTVLGERMATKMRSDLFQKLLHHDMAFFDSHKSGELSAR--LNADVQEFkssfkl 221
Cdd:TIGR03796 193 LRPLLLGMGLTALLQGVLTWLQLYYLRRLEIKLAVGMSARFLWHILRLPVRFFAQRHAGDIASRvqLNDQVAEF------ 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 222 cVSQGLRTFAqtIGCIGSLYFL------SPTMTMYTVAVVPGIILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIR 295
Cdd:TIGR03796 267 -LSGQLATTA--LDAVMLVFYAllmllyDPVLTLIGIAFAAINVLALQLVSRRRVDANRRLQQDAGKLTGVAISGLQSIE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 296 TIRAFAmekLESRLFDN---ELDKARAMQEQLGVG---IGLFQAGTNLFLNGMILSVlygGSNLISKGEMTPGALMSFLV 369
Cdd:TIGR03796 344 TLKASG---LESDFFSRwagYQAKLLNAQQELGVLtqiLGVLPTLLTSLNSALILVV---GGLRVMEGQLTIGMLVAFQS 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 370 SAQTIQRSLSQLsIIFGTAIKGWTAG-GR---VLQFSR----LEPSIPMDTGVciPYHSLWGDIKFEDVSFSYpTRPGHT 441
Cdd:TIGR03796 418 LMSSFLEPVNNL-VGFGGTLQELEGDlNRlddVLRNPVdpllEEPEGSAATSE--PPRRLSGYVELRNITFGY-SPLEPP 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 442 VFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQViGLISQEPVLFATSVEEN 521
Cdd:TIGR03796 494 LIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSV-AMVDQDIFLFEGTVRDN 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 522 IRYGRPDATDEEVREAARAAHVDEFVSRFPSGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILILDEATSALDSHSEH 601
Cdd:TIGR03796 573 LTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEK 652
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115533592 602 MVQEALNNvmKGRTVLIIAHRLSTIRSAQMIYVIKDKKALESGTHEQLMAKKGsLYRKLVE 662
Cdd:TIGR03796 653 IIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGG-AYARLIR 710
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
101-398 |
4.04e-76 |
|
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: 245.55 E-value: 4.04e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 101 AVVCAILSAYINIQIPLCLGDLVNGIVKiikdesnnlRSHFEQLKPSALHLMTLYVAQSALTFLYITFLTVLGERMATKM 180
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIK---------GGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 181 RSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFKLCVSQGLRTFAQTIGCIGSLYFLSPTMTMYTVAVVPGIIL 260
Cdd:cd18557 72 RRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 261 AGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFDNELDKARAMQEQLGVGIGLFQAGTNLFLN 340
Cdd:cd18557 152 ASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIY 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 115533592 341 GMILSVLYGGSNLISKGEMTPGALMSFLVSAQTIQRSLSQLSIIFGTAIKGWTAGGRV 398
Cdd:cd18557 232 LSLLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
175-658 |
7.71e-74 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 248.47 E-value: 7.71e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 175 RMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQefKSSFklCVSQGLRTFAQTI--GCIGSLYF---LSPTMTM 249
Cdd:PRK10789 66 QLAVELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVD--RVVF--AAGEGVLTLVDSLvmGCAVLIVMstqISWQLTL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 250 YTVAVVPGIILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFdnELDKARAMQEQLGVG-- 327
Cdd:PRK10789 142 LALLPMPVMAIMIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALF--AADAEDTGKKNMRVAri 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 328 -------IGLFQAGTNLFLNGmilsvlyGGSNLISKGEMTPGALMSFLVSAQTIQRSLSQLSIIFGTAIKGWTAGGRVLQ 400
Cdd:PRK10789 220 darfdptIYIAIGMANLLAIG-------GGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 401 FSRLEP-------SIPMDTGVcipyhsLWGDIKfedvSFSYPTRPgHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLL 473
Cdd:PRK10789 293 MLAEAPvvkdgsePVPEGRGE------LDVNIR----QFTYPQTD-HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLI 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 474 ERFYEPKSGRVTLDGRDLRELNVEWLRGQvIGLISQEPVLFATSVEENIRYGRPDATDEEVREAARAAHVDEFVSRFPSG 553
Cdd:PRK10789 362 QRHFDVSEGDIRFHDIPLTKLQLDSWRSR-LAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQG 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 554 YSTVVGERGAQLSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRLSTIRSAQMIY 633
Cdd:PRK10789 441 YDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEIL 520
|
490 500
....*....|....*....|....*...
gi 115533592 634 VIKDKKALESGTHEQLMAKKG---SLYR 658
Cdd:PRK10789 521 VMQHGHIAQRGNHDQLAQQSGwyrDMYR 548
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
423-637 |
1.34e-71 |
|
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: 230.94 E-value: 1.34e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 423 GDIKFEDVSFSYPTRPGHTVfENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRgQ 502
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPAL-DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLR-R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 503 VIGLISQEPVLFATSVEENIRYGRPDATDEEVREAARAAHVDEFVSRFPSGYSTVVGERGAQLSGGQKQRIAIARAILKN 582
Cdd:cd03245 79 NIGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 115533592 583 PPILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRLSTIRSAQMIYVIKD 637
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDS 213
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
425-635 |
5.56e-69 |
|
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: 234.10 E-value: 5.56e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPghTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQvI 504
Cdd:TIGR02857 322 LEFSGVSVAYPGRR--PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQ-I 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEPVLFATSVEENIRYGRPDATDEEVREAARAAHVDEFVSRFPSGYSTVVGERGAQLSGGQKQRIAIARAILKNPP 584
Cdd:TIGR02857 399 AWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAP 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 115533592 585 ILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRLSTIRSAQMIYVI 635
Cdd:TIGR02857 479 LLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
175-623 |
2.27e-68 |
|
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: 232.64 E-value: 2.27e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 175 RMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFKLCVSQGLRTFAQTIGCIGSLYFLSPT--MTMYTV 252
Cdd:TIGR02868 83 RSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPaaLILAAG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 253 AVVPGIILAGSAIGAGLRQLSRRAQGQSATASAVSDeALTNIRTIRAF-AMEKLESRLFDNELDKARAMQEQlGVGIGLF 331
Cdd:TIGR02868 163 LLLAGFVAPLVSLRAARAAEQALARLRGELAAQLTD-ALDGAAELVASgALPAALAQVEEADRELTRAERRA-AAATALG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 332 QAGTNLFLNGMILSVLYGGSNLISKGEMTPGALMSFLVSAQTIQRSLSQLSiifgTAIKGWTAGGRVLQfsRLEPSIPMD 411
Cdd:TIGR02868 241 AALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALP----AAAQQLTRVRAAAE--RIVEVLDAA 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 412 TGVCIPYHSLWGD-------IKFEDVSFSYPTRPghTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRV 484
Cdd:TIGR02868 315 GPVAEGSAPAAGAvglgkptLELRDLSAGYPGAP--PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEV 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 485 TLDGRDLRELNVEWLRgQVIGLISQEPVLFATSVEENIRYGRPDATDEEVREAARAAHVDEFVSRFPSGYSTVVGERGAQ 564
Cdd:TIGR02868 393 TLDGVPVSSLDQDEVR-RRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGAR 471
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 115533592 565 LSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRL 623
Cdd:TIGR02868 472 LSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
96-658 |
8.49e-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: 234.85 E-value: 8.49e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 96 GWFFAAV-VCAILSAYINIQIPLCLGDLVNgivKIIKDesnNLRSHFEQLkpsALHLMTLYVAQSAltFLYITFLTVLge 174
Cdd:TIGR03797 135 RRDLLAIlAMGLLGTLLGMLVPIATGILIG---TAIPD---ADRSLLVQI---ALALLAAAVGAAA--FQLAQSLAVL-- 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 175 RMATKMRSDL----FQKLLHHDMAFFDSHKSGELSARLNADVQEFKssfKLCVSqGLRTFAQTIGCI---GSLYFLSPTM 247
Cdd:TIGR03797 202 RLETRMDASLqaavWDRLLRLPVSFFRQYSTGDLASRAMGISQIRR---ILSGS-TLTTLLSGIFALlnlGLMFYYSWKL 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 248 TMytVAVVPGIILAGSAIGAGLRQLS--RRAQGQSATASAVSDEALTNIRTIRAFAMEK----LESRLFDneldKARAMQ 321
Cdd:TIGR03797 278 AL--VAVALALVAIAVTLVLGLLQVRkeRRLLELSGKISGLTVQLINGISKLRVAGAENrafaRWAKLFS----RQRKLE 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 322 ---EQLGVGIGLFQAGTNLFlnGMILsVLYGGSNLISKGEMTPGALMSFLVSAQTIQRSLSQLSiifGTAIKGWTAggrV 398
Cdd:TIGR03797 352 lsaQRIENLLTVFNAVLPVL--TSAA-LFAAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLS---NTLISILAV---I 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 399 LQFSRLEP---SIPMDTGVCIPYHSLWGDIKFEDVSFSYptRP-GHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLE 474
Cdd:TIGR03797 423 PLWERAKPileALPEVDEAKTDPGKLSGAIEVDRVTFRY--RPdGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLL 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 475 RFYEPKSGRVTLDGRDLRELNVEWLRGQvIGLISQEPVLFATSVEENIRYGRPdATDEEVREAARAAHVDEFVSRFPSGY 554
Cdd:TIGR03797 501 GFETPESGSVFYDGQDLAGLDVQAVRRQ-LGVVLQNGRLMSGSIFENIAGGAP-LTLDEAWEAARMAGLAEDIRAMPMGM 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 555 STVVGERGAQLSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALN--NVmkgrTVLIIAHRLSTIRSAQMI 632
Cdd:TIGR03797 579 HTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLErlKV----TRIVIAHRLSTIRNADRI 654
|
570 580
....*....|....*....|....*.
gi 115533592 633 YVIKDKKALESGTHEQLMAKKGSLYR 658
Cdd:TIGR03797 655 YVLDAGRVVQQGTYDELMAREGLFAQ 680
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
201-652 |
4.83e-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: 230.02 E-value: 4.83e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 201 SGELSARLNADVqeFKSSFKLCVSQGLRTFAQTIGCIGSL--YFLSPTMT---------MY------------TVAVVPG 257
Cdd:COG4618 88 GARLDRRLGPRV--FDAAFRAALRGGGGAAAQALRDLDTLrqFLTGPGLFalfdlpwapIFlavlflfhpllgLLALVGA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 258 IILAGSAIGAGL--RQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFDNELDKARAMQEQLGVGIGLFQAGT 335
Cdd:COG4618 166 LVLVALALLNERltRKPLKEANEAAIRANAFAEAALRNAEVIEAMGMLPALRRRWQRANARALALQARASDRAGGFSALS 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 336 NLFLNGMILSVLYGGSNLISKGEMTPGALM--SFLVSaqtiqRSLSQLSIIFGTaIKGWTAGgrVLQFSRLEP---SIPM 410
Cdd:COG4618 246 KFLRLLLQSAVLGLGAYLVIQGEITPGAMIaaSILMG-----RALAPIEQAIGG-WKQFVSA--RQAYRRLNEllaAVPA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 411 DTgvciPYHSL---WGDIKFEDVSFSYP--TRPghtVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVT 485
Cdd:COG4618 318 EP----ERMPLprpKGRLSVENLTVVPPgsKRP---ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVR 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 486 LDGRDLRELNVEWLrGQVIGLISQEPVLFATSVEENI-RYGrpDATDEEVREAARAAHVDEFVSRFPSGYSTVVGERGAQ 564
Cdd:COG4618 391 LDGADLSQWDREEL-GRHIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGAR 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 565 LSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNvMK--GRTVLIIAHRLSTIRSAQMIYVIKDKKALE 642
Cdd:COG4618 468 LSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRA-LKarGATVVVITHRPSLLAAVDKLLVLRDGRVQA 546
|
490
....*....|
gi 115533592 643 SGTHEQLMAK 652
Cdd:COG4618 547 FGPRDEVLAR 556
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
171-662 |
2.31e-66 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 237.62 E-value: 2.31e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 171 VLGERMATKMRSDLFQKLLHHDMAFFD--SHKSGELSARLNADVQEFKSSfklcVSQGLRTFAQTIgcigSLYFLSPTMT 248
Cdd:PTZ00265 892 VIGEKVEKTMKRRLFENILYQEISFFDqdKHAPGLLSAHINRDVHLLKTG----LVNNIVIFTHFI----VLFLVSMVMS 963
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 249 MY----TVAVVPGI------ILAGSAIGAGLRQLSRRAQGQSATASAVSD-------------EALTNIRTIRAFAMEKL 305
Cdd:PTZ00265 964 FYfcpiVAAVLTGTyfifmrVFAIRARLTANKDVEKKEINQPGTVFAYNSddeifkdpsfliqEAFYNMNTVIIYGLEDY 1043
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 306 ESRLFDNELD-KARAMQEQLGVGIGL--FQAGTNLFLNGMilsVLYGGSNLISKGEMTPG----ALMSFLVSAQTIQRSL 378
Cdd:PTZ00265 1044 FCNLIEKAIDySNKGQKRKTLVNSMLwgFSQSAQLFINSF---AYWFGSFLIRRGTILVDdfmkSLFTFLFTGSYAGKLM 1120
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 379 SqlsiifgtaIKGWTAGGRvLQFSRLEPSIPM--------DTGVCIPYHSLW-GDIKFEDVSFSYPTRPGHTVFENLTLS 449
Cdd:PTZ00265 1121 S---------LKGDSENAK-LSFEKYYPLIIRksnidvrdNGGIRIKNKNDIkGKIEIMDVNFRYISRPNVPIYKDLTFS 1190
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 450 IPAGQVVALCGPSGEGKSTITHLLERFYEPK------------------------------------------------- 480
Cdd:PTZ00265 1191 CDSKKTTAIVGETGSGKSTVMSLLMRFYDLKndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgeds 1270
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 481 -----SGRVTLDGRDLRELNVEWLRgQVIGLISQEPVLFATSVEENIRYGRPDATDEEVREAARAAHVDEFVSRFPSGYS 555
Cdd:PTZ00265 1271 tvfknSGKILLDGVDICDYNLKDLR-NLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYD 1349
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 556 TVVGERGAQLSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMK--GRTVLIIAHRLSTIRSAQMIY 633
Cdd:PTZ00265 1350 TNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIV 1429
|
570 580 590
....*....|....*....|....*....|....
gi 115533592 634 VIKDKKALES-----GTHEQLMAKKGSLYRKLVE 662
Cdd:PTZ00265 1430 VFNNPDRTGSfvqahGTHEELLSVQDGVYKKYVK 1463
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
148-658 |
3.73e-65 |
|
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: 228.09 E-value: 3.73e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 148 ALHLMTLYVAQSALTFLYITFLTVLGERMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLnADVQEFKSSFKlcvSQGL 227
Cdd:TIGR01193 199 SIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRF-TDASSIIDALA---STIL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 228 RTFAQ-TIGCIGSLYFLSPTMTMYTVAVVpGIILAGSAIGAGLRQLSRRAQGQSATASAVSD---EALTNIRTIRAFAME 303
Cdd:TIGR01193 275 SLFLDmWILVIVGLFLVRQNMLLFLLSLL-SIPVYAVIIILFKRTFNKLNHDAMQANAVLNSsiiEDLNGIETIKSLTSE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 304 -----KLESRlFDNELDKARAMQeQLGVGIGLFQAGTNLFLNgmiLSVLYGGSNLISKGEMTPGALMSFlvsAQTIQRSL 378
Cdd:TIGR01193 354 aerysKIDSE-FGDYLNKSFKYQ-KADQGQQAIKAVTKLILN---VVILWTGAYLVMRGKLTLGQLITF---NALLSYFL 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 379 SQLSIIFGTAIKGWTAggRV----LQFSRLEPSIPMDTGVCIPYHSLWGDIKFEDVSFSYPTrpGHTVFENLTLSIPAGQ 454
Cdd:TIGR01193 426 TPLENIINLQPKLQAA--RVannrLNEVYLVDSEFINKKKRTELNNLNGDIVINDVSYSYGY--GSNILSDISLTIKMNS 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 455 VVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRgQVIGLISQEPVLFATSVEENIRYG-RPDATDEE 533
Cdd:TIGR01193 502 KTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLR-QFINYLPQEPYIFSGSILENLLLGaKENVSQDE 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 534 VREAARAAHVDEFVSRFPSGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNvMKG 613
Cdd:TIGR01193 581 IWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN-LQD 659
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 115533592 614 RTVLIIAHRLSTIRSAQMIYVIKDKKALESGTHEQLMAKKGSLYR 658
Cdd:TIGR01193 660 KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYAS 704
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
101-398 |
1.02e-64 |
|
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: 215.46 E-value: 1.02e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 101 AVVCAILSAYINIQIPLCLGDLVNgivkIIKDESNNLRSHFEQLKPSALHLMTLYVAQSALTFLYITFLTVLGERMATKM 180
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLID----VASKESGDIEIFGLSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 181 RSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFKLCVSQGLRTFAQTIGCIGSLYFLSPTMTMYTVAVVPGIIL 260
Cdd:cd18573 77 RKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 261 AGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFDNELDKARAMQEQLGVGIGLFQAGTNLFLN 340
Cdd:cd18573 157 GAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGN 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 115533592 341 GMILSVLYGGSNLISKGEMTPGALMSFLVSAQTIQRSLSQLSIIFGTAIKGWTAGGRV 398
Cdd:cd18573 237 LSLLSVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
423-645 |
2.84e-64 |
|
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: 211.58 E-value: 2.84e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 423 GDIKFEDVSFSYptRPG-HTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRG 501
Cdd:cd03244 1 GDIEFKNVSLRY--RPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 502 QvIGLISQEPVLFATSVEENIrygrpD----ATDEEVREAARAAHVDEFVSRFPSGYSTVVGERGAQLSGGQKQRIAIAR 577
Cdd:cd03244 79 R-ISIIPQDPVLFSGTIRSNL-----DpfgeYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115533592 578 AILKNPPILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRLSTIRSAQMIYVIKDKKALESGT 645
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
203-652 |
1.33e-63 |
|
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: 220.30 E-value: 1.33e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 203 ELSARLNADVqeFKSSFKLCVSQG-------------LRTFAQTIGCIGslYFLSPTMTMYTV------------AVVPG 257
Cdd:TIGR01842 76 KLDGALNQPI--FAASFSATLRRGsgdglqalrdldqLRQFLTGPGLFA--FFDAPWMPIYLLvcfllhpwigilALGGA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 258 IILAGSAIgagLRQ-LSRRAQGQSATASAVS----DEALTNIRTIRAFAMEKLESRLFDNELDKARAMQEQLGVGIGLFQ 332
Cdd:TIGR01842 152 VVLVGLAL---LNNrATKKPLKEATEASIRAnnlaDSALRNAEVIEAMGMMGNLTKRWGRFHSKYLSAQSAASDRAGMLS 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 333 AGTNLFLNGMILSVLYGGSNLISKGEMTPGALM--SFLVSaqtiqRSLSQLSII------FGTAIKGWtagGRVLQFSRL 404
Cdd:TIGR01842 229 NLSKYFRIVLQSLVLGLGAYLAIDGEITPGMMIagSILVG-----RALAPIDGAiggwkqFSGARQAY---KRLNELLAN 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 405 EPSipMDTGVCIPYHSlwGDIKFEDVSFSyPTRPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRV 484
Cdd:TIGR01842 301 YPS--RDPAMPLPEPE--GHLSVENVTIV-PPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSV 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 485 TLDGRDLRELNVEWLrGQVIGLISQEPVLFATSVEENI-RYGRpDATDEEVREAARAAHVDEFVSRFPSGYSTVVGERGA 563
Cdd:TIGR01842 376 RLDGADLKQWDRETF-GKHIGYLPQDVELFPGTVAENIaRFGE-NADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGA 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 564 QLSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMK-GRTVLIIAHRLSTIRSAQMIYVIKDKKALE 642
Cdd:TIGR01842 454 TLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKArGITVVVITHRPSLLGCVDKILVLQDGRIAR 533
|
490
....*....|
gi 115533592 643 SGTHEQLMAK 652
Cdd:TIGR01842 534 FGERDEVLAK 543
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
423-657 |
3.80e-60 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 211.89 E-value: 3.80e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 423 GDIKFEDVSFSYptRPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRgQ 502
Cdd:PRK10790 339 GRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLR-Q 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 503 VIGLISQEPVLFATSVEENIRYGRpDATDEEVREAARAAHVDEFVSRFPSGYSTVVGERGAQLSGGQKQRIAIARAILKN 582
Cdd:PRK10790 416 GVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQT 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115533592 583 PPILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRLSTIRSAQMIYVIKDKKALESGTHEQLMAKKGSLY 657
Cdd:PRK10790 495 PQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYW 569
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
302-660 |
1.66e-59 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 209.68 E-value: 1.66e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 302 MEKLESRLFDNEldkaRAMQEQLGVGIGLFqagtnLFLNGMILS-VLYGGSNLISkGEMTPG---ALMSFLVSAqTIQrS 377
Cdd:PRK11160 226 LEQTEQQWLAAQ----RRQANLTGLSQALM-----ILANGLTVVlMLWLAAGGVG-GNAQPGaliALFVFAALA-AFE-A 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 378 LSQLSIIF---GTAIkgwTAGGRVLQFSRLEPSI--PMDTGVCIPYhslwGDIKFEDVSFSYPTRPgHTVFENLTLSIPA 452
Cdd:PRK11160 294 LMPVAGAFqhlGQVI---ASARRINEITEQKPEVtfPTTSTAAADQ----VSLTLNNVSFTYPDQP-QPVLKGLSLQIKA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 453 GQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRgQVIGLISQEPVLFATSVEENIRYGRPDATDE 532
Cdd:PRK11160 366 GEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALR-QAISVVSQRVHLFSATLRDNLLLAAPNASDE 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 533 EVREAAR----AAHVDEfvsrfPSGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALN 608
Cdd:PRK11160 445 ALIEVLQqvglEKLLED-----DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLA 519
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 115533592 609 NVMKGRTVLIIAHRLSTIRSAQMIYVIKDKKALESGTHEQLMAKKG---SLYRKL 660
Cdd:PRK11160 520 EHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGryyQLKQRL 574
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
439-668 |
1.68e-58 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 207.39 E-value: 1.68e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 439 GHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYePKSGRVTLDGRDLRELNVEWLRGQvIGLISQEPVLFATSV 518
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKH-LSWVGQNPQLPHGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 519 EENIRYGRPDATDEEVREAARAAHVDEFVSRFPSGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILILDEATSALDSH 598
Cdd:PRK11174 440 RDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAH 519
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 599 SEHMVQEALNNVMKGRTVLIIAHRLSTIRSAQMIYVIKDKKALESGTHEQLMAKKGSLYRKLveAHNVDS 668
Cdd:PRK11174 520 SEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLL--AHRQEE 587
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
142-668 |
1.05e-57 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 211.81 E-value: 1.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 142 EQLKPSALHLMTLYVAQSALTFLYITFLTVLGERMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEfkssfkl 221
Cdd:PTZ00265 94 ENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQ------- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 222 cVSQGLRTFAQTIGCIGS----LYFLS----PTMTMYTVAVVPGIILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTN 293
Cdd:PTZ00265 167 -VNAGIGTKFITIFTYASaflgLYIWSlfknARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVG 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 294 IRTIRAFAMEK-------LESRLFDNELDKARAMqEQLGVGIglfqagtnlfLNGMILS------------VLYGGSNLI 354
Cdd:PTZ00265 246 IRTVVSYCGEKtilkkfnLSEKLYSKYILKANFM-ESLHIGM----------INGFILAsyafgfwygtriIISDLSNQQ 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 355 SKGEMTPGALMSFLVSaqtIQRSLSQLSIIFGTA---IKGWTAGGRVLQFSRLEPSIPM-DTGVCIPyhslwgDIK---F 427
Cdd:PTZ00265 315 PNNDFHGGSVISILLG---VLISMFMLTIILPNIteyMKSLEATNSLYEIINRKPLVENnDDGKKLK------DIKkiqF 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 428 EDVSFSYPTRPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTL-DGRDLRELNVEWLRGQvIGL 506
Cdd:PTZ00265 386 KNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSK-IGV 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 507 ISQEPVLFATSVEENIRYG--------------------------------------------RPDAT------------ 530
Cdd:PTZ00265 465 VSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnTTDSNeliemrknyqti 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 531 -DEEVREAARAAHVDEFVSRFPSGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNN 609
Cdd:PTZ00265 545 kDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINN 624
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 610 vMKG---RTVLIIAHRLSTIRSAQMIYVIKDKKA---------------------------------------------- 640
Cdd:PTZ00265 625 -LKGnenRITIIIAHRLSTIRYANTIFVLSNRERgstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnagsy 703
|
650 660
....*....|....*....|....*....
gi 115533592 641 -LESGTHEQLMAKKGSLYRKLVEAHNVDS 668
Cdd:PTZ00265 704 iIEQGTHDALMKNKNGIYYTMINNQKVSS 732
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
101-386 |
4.15e-50 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 176.14 E-value: 4.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 101 AVVCAILSAYINIQIPLCLGDLVNGIvkiikdesnNLRSHFEQLKPSALHLMTLYVAQSALTFLYITFLTVLGERMATKM 180
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAA---------LGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 181 RSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFKLCVSQGLRTFAQTIGCIGSLYFLSPTMTMYTVAVVPGIIL 260
Cdd:cd18576 72 RKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 261 AGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFDNELDKARAMQEQLGVGIGLFQAGTNLFLN 340
Cdd:cd18576 152 VAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLF 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 115533592 341 GMILSVLYGGSNLISKGEMTPGALMSFLVSAQTIQRSLSQLSIIFG 386
Cdd:cd18576 232 GAIVAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYG 277
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
98-384 |
5.22e-50 |
|
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: 176.13 E-value: 5.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 98 FFAAVVCAILSAYINIQIPLCLGDLVNGIVKIIKDESNNlrSHFE-QLKPSALHLMTLYVAQSALTFLYITFLTVLGERM 176
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGSGESSP--DEFLdDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 177 ATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFKLCVSQGLRTFAQTIGCIGSLYFLSPTMTMYTVAVVP 256
Cdd:cd18577 79 ARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 257 GIILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFDNELDKARAMQEQLGVGIGLFQAGTN 336
Cdd:cd18577 159 LIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLF 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 115533592 337 LFLNGMILSVLYGGSNLISKGEMTPG----ALMSFLVSAQTIQRSLSQLSII 384
Cdd:cd18577 239 FIIFAMYALAFWYGSRLVRDGEISPGdvltVFFAVLIGAFSLGQIAPNLQAF 290
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
425-653 |
2.78e-49 |
|
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: 171.75 E-value: 2.78e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPtrPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQVi 504
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKV- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEPV--LFATSVEENIRYG------RPDATDEEVREAARAAHVDEFVSRFPSgystvvgergaQLSGGQKQRIAIA 576
Cdd:COG1122 78 GLVFQNPDdqLFAPTVEEDVAFGpenlglPREEIRERVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115533592 577 RAILKNPPILILDEATSALDSHSEHMVQEALNNV-MKGRTVLIIAHRLSTI-RSAQMIYVIKDKKALESGTHEQLMAKK 653
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
101-398 |
7.69e-49 |
|
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: 172.82 E-value: 7.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 101 AVVCAILSAYINIQIPLCLGDLVNGIVKIIKDESNNLRSHFEQlkpSALHLMTLYVAQSALTFLYITFLTVLGERMATKM 180
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDAVTNHSGSGGEEALRALNQ---AVLILLGVVLIGSIATFLRSWLFTLAGERVVARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 181 RSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFKLCVSQGLRTFAQTIGCIGSLYFLSPTMTMYTVAVVPGIIL 260
Cdd:cd18780 78 RKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 261 AGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFDNELDKARAMQEQLGVGIGLFQAGTNLFLN 340
Cdd:cd18780 158 GAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQ 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 115533592 341 GMILSVLYGGSNLISKGEMTPGALMSFLVSAQTIQRSLSQLSIIFGTAIKGWTAGGRV 398
Cdd:cd18780 238 LAIVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
101-398 |
9.52e-48 |
|
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: 169.65 E-value: 9.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 101 AVVCAILSAYINIQIPLCLGDLVNGIVKiikdesnnlRSHFEQLKPSALHLMTLYVAQSALTFLYITFLTVLGERMATKM 180
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVA---------DGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 181 RSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFKLCVSQGLRTFAQTIGCIGSLYFLSPTMTMYTVAVVPGIIL 260
Cdd:cd18572 72 RRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 261 AGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFDNELDKARAMQEQLGVGIGLFQAGTNLFLN 340
Cdd:cd18572 152 ITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQN 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 115533592 341 GMILSVLYGGSNLISKGEMTPGALMSFLVSAQTIQRSLSQLSIIFGTAIKGWTAGGRV 398
Cdd:cd18572 232 GTQVLVLFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
425-621 |
3.66e-47 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 165.37 E-value: 3.66e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPghtVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQVi 504
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQV- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEPVLFATSVEENIRYGRPDATDEEVREAARaahvdEFVSRFpsGYSTVVGERGA-QLSGGQKQRIAIARAILKNP 583
Cdd:COG4619 77 AYVPQEPALWGGTVRDNLPFPFQLRERKFDRERAL-----ELLERL--GLPPDILDKPVeRLSGGERQRLALIRALLLQP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 115533592 584 PILILDEATSALDSHSEHMVQEALNNVM--KGRTVLIIAH 621
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSH 189
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
425-637 |
2.96e-46 |
|
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: 162.64 E-value: 2.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPGHTVF--ENLTLSIPAGQVVALCGPSGEGKSTithLL-----ErfYEPKSGRVTLDGRdlrelnve 497
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFtlKDINLEVPKGELVAIVGPVGSGKSS---LLsallgE--LEKLSGSVSVPGS-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 498 wlrgqvIGLISQEPVLFATSVEENIRYGRPdaTDEE-VREAARAAHVDEFVSRFPSGYSTVVGERGAQLSGGQKQRIAIA 576
Cdd:cd03250 68 ------IAYVSQEPWIQNGTIRENILFGKP--FDEErYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115533592 577 RAILKNPPILILDEATSALDSH-SEHMVQEALNNV-MKGRTVLIIAHRLSTIRSAQMIYVIKD 637
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHvGRHIFENCILGLlLNNKTRILVTHQLQLLPHADQIVVLDN 202
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
98-378 |
1.22e-45 |
|
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: 163.58 E-value: 1.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 98 FFAAVVCAILSAYINIQIPLCLGdlvngivKIIKDESNNLRSHFEQLKPSALHLMTLYVAQSALTFLYITFLTVLGERMA 177
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLG-------RILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 178 TKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFKLCVSQGLRTFAQTIGCIGSLYFLSPTMTMYTVAVVPG 257
Cdd:pfam00664 74 RRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 258 IILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFDNELDKARAMQEQLGVGIGLFQAGTNL 337
Cdd:pfam00664 154 YILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQF 233
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 115533592 338 FLNGMILSVLYGGSNLISKGEMTPGALMSFLVSAQTIQRSL 378
Cdd:pfam00664 234 IGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
425-640 |
4.61e-45 |
|
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: 158.53 E-value: 4.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQvI 504
Cdd:cd03246 1 LEVENVSFRYPGA-EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH-V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEPVLFATSVEENIrygrpdatdeevreaaraahvdefvsrfpsgystvvgergaqLSGGQKQRIAIARAILKNPP 584
Cdd:cd03246 79 GYLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 115533592 585 ILILDEATSALDSHSEHMVQEALNNV-MKGRTVLIIAHRLSTIRSAQMIYVIKDKKA 640
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
425-649 |
4.68e-45 |
|
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: 160.42 E-value: 4.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPtrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYE-----PKSGRVTLDGRDLREL--NVE 497
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLdvDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 498 WLRGQViGLISQEPVLFATSVEENIRYG-------RPDATDEEVREAARAAHVDEFVSRFPSGYStvvgergaqLSGGQK 570
Cdd:cd03260 78 ELRRRV-GMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 571 QRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRLS-TIRSAQMIYVIKDKKALESGTHEQL 649
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQqAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
425-637 |
4.77e-45 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 160.21 E-value: 4.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPGHT-VFENLTLSIPAGQVVALCGPSGEGKSTITHL---LERfyePKSGRVTLDGRDLRELN---VE 497
Cdd:COG1136 5 LELRNLTKSYGTGEGEVtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIlggLDR---PTSGEVLIDGQDISSLSereLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 498 WLRGQVIGLISQEPVLFAT-SVEENIRY-----GRPDATDEE-VREAARAAHVDEFVSRFPSgystvvgergaQLSGGQK 570
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPElTALENVALplllaGVSRKERRErARELLERVGLGDRLDHRPS-----------QLSGGQQ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115533592 571 QRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMK--GRTVLIIAHRLSTIRSAQMIYVIKD 637
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRD 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
425-621 |
1.10e-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: 159.17 E-value: 1.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPG-HTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEwlrgqv 503
Cdd:cd03293 1 LEVRNVSKTYGGGGGaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 504 IGLISQEPVLFA-TSVEENIRYG------RPDATDEEVREAARAAHVDEFVSRFPSgystvvgergaQLSGGQKQRIAIA 576
Cdd:cd03293 75 RGYVFQQDALLPwLTVLDNVALGlelqgvPKAEARERAEELLELVGLSGFENAYPH-----------QLSGGMRQRVALA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 115533592 577 RAILKNPPILILDEATSALDSHSEHMVQEALNNVMK--GRTVLIIAH 621
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTH 190
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
425-650 |
2.36e-44 |
|
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: 159.05 E-value: 2.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPghtVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRgQVI 504
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA-RRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEPVL-FATSVEENIRYGR---------PDATDEE-VREAARAAHVDEFVSRFpsgYSTvvgergaqLSGGQKQRI 573
Cdd:COG1120 78 AYVPQEPPApFGLTVRELVALGRyphlglfgrPSAEDREaVEEALERTGLEHLADRP---VDE--------LSGGERQRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 574 AIARAILKNPPILILDEATSALDSHSEHMVQEALN--NVMKGRTVLIIAHRLS-TIRSAQMIYVIKDKKALESGTHEQLM 650
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRrlARERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
426-639 |
2.36e-44 |
|
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: 157.63 E-value: 2.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 426 KFEDVSFSYPTRPgHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQViG 505
Cdd:cd03225 1 ELKNLSFSYPDGA-RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKV-G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 506 LISQEP--VLFATSVEENI-----RYGRPDATDEE-VREAARAAHVDEFVSRFPSgystvvgergaQLSGGQKQRIAIAR 577
Cdd:cd03225 79 LVFQNPddQFFGPTVEEEVafgleNLGLPEEEIEErVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115533592 578 AILKNPPILILDEATSALDSHSEHMVQEALNNVMK-GRTVLIIAHRLSTIRS-AQMIYVIKDKK 639
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAeGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
423-645 |
7.74e-44 |
|
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: 156.42 E-value: 7.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 423 GDIKFEDVSFSY-PTRPghTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRG 501
Cdd:cd03369 5 GEIEVENLSVRYaPDLP--PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 502 QvIGLISQEPVLFATSVEENI-RYGRpdATDEEVREAARaahvdefvsrfpsgystvVGERGAQLSGGQKQRIAIARAIL 580
Cdd:cd03369 83 S-LTIIPQDPTLFSGTIRSNLdPFDE--YSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115533592 581 KNPPILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRLSTIRSAQMIYVIKDKKALESGT 645
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
425-663 |
8.99e-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: 164.69 E-value: 8.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPGHTVF--ENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLR-- 500
Cdd:COG1123 261 LEVRNLSKRYPVRGKGGVRavDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 501 GQVIGLISQEPV--LFAT-SVEENIRYG---RPDATDEEVREAARAA--HVD---EFVSRFPsgystvvgergAQLSGGQ 569
Cdd:COG1123 341 RRRVQMVFQDPYssLNPRmTVGDIIAEPlrlHGLLSRAERRERVAELleRVGlppDLADRYP-----------HELSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 570 KQRIAIARAILKNPPILILDEATSALDSHsehmVQEALNNVMK------GRTVLIIAHRLSTIRS-AQMIYVIKDKKALE 642
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVS----VQAQILNLLRdlqrelGLTYLFISHDLAVVRYiADRVAVMYDGRIVE 485
|
250 260
....*....|....*....|..
gi 115533592 643 SGTHEQLMAKKGSLY-RKLVEA 663
Cdd:COG1123 486 DGPTEEVFANPQHPYtRALLAA 507
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
154-657 |
2.29e-43 |
|
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: 168.59 E-value: 2.29e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 154 LYVAQSALTFLYITFLTVLGERMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFKLCVSQGLRTFAQT 233
Cdd:TIGR00957 1014 LGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNV 1093
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 234 IGCIGSLYFLSPtmtMYTVAVVP-GII--LAGSAIGAGLRQLSRRaqgQSATASAVS---DEALTNIRTIRAFAmeklES 307
Cdd:TIGR00957 1094 IGALIVILLATP---IAAVIIPPlGLLyfFVQRFYVASSRQLKRL---ESVSRSPVYshfNETLLGVSVIRAFE----EQ 1163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 308 RLFDNELD-KARAMQEQL--------GVGIGLFQAGTNLFLNGMILSVlyggsnlISKGEMTPGAL---MSFLVSAQTIQ 375
Cdd:TIGR00957 1164 ERFIHQSDlKVDENQKAYypsivanrWLAVRLECVGNCIVLFAALFAV-------ISRHSLSAGLVglsVSYSLQVTFYL 1236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 376 RSLSQLSIIFGTAIkgwTAGGRVLQFSRLEPSIPMDTGVCIPyHSLW---GDIKFEDVSFSYptRPG-HTVFENLTLSIP 451
Cdd:TIGR00957 1237 NWLVRMSSEMETNI---VAVERLKEYSETEKEAPWQIQETAP-PSGWpprGRVEFRNYCLRY--REDlDLVLRHINVTIH 1310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 452 AGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQvIGLISQEPVLFATSVEENIR-YGRpdAT 530
Cdd:TIGR00957 1311 GGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFK-ITIIPQDPVLFSGSLRMNLDpFSQ--YS 1387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 531 DEEVREAARAAHVDEFVSRFPSGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNV 610
Cdd:TIGR00957 1388 DEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQ 1467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 115533592 611 MKGRTVLIIAHRLSTIRSAQMIYVIKDKKALESGTHEQLMAKKGSLY 657
Cdd:TIGR00957 1468 FEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFY 1514
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
98-398 |
2.42e-43 |
|
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: 157.71 E-value: 2.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 98 FFAAVVCAILSAYINIQIPLCLGDLVNGIVkiikdesnnLRSHFEQLKPSALHLMTLYVAQSALTFLYITFLTVLGERMA 177
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVI---------PAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 178 TKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFKLCVSQGLRTFAQTIGCIGSLYFLSPTMTMYTVAVVPG 257
Cdd:cd07346 72 FDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 258 IILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFDNELDKARAMQEQLGVGIGLFQAGTNL 337
Cdd:cd07346 152 YVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGL 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115533592 338 FLNGMILSVLYGGSNLISKGEMTPGALMSFLVSAQTIQRSLSQLSIIFGTAIKGWTAGGRV 398
Cdd:cd07346 232 LTALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
425-644 |
4.07e-43 |
|
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: 153.24 E-value: 4.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPGHtVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLreLNVEWLRGQVI 504
Cdd:cd03247 1 LSINNVSFSYPEQEQQ-VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV--SDLEKALSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEPVLFATSVEENIrygrpdatdeevreaaraahvdefvsrfpsgystvvgerGAQLSGGQKQRIAIARAILKNPP 584
Cdd:cd03247 78 SVLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 585 ILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRLSTIRSAQMIYVIKDKKALESG 644
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
98-398 |
6.51e-43 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 156.43 E-value: 6.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 98 FFAAVVCAILSAYINIQIPLCLGDLVNGIvkiikdesnnlrshFEQLKPSALHLMTL-----YVAQSALTFLYITFLTVL 172
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDI--------------FVEKDLEALLLVPLaiiglFLLRGLASYLQTYLMAYV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 173 GERMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFKLCVSQGLRTFAQTIGCIGSLYFLSPTMTMYTV 252
Cdd:cd18552 67 GQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 253 AVVPGIILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFDNELDKARamqeQLGVGIGLFQ 332
Cdd:cd18552 147 VVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLR----RLSMKIARAR 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 333 AGTNL---FLNGMILS-VLYGGSNLISKGEMTPGALMSFLVSAQTIQRSLSQLSIIFGTAIKGWTAGGRV 398
Cdd:cd18552 223 ALSSPlmeLLGAIAIAlVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
154-663 |
7.28e-42 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 163.99 E-value: 7.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 154 LYVAQSALTFLYITFLTVLGERMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSfklcVSQGLRTFAQT 233
Cdd:PLN03232 959 LGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRN----VANLMNMFMNQ 1034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 234 IGCIGSLYFLSPTMTMYTV-AVVPGIILAGSAI---GAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFA----MEKL 305
Cdd:PLN03232 1035 LWQLLSTFALIGTVSTISLwAIMPLLILFYAAYlyyQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKaydrMAKI 1114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 306 ESRLFDNELDKARAMQEQLG-VGIGLFQAGTNLFLNGMILSVL-YGGSNLISKGEMTPGALMSF-----------LVSAQ 372
Cdd:PLN03232 1115 NGKSMDNNIRFTLANTSSNRwLTIRLETLGGVMIWLTATFAVLrNGNAENQAGFASTMGLLLSYtlnittllsgvLRQAS 1194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 373 TIQRSLSQLSIIfGTAIKGWTAGGRVLQFSRLEPSIPMDtgvcipyhslwGDIKFEDVSFSYptRPG-HTVFENLTLSIP 451
Cdd:PLN03232 1195 KAENSLNSVERV-GNYIDLPSEATAIIENNRPVSGWPSR-----------GSIKFEDVHLRY--RPGlPPVLHGLSFFVS 1260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 452 AGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRgQVIGLISQEPVLFATSVEENIRygrP--DA 529
Cdd:PLN03232 1261 PSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLR-RVLSIIPQSPVLFSGTVRFNID---PfsEH 1336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 530 TDEEVREAARAAHVDEFVSRFPSGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNN 609
Cdd:PLN03232 1337 NDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIRE 1416
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 115533592 610 VMKGRTVLIIAHRLSTIRSAQMIYVIKDKKALESGTHEQLMAKKGSLYRKLVEA 663
Cdd:PLN03232 1417 EFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHS 1470
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
425-656 |
1.11e-41 |
|
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: 158.53 E-value: 1.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPGHTVfENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPK---SGRVTLDGRDLRELNvEWLRG 501
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAV-DGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELS-EALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 502 QVIGLISQEP--VLFATSVEENIRYG------RPDATDEEVREAARAAHVDEFVSRFPsgystvvgergAQLSGGQKQRI 573
Cdd:COG1123 83 RRIGMVFQDPmtQLNPVTVGDQIAEAlenlglSRAEARARVLELLEAVGLERRLDRYP-----------HQLSGGQRQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 574 AIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMK--GRTVLIIAHRLSTI-RSAQMIYVIKDKKALESGTHEQLM 650
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEIL 231
|
....*.
gi 115533592 651 AKKGSL 656
Cdd:COG1123 232 AAPQAL 237
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
425-644 |
1.45e-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: 150.73 E-value: 1.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPGH-TVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWL--RG 501
Cdd:cd03257 2 LEVKNLSVSFPTGGGSvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkiRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 502 QVIGLISQEPVL-------FATSVEENIRYGRPDATDEEVREAARAAHV-----DEFVSRFPsgystvvgergAQLSGGQ 569
Cdd:cd03257 82 KEIQMVFQDPMSslnprmtIGEQIAEPLRIHGKLSKKEARKEAVLLLLVgvglpEEVLNRYP-----------HELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115533592 570 KQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNV--MKGRTVLIIAHRLSTIRS-AQMIYVIKDKKALESG 644
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLqeELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
425-621 |
1.93e-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: 151.40 E-value: 1.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPG-HTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELnvewlrGQV 503
Cdd:COG1116 8 LELRGVSKRFPTGGGgVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP------GPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 504 IGLISQEPVLFA-TSVEENIRYG------RPDATDEEVREAARAAHVDEFVSRFPSgystvvgergaQLSGGQKQRIAIA 576
Cdd:COG1116 82 RGVVFQEPALLPwLTVLDNVALGlelrgvPKAERRERARELLELVGLAGFEDAYPH-----------QLSGGMRQRVAIA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 115533592 577 RAILKNPPILILDEATSALDSHSEHMVQEALNNVMK--GRTVLIIAH 621
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTH 197
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
443-593 |
2.45e-41 |
|
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: 147.41 E-value: 2.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 443 FENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQvIGLISQEPVLF-ATSVEEN 521
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKE-IGYVFQDPQLFpRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115533592 522 IRYGRPDATDEEVREAARAAHVDEFVsRFPSGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILILDEATS 593
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKL-GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
425-639 |
6.29e-41 |
|
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: 148.41 E-value: 6.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPGHT-VFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELN-VEW--LR 500
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSeKELaaFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 501 GQVIGLISQEPVLFAT-SVEENIRY-----GRPDATDEE-VREAARAAHVDEFVSRFPSgystvvgergaQLSGGQKQRI 573
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELplllaGVPKKERRErAEELLERVGLGDRLNHYPS-----------ELSGGQQQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115533592 574 AIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMK--GRTVLIIAHRLSTIRSAQMIYVIKDKK 639
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAEYADRIIELRDGK 217
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
425-652 |
1.24e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 148.29 E-value: 1.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPtrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRgqVI 504
Cdd:COG1131 1 IEVRGLTKRYG---DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRR--RI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEPVLFAT-SVEENIR-----YGRPDATdeevreaaRAAHVDEFVSRFpsGYSTVVGERGAQLSGGQKQRIAIARA 578
Cdd:COG1131 76 GYVPQEPALYPDlTVRENLRffarlYGLPRKE--------ARERIDELLELF--GLTDAADRKVGTLSGGMKQRLGLALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115533592 579 ILKNPPILILDEATSALDSHSEHMVQEALNNVMK-GRTVLIIAHRLSTI-RSAQMIYVIKDKKALESGTHEQLMAK 652
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLRELAAeGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
175-663 |
1.37e-39 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 156.82 E-value: 1.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 175 RMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQE-------FKSSFKLCVSQGLRTFAqTIGcigslyFLSpTM 247
Cdd:PLN03130 983 YAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDidrnvavFVNMFLGQIFQLLSTFV-LIG------IVS-TI 1054
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 248 TMYtvAVVPGIILAGSA---IGAGLRQLSRRaqgQSATASAVS---DEALTNIRTIRAFA----MEKLESRLFDNELDKA 317
Cdd:PLN03130 1055 SLW--AIMPLLVLFYGAylyYQSTAREVKRL---DSITRSPVYaqfGEALNGLSTIRAYKaydrMAEINGRSMDNNIRFT 1129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 318 RA-MQEQLGVGIGL-FQAGTNLFLNGMiLSVLyGGSNLISKGEMTPgaLMSFLVS-AQTIQRSLSQLSIIFGTAIKGWTA 394
Cdd:PLN03130 1130 LVnMSSNRWLAIRLeTLGGLMIWLTAS-FAVM-QNGRAENQAAFAS--TMGLLLSyALNITSLLTAVLRLASLAENSLNA 1205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 395 GGRVLQFSRLEPSIP--MDTGVCIPYHSLWGDIKFEDVSFSY-PTRPghTVFENLTLSIPAGQVVALCGPSGEGKSTITH 471
Cdd:PLN03130 1206 VERVGTYIDLPSEAPlvIENNRPPPGWPSSGSIKFEDVVLRYrPELP--PVLHGLSFEISPSEKVGIVGRTGAGKSSMLN 1283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 472 LLERFYEPKSGRVTLDGRDLRELNVEWLRgQVIGLISQEPVLFATSVEENIRygrP--DATDEEVREAARAAHVDEFVSR 549
Cdd:PLN03130 1284 ALFRIVELERGRILIDGCDISKFGLMDLR-KVLGIIPQAPVLFSGTVRFNLD---PfnEHNDADLWESLERAHLKDVIRR 1359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 550 FPSGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRLSTIRSA 629
Cdd:PLN03130 1360 NSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDC 1439
|
490 500 510
....*....|....*....|....*....|....
gi 115533592 630 QMIYVIKDKKALESGTHEQLMAKKGSLYRKLVEA 663
Cdd:PLN03130 1440 DRILVLDAGRVVEFDTPENLLSNEGSAFSKMVQS 1473
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
421-664 |
1.56e-39 |
|
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: 146.21 E-value: 1.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 421 LWGDIKFEDVSFSYPT--RPghtVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEW 498
Cdd:cd03288 16 LGGEIKIHDLCVRYENnlKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 499 LRGQvIGLISQEPVLFATSVEENIRYGRpDATDEEVREAARAAHVDEFVSRFPSGYSTVVGERGAQLSGGQKQRIAIARA 578
Cdd:cd03288 93 LRSR-LSIILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 579 ILKNPPILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRLSTIRSAQMIYVIKDKKALESGTHEQLMAKKGSLYR 658
Cdd:cd03288 171 FVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFA 250
|
....*.
gi 115533592 659 KLVEAH 664
Cdd:cd03288 251 SLVRTD 256
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
425-663 |
1.61e-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: 145.39 E-value: 1.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPghtVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRgqVI 504
Cdd:COG4555 2 IEVENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARR--QI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEPVLFAT-SVEENIRYgrpDATDEEVREAARAAHVDEFVSRFpsGYSTVVGERGAQLSGGQKQRIAIARAILKNP 583
Cdd:COG4555 77 GVLPDERGLYDRlTVRENIRY---FAELYGLFDEELKKRIEELIELL--GLEEFLDRRVGELSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 584 PILILDEATSALDSHSEHMVQEALNNVMK-GRTVLIIAHRLSTI-RSAQMIYVIKDKKALESGTHEQLMAKKG--SLYRK 659
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRALKKeGKTVLFSSHIMQEVeALCDRVVILHKGKVVAQGSLDELREEIGeeNLEDA 231
|
....
gi 115533592 660 LVEA 663
Cdd:COG4555 232 FVAL 235
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
98-368 |
2.37e-39 |
|
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: 146.42 E-value: 2.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 98 FFAAVVCAILSAYINIQIPLCLGDLVNGIVKIikdesnnlrshfEQLKPSALHLMTLYVAQSALTFLYITFLTVLGERMA 177
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAG------------GSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 178 TKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSfklcVSQGL-RTFAQTIGCIGSLYF---LSPTMTMYTVA 253
Cdd:cd18551 69 LDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLREL----ITSGLpQLVTGVLTVVGAVVLmflLDWVLTLVTLA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 254 VVPGIILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFDNELDKARamqeQLGVGIGLFQA 333
Cdd:cd18551 145 VVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLY----RAGLKAAKIEA 220
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 115533592 334 G----TNLFLNGMILSVL-YGGSnLISKGEMTPGALMSFL 368
Cdd:cd18551 221 LigplMGLAVQLALLVVLgVGGA-RVASGALTVGTLVAFL 259
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
425-651 |
2.58e-39 |
|
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: 144.57 E-value: 2.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRpghTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRG--Q 502
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRlrR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 503 VIGLISQEPVLF-ATSVEENI------RYGRPDAT-DEEVREAARAAHVDEFVSRFPsgystvvgergAQLSGGQKQRIA 574
Cdd:cd03261 78 RMGMLFQSGALFdSLTVFENVafplreHTRLSEEEiREIVLEKLEAVGLRGAEDLYP-----------AELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 575 IARAILKNPPILILDEATSALDSHSEHMVQEALNNV--MKGRTVLIIAHRLSTIRS-AQMIYVIKDKKALESGTHEQLMA 651
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
425-663 |
4.88e-39 |
|
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: 144.18 E-value: 4.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRP-GHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQV 503
Cdd:COG1124 2 LEVRNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 504 iGLISQEPVL-------FATSVEENIR-YGRPDaTDEEVREAARAAHVD-EFVSRFPsgystvvgergAQLSGGQKQRIA 574
Cdd:COG1124 82 -QMVFQDPYAslhprhtVDRILAEPLRiHGLPD-REERIAELLEQVGLPpSFLDRYP-----------HQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 575 IARAILKNPPILILDEATSALDSHsehmVQEALNNVMK------GRTVLIIAHRLSTI-RSAQMIYVIKDKKALESGTHE 647
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVS----VQAEILNLLKdlreerGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVA 224
|
250
....*....|....*..
gi 115533592 648 QLMAKKGSLY-RKLVEA 663
Cdd:COG1124 225 DLLAGPKHPYtRELLAA 241
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
425-652 |
1.82e-38 |
|
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: 142.33 E-value: 1.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPG-HTVFENLTLSIPAGQVVALCGPSGEGKST---ITHLLERfyePKSGRVTLDGRDLRELNVEWLR 500
Cdd:cd03258 2 IELKNVSKVFGDTGGkVTALKDVSLSVPKGEIFGIIGRSGAGKSTlirCINGLER---PTSGSVLVDGTDLTLLSGKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 501 G--QVIGLISQEPVLFAT-SVEENIRY-----GRPDATDEEvreaaRAAHVDEFVsrfpsGYSTVVGERGAQLSGGQKQR 572
Cdd:cd03258 79 KarRRIGMIFQHFNLLSSrTVFENVALpleiaGVPKAEIEE-----RVLELLELV-----GLEDKADAYPAQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 573 IAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMK--GRTVLIIAHRLSTIRS-AQMIYVIKDKKALESGTHEQL 649
Cdd:cd03258 149 VGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
...
gi 115533592 650 MAK 652
Cdd:cd03258 229 FAN 231
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
425-651 |
4.30e-38 |
|
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: 141.67 E-value: 4.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRgQVI 504
Cdd:cd03295 1 IEFENVTKRYGG--GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELR-RKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEPVLFA-TSVEENI-------RYGRPDAtDEEVREAARAAHVD--EFVSRFPSgystvvgergaQLSGGQKQRIA 574
Cdd:cd03295 78 GYVIQQIGLFPhMTVEENIalvpkllKWPKEKI-RERADELLALVGLDpaEFADRYPH-----------ELSGGQQQRVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 575 IARAILKNPPILILDEATSALDSHSEHMVQEALNNVMK--GRTVLIIAHRL-STIRSAQMIYVIKDKKALESGTHEQLMA 651
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
425-637 |
8.30e-38 |
|
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: 138.47 E-value: 8.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPtrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWL-RGQV 503
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPpLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 504 IGLISQEPVLFAT-SVEENIRYGrpdatdeevreaaraahvdefvsrfpsgystvvgergaqLSGGQKQRIAIARAILKN 582
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 115533592 583 PPILILDEATSALDSHSEHMVQEALNNV--MKGRTVLIIAHRLS-TIRSAQMIYVIKD 637
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDeAARLADRVVVLRD 176
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
426-639 |
8.64e-38 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 137.76 E-value: 8.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 426 KFEDVSFSYPtrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQvIG 505
Cdd:cd00267 1 EIENLSFRYG---GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRR-IG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 506 LISQepvlfatsveenirygrpdatdeevreaaraahvdefvsrfpsgystvvgergaqLSGGQKQRIAIARAILKNPPI 585
Cdd:cd00267 77 YVPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 115533592 586 LILDEATSALDSHSEHMVQEALNN-VMKGRTVLIIAHRLSTI-RSAQMIYVIKDKK 639
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
425-630 |
1.59e-37 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 139.42 E-value: 1.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPtrPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELN---VEWLRg 501
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 502 QVIGLISQE-PVLFATSVEENIRY-----GRPDAtdeEVREAARAA--HVD--EFVSRFPsgystvvgergAQLSGGQKQ 571
Cdd:COG2884 79 RRIGVVFQDfRLLPDRTVYENVALplrvtGKSRK---EIRRRVREVldLVGlsDKAKALP-----------HELSGGEQQ 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115533592 572 RIAIARAILKNPPILILDEATSALD-SHSEHMVQ--EALNNVmkGRTVLIIAHRLSTIRSAQ 630
Cdd:COG2884 145 RVAIARALVNRPELLLADEPTGNLDpETSWEIMEllEEINRR--GTTVLIATHDLELVDRMP 204
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
425-621 |
2.31e-37 |
|
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: 138.42 E-value: 2.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPtrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEwLRGqvI 504
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-RRN--I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEPVLFAT-SVEENIRYG------RPDATDEEVREAARAAHVDEFVSRFPSgystvvgergaQLSGGQKQRIAIAR 577
Cdd:cd03259 75 GMVFQDYALFPHlTVAENIAFGlklrgvPKAEIRARVRELLELVGLEGLLNRYPH-----------ELSGGQQQRVALAR 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 115533592 578 AILKNPPILILDEATSALDSHSEHMVQEALNNVMK--GRTVLIIAH 621
Cdd:cd03259 144 ALAREPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTH 189
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
424-605 |
4.39e-37 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 141.77 E-value: 4.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 424 DIKFEDVSFSYPtrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEwLRGqv 503
Cdd:COG3842 5 ALELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE-KRN-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 504 IGLISQEPVLFA-TSVEENIRYG------RPDATDEEVREAARAAHVDEFVSRFPsgystvvgergAQLSGGQKQRIAIA 576
Cdd:COG3842 79 VGMVFQDYALFPhLTVAENVAFGlrmrgvPKAEIRARVAELLELVGLEGLADRYP-----------HQLSGGQQQRVALA 147
|
170 180 190
....*....|....*....|....*....|
gi 115533592 577 RAILKNPPILILDEATSALDSHS-EHMVQE 605
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALDAKLrEEMREE 177
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
101-386 |
1.14e-36 |
|
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: 138.77 E-value: 1.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 101 AVVCAILSAYINIQIPLCLGDLVNGIvkIIKDESNNLRSHFeqlkpsaLHLMTLYVAQSALTFLYITFLTVLGERMATKM 180
Cdd:cd18575 1 ALIALLIAAAATLALGQGLRLLIDQG--FAAGNTALLNRAF-------LLLLAVALVLALASALRFYLVSWLGERVVADL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 181 RSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFKLCVSQGLRTFAQTIGCIGSLYFLSPTMTMYTVAVVPGIIL 260
Cdd:cd18575 72 RKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 261 AGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFDNELDKA------RAMQEQL--GVGIGLFQ 332
Cdd:cd18575 152 PIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAfaaalrRIRARALltALVIFLVF 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 115533592 333 AGtnlflngmILSVLYGGSNLISKGEMTPGALMSFLVSAQTIQRSLSQLSIIFG 386
Cdd:cd18575 232 GA--------IVFVLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWG 277
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
425-651 |
3.08e-36 |
|
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: 136.26 E-value: 3.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPtrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVE---WLRG 501
Cdd:COG1127 6 IEVRNLTKSFG---DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 502 QvIGLISQEPVLFaTS--VEENIRYG---RPDATDEEVREAAR----AAHVDEFVSRFPSgystvvgergaQLSGGQKQR 572
Cdd:COG1127 83 R-IGMLFQGGALF-DSltVFENVAFPlreHTDLSEAEIRELVLekleLVGLPGAADKMPS-----------ELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 573 IAIARAILKNPPILILDEATSALDSHS----EHMVQEaLNNVMkGRTVLIIAHRLSTIRS-AQMIYVIKDKKALESGTHE 647
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITsaviDELIRE-LRDEL-GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPE 227
|
....
gi 115533592 648 QLMA 651
Cdd:COG1127 228 ELLA 231
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
425-628 |
7.77e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 135.22 E-value: 7.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPtrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRElnvewlRGQVI 504
Cdd:COG1121 7 IELENLTVSYG---GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR------ARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEPVL---FATSVEENI---RYG------RPDATD-EEVREAARAAHVDEFVSRfpsgystVVGErgaqLSGGQKQ 571
Cdd:COG1121 78 GYVPQRAEVdwdFPITVRDVVlmgRYGrrglfrRPSRADrEAVDEALERVGLEDLADR-------PIGE----LSGGQQQ 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 115533592 572 RIAIARAILKNPPILILDEATSALDSHSEHMVQEALNN-VMKGRTVLIIAHRLSTIRS 628
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVRE 204
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
425-656 |
1.45e-35 |
|
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: 135.25 E-value: 1.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYP--TRPghtVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRD-LRELNVEWLRg 501
Cdd:TIGR04520 1 IEVENVSFSYPesEKP---ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDtLDEENLWEIR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 502 QVIGLISQEP--VLFATSVEENIRYG------RPDATDEEVREAARAAHVDEFVSRFPsgystvvgergAQLSGGQKQRI 573
Cdd:TIGR04520 77 KKVGMVFQNPdnQFVGATVEDDVAFGlenlgvPREEMRKRVDEALKLVGMEDFRDREP-----------HLLSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 574 AIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMK--GRTVLIIAHRLSTIRSAQMIYVIKDKKALESGTHEQLMA 651
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeeGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFS 225
|
....*
gi 115533592 652 KKGSL 656
Cdd:TIGR04520 226 QVELL 230
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
425-651 |
2.72e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 133.34 E-value: 2.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYptrpGHTVFeNLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEwLRGqvI 504
Cdd:COG3840 2 LRLDDLTYRY----GDFPL-RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA-ERP--V 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEPVLFA-TSVEENIRYG-----RPDATD-EEVREAARAAHVDEFVSRFPsgystvvgergAQLSGGQKQRIAIAR 577
Cdd:COG3840 74 SMLFQENNLFPhLTVAQNIGLGlrpglKLTAEQrAQVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVALAR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 578 AILKNPPILILDEATSALDShsehmvqeALNNVM----------KGRTVLIIAHRLSTIRS-AQMIYVIKDKKALESGTH 646
Cdd:COG3840 143 CLVRKRPILLLDEPFSALDP--------ALRQEMldlvdelcreRGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPT 214
|
....*
gi 115533592 647 EQLMA 651
Cdd:COG3840 215 AALLD 219
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
425-645 |
6.59e-35 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 135.21 E-value: 6.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPG-HTVFENLTLSIPAGQVVALCGPSGEGKST----IThLLERfyePKSGRVTLDGRDLRELNVEWL 499
Cdd:COG1135 2 IELENLSKTFPTKGGpVTALDDVSLTIEKGEIFGIIGYSGAGKSTlircIN-LLER---PTSGSVLVDGVDLTALSEREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 500 RG--QVIGLISQEPVLFAT-SVEENIRY-----GRPdatdeevrEAARAAHVDE---FV------SRFPSgystvvgerg 562
Cdd:COG1135 78 RAarRKIGMIFQHFNLLSSrTVAENVALpleiaGVP--------KAEIRKRVAElleLVglsdkaDAYPS---------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 563 aQLSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMK--GRTVLIIAHRLSTIRS-AQMIYVIKDKK 639
Cdd:COG1135 140 -QLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGR 218
|
....*.
gi 115533592 640 ALESGT 645
Cdd:COG1135 219 IVEQGP 224
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
425-621 |
8.78e-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: 132.04 E-value: 8.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPtrpGHTVFENLTLSIPAGQVVALCGPSGEGKST----ITHLlErfyEPKSGRVTLDGRDL--RELNVEW 498
Cdd:COG1126 2 IEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTllrcINLL-E---EPDSGTITVDGEDLtdSKKDINK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 499 LRGQvIGLISQEPVLFA-TSVEENIRY------GRPDAtdeEVREAARA--AHV--DEFVSRFPSgystvvgergaQLSG 567
Cdd:COG1126 75 LRRK-VGMVFQQFNLFPhLTVLENVTLapikvkKMSKA---EAEERAMEllERVglADKADAYPA-----------QLSG 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 115533592 568 GQKQRIAIARAILKNPPILILDEATSALDshSEhMVQEALnNVMK-----GRTVLIIAH 621
Cdd:COG1126 140 GQQQRVAIARALAMEPKVMLFDEPTSALD--PE-LVGEVL-DVMRdlakeGMTMVVVTH 194
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
98-368 |
1.18e-34 |
|
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: 133.33 E-value: 1.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 98 FFAAVVCAILSAYINIQIPLCLGDLVNgivKIIKDEsnnlrsHFEQLKPSALHLMTLYVAQSALTFLYITFLTVLGERMA 177
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIID---SVIGGG------LRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 178 TKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFKLCVSQGLRTFAQTIGCIGSLYFLSPTMTMYTVAVVPG 257
Cdd:cd18542 72 YDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 258 IILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFDNELDKARAMQEQLGVGIGLFQAGTNL 337
Cdd:cd18542 152 IALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDF 231
|
250 260 270
....*....|....*....|....*....|.
gi 115533592 338 FLNGMILSVLYGGSNLISKGEMTPGALMSFL 368
Cdd:cd18542 232 LSGLQIVLVLWVGGYLVINGEITLGELVAFI 262
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
98-369 |
7.40e-34 |
|
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: 130.99 E-value: 7.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 98 FFAAVVCAILSAYINIQIPLCLGDLVNGIvkiikdesNNLRSHFEQLKPSALHLMTLYVAQSALTFLYITFLTVLGERMA 177
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDAL--------TAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 178 TKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFKLCVSQGLRTFAQTIGCIGSLYFLSPTMTMYTVAVVPG 257
Cdd:cd18541 73 YDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 258 IILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFDNELDKARAMQEQLGVGIGLFQAGTNL 337
Cdd:cd18541 153 LALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGL 232
|
250 260 270
....*....|....*....|....*....|...
gi 115533592 338 FLN-GMILSVLYGGSnLISKGEMTPGALMSFLV 369
Cdd:cd18541 233 LIGlSFLIVLWYGGR-LVIRGTITLGDLVAFNS 264
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
428-621 |
8.44e-34 |
|
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: 128.14 E-value: 8.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 428 EDVSFSYptRPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRElnveWLRGQVIGLI 507
Cdd:cd03226 3 ENISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA----KERRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 508 SQEP--VLFATSVEENIRYGRPDATD--EEVREAARAAHVDEFVSRFPsgystvvgergAQLSGGQKQRIAIARAILKNP 583
Cdd:cd03226 77 MQDVdyQLFTDSVREELLLGLKELDAgnEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGK 145
|
170 180 190
....*....|....*....|....*....|....*....
gi 115533592 584 PILILDEATSALDSHSEHMVQEALNNVMK-GRTVLIIAH 621
Cdd:cd03226 146 DLLIFDEPTSGLDYKNMERVGELIRELAAqGKAVIVITH 184
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
426-626 |
8.53e-34 |
|
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: 128.42 E-value: 8.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 426 KFEDVSFSYPtrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRElnvEWLRgqvIG 505
Cdd:cd03235 1 EVEDLTVSYG---GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK---ERKR---IG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 506 LISQEPVL---FATSVEENI---RYGRPDA---TDEEVREAARAAHvdEFVsrfpsGYSTVVGERGAQLSGGQKQRIAIA 576
Cdd:cd03235 72 YVPQRRSIdrdFPISVRDVVlmgLYGHKGLfrrLSKADKAKVDEAL--ERV-----GLSELADRQIGELSGGQQQRVLLA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 115533592 577 RAILKNPPILILDEATSALDSHSEHMVQEALNNV-MKGRTVLIIAHRLSTI 626
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLV 195
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
425-639 |
1.30e-33 |
|
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: 126.36 E-value: 1.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPghtVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRgqVI 504
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKR--RI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEPVLFAT-SVEENIRYgrpdatdeevreaaraahvdefvsrfpsgystvvgergaqlSGGQKQRIAIARAILKNP 583
Cdd:cd03230 76 GYLPEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDP 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 115533592 584 PILILDEATSALDSHSEHMVQEALNNVMK-GRTVLIIAHRLSTIRS-AQMIYVIKDKK 639
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRELKKeGKTILLSSHILEEAERlCDRVAILNNGR 172
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
88-408 |
1.53e-33 |
|
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: 131.03 E-value: 1.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 88 WNLIKPFFGWFFAAVVCAILSAYINiqiPL---CLGDLVNGIVKI----IKDESNNLrshfeqlkpsALHLMTLYVAQSA 160
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVF---PVfaiLFSKLISVFSLPdddeLRSEANFW----------ALMFLVLAIVAGI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 161 LTFLYITFLTVLGERMATKMRSDLFQKLLHHDMAFFD--SHKSGELSARLNADVQEFKSSFKLCVSQGLRTFAQTIGCIG 238
Cdd:cd18578 68 AYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDdpENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 239 -SLYFlSPTMTMYTVAVVPGIILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFDNELDKA 317
Cdd:cd18578 148 iAFVY-GWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 318 RAMQEQLGVGIGLFQAGTNLFLNGMILSVLYGGSNLISKGEMTPG----ALMSFLVSAQTIQRSLSQLSiifgTAIKGWT 393
Cdd:cd18578 227 LKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEqffiVFMALIFGAQSAGQAFSFAP----DIAKAKA 302
|
330
....*....|....*
gi 115533592 394 AGGRVLQFSRLEPSI 408
Cdd:cd18578 303 AAARIFRLLDRKPEI 317
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
425-623 |
3.14e-33 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 128.23 E-value: 3.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPtrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYE--PK---SGRVTLDGRDL--RELNVE 497
Cdd:COG1117 12 IEVRNLNVYYG---DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGarvEGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 498 WLRGQViGLISQEPVLFATSVEENIRYG-------RPDATDEEVREAARAAHV-DEfvsrfpsgystvVGER----GAQL 565
Cdd:COG1117 89 ELRRRV-GMVFQKPNPFPKSIYDNVAYGlrlhgikSKSELDEIVEESLRKAALwDE------------VKDRlkksALGL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 115533592 566 SGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRL 623
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNM 213
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
425-658 |
1.08e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 127.44 E-value: 1.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPGHTVfENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQVi 504
Cdd:PRK13635 6 IRVEHISFRYPDAATYAL-KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQV- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEP--VLFATSVEENIRYG-------RPDATdEEVREAARAAHVDEFVSRFPsgystvvgergAQLSGGQKQRIAI 575
Cdd:PRK13635 84 GMVFQNPdnQFVGATVQDDVAFGlenigvpREEMV-ERVDQALRQVGMEDFLNREP-----------HRLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 576 ARAILKNPPILILDEATSALDSHSEhmvQEALNNV-----MKGRTVLIIAHRLSTIRSAQMIYVIKDKKALESGTHEQLM 650
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGR---REVLETVrqlkeQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIF 228
|
....*...
gi 115533592 651 AKKGSLYR 658
Cdd:PRK13635 229 KSGHMLQE 236
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
425-629 |
1.25e-32 |
|
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: 125.33 E-value: 1.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPtrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDL--RELNVEWLRGQ 502
Cdd:cd03262 1 IEIKNLHKSFG---DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 503 ViGLISQEPVLFA-TSVEENI------RYGRPDAtdeEVREAARAA----HVDEFVSRFPsgystvvgergAQLSGGQKQ 571
Cdd:cd03262 78 V-GMVFQQFNLFPhLTVLENItlapikVKGMSKA---EAEERALELlekvGLADKADAYP-----------AQLSGGQQQ 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115533592 572 RIAIARAILKNPPILILDEATSALDShseHMVQEALnNVMK-----GRTVLIIAHRLSTIRSA 629
Cdd:cd03262 143 RVAIARALAMNPKVMLFDEPTSALDP---ELVGEVL-DVMKdlaeeGMTMVVVTHEMGFAREV 201
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
425-653 |
1.37e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 127.03 E-value: 1.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPtrPGHT-VFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQv 503
Cdd:PRK13632 8 IKVENVSFSYP--NSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKK- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 504 IGLISQEP--VLFATSVEENIRYG------RPDATDEEVREAARAAHVDEFVSRFPSgystvvgergaQLSGGQKQRIAI 575
Cdd:PRK13632 85 IGIIFQNPdnQFIGATVEDDIAFGlenkkvPPKKMKDIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 576 ARAILKNPPILILDEATSALDSHSEHMVQEALNNVMKGR--TVLIIAHRLSTIRSAQMIYVIKDKKALESGTHEQLMAKK 653
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
444-652 |
1.38e-32 |
|
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: 125.91 E-value: 1.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 444 ENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEwLRGqvIGLISQEPVLFA-TSVEENI 522
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-KRD--ISYVPQNYALFPhMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 523 RYG-----RPDAT-DEEVREAARAAHVDEFVSRFPsgystvvgergAQLSGGQKQRIAIARAILKNPPILILDEATSALD 596
Cdd:cd03299 93 AYGlkkrkVDKKEiERKVLEIAEMLGIDHLLNRKP-----------ETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 115533592 597 SHSEHMVQEALNNVMK--GRTVLIIAHRLSTIRS-AQMIYVIKDKKALESGTHEQLMAK 652
Cdd:cd03299 162 VRTKEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
425-627 |
2.58e-32 |
|
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: 127.48 E-value: 2.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPGH-TVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPK---SGRVTLDGRDLRELN---VE 497
Cdd:COG0444 2 LEVRNLKVYFPTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSekeLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 498 WLRGQVIGLISQEPvlfATS----------VEENIRYGRpDATDEEVREAARAA-------HVDEFVSRFPSgystvvge 560
Cdd:COG0444 82 KIRGREIQMIFQDP---MTSlnpvmtvgdqIAEPLRIHG-GLSKAEARERAIELlervglpDPERRLDRYPH-------- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115533592 561 rgaQLSGGQKQRIAIARAILKNPPILILDEATSALD-ShsehmVQEALNNVMK------GRTVLIIAHRLSTIR 627
Cdd:COG0444 150 ---ELSGGMRQRVMIARALALEPKLLIADEPTTALDvT-----IQAQILNLLKdlqrelGLAILFITHDLGVVA 215
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
425-632 |
2.88e-32 |
|
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: 123.74 E-value: 2.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSyptRPGHTVFENLTLSIPAGQVVALCGPSGEGKST----ITHLLErfyePKSGRVTLDGRDLRELNVEWLR 500
Cdd:COG4133 3 LEAENLSCR---RGERLLFSGLSFTLAAGEALALTGPNGSGKTTllriLAGLLP----PSAGEVLWNGEPIRDAREDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 501 gqVIGLISQEPVLFAT-SVEENIR-----YGRPdATDEEVREAARAAHVDEFVSRFPSgystvvgergaQLSGGQKQRIA 574
Cdd:COG4133 76 --RLAYLGHADGLKPElTVRENLRfwaalYGLR-ADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVA 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 115533592 575 IARAILKNPPILILDEATSALDSHSEHMVQEALNN-VMKGRTVLIIAHRLSTIRSAQMI 632
Cdd:COG4133 142 LARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTHQPLELAAARVL 200
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
428-644 |
3.09e-32 |
|
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: 122.93 E-value: 3.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 428 EDVSFSYPtrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRgQVIGLI 507
Cdd:cd03214 3 ENLSVGYG---GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA-RKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 508 SQepvlfatsveenirygrpdatdeevreAARAAHVDEFVSRFpsgYSTvvgergaqLSGGQKQRIAIARAILKNPPILI 587
Cdd:cd03214 79 PQ---------------------------ALELLGLAHLADRP---FNE--------LSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 588 LDEATSALDSHSEHMVQEALNNVMK--GRTVLIIAHRLS-TIRSAQMIYVIKDKKALESG 644
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARerGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
425-653 |
3.26e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 126.00 E-value: 3.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYptRPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQVi 504
Cdd:PRK13647 5 IEVEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKV- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEP--VLFATSVEENIRYG------RPDATDEEVREAARAAHVDEFVSRFPSgystvvgergaQLSGGQKQRIAIA 576
Cdd:PRK13647 82 GLVFQDPddQVFSSTVWDDVAFGpvnmglDKDEVERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115533592 577 RAILKNPPILILDEATSALDSHSEHMVQEALNNVMK-GRTVLIIAHRLSTIRS-AQMIYVIKDKKALESGTHEQLMAKK 653
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNqGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
425-637 |
4.59e-32 |
|
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: 124.60 E-value: 4.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQV- 503
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 504 -IGLISQEPVLFA-TSVEENIRYGRPDAT----------DEEVREAARAAhvdefVSRFpsGYSTVVGERGAQLSGGQKQ 571
Cdd:cd03256 79 qIGMIFQQFNLIErLSVLENVLSGRLGRRstwrslfglfPKEEKQRALAA-----LERV--GLLDKAYQRADQLSGGQQQ 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115533592 572 RIAIARAILKNPPILILDEATSALDSHSEHMVQEAL--NNVMKGRTVLIIAHRLSTIRS-AQMIYVIKD 637
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLkrINREEGITVIVSLHQVDLAREyADRIVGLKD 220
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
423-648 |
6.20e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 127.11 E-value: 6.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 423 GDIKFEDVSFSYPtrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTithLLeR----FYEPKSGRVTLDGRDLRELNVEw 498
Cdd:COG3839 2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKST---LL-RmiagLEDPTSGEILIGGRDVTDLPPK- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 499 LRGqvIGLISQEPVLF-ATSVEENIRYG------RPDATDEEVREAARAAHVDEFVSRFPsgystvvgergAQLSGGQKQ 571
Cdd:COG3839 74 DRN--IAMVFQSYALYpHMTVYENIAFPlklrkvPKAEIDRRVREAAELLGLEDLLDRKP-----------KQLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 572 RIAIARAILKNPPILILDEATSALDSHS-EHMVQEalnnvmkgrtvliIA---HRLSTIrsaqMIYVikdkkalesgTHE 647
Cdd:COG3839 141 RVALGRALVREPKVFLLDEPLSNLDAKLrVEMRAE-------------IKrlhRRLGTT----TIYV----------THD 193
|
.
gi 115533592 648 Q 648
Cdd:COG3839 194 Q 194
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
425-628 |
7.78e-32 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 124.01 E-value: 7.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRG--Q 502
Cdd:COG3638 3 LELRNLSKRYPG--GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRlrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 503 VIGLISQEPVLFA-TSVEENI-----------RYGRPDATDEEVREAARA-AHVD--EFVSRfpsgystvvgeRGAQLSG 567
Cdd:COG3638 81 RIGMIFQQFNLVPrLSVLTNVlagrlgrtstwRSLLGLFPPEDRERALEAlERVGlaDKAYQ-----------RADQLSG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115533592 568 GQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALN--NVMKGRTVLIIAHRLSTIRS 628
Cdd:COG3638 150 GQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRriAREDGITVVVNLHQVDLARR 212
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
425-627 |
3.19e-31 |
|
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: 121.06 E-value: 3.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPGHtvfenLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEwlrGQVI 504
Cdd:cd03298 1 VRLDKIRFSYGEQPMH-----FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA---DRPV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEPVLFA-TSVEENIRYGRP-----DATDEE-VREAARAAHVDEFVSRFPSgystvvgergaQLSGGQKQRIAIAR 577
Cdd:cd03298 73 SMLFQENNLFAhLTVEQNVGLGLSpglklTAEDRQaIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALAR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 115533592 578 AILKNPPILILDEATSALDSHSEHMVQEALNNV--MKGRTVLIIAHRLSTIR 627
Cdd:cd03298 142 VLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhaETKMTVLMVTHQPEDAK 193
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
101-386 |
4.19e-31 |
|
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: 123.22 E-value: 4.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 101 AVVCAILSAYINIQIPLCLGdlvngivKIIkdesNNLRSHF-EQLKPSALHLMTLYVAQSALTF-LYITFLTVLGERMAT 178
Cdd:cd18590 1 AFLFLTLAVICETFIPYYTG-------RVI----DILGGEYqHNAFTSAIGLMCLFSLGSSLSAgLRGGLFMCTLSRLNL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 179 KMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFKLCVSQGLRTFAQTIGCIGSLYFLSPTMTMYTVAVVPGI 258
Cdd:cd18590 70 RLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 259 ILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFDNELDKARAMQEQLGVGIGLFQAGTNLF 338
Cdd:cd18590 150 AIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVL 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 115533592 339 LNGMILSVLYGGSNLISKGEMTPGALMSFLVSAQTIQRSLSQLSIIFG 386
Cdd:cd18590 230 QLGVQVLMLYCGRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYG 277
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
425-621 |
4.54e-31 |
|
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: 121.19 E-value: 4.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPtrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLreLNVEWLRGQVi 504
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPV- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEPVLFA-TSVEENIRYG------RPDATDEEVREAARAAHVDEFVSRFPSgystvvgergaQLSGGQKQRIAIAR 577
Cdd:cd03300 75 NTVFQNYALFPhLTVFENIAFGlrlkklPKAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIAR 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 115533592 578 AILKNPPILILDEATSALDSH-SEHMvQEALNNVMK--GRTVLIIAH 621
Cdd:cd03300 144 ALVNEPKVLLLDEPLGALDLKlRKDM-QLELKRLQKelGITFVFVTH 189
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
175-662 |
1.83e-30 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 128.56 E-value: 1.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 175 RMATKMRSDLFQKLLHHDMAFfdSHK------SGELSARLNADVQEFKS---------SFKLCVSQGLRTFAQTIGC--- 236
Cdd:PLN03232 367 RVGFRLRSTLVAAIFHKSLRL--THEarknfaSGKVTNMITTDANALQQiaeqlhglwSAPFRIIVSMVLLYQQLGVasl 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 237 IGSL--YFLSPTMTMytvavvpgiilagsaIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEK-LESRL---F 310
Cdd:PLN03232 445 FGSLilFLLIPLQTL---------------IVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKsFESRIqgiR 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 311 DNELDKARAMQeqlgvgigLFQAGTNLFLNG--MILSVLYGGSNLISKGEMTPGALMSFLVSAQTIQRSLSQLSIIFGTA 388
Cdd:PLN03232 510 NEELSWFRKAQ--------LLSAFNSFILNSipVVVTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQV 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 389 IKGWTAGGRV----LQFSR-LEPSIPMDTGvcIPYhslwgdIKFEDVSFSYPTRPGHTVFENLTLSIPAGQVVALCGPSG 463
Cdd:PLN03232 582 VNANVSLQRIeellLSEERiLAQNPPLQPG--APA------ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTG 653
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 464 EGK-STITHLLERFYEPKSGRVTLdgrdlrelnvewlRGQViGLISQEPVLFATSVEENIRYGRpDATDEEVREAARAAH 542
Cdd:PLN03232 654 EGKtSLISAMLGELSHAETSSVVI-------------RGSV-AYVPQVSWIFNATVRENILFGS-DFESERYWRAIDVTA 718
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 543 VDEFVSRFPSGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMV-QEALNNVMKGRTVLIIAH 621
Cdd:PLN03232 719 LQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVfDSCMKDELKGKTRVLVTN 798
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 115533592 622 RLSTIRSAQMIYVIKDKKALESGTHEQLmAKKGSLYRKLVE 662
Cdd:PLN03232 799 QLHFLPLMDRIILVSEGMIKEEGTFAEL-SKSGSLFKKLME 838
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
425-621 |
1.84e-30 |
|
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: 118.90 E-value: 1.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPtrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEwLRGqvI 504
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK-DRD--I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEPVLFA-TSVEENIRYG------RPDATDEEVREAARAAHVDEFVSRFPSgystvvgergaQLSGGQKQRIAIAR 577
Cdd:cd03301 75 AMVFQNYALYPhMTVYDNIAFGlklrkvPKDEIDERVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGR 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 115533592 578 AILKNPPILILDEATSALDSHSEHMVQEALNNVMK--GRTVLIIAH 621
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTH 189
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
96-393 |
2.05e-30 |
|
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: 121.40 E-value: 2.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 96 GWFFAAVVCAILSAYINIQIPLCLGDLVNGIVkiikdESNNLRshfEQLKPSALhLMTLYVAQSALTFLYITFLTVLGER 175
Cdd:cd18549 2 KLFFLDLFCAVLIAALDLVFPLIVRYIIDDLL-----PSKNLR---LILIIGAI-LLALYILRTLLNYFVTYWGHVMGAR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 176 MATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQE------------FKSSFKLcvsqglrtfaqtIGCIGSLYFL 243
Cdd:cd18549 73 IETDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDiselahhgpedlFISIITI------------IGSFIILLTI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 244 SPTMTMYTVAVVPGIILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFDNELDKARAMQEQ 323
Cdd:cd18549 141 NVPLTLIVFALLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKK 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 324 LGVGIGLFQAGTNLFLNGMILSVLYGGSNLISKGEMTPGALMSFLVSAQTIQRSLSQLSIIFGTAIKGWT 393
Cdd:cd18549 221 AYKAMAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQKGMA 290
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
425-598 |
2.97e-30 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 122.18 E-value: 2.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRpghTVFENLTLSIPAGQVVALCGPSGEGKSTITHL---LERfyePKSGRVTLDGRDL------RELN 495
Cdd:COG1118 3 IEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIiagLET---PDSGRIVLNGRDLftnlppRERR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 496 VewlrgqviGLISQEPVLFA-TSVEENIRYG---RP---DATDEEVREAARAAHVDEFVSRFPSgystvvgergaQLSGG 568
Cdd:COG1118 77 V--------GFVFQHYALFPhMTVAENIAFGlrvRPpskAEIRARVEELLELVQLEGLADRYPS-----------QLSGG 137
|
170 180 190
....*....|....*....|....*....|
gi 115533592 569 QKQRIAIARAILKNPPILILDEATSALDSH 598
Cdd:COG1118 138 QRQRVALARALAVEPEVLLLDEPFGALDAK 167
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
98-369 |
3.49e-30 |
|
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: 120.49 E-value: 3.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 98 FFAAVVCAILSAYIniqiPLCLGDLVNGIVkIIKDesnnlrshFEQLKPSALHLMTLYVAQSALTFLYITFLTVLGERMA 177
Cdd:cd18784 2 FFFLLAAAVGEIFI----PYYTGQVIDGIV-IEKS--------QDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLN 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 178 TKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFKLCVSQGLRTFAQTIGCIGSLYFLSPTMTMYTVAVVPG 257
Cdd:cd18784 69 IRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 258 IILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFDNELDKARAMQEQLGVGIGLFQAGTNL 337
Cdd:cd18784 149 IAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNEL 228
|
250 260 270
....*....|....*....|....*....|..
gi 115533592 338 FLNGMILSVLYGGSNLISKGEMTPGALMSFLV 369
Cdd:cd18784 229 TELALTVSTLYYGGHLVITGQISGGNLISFIL 260
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
87-622 |
6.31e-30 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 124.92 E-value: 6.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 87 LWNLIKPFF---------GWFFAAVVCAILSAYINIQIPLCLGDLVNGIVKiiKDEsnnlrshfeqlkPSALHLMTLY-- 155
Cdd:COG4178 7 FWRLARPYWrseekwkawGLLALLLLLTLASVGLNVLLNFWNRDFYDALQA--RDA------------AAFWQQLGVFal 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 156 -VAQSALTFLYITFLT-VLGERMATKMRSDLFQKLLHHDMAFFDSHKSGELS---ARLNADVQEF-KSSFKLCVSqGLRT 229
Cdd:COG4178 73 lAAISILLAVYQTYLRqRLQIRWREWLTERLLDRWLSNRAYYRLQLSGGEIDnpdQRIAEDIRLFtETTLSLSLG-LLSS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 230 FAQTIGCIGSLYFLSPTMTM-----------YTVAVVPGIILAGSA---------IGAGLRQLSR----RAqgqsatasa 285
Cdd:COG4178 152 VVTLISFIGILWSLSGSLTFtlggysitipgYMVWAALIYAIIGTLlthligrplIRLNFEQQRReadfRF--------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 286 vsdeALTNIR----TIrAFAM-EKLESRLFDNELDKARAMQEQL---GVGIGLFQAGTNLFlnGMILSVLYGGSNLISkG 357
Cdd:COG4178 223 ----ALVRVRenaeSI-ALYRgEAAERRRLRRRFDAVIANWRRLirrQRNLTFFTTGYGQL--AVIFPILVAAPRYFA-G 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 358 EMTPGALMSfLVSA-QTIQRSLSQLSIIFGTaIKGWTAG-GRVLQFSR-LEPSIPMDTGVCIPYHSLWGDIKFEDVSFSY 434
Cdd:COG4178 295 EITLGGLMQ-AASAfGQVQGALSWFVDNYQS-LAEWRATvDRLAGFEEaLEAADALPEAASRIETSEDGALALEDLTLRT 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 435 PTrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTithLLeR-------FYepkSGRVTLDgrdlrelnvewlRGQVIGLI 507
Cdd:COG4178 373 PD--GRPLLEDLSLSLKPGERLLITGPSGSGKST---LL-RaiaglwpYG---SGRIARP------------AGARVLFL 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 508 SQEPVLFATSVEENIRYGRP--DATDEEVREAARAAHVDEFVSRFpsgysTVVGERGAQLSGGQKQRIAIARAILKNPPI 585
Cdd:COG4178 432 PQRPYLPLGTLREALLYPATaeAFSDAELREALEAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDW 506
|
570 580 590
....*....|....*....|....*....|....*..
gi 115533592 586 LILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHR 622
Cdd:COG4178 507 LFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
425-621 |
9.14e-30 |
|
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: 117.12 E-value: 9.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPtrPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELN---VEWLRg 501
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 502 QVIGLISQEPVLFAT-SVEENIRYGRpDATDEEVREAA-RAAHVDEFVsrfpsGYSTVVGERGAQLSGGQKQRIAIARAI 579
Cdd:cd03292 78 RKIGVVFQDFRLLPDrNVYENVAFAL-EVTGVPPREIRkRVPAALELV-----GLSHKHRALPAELSGGEQQRVAIARAI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 115533592 580 LKNPPILILDEATSALDSHSEHMVQEALNNVMK-GRTVLIIAH 621
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINKaGTTVVVATH 194
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
436-596 |
2.88e-29 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 115.66 E-value: 2.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 436 TRPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPK---SGRVTLDGRDLRELNVEwLRGqvIGLISQEPV 512
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE-QRR--IGILFQDDL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 513 LFA-TSVEENIRYGRPDATDEEVREAARAAHVDE-----FVSRFPsgystvvgergAQLSGGQKQRIAIARAILKNPPIL 586
Cdd:COG4136 87 LFPhLSVGENLAFALPPTIGRAQRRARVEQALEEaglagFADRDP-----------ATLSGGQRARVALLRALLAEPRAL 155
|
170
....*....|
gi 115533592 587 ILDEATSALD 596
Cdd:COG4136 156 LLDEPFSKLD 165
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
425-645 |
3.10e-29 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 119.14 E-value: 3.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPT-RPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRG-- 501
Cdd:PRK11153 2 IELKNISKVFPQgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 502 QVIGLISQEPVLFAT-SVEENIRY-----GRPDAtdeEVReaARAAHVDEFV------SRFPsgystvvgergAQLSGGQ 569
Cdd:PRK11153 82 RQIGMIFQHFNLLSSrTVFDNVALplelaGTPKA---EIK--ARVTELLELVglsdkaDRYP-----------AQLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115533592 570 KQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMK--GRTVLIIAHRLSTIRS-AQMIYVIKDKKALESGT 645
Cdd:PRK11153 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
98-387 |
5.73e-29 |
|
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: 117.12 E-value: 5.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 98 FFAAVVCAILSAYINIQIPLCLGDLVNgivKIIKDESNNLRSHFEQLKPSALHLMTLYVAQSALTFLYITFLTVLGERMA 177
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAID---LIIEGLGGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 178 TKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFKLCVSQGLRTFAQTIGCIGSLYFLSPTMTMYTVAVVPG 257
Cdd:cd18547 78 YDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 258 IILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFD---NELDKA--RAMqeqlgvgiglFQ 332
Cdd:cd18547 158 SLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDeinEELYKAsfKAQ----------FY 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115533592 333 AGT----NLFLN--GMILSVLYGGSnLISKGEMTPGALMSFLVSAQTIQRSLSQLSIIFGT 387
Cdd:cd18547 228 SGLlmpiMNFINnlGYVLVAVVGGL-LVINGALTVGVIQAFLQYSRQFSQPINQISQQINS 287
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
86-590 |
1.60e-28 |
|
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: 120.29 E-value: 1.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 86 ELWNLIKPFFGWFFAAVVCAILSAYINIqiplclgdlvnGIVKIIKDESNNLRSHFEQLKPSALHLMTLYVAQSALTFLY 165
Cdd:COG4615 3 LLRLLLRESRWLLLLALLLGLLSGLANA-----------GLIALINQALNATGAALARLLLLFAGLLVLLLLSRLASQLL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 166 itfLTVLGERMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFKLcVSQGLRTFAQTIGCIGSLYFLSP 245
Cdd:COG4615 72 ---LTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVR-LPELLQSVALVLGCLAYLAWLSP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 246 TMTMYTVAVvpgiILAGSAIGaglRQLSRRAQGQSATASAVSDEALTNIRTIRAFAME-KLESR----LFDNEL-DKARA 319
Cdd:COG4615 148 PLFLLTLVL----LGLGVAGY---RLLVRRARRHLRRAREAEDRLFKHFRALLEGFKElKLNRRrrraFFDEDLqPTAER 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 320 MQEQLGVGIGLF---QAGTNLFLNGMILSVLYGGSNL--ISKGEMTPGAL-MSFLVSAqtiqrsLSQLSIIFGTAIKGWT 393
Cdd:COG4615 221 YRDLRIRADTIFalaNNWGNLLFFALIGLILFLLPALgwADPAVLSGFVLvLLFLRGP------LSQLVGALPTLSRANV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 394 AGGRV----LQFSRLEPSIPMDTGvcIPYHSLWGDIKFEDVSFSYPTRPGHTVFE--NLTLSIPAGQVVALCGPSGEGKS 467
Cdd:COG4615 295 ALRKIeeleLALAAAEPAAADAAA--PPAPADFQTLELRGVTYRYPGEDGDEGFTlgPIDLTIRRGELVFIVGGNGSGKS 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 468 TITHLLERFYEPKSGRVTLDGRDLRELNVEWLRgQVIGLISQEPVLFatsvEENirYGRPD-ATDEEVREAARAAHVDEF 546
Cdd:COG4615 373 TLAKLLTGLYRPESGEILLDGQPVTADNREAYR-QLFSAVFSDFHLF----DRL--LGLDGeADPARARELLERLELDHK 445
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 115533592 547 VS----RFpsgySTVvgergaQLSGGQKQRIAIARAILKNPPILILDE 590
Cdd:COG4615 446 VSvedgRF----STT------DLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
428-650 |
1.95e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 114.48 E-value: 1.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 428 EDVSFSyptRPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVeWLRGQVIGLI 507
Cdd:PRK13548 6 RNLSVR---LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSP-AELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 508 SQEPVL-FATSVEENIRYGR------PDATDEEVREAARAAHVDEFVSRFpsgYstvvgergAQLSGGQKQRIAIARAIL 580
Cdd:PRK13548 82 PQHSSLsFPFTVEEVVAMGRaphglsRAEDDALVAAALAQVDLAHLAGRD---Y--------PQLSGGEQQRVQLARVLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115533592 581 ------KNPPILILDEATSALD-SHSEHMVQEALNNVMK-GRTVLIIAHRLS-TIRSAQMIYVIKDKKALESGTHEQLM 650
Cdd:PRK13548 151 qlwepdGPPRWLLLDEPTSALDlAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
445-652 |
2.05e-28 |
|
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: 114.66 E-value: 2.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 445 NLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWL---RGQVIGLISQEPVLFA-TSVEE 520
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelRRKKISMVFQSFALLPhRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 521 NIRYGRPDA-TDEEVREAaRAAHVDEFVSRFPSGYSTVvgergAQLSGGQKQRIAIARAILKNPPILILDEATSALDSHS 599
Cdd:cd03294 122 NVAFGLEVQgVPRAEREE-RAAEALELVGLEGWEHKYP-----DELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLI 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 115533592 600 EHMVQEALNNVMK--GRTVLIIAHRLS-TIRSAQMIYVIKDKKALESGTHEQLMAK 652
Cdd:cd03294 196 RREMQDELLRLQAelQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
425-644 |
2.43e-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: 113.06 E-value: 2.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRpghTVFENLTLSIPAGqVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRElNVEWLRgQVI 504
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLR-RRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEPVLFAT-SVEENIRY-----GRPDAT-DEEVREAARAAHVDEFVSRFPSgystvvgergaQLSGGQKQRIAIAR 577
Cdd:cd03264 75 GYLPQEFGVYPNfTVREFLDYiawlkGIPSKEvKARVDEVLELVNLGDRAKKKIG-----------SLSGGMRRRVGIAQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115533592 578 AILKNPPILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRLSTIRS-AQMIYVIKDKKALESG 644
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
425-596 |
3.37e-28 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 116.97 E-value: 3.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPtrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEwlrgqvi 504
Cdd:PRK09452 15 VELRGISKSFD---GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 glisQEPV--------LFA-TSVEENIRYG-----RPDA-TDEEVREAARAAHVDEFVSRFPsgystvvgergAQLSGGQ 569
Cdd:PRK09452 85 ----NRHVntvfqsyaLFPhMTVFENVAFGlrmqkTPAAeITPRVMEALRMVQLEEFAQRKP-----------HQLSGGQ 149
|
170 180
....*....|....*....|....*..
gi 115533592 570 KQRIAIARAILKNPPILILDEATSALD 596
Cdd:PRK09452 150 QQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
438-637 |
3.97e-28 |
|
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: 112.42 E-value: 3.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 438 PGHTVFENLTLSIPAGQVVALCGPSGEGKSTIthLLERFYEPK--SGRVTLDGRDLRELNVEWLRGQ---VIGLISQEPV 512
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSL--LLAILGEMQtlEGKVHWSNKNESEPSFEATRSRnrySVAYAAQKPW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 513 LFATSVEENIRYGRPdATDEEVREAARAAHVDEFVSRFPSGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILILDEAT 592
Cdd:cd03290 90 LLNATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 115533592 593 SALDSH-SEHMVQEALNNVMKG--RTVLIIAHRLSTIRSAQMIYVIKD 637
Cdd:cd03290 169 SALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKD 216
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
424-650 |
5.37e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 113.19 E-value: 5.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 424 DIKFEDVSFSYPTRpghTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQV 503
Cdd:PRK11231 2 TLRTENLTVGYGTK---RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 504 IGLISQEPVLFATSVEENIRYGRP---------DATDEE-VREAARAAHVDEFVSRfpsgystvvgeRGAQLSGGQKQRI 573
Cdd:PRK11231 79 ALLPQHHLTPEGITVRELVAYGRSpwlslwgrlSAEDNArVNQAMEQTRINHLADR-----------RLTDLSGGQRQRA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 574 AIARAILKNPPILILDEATSALD-SHsehmvQEALNNVM-----KGRTVLIIAHRLS-TIRSAQMIYVIKDKKALESGTH 646
Cdd:PRK11231 148 FLAMVLAQDTPVVLLDEPTTYLDiNH-----QVELMRLMrelntQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTP 222
|
....
gi 115533592 647 EQLM 650
Cdd:PRK11231 223 EEVM 226
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
148-398 |
8.68e-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: 350008 [Multi-domain] Cd Length: 307 Bit Score: 114.15 E-value: 8.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 148 ALHLMTLYVAQSALTFLYITFLTVLGERMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSsfkLCVSQGL 227
Cdd:cd18564 57 AAALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQD---LLVSGVL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 228 RTFAQT---IGCIGSLYFLSPTMTMYTVAVVPGIILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEK 304
Cdd:cd18564 134 PLLTNLltlVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 305 LESRLFDNE----LD---KARAMQEQLGVGIGLFQA-GTnlflngmiLSVLYGGSNLISKGEMTPGALMSFLVSAQTIQR 376
Cdd:cd18564 214 HEERRFAREnrksLRaglRAARLQALLSPVVDVLVAvGT--------ALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYK 285
|
250 260
....*....|....*....|..
gi 115533592 377 SLSQLSIIFGTAIKGWTAGGRV 398
Cdd:cd18564 286 PVRDLAKLTGRIAKASASAERV 307
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
442-651 |
2.18e-27 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 110.60 E-value: 2.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 442 VFENLTLSIPAGQVVALCGPSGEGKST----ITHLLErfyePKSGRVTLDGRDLRELNVEWL--RGqvIGLISQEPVLFA 515
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTllktIMGLLP----PRSGSIRFDGRDITGLPPHERarAG--IGYVPEGRRIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 516 T-SVEENIRYGRPDATDEEVREAaraahVDEFVSRFPsgystVVGER----GAQLSGGQKQRIAIARAILKNPPILILDE 590
Cdd:cd03224 89 ElTVEENLLLGAYARRRAKRKAR-----LERVYELFP-----RLKERrkqlAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115533592 591 ATSALdshSEHMVQEALNNVMK----GRTVLIIAHRLSTIRS-AQMIYVIKDKKALESGTHEQLMA 651
Cdd:cd03224 159 PSEGL---APKIVEEIFEAIRElrdeGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
425-597 |
2.75e-27 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 110.89 E-value: 2.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPtrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVewlRGQVI 504
Cdd:cd03296 3 IEVRNVSKRFG---DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV---QERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEPVLFA-TSVEENIRYG--------RPDAT--DEEVREAARAAHVDEFVSRFPsgystvvgergAQLSGGQKQRI 573
Cdd:cd03296 77 GFVFQHYALFRhMTVFDNVAFGlrvkprseRPPEAeiRAKVHELLKLVQLDWLADRYP-----------AQLSGGQRQRV 145
|
170 180
....*....|....*....|....
gi 115533592 574 AIARAILKNPPILILDEATSALDS 597
Cdd:cd03296 146 ALARALAVEPKVLLLDEPFGALDA 169
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
429-645 |
5.84e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 110.94 E-value: 5.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 429 DVSFSYPTrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRG-QVIGLI 507
Cdd:PRK13639 6 DLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVrKTVGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 508 SQEP--VLFATSVEENIRYG------RPDATDEEVREAARAAHVDEFVSRFPSgystvvgergaQLSGGQKQRIAIARAI 579
Cdd:PRK13639 84 FQNPddQLFAPTVEEDVAFGplnlglSKEEVEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAGIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115533592 580 LKNPPILILDEATSALDSHSEHMVQEALNNVMK-GRTVLIIAHRLSTI-RSAQMIYVIKDKKALESGT 645
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKeGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGT 220
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
447-627 |
7.84e-27 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 111.75 E-value: 7.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 447 TLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRG--QVIGLISQEPvlFA--------- 515
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPlrRRMQMVFQDP--YAslnprmtvg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 516 TSVEENIRYGRpDATDEEVREAARA--AHVD---EFVSRFPSgystvvgergaQLSGGQKQRIAIARAILKNPPILILDE 590
Cdd:COG4608 116 DIIAEPLRIHG-LASKAERRERVAEllELVGlrpEHADRYPH-----------EFSGGQRQRIGIARALALNPKLIVCDE 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 115533592 591 ATSALD-ShsehmVQEALNNVMK------GRTVLIIAHRLSTIR 627
Cdd:COG4608 184 PVSALDvS-----IQAQVLNLLEdlqdelGLTYLFISHDLSVVR 222
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
438-637 |
9.05e-27 |
|
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: 108.54 E-value: 9.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 438 PGHTVfeNLTLSIPaGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRE------LNVEWLRgqvIGLISQEP 511
Cdd:cd03297 11 PDFTL--KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkinLPPQQRK---IGLVFQQY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 512 VLFA-TSVEENIRYGRPDATDEEVREAaraahVDEFVSRFpsGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILILDE 590
Cdd:cd03297 85 ALFPhLNVRENLAFGLKRKRNREDRIS-----VDELLDLL--GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 115533592 591 ATSALDSHSEHMVQEALNNVMK--GRTVLIIAHRLSTI-RSAQMIYVIKD 637
Cdd:cd03297 158 PFSALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMED 207
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
448-599 |
1.25e-26 |
|
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: 111.73 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 448 LSIPAGQVVALCGPSGEGKSTITHL---LERfyePKSGRVTLDGRDL----RELNVE-WLRGqvIGLISQEPVLFAT-SV 518
Cdd:COG4148 20 FTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEVLqdsaRGIFLPpHRRR--IGYVFQEARLFPHlSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 519 EENIRYGRPDAtdeevREAARAAHVDEFV---------SRFPsgystvvgergAQLSGGQKQRIAIARAILKNPPILILD 589
Cdd:COG4148 95 RGNLLYGRKRA-----PRAERRISFDEVVellgighllDRRP-----------ATLSGGERQRVAIGRALLSSPRLLLMD 158
|
170
....*....|
gi 115533592 590 EATSALDSHS 599
Cdd:COG4148 159 EPLAALDLAR 168
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
98-398 |
1.28e-26 |
|
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: 110.26 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 98 FFAAVVCAILSAYINIQIPLCLGDLVNGIVKIikdesnnlrSHFEQLKPSALHLMTLYVAQSALTFLYITFLTVLGERMA 177
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGPIAH---------GDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 178 TKMRSDLFQKLLHHDMAFFDSHKSGELSARLNAD---VQEFkssfklcVSQGLRTFAQT---IGCIGSLYFLSPTMTMYT 251
Cdd:cd18543 72 HDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDlslVQRF-------LAFGPFLLGNLltlVVGLVVMLVLSPPLALVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 252 VAVVPGIILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLES--------RLFDNELDKARAMqeq 323
Cdd:cd18543 145 LASLPPLVLVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELdrfeaaarRLRATRLRAARLR--- 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115533592 324 lgvgiGLFQAGTNLFLNGMILSVLYGGSNLISKGEMTPGALMSFLVSAQTIQRSLSQLSIIFGTAIKGWTAGGRV 398
Cdd:cd18543 222 -----ARFWPLLEALPELGLAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
425-637 |
1.44e-26 |
|
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: 106.36 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPtrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRdlrelnvewlrgqvi 504
Cdd:cd03216 1 LELRGITKRFG---GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK--------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 glisqePVLFATsveenirygrpdatdeeVREAARAahvdefvsrfpsGYSTVvgergAQLSGGQKQRIAIARAILKNPP 584
Cdd:cd03216 63 ------EVSFAS-----------------PRDARRA------------GIAMV-----YQLSVGERQMVEIARALARNAR 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 115533592 585 ILILDEATSALDSHSehmvQEALNNVMK-----GRTVLIIAHRLSTIRS-AQMIYVIKD 637
Cdd:cd03216 103 LLILDEPTAALTPAE----VERLFKVIRrlraqGVAVIFISHRLDEVFEiADRVTVLRD 157
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
425-656 |
4.02e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 108.67 E-value: 4.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVeWLRGQVI 504
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENV-WDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEP--VLFATSVEENIRYGRP------DATDEEVREAARAAHVDEFVSRFPsgystvvgergAQLSGGQKQRIAIA 576
Cdd:PRK13650 84 GMVFQNPdnQFVGATVEDDVAFGLEnkgiphEEMKERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 577 RAILKNPPILILDEATSALDSHSEhmvQEALNNVMKGR-----TVLIIAHRLSTIRSAQMIYVIKDKKALESGTHEQLMA 651
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGR---LELIKTIKGIRddyqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229
|
....*
gi 115533592 652 KKGSL 656
Cdd:PRK13650 230 RGNDL 234
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
425-637 |
5.70e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 112.03 E-value: 5.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPtrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQVI 504
Cdd:COG1129 5 LEMRGISKSFG---GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEPVLFAT-SVEENIRYGRPDAT-----DEEVREAARAA------HVDefvsrfPSgysTVVGErgaqLSGGQKQR 572
Cdd:COG1129 82 AIIHQELNLVPNlSVAENIFLGREPRRgglidWRAMRRRARELlarlglDID------PD---TPVGD----LSVAQQQL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115533592 573 IAIARAILKNPPILILDEATSALdSHSEhmvQEALNNVM-----KGRTVLIIAHRLSTIRS-AQMIYVIKD 637
Cdd:COG1129 149 VEIARALSRDARVLILDEPTASL-TERE---VERLFRIIrrlkaQGVAIIYISHRLDEVFEiADRVTVLRD 215
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
98-368 |
6.35e-26 |
|
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: 108.39 E-value: 6.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 98 FFAAVVCAILSAYINIQIPLclgdLVNGIVKIIKDESNNLrshfEQLKPSALHLMTLYVAQSALTFLYITFLTVLGERMA 177
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPW----LIRELVDLVTIGSKSL----GLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 178 TKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFKLCVSQGLRTFAQTIGCIGSLYFLSPTMTMYTVAVVPG 257
Cdd:cd18778 73 ADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 258 IILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFDNELDKARAMQEQLGVGIGLFQAGTNL 337
Cdd:cd18778 153 LALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEF 232
|
250 260 270
....*....|....*....|....*....|..
gi 115533592 338 FLN-GMILSVLYGGsNLISKGEMTPGALMSFL 368
Cdd:cd18778 233 LTSlGTVLVLGFGG-RLVLAGELTIGDLVAFL 263
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
425-607 |
6.57e-26 |
|
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: 106.36 E-value: 6.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPGH-TVFENLTLSIPAGQVVALCGPSGEGKSTITHL---LERfyePKSGRVTLDGRDLRELNVEW-- 498
Cdd:COG4181 9 IELRGLTKTVGTGAGElTILKGISLEVEAGESVAIVGASGSGKSTLLGLlagLDR---PTSGTVRLAGQDLFALDEDAra 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 499 -LRGQVIGLISQEPVLFAT-SVEENI-----RYGRPDATD------EEVREAARAAHvdefvsrFPsgystvvgergAQL 565
Cdd:COG4181 86 rLRARHVGFVFQSFQLLPTlTALENVmlpleLAGRRDARArarallERVGLGHRLDH-------YP-----------AQL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 115533592 566 SGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEAL 607
Cdd:COG4181 148 SGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLL 189
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
446-653 |
8.48e-26 |
|
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: 109.43 E-value: 8.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 446 LTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRE------LNVEWLRgqvIGLISQEPVLFA-TSV 518
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKRR---IGYVFQEARLFPhLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 519 EENIRYGRPDATDEEVReaARAAHVDEFVsrfpsGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILILDEATSALDSH 598
Cdd:TIGR02142 93 RGNLRYGMKRARPSERR--ISFERVIELL-----GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 115533592 599 SEHMVQEALNNVMK--GRTVLIIAHRLSTI-RSAQMIYVIKDKKALESGTHEQLMAKK 653
Cdd:TIGR02142 166 RKYEILPYLERLHAefGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
428-663 |
9.38e-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: 111.70 E-value: 9.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 428 EDVSFSYPTRPG---HTVFE-----NLTLSIPAGQVVALCGPSGEGKSTITHLLERFyEPKSGRVTLDGRDLRELNVEWL 499
Cdd:COG4172 279 RDLKVWFPIKRGlfrRTVGHvkavdGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRAL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 500 RG-----QVIgliSQEPvlFAT-----SVEENIRYG----RPDATDEEVREAARAAHVD-----EFVSRFPsgystvvge 560
Cdd:COG4172 358 RPlrrrmQVV---FQDP--FGSlsprmTVGQIIAEGlrvhGPGLSAAERRARVAEALEEvgldpAARHRYP--------- 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 561 rgAQLSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMK--GRTVLIIAHRLSTIRS-AQMIYVIKD 637
Cdd:COG4172 424 --HEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQRehGLAYLFISHDLAVVRAlAHRVMVMKD 501
|
250 260
....*....|....*....|....*..
gi 115533592 638 KKALESGTHEQLMAKKGSLY-RKLVEA 663
Cdd:COG4172 502 GKVVEQGPTEQVFDAPQHPYtRALLAA 528
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
425-644 |
1.07e-25 |
|
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: 105.38 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRpghTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWlrgQVI 504
Cdd:cd03268 1 LKTNDLTKTYGKK---RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL---RRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEPVLFAT-SVEENIRYGR--PDATDEEVREAARAAHVDEFVSRFPSGYSTvvgergaqlsgGQKQRIAIARAILK 581
Cdd:cd03268 75 GALIEAPGFYPNlTARENLRLLArlLGIRKKRIDEVLDVVGLKDSAKKKVKGFSL-----------GMKQRLGIALALLG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115533592 582 NPPILILDEATSALDSHSEHMVQEALNNVMK-GRTVLIIAHRLSTI-RSAQMIYVIKDKKALESG 644
Cdd:cd03268 144 NPDLLILDEPTNGLDPDGIKELRELILSLRDqGITVLISSHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
439-651 |
2.57e-25 |
|
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: 104.83 E-value: 2.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 439 GHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQVIGLISQEPVLFAT-S 517
Cdd:cd03219 12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRTFQIPRLFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 518 VEENIRYGRPDAT----------DEEVREAARAAHVDEFVsrfpsGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILI 587
Cdd:cd03219 92 VLENVMVAAQARTgsglllararREEREARERAEELLERV-----GLADLADRPAGELSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115533592 588 LDEATSAL-DSHSEHMVQ--EALNNvmKGRTVLIIAHRLSTIRS-AQMIYVIKDKKALESGTHEQLMA 651
Cdd:cd03219 167 LDEPAAGLnPEETEELAEliRELRE--RGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
425-621 |
3.04e-25 |
|
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: 104.12 E-value: 3.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPGHTVfENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEwlRGQVI 504
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAV-DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA--ARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEPVLFAT-SVEENIRY-----GRPDATDEEVREAAR-----AAHVDEFVSrfpsgystvvgergaQLSGGQKQRI 573
Cdd:cd03263 78 GYCPQFDALFDElTVREHLRFyarlkGLPKSEIKEEVELLLrvlglTDKANKRAR---------------TLSGGMKRKL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 115533592 574 AIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAH 621
Cdd:cd03263 143 SLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTH 190
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
428-638 |
3.75e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 104.03 E-value: 3.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 428 EDVSFSYPTRPghtVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQViGLI 507
Cdd:PRK10247 11 QNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQV-SYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 508 SQEPVLFATSVEEN------IRYGRPDatdeevrEAARAAHVDEFvsRFPSgysTVVGERGAQLSGGQKQRIAIARAILK 581
Cdd:PRK10247 87 AQTPTLFGDTVYDNlifpwqIRNQQPD-------PAIFLDDLERF--ALPD---TILTKNIAELSGGEKQRISLIRNLQF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 115533592 582 NPPILILDEATSALDSHSEHMVQEalnnvmkgrtvliIAHRLSTIRSAQMIYVIKDK 638
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNE-------------IIHRYVREQNIAVLWVTHDK 198
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
427-625 |
3.89e-25 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 103.01 E-value: 3.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 427 FEDVSFSYPTRPGH---TVFENLTLSIPAGQVVALCGPSGEGKSTITHLL--ERFYEPKSGRVTLDGRDLRElnvEWLRG 501
Cdd:cd03213 6 FRNLTVTVKSSPSKsgkQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDK---RSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 502 QvIGLISQEPVLFAT-SVEENIRYgrpdatdeevreaarAAHVdefvsrfpsgystvvgeRGaqLSGGQKQRIAIARAIL 580
Cdd:cd03213 83 I-IGYVPQDDILHPTlTVRETLMF---------------AAKL-----------------RG--LSGGERKRVSIALELV 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 115533592 581 KNPPILILDEATSALDSHSEHMVQEALNNVMK-GRTVLIIAHRLST 625
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPSS 173
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
425-651 |
4.16e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 104.28 E-value: 4.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPGHtvfenLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNvewlrgqvi 504
Cdd:PRK10771 2 LKLTDITWLYHHLPMR-----FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTP--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 glISQEPV--------LFA-TSVEENIRYG-RP-----DATDEEVREAARAAHVDEFVSRFPSgystvvgergaQLSGGQ 569
Cdd:PRK10771 68 --PSRRPVsmlfqennLFShLTVAQNIGLGlNPglklnAAQREKLHAIARQMGIEDLLARLPG-----------QLSGGQ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 570 KQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMKGR--TVLIIAHRLS-TIRSAQMIYVIKDKKALESGTH 646
Cdd:PRK10771 135 RQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPT 214
|
....*
gi 115533592 647 EQLMA 651
Cdd:PRK10771 215 DELLS 219
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
446-656 |
4.18e-25 |
|
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: 111.58 E-value: 4.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 446 LTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRdlrelnvewlrgqvIGLISQEPVLFATSVEENIRYG 525
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------------VAYVPQQAWIQNDSLRENILFG 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 526 RPdATDEEVREAARAAHVDEFVSRFPSGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILILDEATSALDSH-SEHMVQ 604
Cdd:TIGR00957 723 KA-LNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFE 801
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 115533592 605 EALN--NVMKGRTVLIIAHRLSTIRSAQMIYVIKDKKALESGTHEQLMAKKGSL 656
Cdd:TIGR00957 802 HVIGpeGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
425-626 |
4.50e-25 |
|
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: 104.78 E-value: 4.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSyptRPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSG-RVTLDGRDLRELNVEWLRGQv 503
Cdd:COG1119 4 LELRNVTVR---RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 504 IGLIS---QEPVLFATSVEENI---------RYGRPDATDEE-VREAARAAHVDEFVSRfpsgystvvgeRGAQLSGGQK 570
Cdd:COG1119 80 IGLVSpalQLRFPRDETVLDVVlsgffdsigLYREPTDEQRErARELLELLGLAHLADR-----------PFGTLSQGEQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 115533592 571 QRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMK--GRTVLIIAHRLSTI 626
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAegAPTLVLVTHHVEEI 206
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
425-621 |
5.03e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 104.94 E-value: 5.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYP-TRPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEwlRGQV 503
Cdd:COG4525 4 LTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD--RGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 504 IglisQEPVLFA-TSVEENIRYGRPDATdeeVREAARAAHVDEFVSRfpsgystvVGERGA------QLSGGQKQRIAIA 576
Cdd:COG4525 82 F----QKDALLPwLNVLDNVAFGLRLRG---VPKAERRARAEELLAL--------VGLADFarrriwQLSGGMRQRVGIA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 115533592 577 RAILKNPPILILDEATSALDSHSEHMVQEALNNVMK--GRTVLIIAH 621
Cdd:COG4525 147 RALAADPRFLLMDEPFGALDALTREQMQELLLDVWQrtGKGVFLITH 193
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
98-398 |
6.21e-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: 105.17 E-value: 6.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 98 FFAAVVCAILSAYINIQIPLCLGDLVN-GIVKiikdesnnlrSHFEQLKPSALHLMTLYVAQSALTFLYITFLTVLGERM 176
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDeGIAN----------GDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 177 ATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFKLCVSQGLRTFAQTIGCIGSLYFLSPTMTMYTVAVVP 256
Cdd:cd18548 71 GRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 257 GIILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFDNELDKARAMQEQLGVGIGLFQAGTN 336
Cdd:cd18548 151 ILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMM 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115533592 337 LFLNGMILSVLYGGSNLISKGEMTPGALMSFLVSAQTIQRSLSQLSIIFGTAIKGWTAGGRV 398
Cdd:cd18548 231 LIMNLAIVAILWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKRI 292
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
425-650 |
8.15e-25 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 103.63 E-value: 8.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYptrpGHT-VFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNV-EWLRGQ 502
Cdd:PRK09493 2 IEFKNVSKHF----GPTqVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVdERLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 503 VIGLISQEPVLFA--TSVEeNIRYGrP----DATDEEVREAARA--AHV--DEFVSRFPSgystvvgergaQLSGGQKQR 572
Cdd:PRK09493 78 EAGMVFQQFYLFPhlTALE-NVMFG-PlrvrGASKEEAEKQAREllAKVglAERAHHYPS-----------ELSGGQQQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 573 IAIARAILKNPPILILDEATSALDSHSEHmvqEALnNVMK-----GRTVLIIAHRLSTIR--SAQMIYVIKDKKAlESGT 645
Cdd:PRK09493 145 VAIARALAVKPKLMLFDEPTSALDPELRH---EVL-KVMQdlaeeGMTMVIVTHEIGFAEkvASRLIFIDKGRIA-EDGD 219
|
....*
gi 115533592 646 HEQLM 650
Cdd:PRK09493 220 PQVLI 224
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
98-368 |
1.92e-24 |
|
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: 104.13 E-value: 1.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 98 FFAAVVCAILSAYINIQIPLCLGDLVNGIVKiikdeSNNLRSHFEQLKPSALHLMTLYVAQSALTFLYITFLTVLGERMA 177
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDVLI-----QLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERIT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 178 TKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFKLCVSQGLRTFAQTIGCIGSLYFLSPTMTMYTVAVVPG 257
Cdd:cd18563 76 ADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 258 IILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFDNELDKARAMQEQLGVGIGLFQAGTNL 337
Cdd:cd18563 156 VVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTF 235
|
250 260 270
....*....|....*....|....*....|.
gi 115533592 338 FLNGMILSVLYGGSNLISKGEMTPGALMSFL 368
Cdd:cd18563 236 LTSLGTLIVWYFGGRQVLSGTMTLGTLVAFL 266
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
428-621 |
2.83e-24 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 102.47 E-value: 2.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 428 EDVSFSYPTRPghtVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEwlRGQVIgli 507
Cdd:PRK11248 5 SHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE--RGVVF--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 508 SQEPVLFATSVEENIRYGRPDA--TDEEVREAARA--AHVD--EFVSRFPsgystvvgergAQLSGGQKQRIAIARAILK 581
Cdd:PRK11248 77 QNEGLLPWRNVQDNVAFGLQLAgvEKMQRLEIAHQmlKKVGleGAEKRYI-----------WQLSGGQRQRVGIARALAA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 115533592 582 NPPILILDEATSALDSHSEHMVQEALNNVMK--GRTVLIIAH 621
Cdd:PRK11248 146 NPQLLLLDEPFGALDAFTREQMQTLLLKLWQetGKQVLLITH 187
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
404-662 |
2.92e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 109.06 E-value: 2.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 404 LEPSIPMDTGvcIPyhslwgDIKFEDVSFSYPTRPGHTVFENLTLSIPAGQVVALCGPSGEGK-STITHLLERFYEPKSG 482
Cdd:PLN03130 602 LLPNPPLEPG--LP------AISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKtSLISAMLGELPPRSDA 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 483 RVTLdgrdlrelnvewlRGQViGLISQEPVLFATSVEENIRYGRP-DATDEEvrEAARAAHVDEFVSRFPSGYSTVVGER 561
Cdd:PLN03130 674 SVVI-------------RGTV-AYVPQVSWIFNATVRDNILFGSPfDPERYE--RAIDVTALQHDLDLLPGGDLTEIGER 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 562 GAQLSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMV-QEALNNVMKGRTVLIIAHRLSTIRSAQMIYVIKDKKA 640
Cdd:PLN03130 738 GVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVfDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMI 817
|
250 260
....*....|....*....|..
gi 115533592 641 LESGTHEQLMaKKGSLYRKLVE 662
Cdd:PLN03130 818 KEEGTYEELS-NNGPLFQKLME 838
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
425-651 |
3.07e-24 |
|
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: 101.85 E-value: 3.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRpghTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQVI 504
Cdd:cd03218 1 LRAENLSKRYGKR---KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEPVLFAT-SVEENIRygrpdATDE--EVREAARAAHVDEFVSRFpsGYSTVVGERGAQLSGGQKQRIAIARAILK 581
Cdd:cd03218 78 GYLPQEASIFRKlTVEENIL-----AVLEirGLSKKEREEKLEELLEEF--HITHLRKSKASSLSGGERRRVEIARALAT 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115533592 582 NPPILILDEATSALDSHSEHMVQEALNNVM-KGRTVLIIAHRLS-TIRSAQMIYVIKDKKALESGTHEQLMA 651
Cdd:cd03218 151 NPKFLLLDEPFAGVDPIAVQDIQKIIKILKdRGIGVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
98-376 |
5.18e-24 |
|
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: 102.85 E-value: 5.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 98 FFAAVVCAILSAYINIQIPLCLGDLV-NGIVKIIKDesnnlrshFEQLKPSALHLMTLYVAQSALTFLYITFLTVLGERM 176
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIdDYIVPGQGD--------LQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 177 ATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFklcvSQGLRTFAQ----TIGCIGSLYFLSPTMTMYTV 252
Cdd:cd18544 73 IYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELF----TSGLVTLIGdlllLIGILIAMFLLNWRLALISL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 253 AVVPgIILAGSAIgagLRQLSRRAqgQSATASAVSD------EALTNIRTIRAFAMEKLESRLFD---NELDKARAMQEQ 323
Cdd:cd18544 149 LVLP-LLLLATYL---FRKKSRKA--YREVREKLSRlnaflqESISGMSVIQLFNREKREFEEFDeinQEYRKANLKSIK 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 115533592 324 LGvgiGLFQAGTNLFLNGMILSVLYGGSNLISKGEMTPGALMSFLvsaQTIQR 376
Cdd:cd18544 223 LF---ALFRPLVELLSSLALALVLWYGGGQVLSGAVTLGVLYAFI---QYIQR 269
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
439-597 |
7.07e-24 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 103.62 E-value: 7.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 439 GHT-VFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVewlRGQVIGLISQEPVLFA-T 516
Cdd:PRK10851 13 GRTqVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA---RDRKVGFVFQHYALFRhM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 517 SVEENIRYG--------RPD--ATDEEVREAARAAHVDEFVSRFPSgystvvgergaQLSGGQKQRIAIARAILKNPPIL 586
Cdd:PRK10851 90 TVFDNIAFGltvlprreRPNaaAIKAKVTQLLEMVQLAHLADRYPA-----------QLSGGQKQRVALARALAVEPQIL 158
|
170
....*....|.
gi 115533592 587 ILDEATSALDS 597
Cdd:PRK10851 159 LLDEPFGALDA 169
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
425-626 |
8.97e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 101.27 E-value: 8.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRpghTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKS-----GRVTLDGRDL--RELNVE 497
Cdd:PRK14258 8 IKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 498 WLRGQViGLISQEPVLFATSVEENIRYG------RPDAT-DEEVREAARAAHV-DEFVSRfpsgystvVGERGAQLSGGQ 569
Cdd:PRK14258 85 RLRRQV-SMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEiDDIVESALKDADLwDEIKHK--------IHKSALDLSGGQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 115533592 570 KQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVM--KGRTVLIIAHRLSTI 626
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQV 214
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
439-635 |
1.01e-23 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 100.88 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 439 GHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEwlrgQVIGL-IS---QEPVLF 514
Cdd:COG0411 16 GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPH----RIARLgIArtfQNPRLF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 515 AT-SVEENIRYGR---------------PDATDEEVREAARAAHVDEFVsrfpsGYSTVVGERGAQLSGGQKQRIAIARA 578
Cdd:COG0411 92 PElTVLENVLVAAharlgrgllaallrlPRARREEREARERAEELLERV-----GLADRADEPAGNLSYGQQRRLEIARA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115533592 579 ILKNPPILILDEATSALDSH-SEHMVQ--EALNNVMkGRTVLIIAHRLSTIRS-AQMIYVI 635
Cdd:COG0411 167 LATEPKLLLLDEPAAGLNPEeTEELAEliRRLRDER-GITILLIEHDMDLVMGlADRIVVL 226
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
441-663 |
1.06e-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: 101.04 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 441 TVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRG-----QVIGLISQEPVLFA 515
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAfrrdvQLVFQDSPSAVNPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 516 TSVEENIRYGRPDATD-EEVREAARAAHVDEFVSRFPSgystVVGERGAQLSGGQKQRIAIARAILKNPPILILDEATSA 594
Cdd:TIGR02769 105 MTVRQIIGEPLRHLTSlDESEQKARIAELLDMVGLRSE----DADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSN 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115533592 595 LDSHSEHMVQEALNNVMK--GRTVLIIAHRLSTIRS-AQMIYVIKDKKALESGTHEQLMAKKGSLYRKLVEA 663
Cdd:TIGR02769 181 LDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLLSFKHPAGRNLQSA 252
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
425-623 |
1.09e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 101.01 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTrpgHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYE-----PKSGRVTLDGRDLRELNVE-- 497
Cdd:PRK14243 11 LRTENLNVYYGS---FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYAPDVDpv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 498 WLRGQvIGLISQEPVLFATSVEENIRYG-RPDA----TDEEVREAAR-AAHVDEFVSRfpsgystvVGERGAQLSGGQKQ 571
Cdd:PRK14243 88 EVRRR-IGMVFQKPNPFPKSIYDNIAYGaRINGykgdMDELVERSLRqAALWDEVKDK--------LKQSGLSLSGGQQQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 115533592 572 RIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRL 623
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
439-621 |
1.14e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 103.38 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 439 GHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNvEWLRGqvIGLISQEPVLFA-TS 517
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP-PYQRP--INMMFQSYALFPhMT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 518 VEENIRYG-RPD--ATDE---EVREAARAAHVDEFVSRFPSgystvvgergaQLSGGQKQRIAIARAILKNPPILILDEA 591
Cdd:PRK11607 108 VEQNIAFGlKQDklPKAEiasRVNEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190
....*....|....*....|....*....|..
gi 115533592 592 TSALDSHSEHMVQEALNNVMK--GRTVLIIAH 621
Cdd:PRK11607 177 MGALDKKLRDRMQLEVVDILErvGVTCVMVTH 208
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
428-637 |
1.17e-23 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 105.96 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 428 EDVSFSYPTRPGHT-VFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELN---VEWLRGQV 503
Cdd:PRK10535 8 KDIRRSYPSGEEQVeVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadaLAQLRREH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 504 IGLISQEPVLFA-TSVEENIRYgrpDATDEEVREAARAAHVDEFVSRFpsGYSTVVGERGAQLSGGQKQRIAIARAILKN 582
Cdd:PRK10535 88 FGFIFQRYHLLShLTAAQNVEV---PAVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 115533592 583 PPILILDEATSALDSHSEHMVQEALNNVM-KGRTVLIIAHRLSTIRSAQMIYVIKD 637
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRD 218
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
425-652 |
1.36e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 101.03 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPgHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKS---GRVTLDGRDLRELNVEWLRG 501
Cdd:PRK13640 6 VEFKHVSFTYPDSK-KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 502 QViGLISQEP--VLFATSVEENIRYGRpdatdeEVREAARAAHVdEFVSRFPS--GYSTVVGERGAQLSGGQKQRIAIAR 577
Cdd:PRK13640 85 KV-GIVFQNPdnQFVGATVGDDVAFGL------ENRAVPRPEMI-KIVRDVLAdvGMLDYIDSEPANLSGGQKQRVAIAG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115533592 578 AILKNPPILILDEATSALDSHSEHMVQEALNNVMK--GRTVLIIAHRLSTIRSAQMIYVIKDKKALESGTHEQLMAK 652
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
425-645 |
1.69e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 100.89 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYptRPGhTVFE-----NLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDL--RELNVE 497
Cdd:PRK13637 3 IKIENLTHIY--MEG-TPFEkkaldNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 498 WLRGQViGLISQEP--VLFATSVEENIRYG--RPDATDEE----VREAARAAHVDefvsrfpsgYSTVVGERGAQLSGGQ 569
Cdd:PRK13637 80 DIRKKV-GLVFQYPeyQLFEETIEKDIAFGpiNLGLSEEEienrVKRAMNIVGLD---------YEDYKDKSPFELSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115533592 570 KQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMK--GRTVLIIAHRLSTI-RSAQMIYVIKDKKALESGT 645
Cdd:PRK13637 150 KRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGT 228
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
423-656 |
2.07e-23 |
|
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: 100.31 E-value: 2.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 423 GDIKFEDVSFSYpTRPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKsGRVTLDGRDLRELNVEWLRgQ 502
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWR-K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 503 VIGLISQEPVLFATSVEENIR-YGRpdATDEEVREAARAAHVDEFVSRFPSGYSTVVGERGAQLSGGQKQRIAIARAILK 581
Cdd:cd03289 78 AFGVIPQKVFIFSGTFRKNLDpYGK--WSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115533592 582 NPPILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRLSTIRSAQMIYVIKDKKALESGTHEQLMAKKGSL 656
Cdd:cd03289 156 KAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
428-651 |
2.91e-23 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 98.90 E-value: 2.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 428 EDVSFSYPtrpGHTVFENLTLSIPAGQVVALCGPSGEGKST----ITHLLErfyePKSGRVTLDGRDLRELNVEWL--RG 501
Cdd:COG0410 7 ENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTllkaISGLLP----PRSGSIRFDGEDITGLPPHRIarLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 502 qvIGLISQEPVLFAT-SVEENIR---YGRPDAtdeevreAARAAHVDEFVSRFPsgystVVGER----GAQLSGGQKQRI 573
Cdd:COG0410 80 --IGYVPEGRRIFPSlTVEENLLlgaYARRDR-------AEVRADLERVYELFP-----RLKERrrqrAGTLSGGEQQML 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 574 AIARAILKNPPILILDEATSALdshSEHMVQE------ALNNvmKGRTVLIIAHRLSTIRS-AQMIYVIKDKKALESGTH 646
Cdd:COG0410 146 AIGRALMSRPKLLLLDEPSLGL---APLIVEEifeiirRLNR--EGVTILLVEQNARFALEiADRAYVLERGRIVLEGTA 220
|
....*
gi 115533592 647 EQLMA 651
Cdd:COG0410 221 AELLA 225
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
437-607 |
3.05e-23 |
|
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: 97.95 E-value: 3.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 437 RPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGqvIGLISQEPVLFAT 516
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARG--LLYLGHAPGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 517 -SVEENIRYGRPDATDEEVREAaraahVDEfvsrfpsgystvVGERG------AQLSGGQKQRIAIARAILKNPPILILD 589
Cdd:cd03231 88 lSVLENLRFWHADHSDEQVEEA-----LAR------------VGLNGfedrpvAQLSAGQQRRVALARLLLSGRPLWILD 150
|
170
....*....|....*...
gi 115533592 590 EATSALDSHSEHMVQEAL 607
Cdd:cd03231 151 EPTTALDKAGVARFAEAM 168
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
131-663 |
6.84e-23 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 104.61 E-value: 6.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 131 KDESNNLRSHFEQL-----KPSALHLMTLYVAQS----ALTF-----LYITFLTVlGERMATKMrsdlFQKLLHHDMAFF 196
Cdd:TIGR01271 902 DQQHANASSPDVQKpviitPTSAYYIFYIYVGTAdsvlALGFfrglpLVHTLLTV-SKRLHEQM----LHSVLQAPMAVL 976
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 197 DSHKSGELSARLNADVQEFKSSFKLCVSQGLRTFAQTIGCIGSLYFLSPTMTMYTVAVVPGIILAGSAIgagLRQLSRRA 276
Cdd:TIGR01271 977 NTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYF---LRTSQQLK 1053
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 277 QGQSATASAVSDEALTNIR---TIRAFAMEKLESRLFDNELDKARAMQEQLGVGIGLFQagtnlFLNGMILSVLYGGSNL 353
Cdd:TIGR01271 1054 QLESEARSPIFSHLITSLKglwTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQ-----MRIDIIFVFFFIAVTF 1128
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 354 ISKG--EMTPGALMSFLVSAQTIQRSLsQLSIIFGTAIKGWTAG-GRVLQFSRLEPSIPMDTGVCIPYH----------- 419
Cdd:TIGR01271 1129 IAIGtnQDGEGEVGIILTLAMNILSTL-QWAVNSSIDVDGLMRSvSRVFKFIDLPQEEPRPSGGGGKYQlstvlvienph 1207
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 420 --SLW---GDIKFEDVSFSYpTRPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKsGRVTLDGRDLREL 494
Cdd:TIGR01271 1208 aqKCWpsgGQMDVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSV 1285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 495 NVEWLRgQVIGLISQEPVLFATSVEENIR-YGRpdATDEEVREAARAAHVDEFVSRFPSGYSTVVGERGAQLSGGQKQRI 573
Cdd:TIGR01271 1286 TLQTWR-KAFGVIPQKVFIFSGTFRKNLDpYEQ--WSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLM 1362
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 574 AIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRLSTIRSAQMIYVIKDKKALESGTHEQLMAKK 653
Cdd:TIGR01271 1363 CLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNET 1442
|
570
....*....|
gi 115533592 654 gSLYRKLVEA 663
Cdd:TIGR01271 1443 -SLFKQAMSA 1451
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
425-640 |
9.72e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 97.92 E-value: 9.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRpghTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYE--PK---SGRVTLDGRDL---RELNV 496
Cdd:PRK14239 6 LQVSDLSVYYNKK---KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIyspRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 497 EwLRGQvIGLISQEPVLFATSVEENIRYG-------RPDATDEEVREAARAAHV-DEFVSRFpsgYSTVVGergaqLSGG 568
Cdd:PRK14239 83 D-LRKE-IGMVFQQPNPFPMSIYENVVYGlrlkgikDKQVLDEAVEKSLKGASIwDEVKDRL---HDSALG-----LSGG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115533592 569 QKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHrlstirSAQMIYVIKDKKA 640
Cdd:PRK14239 153 QQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTR------SMQQASRISDRTG 218
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
425-656 |
9.93e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 98.28 E-value: 9.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPGHTVfENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRgQVI 504
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTL-KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLR-KHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEP--VLFATSVEENIRYGRPD---ATDEEVREAARAAHVDEFVSRFPSgystvvgERGAqLSGGQKQRIAIARAI 579
Cdd:PRK13648 86 GIVFQNPdnQFVGSIVKYDVAFGLENhavPYDEMHRRVSEALKQVDMLERADY-------EPNA-LSGGQKQRVAIAGVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115533592 580 LKNPPILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIA--HRLSTIRSAQMIYVIKDKKALESGTHEQLMAKKGSL 656
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISitHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEEL 236
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
425-645 |
1.16e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 98.24 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPT---RPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRG 501
Cdd:PRK13633 5 IKCKNVSYKYESneeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 502 QVIGLISQEP--VLFATSVEENIRYG------RPDATDEEVREAARAAHVDEFVSRFPSgystvvgergaQLSGGQKQRI 573
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGpenlgiPPEEIRERVDESLKKVGMYEYRRHAPH-----------LLSGGQKQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115533592 574 AIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMK--GRTVLIIAHRLSTIRSAQMIYVIKDKKALESGT 645
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
440-597 |
1.19e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 99.79 E-value: 1.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 440 HTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEwlrGQVIGLISQEPVLFA-TSV 518
Cdd:PRK11432 19 NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ---QRDICMVFQSYALFPhMSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 519 EENIRYG-----RPDA-TDEEVREAARAAHVDEFVSRFPSgystvvgergaQLSGGQKQRIAIARAILKNPPILILDEAT 592
Cdd:PRK11432 96 GENVGYGlkmlgVPKEeRKQRVKEALELVDLAGFEDRYVD-----------QISGGQQQRVALARALILKPKVLLFDEPL 164
|
....*
gi 115533592 593 SALDS 597
Cdd:PRK11432 165 SNLDA 169
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
428-663 |
1.48e-22 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 102.07 E-value: 1.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 428 EDVSFSYPTRPGHT-VFENLTLSIPAGQVVALCGPSGEGKS----TITHLLERFYEPKSGRVTLDGRDL-----RELNVe 497
Cdd:COG4172 10 EDLSVAFGQGGGTVeAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLlglseRELRR- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 498 wLRGQVIGLISQEPVlfaTS------VEENI--------RYGRPDATD------EEV--REAARAahvdefVSRFPSgys 555
Cdd:COG4172 89 -IRGNRIAMIFQEPM---TSlnplhtIGKQIaevlrlhrGLSGAAARAralellERVgiPDPERR------LDAYPH--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 556 tvvgergaQLSGGQKQRIAIARAILKNPPILILDEATSALDSHsehmVQEALNNVMK------GRTVLIIAHRLSTIRS- 628
Cdd:COG4172 156 --------QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVT----VQAQILDLLKdlqrelGMALLLITHDLGVVRRf 223
|
250 260 270
....*....|....*....|....*....|....*.
gi 115533592 629 AQMIYVIKDKKALESGTHEQLMAKKGSLY-RKLVEA 663
Cdd:COG4172 224 ADRVAVMRQGEIVEQGPTAELFAAPQHPYtRKLLAA 259
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
431-628 |
1.58e-22 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 96.28 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 431 SFSYPTRPGHTVfENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGqvIGLISQE 510
Cdd:cd03266 10 RFRDVKKTVQAV-DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR--LGFVSDS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 511 PVLFA-TSVEENIRY-GRPDAtdeeVREAARAAHVDEFVSRFpsGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILIL 588
Cdd:cd03266 87 TGLYDrLTARENLEYfAGLYG----LKGDELTARLEELADRL--GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 115533592 589 DEATSALDSHSEHMVQEALNNVMK-GRTVLIIAHRLSTIRS 628
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVER 201
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
425-650 |
1.65e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 97.08 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPtrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLrGQVI 504
Cdd:COG4604 2 IEIKNVSKRYG---GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSREL-AKRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEPVlFAT--SVEENI---RY----GRPDATDEE-VREAARAAHVDEFVSRFPSgystvvgergaQLSGGQKQRIA 574
Cdd:COG4604 78 AILRQENH-INSrlTVRELVafgRFpyskGRLTAEDREiIDEAIAYLDLEDLADRYLD-----------ELSGGQRQRAF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 575 IARAILKNPPILILDEATSALDSHseHMVQealnnVMK---------GRTVLIIAHRLS-TIRSAQMIYVIKDKKALESG 644
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPLNNLDMK--HSVQ-----MMKllrrladelGKTVVIVLHDINfASCYADHIVAMKDGRVVAQG 218
|
....*.
gi 115533592 645 THEQLM 650
Cdd:COG4604 219 TPEEII 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
439-651 |
1.99e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 97.13 E-value: 1.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 439 GHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRV-----TLDGRdlRELN-----VEWLRGQViGLIS 508
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTA--RSLSqqkglIRQLRQHV-GFVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 509 QEPVLFA-TSVEENIRYGrPDATDEEVREAArAAHVDEFVSRFP-SGYSTVVGERgaqLSGGQKQRIAIARAILKNPPIL 586
Cdd:PRK11264 92 QNFNLFPhRTVLENIIEG-PVIVKGEPKEEA-TARARELLAKVGlAGKETSYPRR---LSGGQQQRVAIARALAMRPEVI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 587 ILDEATSALDShseHMVQEALNNVM----KGRTVLIIAHRLSTIRSAQMIYVIKDK-KALESGTHEQLMA 651
Cdd:PRK11264 167 LFDEPTSALDP---ELVGEVLNTIRqlaqEKRTMVIVTHEMSFARDVADRAIFMDQgRIVEQGPAKALFA 233
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
425-653 |
2.15e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 97.61 E-value: 2.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGR--DLRELNVEWLRgQ 502
Cdd:PRK13636 6 LKVEELNYNYSD--GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLR-E 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 503 VIGLISQEP--VLFATSVEENIRYGRPDAT--DEEVREaaraaHVDEFVSRfpSGYSTVVGERGAQLSGGQKQRIAIARA 578
Cdd:PRK13636 83 SVGMVFQDPdnQLFSASVYQDVSFGAVNLKlpEDEVRK-----RVDNALKR--TGIEHLKDKPTHCLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115533592 579 ILKNPPILILDEATSALDSHSEHMVQEALNNVMK--GRTVLIIAHRLSTIR-SAQMIYVIKDKKALESGTHEQLMAKK 653
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
425-651 |
2.23e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 97.37 E-value: 2.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELN-VEWLRgQV 503
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIR-KL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 504 IGLISQEP--VLFATSVEENIRYG------RPDATDEEVREAARAAHVDEFVSRFPSgystvvgergaQLSGGQKQRIAI 575
Cdd:PRK13644 79 VGIVFQNPetQFVGRTVEEDLAFGpenlclPPIEIRKRVDRALAEIGLEKYRHRSPK-----------TLSGGQGQCVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115533592 576 ARAILKNPPILILDEATSALDSHSEHMVQEALNNVM-KGRTVLIIAHRLSTIRSAQMIYVIKDKKALESGTHEQLMA 651
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHeKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
404-663 |
2.44e-22 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 102.93 E-value: 2.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 404 LEPSIPMDTGvciPYHSLWGDIKFEDVSFSYptRPG-HTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSG 482
Cdd:PTZ00243 1291 IEPASPTSAA---PHPVQAGSLVFEGVQMRY--REGlPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGG 1365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 483 RVTLDGRDLRELNVEWLRGQvIGLISQEPVLFATSVEENIRygrP--DATDEEVREAARAAHVDEFVSRFPSGYSTVVGE 560
Cdd:PTZ00243 1366 EIRVNGREIGAYGLRELRRQ-FSMIPQDPVLFDGTVRQNVD---PflEASSAEVWAALELVGLRERVASESEGIDSRVLE 1441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 561 RGAQLSGGQKQRIAIARAILKNPPILIL-DEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRLSTIRSAQMIYVIKDKK 639
Cdd:PTZ00243 1442 GGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGA 1521
|
250 260
....*....|....*....|....
gi 115533592 640 ALESGTHEQLMAKKGSLYRKLVEA 663
Cdd:PTZ00243 1522 VAEMGSPRELVMNRQSIFHSMVEA 1545
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
425-651 |
2.46e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 97.47 E-value: 2.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQvI 504
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRK-I 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEP--VLFATSVEENIRYGRPDA--TDEE----VREAARAAHVDEFVSRFPsgystvvgergAQLSGGQKQRIAIA 576
Cdd:PRK13642 84 GMVFQNPdnQFVGATVEDDVAFGMENQgiPREEmikrVDEALLAVNMLDFKTREP-----------ARLSGGQKQRVAVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115533592 577 RAILKNPPILILDEATSALDSHSEHMVQEALNNVMKGR--TVLIIAHRLSTIRSAQMIYVIKDKKALESGTHEQLMA 651
Cdd:PRK13642 153 GIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
438-629 |
2.58e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 94.99 E-value: 2.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 438 PGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGrdlrelnvewlrGQVIGLISQ---EPVLF 514
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG------------GARVAYVPQrseVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 515 ATSVEENIRYGR--PDATDEEVREAARAAhVDEFVSRFpsGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILILDEAT 592
Cdd:NF040873 71 PLTVRDLVAMGRwaRRGLWRRLTRDDRAA-VDDALERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 115533592 593 SALDSHSEHMVQEALNN-VMKGRTVLIIAHRLSTIRSA 629
Cdd:NF040873 148 TGLDAESRERIIALLAEeHARGATVVVVTHDLELVRRA 185
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
442-621 |
4.08e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 96.14 E-value: 4.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 442 VFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYE--PK---SGRVTLDGRDLRELNVEWLRGQViGLISQEPVLFAT 516
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDVIELRRRV-QMVFQIPNPIPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 517 -SVEENIRYG--------RPDATDEEVREAARAAHV-DEFVSRfpsgystvVGERGAQLSGGQKQRIAIARAILKNPPIL 586
Cdd:PRK14247 97 lSIFENVALGlklnrlvkSKKELQERVRWALEKAQLwDEVKDR--------LDAPAGKLSGGQQQRLCIARALAFQPEVL 168
|
170 180 190
....*....|....*....|....*....|....*
gi 115533592 587 ILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAH 621
Cdd:PRK14247 169 LADEPTANLDPENTAKIESLFLELKKDMTIVLVTH 203
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
428-642 |
4.31e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 96.29 E-value: 4.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 428 EDVSFSYPT------RPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRG 501
Cdd:PRK10419 7 SGLSHHYAHgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 502 -------------------QVIGLISQEPVLFATSVEENIRYGRpdatdeeVREAARAAHVD-EFVSRFPsgystvvger 561
Cdd:PRK10419 87 frrdiqmvfqdsisavnprKTVREIIREPLRHLLSLDKAERLAR-------ASEMLRAVDLDdSVLDKRP---------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 562 gAQLSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMK--GRTVLIIAHRLSTI-RSAQMIYVIKDK 638
Cdd:PRK10419 150 -PQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVeRFCQRVMVMDNG 228
|
....
gi 115533592 639 KALE 642
Cdd:PRK10419 229 QIVE 232
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
428-637 |
6.44e-22 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 96.01 E-value: 6.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 428 EDVSFSYPtrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQVIGLI 507
Cdd:PRK10575 15 RNVSFRVP---GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 508 SQEPVLFATSVEENI---RY------GRPDATD-EEVREAARAAHVDEFVSRFPSgystvvgergaQLSGGQKQRIAIAR 577
Cdd:PRK10575 92 QQLPAAEGMTVRELVaigRYpwhgalGRFGAADrEKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRAWIAM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 578 AILKNPPILILDEATSALDshSEHMVQealnnvmkgrtVLIIAHRLSTIRSAQMIYVIKD 637
Cdd:PRK10575 161 LVAQDSRCLLLDEPTSALD--IAHQVD-----------VLALVHRLSQERGLTVIAVLHD 207
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
425-621 |
1.19e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 96.82 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPghtVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRElNVEWLRGQvI 504
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARAR-I 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEPVL-FATSVEENI----RYGRPDATDEEvreaARAAHVDEFvSRFPSGYSTvvgeRGAQLSGGQKQRIAIARAI 579
Cdd:PRK13536 117 GVVPQFDNLdLEFTVRENLlvfgRYFGMSTREIE----AVIPSLLEF-ARLESKADA----RVSDLSGGMKRRLTLARAL 187
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 115533592 580 LKNPPILILDEATSALDSHSEHMVQEALNNVM-KGRTVLIIAH 621
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTH 230
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
425-658 |
1.34e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 95.25 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYptRPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRgQVI 504
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVR-KFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEP--VLFATSVEENIRYGRPD-ATDEE-----VREAARAAHVDEFVSRFPSgystvvgergaQLSGGQKQRIAIA 576
Cdd:PRK13652 81 GLVFQNPddQIFSPTVEQDIAFGPINlGLDEEtvahrVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 577 RAILKNPPILILDEATSALDSHSEHMVQEALNNVMK--GRTVLIIAHRLSTIRS-AQMIYVIKDKKALESGTHEQLMAKK 653
Cdd:PRK13652 150 GVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQP 229
|
....*
gi 115533592 654 GSLYR 658
Cdd:PRK13652 230 DLLAR 234
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
424-656 |
2.89e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 94.70 E-value: 2.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 424 DIKFEDVSFSYPTRpghTVFENLTL-----SIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDL----REL 494
Cdd:PRK13634 2 DITFQKVEHRYQYK---TPFERRALydvnvSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 495 NVEWLRGQViGLISQ--EPVLFATSVEENIRYGRPD--ATDEEVREAARAAHvdEFVsrfpsGYSTVVGERGA-QLSGGQ 569
Cdd:PRK13634 79 KLKPLRKKV-GIVFQfpEHQLFEETVEKDICFGPMNfgVSEEDAKQKAREMI--ELV-----GLPEELLARSPfELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 570 KQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVM--KGRTVLIIAHRLSTI-RSAQMIYVIKDKKALESGTH 646
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHkeKGLTTVLVTHSMEDAaRYADQIVVMHKGTVFLQGTP 230
|
250
....*....|
gi 115533592 647 EQLMAKKGSL 656
Cdd:PRK13634 231 REIFADPDEL 240
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
442-661 |
4.35e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 93.19 E-value: 4.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 442 VFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGR------DLRELNVEWLRGQViGLISQEPVLFA 515
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEV-GMVFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 516 -TSVEENIRYGRPDATDEEVREAARAahVDEFVSRFpsGYSTVVGER----GAQLSGGQKQRIAIARAILKNPPILILDE 590
Cdd:PRK14246 104 hLSIYDNIAYPLKSHGIKEKREIKKI--VEECLRKV--GLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115533592 591 ATSALDSHSEHMVQEALNNVMKGRTVLIIAHRLSTI-RSAQMIYVIKDKKALESG-THEQLMAKKGSLYRKLV 661
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGsSNEIFTSPKNELTEKYV 252
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
445-660 |
4.49e-21 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 98.70 E-value: 4.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 445 NLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVtldgrdlrelnveWLRgQVIGLISQEPVLFATSVEENIRY 524
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAE-RSIAYVPQQAWIMNATVRGNILF 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 525 GRPDATdEEVREAARAAHVDEFVSRFPSGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILILDEATSALDSH-SEHMV 603
Cdd:PTZ00243 744 FDEEDA-ARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVV 822
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 115533592 604 QEALNNVMKGRTVLIIAHRLSTIRSAQMIYVIKDKKALESGTHEQLMAKkgSLYRKL 660
Cdd:PTZ00243 823 EECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRT--SLYATL 877
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
427-621 |
4.75e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.06 E-value: 4.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 427 FEDVSFSYPTRPghtVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDgrdlrelnvewlRGQVIGL 506
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP------------KGLRIGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 507 ISQEPVLFAT-SVEENIR----------------YGRPDATDEEVREAAR------AAHVDEFVSR---------FP-SG 553
Cdd:COG0488 66 LPQEPPLDDDlTVLDTVLdgdaelraleaeleelEAKLAEPDEDLERLAElqeefeALGGWEAEARaeeilsglgFPeED 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115533592 554 YSTVVGErgaqLSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNvMKGrTVLIIAH 621
Cdd:COG0488 146 LDRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKN-YPG-TVLVVSH 207
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
425-647 |
5.40e-21 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 92.77 E-value: 5.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTrpgHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDG------RDLRELNVEW 498
Cdd:COG4161 3 IQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 499 LRGQViGLISQE----PVLfatSVEENI--------RYGRPDATDEEVREAARAaHVDEFVSRFPsgystvvgergAQLS 566
Cdd:COG4161 80 LRQKV-GMVFQQynlwPHL---TVMENLieapckvlGLSKEQAREKAMKLLARL-RLTDKADRFP-----------LHLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 567 GGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMK-GRTVLIIAHRLSTIR--SAQMIYvIKDKKALES 643
Cdd:COG4161 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARkvASQVVY-MEKGRIIEQ 222
|
....
gi 115533592 644 GTHE 647
Cdd:COG4161 223 GDAS 226
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
445-652 |
6.82e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 92.44 E-value: 6.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 445 NLTLSIPAGQVVALCGPSGEGKSTITHLL---ERfYEPKSGRVTLDGRDLRELNVE--WLRGqvIGLISQEPV------- 512
Cdd:COG0396 18 GVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDILELSPDerARAG--IFLAFQYPVeipgvsv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 513 -LFATSVEENIRYGRPDATD--EEVREAARAAHVDE-FVSRFpsgystvVGErGaqLSGGQKQRIAIARAILKNPPILIL 588
Cdd:COG0396 95 sNFLRTALNARRGEELSAREflKLLKEKMKELGLDEdFLDRY-------VNE-G--FSGGEKKRNEILQMLLLEPKLAIL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 589 DEATSALDSHSEHMVQEALNNVM-KGRTVLIIAH--RLSTIRSAQMIYVIKDKKALESGTHE---QLMAK 652
Cdd:COG0396 165 DETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGKElalELEEE 234
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
425-621 |
1.03e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.90 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPtrpGHTVFENLTLSIPAGQVVALCGPSGEGKST----ITHLLErfyePKSGRVTLdGRDLRelnvewlr 500
Cdd:COG0488 316 LELEGLSKSYG---DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTllklLAGELE----PDSGTVKL-GETVK-------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 501 gqvIGLISQEPVLFAT--SVEENIRYGRPDATDEEVREaaraahvdeFVSRFpsGYStvvGERG----AQLSGGQKQRIA 574
Cdd:COG0488 380 ---IGYFDQHQEELDPdkTVLDELRDGAPGGTEQEVRG---------YLGRF--LFS---GDDAfkpvGVLSGGEKARLA 442
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 115533592 575 IARAILKNPPILILDEATSALDSHSEHMVQEALNNvMKGrTVLIIAH 621
Cdd:COG0488 443 LAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDD-FPG-TVLLVSH 487
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
444-621 |
1.05e-20 |
|
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: 91.37 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 444 ENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEwlRGQVIGLISQEPVLfatSVEENIr 523
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPD--RMVVFQNYSLLPWL---TVRENI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 524 YGRPDATDEEVREAARAAHVDEFVSRFpsGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMV 603
Cdd:TIGR01184 76 ALAVDRVLPDLSKSERRAIVEEHIALV--GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180
....*....|....*....|
gi 115533592 604 QEALNNVMK--GRTVLIIAH 621
Cdd:TIGR01184 154 QEELMQIWEehRVTVLMVTH 173
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
425-626 |
1.20e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 92.58 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSY-PTRPGHTV-FENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLR----ELNVEW 498
Cdd:PRK13641 3 IKFENVDYIYsPGTPMEKKgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 499 LRGQViGLISQ--EPVLFATSVEENIRYGRPD--ATDEEVREAARaahvdEFVSRFpsGYSTVVGERGA-QLSGGQKQRI 573
Cdd:PRK13641 83 LRKKV-SLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAKEKAL-----KWLKKV--GLSEDLISKSPfELSGGQMRRV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 115533592 574 AIARAILKNPPILILDEATSALDSHSEH-MVQEALNNVMKGRTVLIIAHRLSTI 626
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKeMMQLFKDYQKAGHTVILVTHNMDDV 208
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
97-368 |
1.92e-20 |
|
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: 92.15 E-value: 1.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 97 WFFAAVVCAILSAYINIQIPLclgdlvngIVKIIKDESNnLRSHFEQLKPSALHLMTLYVAQSALTFLYITFLTVLGERM 176
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPY--------LIKIAIDEYI-PNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 177 ATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADV---QEFkssfklcVSQGLRTFA----QTIGCIGSLYFLSPTMTM 249
Cdd:cd18545 72 LYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVnslSDL-------LSNGLINLIpdllTLVGIVIIMFSLNVRLAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 250 YTVAVVPGIILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFDNELDKARAMQEQLGVGIG 329
Cdd:cd18545 145 VTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNA 224
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 115533592 330 LFQAGTNLFLN-GMILSVLYGGSNLISkGEMTPGALMSFL 368
Cdd:cd18545 225 LFWPLVELISAlGTALVYWYGGKLVLG-GAITVGVLVAFI 263
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
425-639 |
2.32e-20 |
|
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: 87.89 E-value: 2.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPtrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRdlrelnvewlrgqvi 504
Cdd:cd03221 1 IELENLSKTYG---GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST--------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 glisqepvlfatsveenirygrpdatdeevreaARAAHVDefvsrfpsgystvvgergaQLSGGQKQRIAIARAILKNPP 584
Cdd:cd03221 63 ---------------------------------VKIGYFE-------------------QLSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 585 ILILDEATSALDSHSehmvQEALNNVMKG--RTVLIIAH-R--LSTIrsAQMIYVIKDKK 639
Cdd:cd03221 91 LLLLDEPTNHLDLES----IEALEEALKEypGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
116-668 |
2.37e-20 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 96.52 E-value: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 116 PLCLGdlvngivKIIKDESNNLRSHFEQLKPSALHLMTLYVAQSALTFLYITFLTVLGERMATKMRSDLFQKLLHHDMAF 195
Cdd:TIGR01271 100 PLLLG-------RIIASYDPFNAPEREIAYYLALGLCLLFIVRTLLLHPAIFGLHHLGMQMRIALFSLIYKKTLKLSSRV 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 196 FDSHKSGELSARLNADVQEFKSSFklcvsqGLRTFA-----QTIGCIGSLYFLSPTMTMYTVAVVPGIILAGSAIGAGLR 270
Cdd:TIGR01271 173 LDKISTGQLVSLLSNNLNKFDEGL------ALAHFVwiaplQVILLMGLIWELLEVNGFCGLGFLILLALFQACLGQKMM 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 271 QLSRRAQGQSATASAVSDEALTNIRTIRAF----AMEKLESRLFDNELDKARAmqeqlgVGIGLFQAGTNLFLNGMILSV 346
Cdd:TIGR01271 247 PYRDKRAGKISERLAITSEIIENIQSVKAYcweeAMEKIIKNIRQDELKLTRK------IAYLRYFYSSAFFFSGFFVVF 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 347 LYGGSNLISKGEMTPGAL--MSF-LVSAQTIQRSlsqlsiiFGTAIKGW--TAGG-------------RVLQFSRLEPSI 408
Cdd:TIGR01271 321 LSVVPYALIKGIILRRIFttISYcIVLRMTVTRQ-------FPGAIQTWydSLGAitkiqdflckeeyKTLEYNLTTTEV 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 409 PM-------DTGVcipyHSLWGDIKFED-----------VSFSYPTRPGHTVFENLTLSIPAGQVVALCGPSGEGKSTIT 470
Cdd:TIGR01271 394 EMvnvtaswDEGI----GELFEKIKQNNkarkqpngddgLFFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLL 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 471 HLLERFYEPKSGRVTLDGRdlrelnvewlrgqvIGLISQEPVLFATSVEENIRYGRpdATDE-EVREAARAAHVDEFVSR 549
Cdd:TIGR01271 470 MMIMGELEPSEGKIKHSGR--------------ISFSPQTSWIMPGTIKDNIIFGL--SYDEyRYTSVIKACQLEEDIAL 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 550 FPSGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEA-LNNVMKGRTVLIIAHRLSTIRS 628
Cdd:TIGR01271 534 FPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFEScLCKLMSNKTRILVTSKLEHLKK 613
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 115533592 629 AQMIYVIKDKKALESGTHEQLMAKKGSLYRKLVEAHNVDS 668
Cdd:TIGR01271 614 ADKILLLHEGVCYFYGTFSELQAKRPDFSSLLLGLEAFDN 653
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
425-626 |
2.53e-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: 2.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTrpgHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNvewlrGQVI 504
Cdd:cd03269 1 LEVENVTKRFGR---VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-----RNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEPVLF-ATSVEENIRY-----GRPdatdeevREAARAaHVDEFVSRFpsGYSTVVGERGAQLSGGQKQRIAIARA 578
Cdd:cd03269 73 GYLPEERGLYpKMKVIDQLVYlaqlkGLK-------KEEARR-RIDEWLERL--ELSEYANKRVEELSKGNQQKVQFIAA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 115533592 579 ILKNPPILILDEATSALDSHSEHMVQEALNNVM-KGRTVLIIAHRLSTI 626
Cdd:cd03269 143 VIHDPELLILDEPFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELV 191
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
424-644 |
2.63e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 93.75 E-value: 2.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 424 DIKFEDVSFSyptrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLrGQV 503
Cdd:PRK09536 5 DVSDLSVEFG-----DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAA-SRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 504 IGLISQEPVL-FATSVEENIRYGR---------PDATDEE-VREAARAAHVDEFVSR-FPSgystvvgergaqLSGGQKQ 571
Cdd:PRK09536 79 VASVPQDTSLsFEFDVRQVVEMGRtphrsrfdtWTETDRAaVERAMERTGVAQFADRpVTS------------LSGGERQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115533592 572 RIAIARAILKNPPILILDEATSALDSHseHMVQE---ALNNVMKGRTVLIIAHRLS-TIRSAQMIYVIKDKKALESG 644
Cdd:PRK09536 147 RVLLARALAQATPVLLLDEPTASLDIN--HQVRTlelVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAG 221
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
445-621 |
2.97e-20 |
|
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: 90.02 E-value: 2.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 445 NLTLSIPAGQVVALCGPSGEGKST----ITHLLERFYEpKSGRVTLDGRDLRelnvewlRGQV---IGLISQEPVLFAT- 516
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTlldaISGRVEGGGT-TSGQILFNGQPRK-------PDQFqkcVAYVRQDDILLPGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 517 SVEENIRYGRPDATDEEVREAARAAhVDEFVSRFPSGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILILDEATSALD 596
Cdd:cd03234 97 TVRETLTYTAILRLPRKSSDAIRKK-RVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180
....*....|....*....|....*.
gi 115533592 597 SHSEHMVQEALNNVMK-GRTVLIIAH 621
Cdd:cd03234 176 SFTALNLVSTLSQLARrNRIVILTIH 201
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
430-661 |
3.53e-20 |
|
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: 91.07 E-value: 3.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 430 VSFSYPTRPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQVIglisQ 509
Cdd:cd03291 40 LFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTI----K 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 510 EPVLFATSVEEnIRYgrpdatdeevREAARAAHVDEFVSRFPSGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILILD 589
Cdd:cd03291 116 ENIIFGVSYDE-YRY----------KSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLD 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115533592 590 EATSALDSHSEHMVQEA-LNNVMKGRTVLIIAHRLSTIRSAQMIYVIKDKKALESGTHEQLMAKKGSLYRKLV 661
Cdd:cd03291 185 SPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLM 257
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
425-656 |
4.64e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 90.99 E-value: 4.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYP--TRPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDL----RELNVEW 498
Cdd:PRK13646 3 IRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 499 LRgQVIGLISQ--EPVLFATSVEENIRYGRPD--ATDEEVREAARAAHVDEFVSRfpsgysTVVGERGAQLSGGQKQRIA 574
Cdd:PRK13646 83 VR-KRIGMVFQfpESQLFEDTVEREIIFGPKNfkMNLDEVKNYAHRLLMDLGFSR------DVMSQSPFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 575 IARAILKNPPILILDEATSALDSHSEHMVQEALNNVM--KGRTVLIIAHRLSTI-RSAQMIYVIKDKKALESGTHEQLMA 651
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFK 235
|
....*
gi 115533592 652 KKGSL 656
Cdd:PRK13646 236 DKKKL 240
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
428-624 |
5.38e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 90.12 E-value: 5.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 428 EDVSFSYPTRpghTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVtLDGR----DLRElnvewlrgqV 503
Cdd:PRK11247 16 NAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTaplaEARE---------D 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 504 IGLISQEPVLFA-TSVEENIRYG-----RPDATD--EEVREAARAahvdefvsrfpsgystvvGERGAQLSGGQKQRIAI 575
Cdd:PRK11247 83 TRLMFQDARLLPwKKVIDNVGLGlkgqwRDAALQalAAVGLADRA------------------NEWPAALSGGQKQRVAL 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 115533592 576 ARAILKNPPILILDEATSALDSHSEHMVQEALNNVMK--GRTVLIIAHRLS 624
Cdd:PRK11247 145 ARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQqhGFTVLLVTHDVS 195
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
437-596 |
7.82e-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: 88.18 E-value: 7.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 437 RPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWlrGQVIGLISQEPVLFAT 516
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP--HENILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 517 -SVEENIRYGRPDATDEevreaaraahvdefvSRFPSGYSTVVGERG------AQLSGGQKQRIAIARAILKNPPILILD 589
Cdd:TIGR01189 88 lSALENLHFWAAIHGGA---------------QRTIEDALAAVGLTGfedlpaAQLSAGQQRRLALARLWLSRRPLWILD 152
|
....*..
gi 115533592 590 EATSALD 596
Cdd:TIGR01189 153 EPTTALD 159
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
444-657 |
7.87e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 92.40 E-value: 7.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 444 ENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELN---VEWLRGQVIGLISQEPVLFA-TSVE 519
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaeLREVRRKKIAMVFQSFALMPhMTVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 520 ENIRYGRPDA--TDEEVREAARAAHVDEFVSRFPSGYSTvvgergaQLSGGQKQRIAIARAILKNPPILILDEATSALDS 597
Cdd:PRK10070 125 DNTAFGMELAgiNAEERREKALDALRQVGLENYAHSYPD-------ELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115533592 598 HSEHMVQEALNNVMKG--RTVLIIAHRL-STIRSAQMIYVIKDKKALESGTHEQLMAKKGSLY 657
Cdd:PRK10070 198 LIRTEMQDELVKLQAKhqRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
442-624 |
8.43e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 88.72 E-value: 8.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 442 VFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEW---LRGQVIGLISQ-EPVLFATS 517
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQKLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 518 VEEN------IRYGRPDATDEEVREAARAAHVDEFVSRFPSgystvvgergaQLSGGQKQRIAIARAILKNPPILILDEA 591
Cdd:PRK11629 104 ALENvampllIGKKKPAEINSRALEMLAAVGLEHRANHRPS-----------ELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190
....*....|....*....|....*....|....*
gi 115533592 592 TSALDSHSEHMVQEALN--NVMKGRTVLIIAHRLS 624
Cdd:PRK11629 173 TGNLDARNADSIFQLLGelNRLQGTAFLVVTHDLQ 207
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
439-651 |
1.51e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 89.38 E-value: 1.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 439 GHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEP-----KSGRVTLDGRDL---RELnVEWLRGqvIGLISQE 510
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIfnyRDV-LEFRRR--VGMLFQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 511 PVLFATSVEENIRYG---RPDATDEEVREAARAAHVDefvsrfpSGYSTVVGERGA----QLSGGQKQRIAIARAILKNP 583
Cdd:PRK14271 110 PNPFPMSIMDNVLAGvraHKLVPRKEFRGVAQARLTE-------VGLWDAVKDRLSdspfRLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115533592 584 PILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRLS-TIRSAQMIYVIKDKKALESGTHEQLMA 651
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
151-367 |
2.51e-19 |
|
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: 89.04 E-value: 2.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 151 LMTLYVAQSALTFLYITFLTVLGERMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNaDVQEFKSSF-KLCVSQGLRT 229
Cdd:cd18570 48 LILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFN-DANKIREAIsSTTISLFLDL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 230 F-AQTIGCIgsLYFLSPTMTMYTVAVVPGIILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESR 308
Cdd:cd18570 127 LmVIISGII--LFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLK 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 115533592 309 LFDNELDKARAMQEQLGVGIGLFQAGTNLFLNGMILSVLYGGSNLISKGEMTPGALMSF 367
Cdd:cd18570 205 KIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSYLVIKGQLSLGQLIAF 263
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
439-654 |
2.68e-19 |
|
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: 86.43 E-value: 2.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 439 GHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERF--YEPKSGRVTLDGRDLRELNVE--WLRGqvIGLISQEPVLF 514
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEerARLG--IFLAFQYPPEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 515 A-TSVEENIRYgrpdatdeevreaaraahVDEfvsrfpsgystvvgergaQLSGGQKQRIAIARAILKNPPILILDEATS 593
Cdd:cd03217 90 PgVKNADFLRY------------------VNE------------------GFSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115533592 594 ALDSHSEHMVQEALNNVM-KGRTVLIIAH--RLSTIRSAQMIYVIKDKKALESGTHE--QLMAKKG 654
Cdd:cd03217 134 GLDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKElaLEIEKKG 199
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
440-650 |
3.10e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 88.12 E-value: 3.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 440 HTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLrGQVIGLISQEPVLFA-TSV 518
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEV-ARRIGLLAQNATTPGdITV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 519 EENIRYGR----PDAT-----DEE-VREAARAahvdefvsrfpSGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILIL 588
Cdd:PRK10253 99 QELVARGRyphqPLFTrwrkeDEEaVTKAMQA-----------TGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115533592 589 DEATSALDSHSEHMVQEALN--NVMKGRTVLIIAHRLS-TIRSAQMIYVIKDKKALESGTHEQLM 650
Cdd:PRK10253 168 DEPTTWLDISHQIDLLELLSelNREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
436-632 |
3.50e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.47 E-value: 3.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 436 TRPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVewlRGQVIGLISQEPVLFA 515
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV---AEACHYLGHRNAMKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 516 TSVEENIR-----YGRPDATDEEVREA---ARAAHVdefvsrfPSGYstvvgergaqLSGGQKQRIAIARAILKNPPILI 587
Cdd:PRK13539 88 LTVAENLEfwaafLGGEELDIAAALEAvglAPLAHL-------PFGY----------LSAGQKRRVALARLLVSNRPIWI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 115533592 588 LDEATSALDSHSehmvQEALNNVMKGR-----TVLIIAHRLSTIRSAQMI 632
Cdd:PRK13539 151 LDEPTAALDAAA----VALFAELIRAHlaqggIVIAATHIPLGLPGAREL 196
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
156-368 |
3.59e-19 |
|
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: 88.31 E-value: 3.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 156 VAQSALTFLYITFLTVLGERMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFkSSFklcVSQGLRTFAQTI- 234
Cdd:cd18546 50 LAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDAL-SEL---LQTGLVQLVVSLl 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 235 ---GCIGSLYFLSPTMTMYTVAVVPgIILAGSAIgagLRQLSRRAQGQSATASA--VSD--EALTNIRTIRAFAMEKLES 307
Cdd:cd18546 126 tlvGIAVVLLVLDPRLALVALAALP-PLALATRW---FRRRSSRAYRRARERIAavNADlqETLAGIRVVQAFRRERRNA 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115533592 308 RLFDNELDKARAMQEQLGVGIGLFQAGTNLFLNGMILSVLYGGSNLISKGEMTPGALMSFL 368
Cdd:cd18546 202 ERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLTVGVLVAFL 262
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
439-651 |
4.69e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 86.87 E-value: 4.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 439 GHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRD--LRELNVEWLRGqvIGLISQEPVLFAT 516
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDisLLPLHARARRG--IGYLPQEASIFRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 517 -SVEENIRYG---RPDATDEEvreaaRAAHVDEFVSRFpsGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILILDEAT 592
Cdd:PRK10895 93 lSVYDNLMAVlqiRDDLSAEQ-----REDRANELMEEF--HIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115533592 593 SALDSHSEHMVQEALNNVM-KGRTVLIIAHRL-STIRSAQMIYVIKDKKALESGTHEQLMA 651
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHLRdSGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
442-621 |
4.76e-19 |
|
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: 86.72 E-value: 4.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 442 VFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGR----DL-----RELnVEwLRGQVIGLISQ--- 509
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLaqaspREI-LA-LRRRTIGYVSQflr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 510 ------------EPvLFATSVEEnirygrpdatdEEVREAARaahvdEFVSRFPsgystvVGERGAQL-----SGGQKQR 572
Cdd:COG4778 104 viprvsaldvvaEP-LLERGVDR-----------EEARARAR-----ELLARLN------LPERLWDLppatfSGGEQQR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 115533592 573 IAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVM-KGRTVLIIAH 621
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKaRGTAIIGIFH 210
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
441-649 |
5.11e-19 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 86.42 E-value: 5.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 441 TVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWL--RGqvIGLISQEPVLFAT-S 517
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERarAG--IAYVPQGREIFPRlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 518 VEENIRYGRPdatdeevREAARAAHVDEFV-SRFPSgYSTVVGERGAQLSGGQKQRIAIARAILKNPPILILDEATSALD 596
Cdd:TIGR03410 92 VEENLLTGLA-------ALPRRSRKIPDEIyELFPV-LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQ 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 115533592 597 SHSEHMVQEALNNV--MKGRTVLIIAHRLSTIRS-AQMIYVIKDKKALESGTHEQL 649
Cdd:TIGR03410 164 PSIIKDIGRVIRRLraEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
425-662 |
5.11e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.92 E-value: 5.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPG--------HTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYePKSGRVTLDGRDLRELNv 496
Cdd:PRK15134 276 LDVEQLQVAFPIRKGilkrtvdhNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLN- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 497 ewlRGQVIGLISQEPVLF-------------ATSVEENIRYGRPDAT----DEEVREAARAAHVD-EFVSRFPsgystvv 558
Cdd:PRK15134 354 ---RRQLLPVRHRIQVVFqdpnsslnprlnvLQIIEEGLRVHQPTLSaaqrEQQVIAVMEEVGLDpETRHRYP------- 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 559 gergAQLSGGQKQRIAIARAILKNPPILILDEATSALDshseHMVQEALNNVMKGR------TVLIIAHRLSTIRSA--Q 630
Cdd:PRK15134 424 ----AEFSGGQRQRIAIARALILKPSLIILDEPTSSLD----KTVQAQILALLKSLqqkhqlAYLFISHDLHVVRALchQ 495
|
250 260 270
....*....|....*....|....*....|...
gi 115533592 631 MIyVIKDKKALESGTHEQLMAKKGSLY-RKLVE 662
Cdd:PRK15134 496 VI-VLRQGEVVEQGDCERVFAAPQQEYtRQLLA 527
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
425-653 |
5.22e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 86.61 E-value: 5.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTrpgHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGR--DLR----ELNVEW 498
Cdd:PRK11124 3 IQLNGINCFYGA---HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSktpsDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 499 LRgQVIGLISQEPVLFA-TSVEENIrygrPDA-------TDEEVREAARAA----HVDEFVSRFPsgystvvgergAQLS 566
Cdd:PRK11124 80 LR-RNVGMVFQQYNLWPhLTVQQNL----IEApcrvlglSKDQALARAEKLlerlRLKPYADRFP-----------LHLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 567 GGQKQRIAIARAILKNPPILILDEATSALDShsehmvqEALNNVMKgrtvliIAHRLSTIRSAQMIYvikdkkalesgTH 646
Cdd:PRK11124 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDP-------EITAQIVS------IIRELAETGITQVIV-----------TH 199
|
....*..
gi 115533592 647 EQLMAKK 653
Cdd:PRK11124 200 EVEVARK 206
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
445-623 |
9.06e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 90.09 E-value: 9.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 445 NLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDG--------RDLRELNvewlrgqvIGLISQEPVLFAT 516
Cdd:COG3845 23 DVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpvrirspRDAIALG--------IGMVHQHFMLVPN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 517 -SVEENIRYGRPDATDEEVREAARAAHVDEFVSRF-----PSgysTVVGergaQLSGGQKQRIAIARAILKNPPILILDE 590
Cdd:COG3845 95 lTVAENIVLGLEPTKGGRLDRKAARARIRELSERYgldvdPD---AKVE----DLSVGEQQRVEILKALYRGARILILDE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 115533592 591 ATSALDshsehmVQEA--LNNVMK-----GRTVLIIAHRL 623
Cdd:COG3845 168 PTAVLT------PQEAdeLFEILRrlaaeGKSIIFITHKL 201
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
425-621 |
1.12e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 87.17 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTrpgHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRElNVEWLRGQVi 504
Cdd:PRK13537 8 IDFRNVEKRYGD---KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRV- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQ----EPVLfatSVEENIR-----YGRPDATDEevreaARAAHVDEFvSRFPSGYSTVVGErgaqLSGGQKQRIAI 575
Cdd:PRK13537 83 GVVPQfdnlDPDF---TVRENLLvfgryFGLSAAAAR-----ALVPPLLEF-AKLENKADAKVGE----LSGGMKRRLTL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 115533592 576 ARAILKNPPILILDEATSALDSHSEHMVQEALNNVM-KGRTVLIIAH 621
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTH 196
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
445-649 |
1.38e-18 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 85.11 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 445 NLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRgqVIGLISQEPVL-FATSVEENIR 523
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRR--RIGIVFQDLSVdDELTGWENLY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 524 -----YGRPDAT-DEEVREAARAAHVDEFVSRFPSGYstvvgergaqlSGGQKQRIAIARAILKNPPILILDEATSALDS 597
Cdd:cd03265 96 iharlYGVPGAErRERIDELLDFVGLLEAADRLVKTY-----------SGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 115533592 598 HSEHMVQEALNNVMK--GRTVLIIAHRLSTIRS-AQMIYVIKDKKALESGTHEQL 649
Cdd:cd03265 165 QTRAHVWEYIEKLKEefGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
418-628 |
1.69e-18 |
|
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: 84.89 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 418 YHSLWGDIKFEDVSFSYPTRPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRdlrelnVE 497
Cdd:cd03220 13 YKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR------VS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 498 WLRGQVIGLisqEPVLfatSVEENIR-----YG-RPDATDEEVREAARAAHVDEFVSRFPSGYSTvvgergaqlsgGQKQ 571
Cdd:cd03220 87 SLLGLGGGF---NPEL---TGRENIYlngrlLGlSRKEIDEKIDEIIEFSELGDFIDLPVKTYSS-----------GMKA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 115533592 572 RIAIARAILKNPPILILDEATSALDSHSEHMVQEALNN-VMKGRTVLIIAHRLSTIRS 628
Cdd:cd03220 150 RLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRElLKQGKTVILVSHDPSSIKR 207
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
147-368 |
2.47e-18 |
|
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: 85.99 E-value: 2.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 147 SALHLMTLYVAQSALTFLY--ITFLTVLGeRMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFKLCVS 224
Cdd:cd18589 37 AAITVMSLLTIASAVSEFVcdLIYNITMS-RIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 225 QGLRTFAQTIGCIGSLYFLSPTMTMYTVAVVPGIILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEK 304
Cdd:cd18589 116 LLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEE 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115533592 305 LESRLFDNELDKARAMQEQLGVGIGLFQAGTNLFLNGMILSVLYGGSNLISKGEMTPGALMSFL 368
Cdd:cd18589 196 GEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGGQLVTAGTVSSGDLVTFV 259
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
428-665 |
3.32e-18 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 84.89 E-value: 3.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 428 EDVSFSYPTRPG------HTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWlRG 501
Cdd:COG4167 8 RNLSKTFKYRTGlfrrqqFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY-RC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 502 QVIGLISQEPvlfATSVEENIRYGR----PDATDEEVREAARAAHVDEFVSRfpsgystvVGERGAQ-------LSGGQK 570
Cdd:COG4167 87 KHIRMIFQDP---NTSLNPRLNIGQileePLRLNTDLTAEEREERIFATLRL--------VGLLPEHanfyphmLSSGQK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 571 QRIAIARAILKNPPILILDEATSALDshsehM-VQEALNNVM------KGRTVLIIAHRLSTIR--SAQMIyVIKDKKAL 641
Cdd:COG4167 156 QRVALARALILQPKIIIADEALAALD-----MsVRSQIINLMlelqekLGISYIYVSQHLGIVKhiSDKVL-VMHQGEVV 229
|
250 260
....*....|....*....|....*
gi 115533592 642 ESG-THEQLMAKKGSLYRKLVEAHN 665
Cdd:COG4167 230 EYGkTAEVFANPQHEVTKRLIESHF 254
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
449-652 |
3.49e-18 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 86.17 E-value: 3.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 449 SIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVE---WLRGQV----------------IGLISQ 509
Cdd:PRK11308 37 TLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqkLLRQKIqivfqnpygslnprkkVGQILE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 510 EPVLFATSVeenirygrpdaTDEEVREAARA--AHVD---EFVSRFPSGYStvvgergaqlsGGQKQRIAIARAILKNPP 584
Cdd:PRK11308 117 EPLLINTSL-----------SAAERREKALAmmAKVGlrpEHYDRYPHMFS-----------GGQRQRIAIARALMLDPD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115533592 585 ILILDEATSALDSHsehmVQ-EALNNVMK-----GRTVLIIAHRLSTIRS-AQMIYVIKDKKALESGTHEQLMAK 652
Cdd:PRK11308 175 VVVADEPVSALDVS----VQaQVLNLMMDlqqelGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
433-590 |
5.55e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 83.54 E-value: 5.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 433 SYPTRpghTVFENLTLSIPAGQVVALCGPSGEGKSTIthllerFY------EPKSGRVTLDGRDLRELNVeWLRGQV-IG 505
Cdd:COG1137 12 SYGKR---TVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPM-HKRARLgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 506 LISQEPVLFAT-SVEENIRygrpdATDE--EVREAARAAHVDEFVSRFpsGYSTVVGERGAQLSGGQKQRIAIARAILKN 582
Cdd:COG1137 82 YLPQEASIFRKlTVEDNIL-----AVLElrKLSKKEREERLEELLEEF--GITHLRKSKAYSLSGGERRRVEIARALATN 154
|
....*...
gi 115533592 583 PPILILDE 590
Cdd:COG1137 155 PKFILLDE 162
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
425-645 |
7.34e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 84.41 E-value: 7.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTrpgHTVFE-----NLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLREL----N 495
Cdd:PRK13649 3 INLQNVSYTYQA---GTPFEgralfDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 496 VEWLRGQViGLISQ--EPVLFATSVEENIRYGRPD--ATDEEVREAARA--AHV---DEFVSRFPsgystvvgergAQLS 566
Cdd:PRK13649 80 IKQIRKKV-GLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALAREklALVgisESLFEKNP-----------FELS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 567 GGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNV-MKGRTVLIIAHRLSTIRS-AQMIYVIKDKKALESG 644
Cdd:PRK13649 148 GGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSG 227
|
.
gi 115533592 645 T 645
Cdd:PRK13649 228 K 228
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
442-647 |
7.95e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 83.74 E-value: 7.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 442 VFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPK-----SGRVTLDGRDLRELNVEWLR-GQVIGLISQEPVLFA 515
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDPIEvRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 516 -TSVEENIRYG--------RPDATDEEVREA-ARAAHVDEFVSRfpsgystvVGERGAQLSGGQKQRIAIARAILKNPPI 585
Cdd:PRK14267 99 hLTIYDNVAIGvklnglvkSKKELDERVEWAlKKAALWDEVKDR--------LNDYPSNLSGGQRQRLVIARALAMKPKI 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115533592 586 LILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAH------RLST----IRSAQMIYVIKDKKALESGTHE 647
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHspaqaaRVSDyvafLYLGKLIEVGPTRKVFENPEHE 242
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
425-622 |
1.41e-17 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 80.66 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLdgrdlrelnvewLRGQVI 504
Cdd:cd03223 1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM------------PEGEDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEPVLFATSVEENIRYgrpdatdeevreaaraahvdefvsrfPSGystvvgergAQLSGGQKQRIAIARAILKNPP 584
Cdd:cd03223 67 LFLPQRPYLPLGTLREQLIY--------------------------PWD---------DVLSGGEQQRLAFARLLLHKPK 111
|
170 180 190
....*....|....*....|....*....|....*...
gi 115533592 585 ILILDEATSALDSHSEHMVQEALNNvmKGRTVLIIAHR 622
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLLKE--LGITVISVGHR 147
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
425-626 |
1.54e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 83.39 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYptRPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELnvewLRGQVI 504
Cdd:PRK15056 7 IVVNDVTVTW--RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA----LQKNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQE-------PVLfatsVEENI---RYG------RPDATDEEVREAArAAHVDEFVSRFPSgystvVGErgaqLSGG 568
Cdd:PRK15056 81 AYVPQSeevdwsfPVL----VEDVVmmgRYGhmgwlrRAKKRDRQIVTAA-LARVDMVEFRHRQ-----IGE----LSGG 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 115533592 569 QKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVM-KGRTVLIIAHRLSTI 626
Cdd:PRK15056 147 QKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
439-649 |
3.49e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 82.46 E-value: 3.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 439 GHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVewlrgQVIGLISQEPVLFAT-S 517
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDR-----RRIGYLPEERGLYPKmK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 518 VEENIRY-----GRPDAtdeevrEAARAAhvDEFVSRFPsgystvVGERGA----QLSGGQKQRIAIARAILKNPPILIL 588
Cdd:COG4152 88 VGEQLVYlarlkGLSKA------EAKRRA--DEWLERLG------LGDRANkkveELSKGNQQKVQLIAALLHDPELLIL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115533592 589 DEATSALDSHSEHMVQEALNNVM-KGRTVLIIAHRLSTI-RSAQMIYVIKDKKALESGTHEQL 649
Cdd:COG4152 154 DEPFSGLDPVNVELLKDVIRELAaKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEI 216
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
453-624 |
3.95e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.10 E-value: 3.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 453 GQVVALCGPSGEGKSTITHLLErFYEPK----SGRVTLDGR--DLRELNvewlrgQVIGLISQEPVLFAT-SVEENI--- 522
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMpiDAKEMR------AISAYVQQDDLFIPTlTVREHLmfq 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 523 ---RYGRPDATDEevreaaRAAHVDEFVSR--FPSGYSTVVGERGAQ--LSGGQKQRIAIARAILKNPPILILDEATSAL 595
Cdd:TIGR00955 124 ahlRMPRRVTKKE------KRERVDEVLQAlgLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGL 197
|
170 180 190
....*....|....*....|....*....|
gi 115533592 596 DSHSEHMVQEALNNV-MKGRTVLIIAHRLS 624
Cdd:TIGR00955 198 DSFMAYSVVQVLKGLaQKGKTIICTIHQPS 227
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
447-649 |
4.82e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 82.83 E-value: 4.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 447 TLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRG--QVIGLISQEPV-------LFATS 517
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAvrSDIQMIFQDPLaslnprmTIGEI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 518 VEENIRYGRPDATDEEVREAARAAH-----VDEFVSRFPSgystvvgergaQLSGGQKQRIAIARAILKNPPILILDEAT 592
Cdd:PRK15079 121 IAEPLRTYHPKLSRQEVKDRVKAMMlkvglLPNLINRYPH-----------EFSGGQCQRIGIARALILEPKLIICDEPV 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 593 SALDSHSEHMVQEALNNVMK--GRTVLIIAHRLSTIRS-AQMIYVIKDKKALESGTHEQL 649
Cdd:PRK15079 190 SALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
440-623 |
4.83e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 81.67 E-value: 4.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 440 HTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNvEWLRGQVIGLISQEPVL---FAT 516
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP-EYKRAKYIGRVFQDPMMgtaPSM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 517 SVEENI--------RYGRPDATDEEVREAARaahvdEFVSRFPSGY----STVVGergaQLSGGQKQRIAIARAILKNPP 584
Cdd:COG1101 98 TIEENLalayrrgkRRGLRRGLTKKRRELFR-----ELLATLGLGLenrlDTKVG----LLSGGQRQALSLLMATLTKPK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 115533592 585 ILILDEATSALDSHSEHMVQEALNNVMKGR--TVLIIAHRL 623
Cdd:COG1101 169 LLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNM 209
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
441-635 |
5.56e-17 |
|
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: 80.84 E-value: 5.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 441 TVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLR------GQVIGLISQEPVLF 514
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRrigvvfGQKTQLWWDLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 515 ATSVEENIrYGRPDAtdeevREAARAAHVDEFVSRFPSGYSTVvgergAQLSGGQKQRIAIARAILKNPPILILDEATSA 594
Cdd:cd03267 115 SFYLLAAI-YDLPPA-----RFKKRLDELSELLDLEELLDTPV-----RQLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 115533592 595 LDSHSEHMVQEALN--NVMKGRTVLIIAHRLSTIRS-AQMIYVI 635
Cdd:cd03267 184 LDVVAQENIRNFLKeyNRERGTTVLLTSHYMKDIEAlARRVLVI 227
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
156-382 |
5.65e-17 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 81.87 E-value: 5.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 156 VAQSALTFLYITFLTVLGERMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNA--DVQEFkssfklCVSQGLRTF--- 230
Cdd:cd18782 53 LLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRISEldTIRGF------LTGTALTTLldv 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 231 AQTIGCIGSLYFLSPTMTMYTVAVVPGIILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLF 310
Cdd:cd18782 127 LFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRW 206
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115533592 311 DNELdkARAMQEQLGVG-IGLFQAGTNLFLNGMI-LSVLYGGSNLISKGEMTPGALMSFLVSAQTIQRSLSQLS 382
Cdd:cd18782 207 QNRY--ARSLGEGFKLTvLGTTSGSLSQFLNKLSsLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLS 278
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
425-626 |
6.61e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 80.30 E-value: 6.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYptRPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRD---LRELNVEWLRG 501
Cdd:PRK10908 2 IRFEHVSKAY--LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrLKNREVPFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 502 QvIGLISQEP-VLFATSVEENIryGRP----DATDEEVREAARAAhVDEF-----VSRFPsgystvvgergAQLSGGQKQ 571
Cdd:PRK10908 80 Q-IGMIFQDHhLLMDRTVYDNV--AIPliiaGASGDDIRRRVSAA-LDKVglldkAKNFP-----------IQLSGGEQQ 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 115533592 572 RIAIARAILKNPPILILDEATSALDSH-SEHMVQ--EALNNVmkGRTVLIIAHRLSTI 626
Cdd:PRK10908 145 RVGIARAVVNKPAVLLADEPTGNLDDAlSEGILRlfEEFNRV--GVTVLMATHDIGLI 200
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
425-651 |
7.42e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 80.96 E-value: 7.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPghtVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRG--Q 502
Cdd:PRK11831 8 VDMRGVSFTRGNRC---IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTvrK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 503 VIGLISQEPVLFA-TSVEENIRYgrpdatdeEVREaaraaHvdefvSRFPSG--YSTV------VGERGA------QLSG 567
Cdd:PRK11831 85 RMSMLFQSGALFTdMNVFDNVAY--------PLRE-----H-----TQLPAPllHSTVmmkleaVGLRGAaklmpsELSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 568 GQKQRIAIARAILKNPPILILDEATSALDSHSE----HMVQEaLNNVMkGRTVLIIAHRLSTIRS-AQMIYVIKDKKALE 642
Cdd:PRK11831 147 GMARRAALARAIALEPDLIMFDEPFVGQDPITMgvlvKLISE-LNSAL-GVTCVVVSHDVPEVLSiADHAYIVADKKIVA 224
|
....*....
gi 115533592 643 SGTHEQLMA 651
Cdd:PRK11831 225 HGSAQALQA 233
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
444-664 |
1.08e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 80.13 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 444 ENLTLSIPAGQVVALCGPSGEGKS-TITHLLERF---YEPKSGRVTLDGRdlrELNVEWLRGQVIGLISQEP-------- 511
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGRVLLDGK---PVAPCALRGRKIATIMQNPrsafnplh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 512 VLFATSVEENIRYGRPdATDEEVREAARAAHVDEfVSRFPSGYSTvvgergaQLSGGQKQRIAIARAILKNPPILILDEA 591
Cdd:PRK10418 97 TMHTHARETCLALGKP-ADDATLTAALEAVGLEN-AARVLKLYPF-------EMSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115533592 592 TSALDSHSEHMVQEALNNVMKGRT--VLIIAHRLSTI-RSAQMIYVIKDKKALESG-THEQLMAKKGSLYRKLVEAH 664
Cdd:PRK10418 168 TTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQGdVETLFNAPKHAVTRSLVSAH 244
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
154-382 |
1.26e-16 |
|
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: 80.99 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 154 LYVAQSALTflyitflTVLGERMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFKLCVSQGLRTFAQT 233
Cdd:cd18550 55 LGVVQTYLS-------ARIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 234 IGCIGSLYFLSPTMTMYTVAVVPGIILAGSAIGAGLRQLSRRAQGQSATASAVSDEALT--NIRTIRAFAMEKLESRLFD 311
Cdd:cd18550 128 VATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLSvsGALLVKLFGREDDEAARFA 207
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115533592 312 NELDKARAMQEQLGVGIGLFQAGTNLFLNGMILSVLYGGSNLISKGEMTPGALMSFLVSAQTIQRSLSQLS 382
Cdd:cd18550 208 RRSRELRDLGVRQALAGRWFFAALGLFTAIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLL 278
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
425-665 |
1.47e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 79.74 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPG-------------------HTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVT 485
Cdd:COG1134 5 IEVENVSKSYRLYHEpsrslkelllrrrrtrreeFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 486 LDGRdlrelnVEWLrgqvIGLisqepvlfAT------SVEENIR-----YGrpdATDEEVREaaRAAHVDEF--VSRF-- 550
Cdd:COG1134 85 VNGR------VSAL----LEL--------GAgfhpelTGRENIYlngrlLG---LSRKEIDE--KFDEIVEFaeLGDFid 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 551 -PSG-YSTvvgergaqlsgGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMK-GRTVLIIAHRLSTIR 627
Cdd:COG1134 142 qPVKtYSS-----------GMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELREsGRTVIFVSHSMGAVR 210
|
250 260 270
....*....|....*....|....*....|....*....
gi 115533592 628 S-AQMIYVIKDKKALESGTHEQLMAkkgsLYRKLVEAHN 665
Cdd:COG1134 211 RlCDRAIWLEKGRLVMDGDPEEVIA----AYEALLAGRE 245
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
98-385 |
1.96e-16 |
|
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: 80.69 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 98 FFAAVVCAILSAYINIQIPLCLGDLVNGIVKiiKDESNNLR--------SHFEQLKPSALHLMTLYVAQSALTFLYITFL 169
Cdd:cd18565 1 LVLGLLASILNRLFDLAPPLLIGVAIDAVFN--GEASFLPLvpaslgpaDPRGQLWLLGGLTVAAFLLESLFQYLSGVLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 170 TVLGERMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFKLCVSQGLRTFAQTIGCIGSLYFLSPTMTM 249
Cdd:cd18565 79 RRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 250 YTVAVVPgiilagsAIGAGLRQLSRRAQGQ-SATASAVSD------EALTNIRTIRAFAMEKLES--------RLFDNEL 314
Cdd:cd18565 159 VALLPVP-------LIIAGTYWFQRRIEPRyRAVREAVGDlnarleNNLSGIAVIKAFTAEDFERervadaseEYRDANW 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115533592 315 DKARamqeqlgVGIGlFQAGTNLFLN-GMILSVLYGGSNLIS-----KGEMTPGALMSFLVSAQTIQRSLSQLSIIF 385
Cdd:cd18565 232 RAIR-------LRAA-FFPVIRLVAGaGFVATFVVGGYWVLDgpplfTGTLTVGTLVTFLFYTQRLLWPLTRLGDLI 300
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
445-596 |
2.12e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 81.07 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 445 NLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRE------LNVEWLRgqvIGLISQEPVLFA-TS 517
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDaekgicLPPEKRR---IGYVFQDARLFPhYK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 518 VEENIRYGrpdatdeeVREAaRAAHVDEFVS---------RFPSGystvvgergaqLSGGQKQRIAIARAILKNPPILIL 588
Cdd:PRK11144 93 VRGNLRYG--------MAKS-MVAQFDKIVAllgieplldRYPGS-----------LSGGEKQRVAIGRALLTAPELLLM 152
|
....*...
gi 115533592 589 DEATSALD 596
Cdd:PRK11144 153 DEPLASLD 160
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
425-596 |
2.66e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 81.04 E-value: 2.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHL---LERFyepKSGRVTLDGRDLRELNVEwLRG 501
Cdd:PRK11650 4 LKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMvagLERI---TSGEIWIGGRVVNELEPA-DRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 502 qvIGLISQEPVLFA-TSVEENIRYG---R--PDAT-DEEVREAARAAHVDEFVSRFPsgystvvgergAQLSGGQKQRIA 574
Cdd:PRK11650 78 --IAMVFQNYALYPhMSVRENMAYGlkiRgmPKAEiEERVAEAARILELEPLLDRKP-----------RELSGGQRQRVA 144
|
170 180
....*....|....*....|..
gi 115533592 575 IARAILKNPPILILDEATSALD 596
Cdd:PRK11650 145 MGRAIVREPAVFLFDEPLSNLD 166
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
438-644 |
4.81e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 81.37 E-value: 4.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 438 PGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQVIGLISQE-PVLFAT 516
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGIIYQElSVIDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 517 SVEENIRYGR---------PDATDEEVREaaRAAHVDEFVsrfpsGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILI 587
Cdd:PRK09700 96 TVLENLYIGRhltkkvcgvNIIDWREMRV--RAAMMLLRV-----GLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVII 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 115533592 588 LDEATSALDSHSEHMVQEALNNVMK-GRTVLIIAHRLSTIRS-AQMIYVIKDKKALESG 644
Cdd:PRK09700 169 MDEPTSSLTNKEVDYLFLIMNQLRKeGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
441-645 |
5.60e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 79.51 E-value: 5.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 441 TVFENLTLSIPAGQVVALCGPSGEGKST-ITHL------------LERFY---EPKSGRVTLDGRDLRELNVEWLRgQVI 504
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTlVTHFnglikskygtiqVGDIYigdKKNNHELITNPYSKKIKNFKELR-RRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEP--VLFATSVEENIRYGrPDATDEEVREAARAAHV--------DEFVSRFPSGystvvgergaqLSGGQKQRIA 574
Cdd:PRK13631 119 SMVFQFPeyQLFKDTIEKDIMFG-PVALGVKKSEAKKLAKFylnkmgldDSYLERSPFG-----------LSGGQKRRVA 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115533592 575 IARAILKNPPILILDEATSALDSHSEH-MVQEALNNVMKGRTVLIIAHRLSTI-RSAQMIYVIKDKKALESGT 645
Cdd:PRK13631 187 IAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGT 259
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
445-649 |
1.10e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 77.34 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 445 NLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLrelnvEWLRGQVI---GLIS--QEPVLFA--TS 517
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHI-----EGLPGHQIarmGVVRtfQHVRLFRemTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 518 VEE-----------NIRYG---RPDATDEEvREA-ARAAHVDEFVsrfpsGYSTVVGERGAQLSGGQKQRIAIARAILKN 582
Cdd:PRK11300 98 IENllvaqhqqlktGLFSGllkTPAFRRAE-SEAlDRAATWLERV-----GLLEHANRQAGNLAYGQQRRLEIARCMVTQ 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 583 PPILILDEATSALDSHSEHMVQEALNNVMK--GRTVLIIAHRLSTIRS-AQMIYVIKDKKALESGTHEQL 649
Cdd:PRK11300 172 PEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
438-651 |
1.20e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.96 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 438 PGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQVIGLISQE----PVL 513
Cdd:PRK11288 15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAIIYQElhlvPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 514 fatSVEENIRYGRPDATDEEVREAARAAHVDEFVSRF-----PSgysTVVGErgaqLSGGQKQRIAIARAILKNPPILIL 588
Cdd:PRK11288 95 ---TVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLgvdidPD---TPLKY----LSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115533592 589 DEATSALdSHSEhmvQEALNNVM-----KGRTVLIIAHRLSTI-RSAQMIYVIKDKK------ALESGTHEQLMA 651
Cdd:PRK11288 165 DEPTSSL-SARE---IEQLFRVIrelraEGRVILYVSHRMEEIfALCDAITVFKDGRyvatfdDMAQVDRDQLVQ 235
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
440-663 |
1.41e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 80.13 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 440 HTVFENLTLSIPAGQVVALCGPSGEGKS-TITHLLERFYEPK----SGRVTLDGRDL---RELNVEWLRGQVIGLISQEP 511
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLlhaSEQTLRGVRGNKIAMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 512 VlfatsVEENirygrPDATDE----EV--------REAARAahvdEFVSRFPSgystvVGERGA---------QLSGGQK 570
Cdd:PRK15134 102 M-----VSLN-----PLHTLEkqlyEVlslhrgmrREAARG----EILNCLDR-----VGIRQAakrltdyphQLSGGER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 571 QRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMK--GRTVLIIAHRLSTIRS-AQMIYVIKDKKALESGTHE 647
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAA 242
|
250
....*....|....*..
gi 115533592 648 QLMAKKGSLY-RKLVEA 663
Cdd:PRK15134 243 TLFSAPTHPYtQKLLNS 259
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
437-631 |
1.62e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 75.61 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 437 RPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLR-----GQVIGLisqEP 511
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQdllylGHQPGI---KT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 512 VLfatSVEENIRYGRPDA--TDEEVREAARAAhvdefvsrfpsgystvVGERG------AQLSGGQKQRIAIARAILKNP 583
Cdd:PRK13538 88 EL---TALENLRFYQRLHgpGDDEALWEALAQ----------------VGLAGfedvpvRQLSAGQQRRVALARLWLTRA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 115533592 584 PILILDEATSALDSHS-----EHMVQEALNnvmkGRTVLIIAHRLSTIRSAQM 631
Cdd:PRK13538 149 PLWILDEPFTAIDKQGvarleALLAQHAEQ----GGMVILTTHQDLPVASDKV 197
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
425-645 |
1.93e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 77.47 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSY-PTRP-GHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDG----RDLRELNVEW 498
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 499 LRGQViGLISQEP--VLFATSVEENIRYGrPDATDEEVREAAR-AAHVDEFVsrfpsGYSTVVGERGA-QLSGGQKQRIA 574
Cdd:PRK13643 82 VRKKV-GVVFQFPesQLFEETVLKDVAFG-PQNFGIPKEKAEKiAAEKLEMV-----GLADEFWEKSPfELSGGQMRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115533592 575 IARAILKNPPILILDEATSALDSHSEHMVQEALNNVMK-GRTVLIIAHRLSTIRS-AQMIYVIKDKKALESGT 645
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
438-639 |
2.14e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 79.20 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 438 PGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYePK---SGRVTLDGRDLRELNVEWLRGQVIGLISQEPVLF 514
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDTERAGIAIIHQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 515 AT-SVEENI-------RYGRPDaTDEEVREAAR-AAHVDEFVSrfpsgystvVGERGAQLSGGQKQRIAIARAILKNPPI 585
Cdd:PRK13549 95 KElSVLENIflgneitPGGIMD-YDAMYLRAQKlLAQLKLDIN---------PATPVGNLGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 586 LILDEATSALdSHSEhmvQEALNNVMK-----GRTVLIIAHRLSTIRS-AQMIYVIKDKK 639
Cdd:PRK13549 165 LILDEPTASL-TESE---TAVLLDIIRdlkahGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
444-649 |
2.75e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 79.51 E-value: 2.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 444 ENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELN-------------VEWLRGQVIGLISQE 510
Cdd:PRK10261 33 RNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrqvielseqsaaqMRHVRGADMAMIFQE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 511 PV-----LFAT--SVEENIRYGRPDATDEEVREA------ARAAHVDEFVSRFPSgystvvgergaQLSGGQKQRIAIAR 577
Cdd:PRK10261 113 PMtslnpVFTVgeQIAESIRLHQGASREEAMVEAkrmldqVRIPEAQTILSRYPH-----------QLSGGMRQRVMIAM 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115533592 578 AILKNPPILILDEATSALDSHSEHMVQEALNNVMKGRT--VLIIAHRLSTIRS-AQMIYVIKDKKALESGTHEQL 649
Cdd:PRK10261 182 ALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQI 256
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
440-655 |
3.01e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 76.16 E-value: 3.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 440 HTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLR-------ELNV------EWLRGQVIGL 506
Cdd:PRK10619 18 HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgQLKVadknqlRLLRTRLTMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 507 ISQEPVLFATSVEENIR--------YGRPDATDEEVREAARAAHVDEFVSRFPsgystvvgergAQLSGGQKQRIAIARA 578
Cdd:PRK10619 98 FQHFNLWSHMTVLENVMeapiqvlgLSKQEARERAVKYLAKVGIDERAQGKYP-----------VHLSGGQQQRVSIARA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 579 ILKNPPILILDEATSALDShseHMVQEALNNVMK----GRTVLIIAHRLSTIR--SAQMIYVIKDKKAlESGTHEQLMAK 652
Cdd:PRK10619 167 LAMEPEVLLFDEPTSALDP---ELVGEVLRIMQQlaeeGKTMVVVTHEMGFARhvSSHVIFLHQGKIE-EEGAPEQLFGN 242
|
...
gi 115533592 653 KGS 655
Cdd:PRK10619 243 PQS 245
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
420-645 |
3.48e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 76.59 E-value: 3.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 420 SLWGDIKFEDVSFSYPTRpghTVFE-----NLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRvTLDG------ 488
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKK---TPFEfkalnNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQ-TIVGdyaipa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 489 --RDLRElnVEWLRGQvIGLISQEP--VLFATSVEENIRYGrPDATDEEVREAARAahVDEFVS--RFPSGYstvVGERG 562
Cdd:PRK13645 78 nlKKIKE--VKRLRKE-IGLVFQFPeyQLFQETIEKDIAFG-PVNLGENKQEAYKK--VPELLKlvQLPEDY---VKRSP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 563 AQLSGGQKQRIAIARAILKNPPILILDEATSALDSHSEH---MVQEALNNVMKGRTVLIIAHRLSTIRSAQMIYVIKDKK 639
Cdd:PRK13645 149 FELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfiNLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGK 228
|
....*.
gi 115533592 640 ALESGT 645
Cdd:PRK13645 229 VISIGS 234
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
425-649 |
1.09e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 75.51 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSY-PTRPGH-TVFENLTLSIPAGQVVALCGPSGEGKST-ITHL----------LERFYE-----PKSGRVTL 486
Cdd:PRK13651 3 IKVKNIVKIFnKKLPTElKALDNVSVEINQGEFIAIIGQTGSGKTTfIEHLnalllpdtgtIEWIFKdeknkKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 487 DGRDL-------REL-NVEWLRGQViGLISQ--EPVLFATSVEENIRYGrPDATDEEVREA-ARAAHVDEFVSrFPSGYS 555
Cdd:PRK13651 83 VLEKLviqktrfKKIkKIKEIRRRV-GVVFQfaEYQLFEQTIEKDIIFG-PVSMGVSKEEAkKRAAKYIELVG-LDESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 556 tvvgERGA-QLSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMK-GRTVLIIAHRL-STIRSAQMI 632
Cdd:PRK13651 160 ----QRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKqGKTIILVTHDLdNVLEWTKRT 235
|
250
....*....|....*...
gi 115533592 633 YVIKDKKALESG-THEQL 649
Cdd:PRK13651 236 IFFKDGKIIKDGdTYDIL 253
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
425-649 |
1.39e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 76.63 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPtrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQVI 504
Cdd:PRK15439 12 LCARSISKQYS---GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEPVLFAT-SVEENIRYGRPDATDEEVREAARAA----HVDEFVSrfpsgystvvgerGAQLSGGQKQRIAIARAI 579
Cdd:PRK15439 89 YLVPQEPLLFPNlSVKENILFGLPKRQASMQKMKQLLAalgcQLDLDSS-------------AGSLEVADRQIVEILRGL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115533592 580 LKNPPILILDEATSALDSHSEHMVQEALNNVM-KGRTVLIIAHRLSTIRS-AQMIYVIKDKKALESGTHEQL 649
Cdd:PRK15439 156 MRDSRILILDEPTASLTPAETERLFSRIRELLaQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
440-660 |
1.82e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 73.89 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 440 HTVFENLTLSIPAGQVVALCGPSGEGKSTITHLL----------ERFYEPKSGRVTLDGRDLRELNVEwlRGQVIGLISQ 509
Cdd:PRK09984 17 HQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLsglitgdksaGSHIELLGRTVQREGRLARDIRKS--RANTGYIFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 510 EPVLFATSVEENIRYGRPDAT-----------DEEVREAARAahvdefVSRFpsGYSTVVGERGAQLSGGQKQRIAIARA 578
Cdd:PRK09984 95 FNLVNRLSVLENVLIGALGSTpfwrtcfswftREQKQRALQA------LTRV--GMVHFAHQRVSTLSGGQQQRVAIARA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 579 ILKNPPILILDEATSALDSHSEHMVQEALNNVMK--GRTVLIIAHRLS-TIRSAQMIYVIKDKKALESGTHEQLMAKK-G 654
Cdd:PRK09984 167 LMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDNERfD 246
|
....*.
gi 115533592 655 SLYRKL 660
Cdd:PRK09984 247 HLYRSI 252
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
446-650 |
2.78e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 73.04 E-value: 2.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 446 LTLSIPAGQVVALCGPSGEGKSTithLLERF--YEPKSGRVTLDGRDLRELNVEWLRGQVIGLISQEPVLFATSVEENIR 523
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMagLLPGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 524 YGRPDATdeevREAARAAHVDEFVSRFpsGYSTVVGERGAQLSGGQKQRIAIARAILK-----NP--PILILDEATSALD 596
Cdd:PRK03695 92 LHQPDKT----RTEAVASALNEVAEAL--GLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNSLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115533592 597 shsehMVQE-ALNNVMK-----GRTVLIIAHRLS-TIRSAQMIYVIKDKKALESGTHEQLM 650
Cdd:PRK03695 166 -----VAQQaALDRLLSelcqqGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
439-623 |
6.86e-14 |
|
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: 75.82 E-value: 6.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 439 GHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLrELNVEWLRgQVIGLISQEPVLF--AT 516
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVR-QSLGMCPQHNILFhhLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 517 SVEENIRYGRPDATDEEVREAARAAHVDEfvsrfpSGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILILDEATSALD 596
Cdd:TIGR01257 1020 VAEHILFYAQLKGRSWEEAQLEMEAMLED------TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
170 180
....*....|....*....|....*..
gi 115533592 597 SHSEHMVQEALNNVMKGRTVLIIAHRL 623
Cdd:TIGR01257 1094 PYSRRSIWDLLLKYRSGRTIIMSTHHM 1120
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
439-596 |
7.81e-14 |
|
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: 70.15 E-value: 7.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 439 GHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQVIGLISQEPV---LFA 515
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYVPEDRKregLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 516 T-SVEENIRYGRpdatdeevreaaraahvdefvsrfpsgystvvgergaQLSGGQKQRIAIARAILKNPPILILDEATSA 594
Cdd:cd03215 92 DlSVAENIALSS-------------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
..
gi 115533592 595 LD 596
Cdd:cd03215 135 VD 136
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
98-371 |
8.24e-14 |
|
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: 72.69 E-value: 8.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 98 FFAAVVCAILSAYINIQIPLCLGDLVN-----GIVKIIKDES--NNLRSHFEQLKPSALHLMTLYVAQSALT----FLYI 166
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDsftngGMTNITGNSSglNSSAGPFEKLEEEMTLYAYYYLIIGAIVlitaYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 167 TFLTVLGERMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSfklcVSQGLRTFAQTIGCIGSLYFLSPT 246
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEG----IGDKIGVIFQNIATFGTGFIIGFI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 247 ----MTMYTVAVVPGIILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFDNELDKARAMQE 322
Cdd:cd18558 157 rgwkLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGI 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 115533592 323 QLGVGIGLFQAGTNLFLNGMILSVLYGGSNLISKGEMTPGALMSFLVSA 371
Cdd:cd18558 237 KKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSV 285
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
441-599 |
8.97e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 71.35 E-value: 8.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 441 TVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEW---LRGQVIGLISQEPVLFAT- 516
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLRAKHVGFVFQSFMLIPTl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 517 SVEENIRYGRPDATDEEVREAARAAHVDEFVSrfpsgystvVGER----GAQLSGGQKQRIAIARAILKNPPILILDEAT 592
Cdd:PRK10584 104 NALENVELPALLRGESSRQSRNGAKALLEQLG---------LGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADEPT 174
|
....*..
gi 115533592 593 SALDSHS 599
Cdd:PRK10584 175 GNLDRQT 181
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
151-382 |
1.28e-13 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 71.82 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 151 LMTLYVAQSALTFLYITFLTVlgeRMATKMRSDLFQKLLHHDMAFFDSHKSGELSARL--NADVQEFKSSfklcvsQGLR 228
Cdd:cd18568 51 VGIFQILLSAVRQYLLDYFAN---RIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRFqeNQKIRRFLTR------SALT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 229 TF---AQTIGCIGSLYFLSPTMTMYTVAVVPGIILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAME-- 303
Cdd:cd18568 122 TIldlLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAErp 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 304 ---KLESRLfdNELDKARAMQEQLGVGIGLFQAGTNLFLNgmiLSVLYGGSNLISKGEMTPGALMSFLVSAQTIQRSLSQ 380
Cdd:cd18568 202 irwRWENKF--AKALNTRFRGQKLSIVLQLISSLINHLGT---IAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLA 276
|
..
gi 115533592 381 LS 382
Cdd:cd18568 277 LV 278
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
429-652 |
1.46e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 71.58 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 429 DVSFSYPTRPghtVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGR--DLRELNVEWLRGQViGL 506
Cdd:PRK13638 6 DLWFRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQV-AT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 507 ISQEP--VLFATSVEENIRYGRPDATdeeVREAARAAHVDEFVsrfpsgysTVVGERGAQ------LSGGQKQRIAIARA 578
Cdd:PRK13638 82 VFQDPeqQIFYTDIDSDIAFSLRNLG---VPEAEITRRVDEAL--------TLVDAQHFRhqpiqcLSHGQKKRVAIAGA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115533592 579 ILKNPPILILDEATSALDSHSE-HMVQEALNNVMKGRTVLIIAHRLSTIRS-AQMIYVIKDKKALESGTHEQLMAK 652
Cdd:PRK13638 151 LVLQARYLLLDEPTAGLDPAGRtQMIAIIRRIVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFAC 226
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
425-603 |
1.71e-13 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 73.74 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPghTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVtldgrdLRELNVE---WLRG 501
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV------FRSAKVRmavFSQH 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 502 QVIGL-ISQEPVLFATSVeenirygRPDATDEEVReaaraAHVDEFvsrfpsgysTVVGERGAQ----LSGGQKQRIAIA 576
Cdd:PLN03073 581 HVDGLdLSSNPLLYMMRC-------FPGVPEQKLR-----AHLGSF---------GVTGNLALQpmytLSGGQKSRVAFA 639
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 115533592 577 RAILKNPPILILDEATSALD---------------------SHSEHMV 603
Cdd:PLN03073 640 KITFKKPHILLLDEPSNHLDldavealiqglvlfqggvlmvSHDEHLI 687
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
425-627 |
3.58e-13 |
|
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: 72.86 E-value: 3.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRdlrelnvewlrgQVI 504
Cdd:TIGR00954 452 IKFENIPLVTPN--GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAK------------GKL 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEP----------VLFATSVEENIRYGRPDATDEEVREAAraaHVDEFVSRfpSGYSTVVGERGAQLSGGQKQRIA 574
Cdd:TIGR00954 518 FYVPQRPymtlgtlrdqIIYPDSSEDMKRRGLSDKDLEQILDNV---QLTHILER--EGGWSAVQDWMDVLSGGEKQRIA 592
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 115533592 575 IARAILKNPPILILDEATSALDSHSEHMVQEALNNVmkGRTVLIIAHRLSTIR 627
Cdd:TIGR00954 593 MARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKSLWK 643
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
425-651 |
3.95e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 72.14 E-value: 3.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPT--RPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSG----RVTLDGRDLRELNVEw 498
Cdd:TIGR03269 280 IKVRNVSKRYISvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevnvRVGDEWVDMTKPGPD- 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 499 LRGQV---IGLISQEPVLFA-TSVEENIrygrPDATDEEV-REAAR--AAHVDEFVSrFPSGYSTVVGER-GAQLSGGQK 570
Cdd:TIGR03269 359 GRGRAkryIGILHQEYDLYPhRTVLDNL----TEAIGLELpDELARmkAVITLKMVG-FDEEKAEEILDKyPDELSEGER 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 571 QRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMK--GRTVLIIAHRLSTI-----RSAQMiyviKDKKALES 643
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVldvcdRAALM----RDGKIVKI 509
|
....*...
gi 115533592 644 GTHEQLMA 651
Cdd:TIGR03269 510 GDPEEIVE 517
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
436-596 |
4.53e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.20 E-value: 4.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 436 TRPGHTVfENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRG--QVIGLISQEPvl 513
Cdd:PRK10261 334 TREVHAV-EKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQAlrRDIQFIFQDP-- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 514 FAT---------SVEENIRYGRPDATDEEVREAA----RAAHVDEFVSRFPSgystvvgergaQLSGGQKQRIAIARAIL 580
Cdd:PRK10261 411 YASldprqtvgdSIMEPLRVHGLLPGKAAAARVAwlleRVGLLPEHAWRYPH-----------EFSGGQRQRICIARALA 479
|
170
....*....|....*.
gi 115533592 581 KNPPILILDEATSALD 596
Cdd:PRK10261 480 LNPKVIIADEAVSALD 495
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
439-646 |
5.04e-13 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 69.43 E-value: 5.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 439 GHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLL--ERFYEPKSGRVTLDGRDLRELNVEWLRGQVIGLISQEPV---- 512
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPEDRAGEGIFMAFQYPVeipg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 513 -----LFATSVEENIRYGRPDATD-----EEVREAARAAHV-DEFVSRfpsgySTVVGergaqLSGGQKQRIAIARAILK 581
Cdd:PRK09580 93 vsnqfFLQTALNAVRSYRGQEPLDrfdfqDLMEEKIALLKMpEDLLTR-----SVNVG-----FSGGEKKRNDILQMAVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115533592 582 NPPILILDEATSALDSHSEHMVQEALNNVMKG-RTVLIIAH--RLSTIRSAQMIYVIKDKKALESGTH 646
Cdd:PRK09580 163 EPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF 230
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
437-650 |
6.58e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 69.47 E-value: 6.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 437 RPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLE-RFYEPK-------SGRVTLDGRDLRELNVEWLRGQVIGLIS 508
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 509 QEPVLFATSVEENIRYGR-PDATdeevREAARAAHVDEFVSRF--PSGYSTVVGERGAQLSGGQKQRIAIARAILK---- 581
Cdd:PRK13547 91 AAQPAFAFSAREIVLLGRyPHAR----RAGALTHRDGEIAWQAlaLAGATALVGRDVTTLSGGELARVQFARVLAQlwpp 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115533592 582 -----NPPILILDEATSALDSHSEHMVQEALNNVMK--GRTVLIIAHRLS-TIRSAQMIYVIKDKKALESGTHEQLM 650
Cdd:PRK13547 167 hdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNlAARHADRIAMLADGAIVAHGAPADVL 243
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
436-643 |
9.79e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 70.97 E-value: 9.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 436 TRPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKS--GRVTLDG-----RDLRELNVewlRGQVIglIS 508
Cdd:NF040905 10 TFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGevcrfKDIRDSEA---LGIVI--IH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 509 QE----PVLfatSVEENI-------RYGRPD--ATDEEVREAARAAHVDEfvsrFPsgySTVVGERGAqlsgGQKQRIAI 575
Cdd:NF040905 85 QElaliPYL---SIAENIflgneraKRGVIDwnETNRRARELLAKVGLDE----SP---DTLVTDIGV----GKQQLVEI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 576 ARAILKNPPILILDEATSAL-DSHSEHMVQEALNNVMKGRTVLIIAHRLSTIRS-AQMIYVIKDKKALES 643
Cdd:NF040905 151 AKALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIET 220
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
453-633 |
1.67e-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: 65.47 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 453 GQVVALCGPSGEGKSTITHLLERFYEPKSGRV-TLDGRDLRELNVEWLRGqviglisqepvlfatsveenirygrpdatd 531
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGViYIDGEDILEEVLDQLLL------------------------------ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 532 eevreaaraahvdefvsrfpsgysTVVGERGAQLSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEAL---- 607
Cdd:smart00382 52 ------------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrl 107
|
170 180
....*....|....*....|....*....
gi 115533592 608 ---NNVMKGRTVLIIAHRLSTIRSAQMIY 633
Cdd:smart00382 108 lllLKSEKNLTVILTTNDEKDLGPALLRR 136
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
439-637 |
2.04e-12 |
|
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: 69.85 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 439 GHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYE--PKSGRVTLDGRDLRELNVEWLRGQVIGLISQEPVLFAT 516
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAGIVIIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 517 -SVEENIRYGrpdatdEEVREAARAAHVDEFVSRFPSGYSTV------VGERGAQLSGGQKQRIAIARAILKNPPILILD 589
Cdd:TIGR02633 93 lSVAENIFLG------NEITLPGGRMAYNAMYLRAKNLLRELqldadnVTRPVGDYGGGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 115533592 590 EATSALDSHSEHMVQEALNNV-MKGRTVLIIAHRLSTIRS-AQMIYVIKD 637
Cdd:TIGR02633 167 EPSSSLTEKETEILLDIIRDLkAHGVACVYISHKLNEVKAvCDTICVIRD 216
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
444-596 |
2.26e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 67.89 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 444 ENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWlRGQVIGLISQEPvlfATSVEENIR 523
Cdd:PRK15112 30 KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY-RSQRIRMIFQDP---STSLNPRQR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 524 YGR----PDATDEEVREAARAAHVDEFVSRfpsgystvVGERGAQ-------LSGGQKQRIAIARAILKNPPILILDEAT 592
Cdd:PRK15112 106 ISQildfPLRLNTDLEPEQREKQIIETLRQ--------VGLLPDHasyyphmLAPGQKQRLGLARALILRPKVIIADEAL 177
|
....
gi 115533592 593 SALD 596
Cdd:PRK15112 178 ASLD 181
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
424-651 |
2.85e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 68.90 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 424 DIKFEDVSFSYptrpGHTVF-ENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEwLRGq 502
Cdd:PRK11000 3 SVTLRNVTKAY----GDVVIsKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA-ERG- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 503 vIGLISQEPVLFA-TSVEENIRYGRPDA------TDEEVREAARAAHVDEFVSRFPSGystvvgergaqLSGGQKQRIAI 575
Cdd:PRK11000 77 -VGMVFQSYALYPhLSVAENMSFGLKLAgakkeeINQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAI 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115533592 576 ARAILKNPPILILDEATSALDShsehmvqeALNNVMKgrtvlIIAHRLSTIRSAQMIYVikdkkalesgTHEQLMA 651
Cdd:PRK11000 145 GRTLVAEPSVFLLDEPLSNLDA--------ALRVQMR-----IEISRLHKRLGRTMIYV----------THDQVEA 197
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
425-625 |
4.74e-12 |
|
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: 65.34 E-value: 4.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPGH-TVFENLTLSIPAGQVVALCGPSGEGKSTithLLERFYEPK-----SGRVTLDGRdlrELNVEW 498
Cdd:cd03232 4 LTWKNLNYTVPVKGGKrQLLNNISGYVKPGTLTALMGESGAGKTT---LLDVLAGRKtagviTGEILINGR---PLDKNF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 499 LRgqVIGLISQEPVLFatsveenirygrPDATdeeVREAARaahvdefvsrfpsgYSTVVgeRGaqLSGGQKQRIAIARA 578
Cdd:cd03232 78 QR--STGYVEQQDVHS------------PNLT---VREALR--------------FSALL--RG--LSVEQRKRLTIGVE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 115533592 579 ILKNPPILILDEATSALDSHSEHMVQEALNNV-MKGRTVLIIAHRLST 625
Cdd:cd03232 123 LAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLaDSGQAILCTIHQPSA 170
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
442-595 |
4.86e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 66.44 E-value: 4.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 442 VFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQVIGLISQEPVLFA-TSVEE 520
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRRVFSrMTVEE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115533592 521 NIRYGRPDATDEEVREaaRAAHVDEFvsrFPSGYSTVVgERGAQLSGGQKQRIAIARAILKNPPILILDEATSAL 595
Cdd:PRK11614 100 NLAMGGFFAERDQFQE--RIKWVYEL---FPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
433-619 |
6.58e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 68.13 E-value: 6.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 433 SYPTRPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLL--ERfyEPKSGRVTLDGRDLRELNVEWLRGQVIGLISQE 510
Cdd:COG3845 264 SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPRERRRLGVAYIPED 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 511 PVLFAT----SVEENI---RYGRPDATD------EEVREAARAAhVDEFVSRFPSGYSTVvgergAQLSGGQKQRIAIAR 577
Cdd:COG3845 342 RLGRGLvpdmSVAENLilgRYRRPPFSRggfldrKAIRAFAEEL-IEEFDVRTPGPDTPA-----RSLSGGNQQKVILAR 415
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 115533592 578 AILKNPPILILDEATSALDSHSEHMVQEALNNVM-KGRTVLII 619
Cdd:COG3845 416 ELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLI 458
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
425-623 |
1.23e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 65.14 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRpghTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRdlrelnvewLRgqvI 504
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR---I 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEPVLFAT---SVEENIRYgRPDATDEEVREA---ARAAHVDEFVSRfpsgystvvgergaQLSGGQKQRIAIARA 578
Cdd:PRK09544 70 GYVPQKLYLDTTlplTVNRFLRL-RPGTKKEDILPAlkrVQAGHLIDAPMQ--------------KLSGGETQRVLLARA 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 115533592 579 ILKNPPILILDEATSALDSHSEHMVQEALNNVMK--GRTVLIIAHRL 623
Cdd:PRK09544 135 LLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDL 181
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
429-592 |
1.27e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 67.35 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 429 DVSFSYPTR---PGHTVFE--NLT---------LSIPAGQVVALCGPSGEGKSTITHLLerF--YEPKSGRVTLDGRDLR 492
Cdd:COG1129 240 ELEDLFPKRaaaPGEVVLEveGLSvggvvrdvsFSVRAGEILGIAGLVGAGRTELARAL--FgaDPADSGEIRLDGKPVR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 493 ELNVE--WLRGqvIGLIS----QEPVLFATSVEENI---------RYGRpdatdeeVREAARAAHVDEFVSRF---PSGY 554
Cdd:COG1129 318 IRSPRdaIRAG--IAYVPedrkGEGLVLDLSIRENItlasldrlsRGGL-------LDRRRERALAEEYIKRLrikTPSP 388
|
170 180 190
....*....|....*....|....*....|....*...
gi 115533592 555 STVVGergaQLSGGQKQRIAIARAILKNPPILILDEAT 592
Cdd:COG1129 389 EQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
417-621 |
1.31e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 67.30 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 417 PYHSLWGDIKFEDVSFSYPTRPGHTVFENLTLSipAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNV 496
Cdd:PRK10522 315 QAFPDWQTLELRNVTFAYQDNGFSVGPINLTIK--RGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 497 EWLRgQVIGLISQEPVLFatsveenirygrpDATDEEVREAARAAHVDEFVSRFPSGYS-TVVGERGA--QLSGGQKQRI 573
Cdd:PRK10522 393 EDYR-KLFSAVFTDFHLF-------------DQLLGPEGKPANPALVEKWLERLKMAHKlELEDGRISnlKLSKGQKKRL 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 115533592 574 AIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMK--GRTVLIIAH 621
Cdd:PRK10522 459 ALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQemGKTIFAISH 508
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
154-375 |
1.41e-11 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 65.68 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 154 LYVAQSALTFLYITFLTVLGERMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNA--DVQEFKSSfklcvsQGLRTFA 231
Cdd:cd18566 51 AILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERLNSleQIREFLTG------QALLALL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 232 Q---TIGCIGSLYFLSPTMTMytVAVVPGIILAGSAIGAGLRqlSRRAQGQSATASAVSD----EALTNIRTIRAFAMEK 304
Cdd:cd18566 125 DlpfVLIFLGLIWYLGGKLVL--VPLVLLGLFVLVAILLGPI--LRRALKERSRADERRQnfliETLTGIHTIKAMAMEP 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115533592 305 LESRLFDNELDKARAMQEQLGVGIGLFQAGTNLFLNGMILSVLYGGSNLISKGEMTPGALMSF-LVSAQTIQ 375
Cdd:cd18566 201 QMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLVINGDLTVGALIACtMLSGRVLQ 272
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
154-368 |
1.88e-11 |
|
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: 65.56 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 154 LYVAQSALTFLYITFLTVLGERMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNA--DVQEFkssfklcVSQGLRTF- 230
Cdd:cd18567 51 LLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFEKRHLGDIVSRFGSldEIQQT-------LTTGFVEAl 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 231 ---AQTIGCIGSLYFLSPTMTMytvavvpgIILAGSAIGAGLRQLS----RRAQGQSATASAVSD----EALTNIRTIRA 299
Cdd:cd18567 124 ldgLMAILTLVMMFLYSPKLAL--------IVLAAVALYALLRLALypplRRATEEQIVASAKEQshflETIRGIQTIKL 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115533592 300 FAMEKLESRLFDNELdkARAMQEQLGVG-IGLFQAGTNLFLNGMI-LSVLYGGSNLISKGEMTPGALMSFL 368
Cdd:cd18567 196 FGREAEREARWLNLL--VDAINADIRLQrLQILFSAANGLLFGLEnILVIYLGALLVLDGEFTVGMLFAFL 264
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
430-621 |
1.97e-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: 66.88 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 430 VSFSYPtrPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDgrdlrelnvewlRGQVIGLISQ 509
Cdd:TIGR03719 10 VSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ------------PGIKVGYLPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 510 EPVLFAT-SVEENI-------------------RYGRPDA----------TDEEVREAARAAHVDEFVS------RFPSG 553
Cdd:TIGR03719 76 EPQLDPTkTVRENVeegvaeikdaldrfneisaKYAEPDAdfdklaaeqaELQEIIDAADAWDLDSQLEiamdalRCPPW 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115533592 554 YSTVvgergAQLSGGQKQRIAIARAILKNPPILILDEATSALDSHS----EHMVQEalnnvMKGrTVLIIAH 621
Cdd:TIGR03719 156 DADV-----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQE-----YPG-TVVAVTH 216
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
151-375 |
2.04e-11 |
|
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: 65.21 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 151 LMTLYVAQSALTFLYITFLTVLGERMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLN--ADVQEF--KSSFKLCVSqg 226
Cdd:cd18588 48 LLVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFESRQVGDTVARVRelESIRQFltGSALTLVLD-- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 227 lrtFAQTIGCIGSLYFLSPTMTMYTVAVVPGIILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLE 306
Cdd:cd18588 126 ---LVFSVVFLAVMFYYSPTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQF 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115533592 307 SRLFDNELdkARAMQEQLGVGI--GLFQAGTNLFLNGMILSVLYGGSNLISKGEMTPGALMSF-LVSAQTIQ 375
Cdd:cd18588 203 QRRWEELL--ARYVKASFKTANlsNLASQIVQLIQKLTTLAILWFGAYLVMDGELTIGQLIAFnMLAGQVSQ 272
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
424-623 |
2.69e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 65.52 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 424 DIKFEDVSFSYPTrpGH-TVFENLTLSIPAGQVVALCGPSGEGKS----TITHLLerfyePKSGRVT----LDGRDL--- 491
Cdd:PRK09473 14 DVKDLRVTFSTPD--GDvTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLL-----AANGRIGgsatFNGREIlnl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 492 --RELNVewLRGQVIGLISQEPVlfaTSVEENIR--------------YGRPDATDEEVR--EAARAAHVDEFVSRFPSg 553
Cdd:PRK09473 87 peKELNK--LRAEQISMIFQDPM---TSLNPYMRvgeqlmevlmlhkgMSKAEAFEESVRmlDAVKMPEARKRMKMYPH- 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115533592 554 ystvvgergaQLSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMK--GRTVLIIAHRL 623
Cdd:PRK09473 161 ----------EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDL 222
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
441-651 |
3.09e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.44 E-value: 3.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 441 TVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKS--GRVTLDGRDLRELNVewlrgQVIGLISQEPVLFA-TS 517
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQIL-----KRTGFVTQDDILYPhLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 518 VEENI------RYGRPDATDEEVREAaraahvDEFVSRF--PSGYSTVVGE---RGaqLSGGQKQRIAIARAILKNPPIL 586
Cdd:PLN03211 157 VRETLvfcsllRLPKSLTKQEKILVA------ESVISELglTKCENTIIGNsfiRG--ISGGERKRVSIAHEMLINPSLL 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115533592 587 ILDEATSALDSHSEH-MVQEALNNVMKGRTVLIIAHRLSTiRSAQM---IYVIKDKKALESGTHEQLMA 651
Cdd:PLN03211 229 ILDEPTSGLDATAAYrLVLTLGSLAQKGKTIVTSMHQPSS-RVYQMfdsVLVLSEGRCLFFGKGSDAMA 296
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
425-621 |
4.46e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 65.59 E-value: 4.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPtrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERF--YEPKSGRV----------------TL 486
Cdd:TIGR03269 1 IEVKNLTKKFD---GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 487 DGR-------DLRELNVE-W-----LRGQV---IGLISQEPvlFA----TSVEENIRYGRPDATDEEVREAARAAHVDEF 546
Cdd:TIGR03269 78 VGEpcpvcggTLEPEEVDfWnlsdkLRRRIrkrIAIMLQRT--FAlygdDTVLDNVLEALEEIGYEGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 547 VSrfpsgystvVGER----GAQLSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMK--GRTVLIIA 620
Cdd:TIGR03269 156 VQ---------LSHRithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMVLTS 226
|
.
gi 115533592 621 H 621
Cdd:TIGR03269 227 H 227
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
450-597 |
6.34e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.90 E-value: 6.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 450 IPAGQVVALCGPSGEGKST----ITHLLERFYEPKSGRVTLDGRDLRELnVEWLRGQVIgLISQEPVLFAT-SVEENIRY 524
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITYDGITPEEI-KKHYRGDVV-YNAETDVHFPHlTVGETLDF 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 525 G--------RPDATDEEVReAARAAHVDEFVSRFPSGYSTVVGE---RGaqLSGGQKQRIAIARAILKNPPILILDEATS 593
Cdd:TIGR00956 162 AarcktpqnRPDGVSREEY-AKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGAKIQCWDNATR 238
|
....
gi 115533592 594 ALDS 597
Cdd:TIGR00956 239 GLDS 242
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
442-654 |
1.17e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 62.35 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 442 VFENLTLSIPAGQVVALCGPSGEGKSTITHLLERF--YEPKSGRVTLDGRDLRELNVEwLRGQV-IGLISQEPVLFA-TS 517
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLgIFLAFQYPIEIPgVS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 518 VEENIR---------YGRPDATD----EEVREAARAAHVDE-FVSRFpsgystvVGErgaQLSGGQKQRIAIARAILKNP 583
Cdd:CHL00131 101 NADFLRlaynskrkfQGLPELDPleflEIINEKLKLVGMDPsFLSRN-------VNE---GFSGGEKKRNEILQMALLDS 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115533592 584 PILILDEATSALDSHSEHMVQEALNNVM-KGRTVLIIAH--RLSTIRSAQMIYVIKDKKALESGTHE--QLMAKKG 654
Cdd:CHL00131 171 ELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGDAElaKELEKKG 246
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
438-626 |
1.29e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.25 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 438 PGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQVIGLISQEPVLFAT- 516
Cdd:PRK10762 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIGIIHQELNLIPQl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 517 SVEENIRYGRPDAT-------DEEVREAaraahvDEFVSRFPSGYS--TVVGErgaqLSGGQKQRIAIARAILKNPPILI 587
Cdd:PRK10762 95 TIAENIFLGREFVNrfgridwKKMYAEA------DKLLARLNLRFSsdKLVGE----LSIGEQQMVEIAKVLSFESKVII 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 115533592 588 LDEATSAL-DSHSehmvqEALNNVMK-----GRTVLIIAHRLSTI 626
Cdd:PRK10762 165 MDEPTDALtDTET-----ESLFRVIRelksqGRGIVYISHRLKEI 204
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
421-650 |
1.56e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 62.25 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 421 LWGDIK-FEDVSFS-YPtrpghtvfenltlsipaGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRD--LRELN- 495
Cdd:PRK11701 15 LYGPRKgCRDVSFDlYP-----------------GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqLRDLYa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 496 -----------VEW----------LRGQV-----IGlisqEPvLFATSVEEnirYG--RPDATD--EEVR-EAARaahVD 544
Cdd:PRK11701 78 lseaerrrllrTEWgfvhqhprdgLRMQVsaggnIG----ER-LMAVGARH---YGdiRATAGDwlERVEiDAAR---ID 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 545 EFVSRFpsgystvvgergaqlSGGQKQRIAIARAILKNPPILILDEATSALDSHsehmVQEALNNVMKGRT------VLI 618
Cdd:PRK11701 147 DLPTTF---------------SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVS----VQARLLDLLRGLVrelglaVVI 207
|
250 260 270
....*....|....*....|....*....|...
gi 115533592 619 IAHRLSTIRS-AQMIYVIKDKKALESGTHEQLM 650
Cdd:PRK11701 208 VTHDLAVARLlAHRLLVMKQGRVVESGLTDQVL 240
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
147-381 |
2.04e-10 |
|
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: 62.15 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 147 SALHLMTLYVA-----QSALTFLYITFLTVLGERMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNA--DVQEFKSsf 219
Cdd:cd18783 39 STLYVLTIGVViallfEGILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAGVLTKHMQQieRIRQFLT-- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 220 klcvSQGLRTFAQTIGCIG---SLYFLSPTMTMYTVA---VVPGIILAGSAIgagLRQLSRRAQGQSATASAVSDEALTN 293
Cdd:cd18783 117 ----GQLFGTLLDATSLLVflpVLFFYSPTLALVVLAfsaLIALIILAFLPP---FRRRLQALYRAEGERQAFLVETVHG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 294 IRTIRAFAMEKLESRLFDNELdkARAMQEQLGVG-IGLFQAGTNLFLN-GMILSVLYGGSNLISKGEMTPGALMSFLVSA 371
Cdd:cd18783 190 IRTVKSLALEPRQRREWDERV--ARAIRARFAVGrLSNWPQTLTGPLEkLMTVGVIWVGAYLVFAGSLTVGALIAFNMLA 267
|
250
....*....|
gi 115533592 372 QTIQRSLSQL 381
Cdd:cd18783 268 GRVAGPLVQL 277
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
97-386 |
2.78e-10 |
|
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: 61.73 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 97 WFFAAVVCAILSAYINIQIPLCLGDLVNGIVKiikdesnnlRSHFEQLKPSALHLMTLYVAQSALTFLYITFLTVLGERM 176
Cdd:cd18540 3 LLILLIILMLLVALLDAVFPLLTKYAIDHFIT---------PGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 177 ATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFKLCVSQGLRTFAQTIGCIGSLYFLSPTMTMYTVAVVP 256
Cdd:cd18540 74 SYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 257 GIILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFDNeldKARAMQEQlGVGIGLFQAgtn 336
Cdd:cd18540 154 VLAVVSIYFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREEKNLREFKE---LTEEMRRA-SVRAARLSA--- 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 115533592 337 LFLNG-MILS------VLYGGSNLISKGEMTPGALMSFLVSAQTIQRSLSQLSIIFG 386
Cdd:cd18540 227 LFLPIvLFLGsiatalVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLA 283
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
445-635 |
3.09e-10 |
|
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: 61.09 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 445 NLTLSIPAGQVVALCGPSGEGKSTITH--LLERFYEPKSGRVTLDGRDLRELNVEWLrGQVIgLISQEPV---------- 512
Cdd:cd03271 13 NIDVDIPLGVLTCVTGVSGSGKSSLINdtLYPALARRLHLKKEQPGNHDRIEGLEHI-DKVI-VIDQSPIgrtprsnpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 513 ----------LFAtSVEENIRYGR------------PDATDEEVREAAraahvdEFVSRFPS-------------GYSTV 557
Cdd:cd03271 91 ytgvfdeireLFC-EVCKGKRYNRetlevrykgksiADVLDMTVEEAL------EFFENIPKiarklqtlcdvglGYIKL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 558 vGERGAQLSGGQKQRIAIARAILK---NPPILILDEATSALDSHSEHMVQEALNN-VMKGRTVLIIAHRLSTIRSAQmiY 633
Cdd:cd03271 164 -GQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRlVDKGNTVVVIEHNLDVIKCAD--W 240
|
..
gi 115533592 634 VI 635
Cdd:cd03271 241 II 242
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
440-622 |
4.58e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.97 E-value: 4.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 440 HTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYepkSGRVTLDGRDLRELNvewlrgqviglISQEpvlfaTSVE 519
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL---KGTPVAGCVDVPDNQ-----------FGRE-----ASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 520 ENIryGRPDATDEEVREAARAahvdefvsrfpsGYSTVVG--ERGAQLSGGQKQRIAIARAILKNPPILILDEATSALDS 597
Cdd:COG2401 104 DAI--GRKGDFKDAVELLNAV------------GLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180
....*....|....*....|....*....
gi 115533592 598 HS----EHMVQEALNNvmKGRTVLIIAHR 622
Cdd:COG2401 170 QTakrvARNLQKLARR--AGITLVVATHH 196
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
151-367 |
5.39e-10 |
|
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: 60.99 E-value: 5.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 151 LMTLYVAQSALTFLYITFLTVLGERMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADV--QEFKSsfklcvSQGLR 228
Cdd:cd18555 48 ILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFENRSSGDLLFRANSNVyiRQILS------NQVIS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 229 TFAQ---TIGCIGSLYFLSPTMTMYTVAVvpGIILAG-SAIGAG-LRQLSRRA-QGQSATASAVSdEALTNIRTIRAFAM 302
Cdd:cd18555 122 LIIDlllLVIYLIYMLYYSPLLTLIVLLL--GLLIVLlLLLTRKkIKKLNQEEiVAQTKVQSYLT-ETLYGIETIKSLGS 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115533592 303 EKLE----SRLFDNELDKARAMQEQLGVgIGLFQAGTNLFLNGMILSVlygGSNLISKGEMTPGALMSF 367
Cdd:cd18555 199 EKNIykkwENLFKKQLKAFKKKERLSNI-LNSISSSIQFIAPLLILWI---GAYLVINGELTLGELIAF 263
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
444-661 |
6.21e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 61.26 E-value: 6.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 444 ENLTLSIPAGQVVALCGPSGEGKST----ITHLLErfyePKSGRVTLDGRDLRELNVEWLR--GQVIGLISQepVLFATS 517
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTtikmLTGILV----PTSGEVRVLGYVPFKRRKEFARriGVVFGQRSQ--LWWDLP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 518 VEENIR-----YGRPDAtdeEVREaaraaHVDEFVSRFPsgystvVGE------RgaQLSGGQKQRIAIARAILKNPPIL 586
Cdd:COG4586 113 AIDSFRllkaiYRIPDA---EYKK-----RLDELVELLD------LGElldtpvR--QLSLGQRMRCELAAALLHRPKIL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115533592 587 ILDEATSALDSHSEHMVQEALN--NVMKGRTVLIIAHRLSTI-RSAQMIYVIKDKKALESGTHEQLmAKKGSLYRKLV 661
Cdd:COG4586 177 FLDEPTIGLDVVSKEAIREFLKeyNRERGTTILLTSHDMDDIeALCDRVIVIDHGRIIYDGSLEEL-KERFGPYKTIV 253
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
425-596 |
1.09e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 61.68 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYptrpGHTV-FENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVewlRGQV 503
Cdd:NF033858 2 ARLEGVSHRY----GKTVaLDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARH---RRAV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 504 IGLISQEPV-----LFAT-SVEENIRY-GR---PDATDEEVR--EAARAAHVDEFVSRfPSGystvvgergaQLSGGQKQ 571
Cdd:NF033858 75 CPRIAYMPQglgknLYPTlSVFENLDFfGRlfgQDAAERRRRidELLRATGLAPFADR-PAG----------KLSGGMKQ 143
|
170 180
....*....|....*....|....*
gi 115533592 572 RIAIARAILKNPPILILDEATSALD 596
Cdd:NF033858 144 KLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
443-596 |
1.53e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.83 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 443 FENLTLSIPAGQVVALCGPSGEGKstiTHLLERFY---EPKSGRVTLDGRDLRELNVE--WLRG--------QVIGLISQ 509
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGR---TELAETLYglrPARGGRIMLNGKEINALSTAqrLARGlvylpedrQSSGLYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 510 EPVLFAT-SVEEN-----IRYGRPDATDEEVREA--ARAAHVDEFVSRfpsgystvvgergaqLSGGQKQRIAIARAILK 581
Cdd:PRK15439 356 APLAWNVcALTHNrrgfwIKPARENAVLERYRRAlnIKFNHAEQAART---------------LSGGNQQKVLIAKCLEA 420
|
170
....*....|....*
gi 115533592 582 NPPILILDEATSALD 596
Cdd:PRK15439 421 SPQLLIVDEPTRGVD 435
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
428-654 |
2.14e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 60.29 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 428 EDVSFSYPTRPghtVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRvtldgrdlrelnVEWLRGQVIGLI 507
Cdd:PRK15064 323 ENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT------------VKWSENANIGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 508 SQEPVL-FATSV---------------EENIR--YGRPDATDEEVREAARAahvdefvsrfpsgystvvgergaqLSGGQ 569
Cdd:PRK15064 388 AQDHAYdFENDLtlfdwmsqwrqegddEQAVRgtLGRLLFSQDDIKKSVKV------------------------LSGGE 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 570 KQRIAIARAILKNPPILILDEATSALDSHSehmvQEALNNVM---KGrTVLIIAHRLSTIRS-AQMIYVIKDKKALE-SG 644
Cdd:PRK15064 444 KGRMLFGKLMMQKPNVLVMDEPTNHMDMES----IESLNMALekyEG-TLIFVSHDREFVSSlATRIIEITPDGVVDfSG 518
|
250
....*....|
gi 115533592 645 THEQLMAKKG 654
Cdd:PRK15064 519 TYEEYLRSQG 528
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
423-621 |
2.22e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.35 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 423 GDIKF--EDVSFSYPtrpGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLdGRDLR-------- 492
Cdd:PRK11147 316 GKIVFemENVNYQID---GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEvayfdqhr 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 493 -ELNVEwlrgqviglisqepvlfaTSVEENIRYGRpdatdEEVREAARAAHVDEFVSRF---PSGYSTVVgergAQLSGG 568
Cdd:PRK11147 392 aELDPE------------------KTVMDNLAEGK-----QEVMVNGRPRHVLGYLQDFlfhPKRAMTPV----KALSGG 444
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 115533592 569 QKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNvMKGrTVLIIAH 621
Cdd:PRK11147 445 ERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDS-YQG-TVLLVSH 495
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
429-622 |
5.30e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.50 E-value: 5.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 429 DVSFSYPTRPghtVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLR-----GQV 503
Cdd:PRK13540 6 ELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKqlcfvGHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 504 IGLisqEPVLfatSVEENIRYG-RPDATDEEVREAARAAHVDEFVSrFPSGYstvvgergaqLSGGQKQRIAIARAILKN 582
Cdd:PRK13540 83 SGI---NPYL---TLRENCLYDiHFSPGAVGITELCRLFSLEHLID-YPCGL----------LSSGQKRQVALLRLWMSK 145
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 115533592 583 PPILILDEATSALDSHS-EHMVQEALNNVMKGRTVLIIAHR 622
Cdd:PRK13540 146 AKLWLLDEPLVALDELSlLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
426-628 |
7.11e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 58.75 E-value: 7.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 426 KFEDVSFSYPTRPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQVIG 505
Cdd:PRK13545 23 KLKDLFFRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 506 LisqepvlfatsveENIRYG--RPDATDEEVREAA----RAAHVDEFVSRFPSGYSTvvgergaqlsgGQKQRIAIARAI 579
Cdd:PRK13545 103 I-------------ENIELKglMMGLTKEKIKEIIpeiiEFADIGKFIYQPVKTYSS-----------GMKSRLGFAISV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 115533592 580 LKNPPILILDEATSALDSHSEHMVQEALNNVM-KGRTVLIIAHRLSTIRS 628
Cdd:PRK13545 159 HINPDILVIDEALSVGDQTFTKKCLDKMNEFKeQGKTIFFISHSLSQVKS 208
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
430-621 |
7.52e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.59 E-value: 7.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 430 VSFSYPtrPGHTVFENLTLSIPAGQVVALCGPSGEGKSTithLLerfyepksgRVtLDGRDlRELNVE-WLR-GQVIGLI 507
Cdd:PRK11819 12 VSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKST---LL---------RI-MAGVD-KEFEGEaRPApGIKVGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 508 SQEPVLFAT-SVEENI-------------------RYGRPDA-TD---------EEVREAARAAHVDEFVS------RFP 551
Cdd:PRK11819 76 PQEPQLDPEkTVRENVeegvaevkaaldrfneiyaAYAEPDAdFDalaaeqgelQEIIDAADAWDLDSQLEiamdalRCP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115533592 552 SGYSTVvgergAQLSGGQKQRIAIARAILKNPPILILDEATSALDSHS----EHMVQEalnnvMKGrTVLIIAH 621
Cdd:PRK11819 156 PWDAKV-----TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESvawlEQFLHD-----YPG-TVVAVTH 218
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
425-625 |
7.60e-09 |
|
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: 58.79 E-value: 7.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRpghTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLdgrdlrelnvewlrGQVI 504
Cdd:TIGR03719 323 IEAENLTKAFGDK---LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI--------------GETV 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLI----SQEPVLFATSVEENIrygrPDATDE----EVREAARAahvdeFVSRFpsgystvvGERGA-------QLSGGQ 569
Cdd:TIGR03719 386 KLAyvdqSRDALDPNKTVWEEI----SGGLDIiklgKREIPSRA-----YVGRF--------NFKGSdqqkkvgQLSGGE 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115533592 570 KQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVmkGRTVLIIAH------RLST 625
Cdd:TIGR03719 449 RNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVISHdrwfldRIAT 508
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
429-596 |
9.12e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.01 E-value: 9.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 429 DVSFSYPTRPghtVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNvewlRGQVIGLIS 508
Cdd:PRK13543 16 ALAFSRNEEP---VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD----RSRFMAYLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 509 QEPVLFAT-SVEENIRY-----GRpdatdeevreaaRAahvdefvSRFPSGYSTVVGERG------AQLSGGQKQRIAIA 576
Cdd:PRK13543 89 HLPGLKADlSTLENLHFlcglhGR------------RA-------KQMPGSALAIVGLAGyedtlvRQLSAGQKKRLALA 149
|
170 180
....*....|....*....|
gi 115533592 577 RAILKNPPILILDEATSALD 596
Cdd:PRK13543 150 RLWLSPAPLWLLDEPYANLD 169
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
444-649 |
1.30e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 57.06 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 444 ENLTLSIPAGQVVALCGPSGEGKS----TITHLLERFYEPKSGRVTLDGRDLRELNvEWLRGQVIG----LISQEP---- 511
Cdd:PRK11022 24 DRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRIS-EKERRNLVGaevaMIFQDPmtsl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 512 ---------VLFATSVEE--NIRYGRPDATD--EEVREAARAAHVDEFvsrfPSgystvvgergaQLSGGQKQRIAIARA 578
Cdd:PRK11022 103 npcytvgfqIMEAIKVHQggNKKTRRQRAIDllNQVGIPDPASRLDVY----PH-----------QLSGGMSQRVMIAMA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115533592 579 ILKNPPILILDEATSALDSHSEHMVQEALNNVMKGR--TVLIIAHRLSTI-RSAQMIYVIKDKKALESGTHEQL 649
Cdd:PRK11022 168 IACRPKLLIADEPTTALDVTIQAQIIELLLELQQKEnmALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
435-597 |
1.84e-08 |
|
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: 54.96 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 435 PTRPGHTVFENLTLSIPAGQVVALCGPSGEGKST----ITHLLERFYEPkSGRVTLDGRDLRElNVEWLRGQVIgLISQE 510
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSV-EGDIHYNGIPYKE-FAEKYPGEII-YVSEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 511 PVLFAT-SVEENIrygrpdatdeevrEAARAAHVDEFVsrfpsgystvvgeRGaqLSGGQKQRIAIARAILKNPPILILD 589
Cdd:cd03233 92 DVHFPTlTVRETL-------------DFALRCKGNEFV-------------RG--ISGGERKRVSIAEALVSRASVLCWD 143
|
....*...
gi 115533592 590 EATSALDS 597
Cdd:cd03233 144 NSTRGLDS 151
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
101-392 |
1.89e-08 |
|
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: 56.35 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 101 AVVCAILSAYINIQIPLCLGDLVNGIVkiikdesnnlrSHFEQLKPSALHLMTLY----VAQSALTFL-YITFLTVlGER 175
Cdd:cd18582 1 ALLLLVLAKLLNVAVPFLLKYAVDALS-----------APASALLAVPLLLLLAYglarILSSLFNELrDALFARV-SQR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 176 MATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFKLCVSQGLRTFAQTIG-CIGSLYFLSPTMTMYTVAV 254
Cdd:cd18582 69 AVRRLALRVFRHLHSLSLRFHLSRKTGALSRAIERGTRGIEFLLRFLLFNILPTILELLLvCGILWYLYGWSYALITLVT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 255 VpGIILAGSAIGAGLRQLSRRAQGQS-ATASAVSDEALTNIRTIRAFAMEKLESRLFDNELDKARAMQEQLGVGIGLFQA 333
Cdd:cd18582 149 V-ALYVAFTIKVTEWRTKFRREMNEAdNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNI 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115533592 334 GTNLFLNGMILSVLYGGSNLISKGEMTPGAlmsfLVSAQTIqrsLSQLSI---IFGTAIKGW 392
Cdd:cd18582 228 GQALIISLGLTAIMLLAAQGVVAGTLTVGD----FVLVNTY---LLQLYQplnFLGFVYREI 282
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
453-626 |
2.81e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.43 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 453 GQVVALCGPSGEGKSTithLLERFYEPKSGRVTLDGRDL---RELNVEWLRgqVIGLISQEPVLFATS-VEENIRYGRPD 528
Cdd:TIGR00956 789 GTLTALMGASGAGKTT---LLNVLAERVTTGVITGGDRLvngRPLDSSFQR--SIGYVQQQDLHLPTStVRESLRFSAYL 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 529 ATDEEVREAARAAHVDEFVS--RFPSGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILI-LDEATSALDSHSEHMVQE 605
Cdd:TIGR00956 864 RQPKSVSKSEKMEYVEEVIKllEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICK 943
|
170 180
....*....|....*....|..
gi 115533592 606 ALNNVMK-GRTVLIIAHRLSTI 626
Cdd:TIGR00956 944 LMRKLADhGQAILCTIHQPSAI 965
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
179-398 |
3.25e-08 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 55.50 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 179 KMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFKLCVSQGLRTFAQTIGCIGSLYFLSPTMTMYTVAVVPGI 258
Cdd:cd18554 80 DIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 259 ILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFDNELDKAramqEQLGVGIGLFQAGTNLF 338
Cdd:cd18554 160 ILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHF----LTRALKHTRWNAKTFSA 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115533592 339 LNGMI----LSVLYGGSNLISKGEMTPGALMSFLVSAQTIQRSLSQLSIIFGTAIKGWTAGGRV 398
Cdd:cd18554 236 VNTITdlapLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
535-664 |
4.32e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.51 E-value: 4.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 535 REAARAaHVDEFVSRFpsGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNVMK-G 613
Cdd:NF000106 118 RKDARA-RADELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRdG 194
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 115533592 614 RTVLIIAHRLSTIRS-AQMIYVIKDKKALESGTHEQLMAKKGSLYRKLVEAH 664
Cdd:NF000106 195 ATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKVGGRTLQIRPAH 246
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
448-623 |
6.06e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.97 E-value: 6.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 448 LSIP-AGQVVALCGPSGEGKSTITHLLERFYEPKSGRVtldgrdlrELNVEWlrgqviglisqEPVL-----------FA 515
Cdd:PRK13409 93 LPIPkEGKVTGILGPNGIGKTTAVKILSGELIPNLGDY--------EEEPSW-----------DEVLkrfrgtelqnyFK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 516 TSVEENIRYGR--------PDATDEEVREAARAAH----VDEFVSRFpsGYSTVVGERGAQLSGGQKQRIAIARAILKNP 583
Cdd:PRK13409 154 KLYNGEIKVVHkpqyvdliPKVFKGKVRELLKKVDergkLDEVVERL--GLENILDRDISELSGGELQRVAIAAALLRDA 231
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 115533592 584 PILILDEATSALDSHSEHMVQEALNNVMKGRTVLIIAHRL 623
Cdd:PRK13409 232 DFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
444-596 |
9.89e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.01 E-value: 9.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 444 ENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLRGQVIGLISQEP----VLFATSVE 519
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYISEDRkrdgLVLGMSVK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 520 EN-----IRY-----GRPDATDEevREAaraahVDEFVSRF----PSgYSTVVGErgaqLSGGQKQRIAIARAILKNPPI 585
Cdd:PRK10762 349 ENmsltaLRYfsragGSLKHADE--QQA-----VSDFIRLFniktPS-MEQAIGL----LSGGNQQKVAIARGLMTRPKV 416
|
170
....*....|.
gi 115533592 586 LILDEATSALD 596
Cdd:PRK10762 417 LILDEPTRGVD 427
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
437-624 |
1.28e-07 |
|
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: 53.14 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 437 RPGHTVFENLTLSIPA-GQVVALCGPSGEGKSTITHLLE--------RFYEPKSGRVTLD---GRDLRELNVEWLRGQVI 504
Cdd:cd03236 9 RYGPNSFKLHRLPVPReGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFTKLLEGDVK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLIS-----QEPVLFATSVEENIrygrpDATDEevREAaraahVDEFVSRFpsGYSTVVGERGAQLSGGQKQRIAIARAI 579
Cdd:cd03236 89 VIVKpqyvdLIPKAVKGKVGELL-----KKKDE--RGK-----LDELVDQL--ELRHVLDRNIDQLSGGELQRVAIAAAL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 115533592 580 LKNPPILILDEATSALDSHSEHMVQEALNNVMK-GRTVLIIAHRLS 624
Cdd:cd03236 155 ARDADFYFFDEPSSYLDIKQRLNAARLIRELAEdDNYVLVVEHDLA 200
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
443-626 |
1.38e-07 |
|
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: 54.79 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 443 FENLTLSIPAGQ-----VVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRdlrelnvewlrgqviglISQEPvlfats 517
Cdd:COG1245 351 YGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-----------------ISYKP------ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 518 veeniRYGRPDaTDEEVREAARAAHVDEFVSrfpSGYSTVVGER----------GAQLSGGQKQRIAIARAILKNPPILI 587
Cdd:COG1245 408 -----QYISPD-YDGTVEEFLRSANTDDFGS---SYYKTEIIKPlgleklldknVKDLSGGELQRVAIAACLSRDADLYL 478
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 115533592 588 LDEATSALDSHSEHMVQEALNNVM--KGRTVLIIAHRLSTI 626
Cdd:COG1245 479 LDEPSAHLDVEQRLAVAKAIRRFAenRGKTAMVVDHDIYLI 519
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
156-367 |
1.84e-07 |
|
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350013 [Multi-domain] Cd Length: 294 Bit Score: 53.25 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 156 VAQSALTFLYITFLTVLGERMATKMRSDLFQKLLHHDMAFFDSHKSGELSAR--LNADVQEFKSSfklcvsqglrTFAQT 233
Cdd:cd18569 53 LLQGLLTWLQQYYLLRLETKLALSSSSRFFWHVLRLPVEFFSQRYAGDIASRvqSNDRVANLLSG----------QLATT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 234 -IGCIGSLYFL------SPTMTMYTVAVVPGIILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEK-- 304
Cdd:cd18569 123 vLNLVMAVFYAllmlqyDVPLTLIGIAIALLNLLVLRLVSRKRVDLNRRLLQDSGKLTGTTMSGLQMIETLKASGAESdf 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115533592 305 ------LESRLFDNELDKARAMQeQLGVGIGLFQAGTNLflngMILSVlygGSNLISKGEMTPGALMSF 367
Cdd:cd18569 203 fsrwagYQAKVLNAQQELGRTNQ-LLGALPTLLSALTNA----AILGL---GGLLVMDGALTIGMLVAF 263
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
445-596 |
1.87e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 54.36 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 445 NLTLSIPAGQVVALCGPSGEGKST----ITHLLErfyePKSGRVTLDGR--DLRELNVewlRGQViGLISQEPVLFAT-S 517
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTtmkmLTGLLP----ASEGEAWLFGQpvDAGDIAT---RRRV-GYMSQAFSLYGElT 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 518 VEENIR-----YGRPdatdeevrEAARAAHVDEFVSRFpsGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILILDEAT 592
Cdd:NF033858 356 VRQNLElharlFHLP--------AAEIAARVAEMLERF--DLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
....
gi 115533592 593 SALD 596
Cdd:NF033858 426 SGVD 429
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
425-639 |
2.16e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.02 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRpghTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDgrdlrelnvewlRGQVI 504
Cdd:PRK10636 313 LKMEKVSAGYGDR---IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA------------KGIKL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEPVLFATSVEENIRY-GR--PDATDEEVREaaraahvdeFVSRFpsGYS-TVVGERGAQLSGGQKQRIAIARAIL 580
Cdd:PRK10636 378 GYFAQHQLEFLRADESPLQHlARlaPQELEQKLRD---------YLGGF--GFQgDKVTEETRRFSGGEKARLVLALIVW 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 581 KNPPILILDEATSALDSHSEHMVQEALNNvMKGRTVlIIAHRLSTIRS-AQMIYVIKDKK 639
Cdd:PRK10636 447 QRPNLLLLDEPTNHLDLDMRQALTEALID-FEGALV-VVSHDRHLLRStTDDLYLVHDGK 504
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
448-625 |
3.09e-07 |
|
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: 53.63 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 448 LSIP-AGQVVALCGPSGEGKSTITHLLerfyepkSGRVTLD-GRDLRElnVEW------LRGQVIglisQEpvLFATSVE 519
Cdd:COG1245 93 LPVPkKGKVTGILGPNGIGKSTALKIL-------SGELKPNlGDYDEE--PSWdevlkrFRGTEL----QD--YFKKLAN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 520 ENIRYGR--------PDATDEEVREAARAAH----VDEFVSRFpsGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILI 587
Cdd:COG1245 158 GEIKVAHkpqyvdliPKVFKGTVRELLEKVDergkLDELAEKL--GLENILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 115533592 588 LDEATSALDShSEHM-----VQEALNnvmKGRTVLIIAHRLST 625
Cdd:COG1245 236 FDEPSSYLDI-YQRLnvarlIRELAE---EGKYVLVVEHDLAI 274
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
445-632 |
3.20e-07 |
|
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: 50.78 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 445 NLTLSIPAGQVVALCGPSGEGKSTIthLLERFYEPKSGRVTldgrDLRELNvewlrgqvigliSQEPVLFATSVEENIRY 524
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYASGKARLI----SFLPKF------------SRNKLIFIDQLQFLIDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 525 GRpdatdeevreaaraahvdefvsrfpsGYSTVvGERGAQLSGGQKQRIAIARAILKNPP--ILILDEATSALDSHSEHM 602
Cdd:cd03238 75 GL--------------------------GYLTL-GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQ 127
|
170 180 190
....*....|....*....|....*....|.
gi 115533592 603 VQEALNN-VMKGRTVLIIAHRLSTIRSAQMI 632
Cdd:cd03238 128 LLEVIKGlIDLGNTVILIEHNLDVLSSADWI 158
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
396-626 |
4.88e-07 |
|
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: 52.90 E-value: 4.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 396 GRvlQFSRLEPSIPMDTGVCIpyhslwgdIKFEDVSFSYPTRPGHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLER 475
Cdd:TIGR02633 239 GR--EITSLYPHEPHEIGDVI--------LEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 476 FYEPK-SGRVTLDGRDLRELNVEWLRGQVIGLISQE-------PVLfatSVEENI------RY---GRPDATDEE--VRE 536
Cdd:TIGR02633 309 AYPGKfEGNVFINGKPVDIRNPAQAIRAGIAMVPEDrkrhgivPIL---GVGKNItlsvlkSFcfkMRIDAAAELqiIGS 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 537 AARAAHVDEFVSRFPSGystvvgergaQLSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNN-VMKGRT 615
Cdd:TIGR02633 386 AIQRLKVKTASPFLPIG----------RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVA 455
|
250
....*....|.
gi 115533592 616 VLIIAHRLSTI 626
Cdd:TIGR02633 456 IIVVSSELAEV 466
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
443-621 |
6.01e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.59 E-value: 6.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 443 FENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDgrdlrelnvewlRGQVIGLISQE------------ 510
Cdd:PRK15064 17 FENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD------------PNERLGKLRQDqfafeeftvldt 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 511 -----PVLFATSVEENIRYGRPDATDEEvreaarAAHVDEFVSRFPS--GYS--TVVGE--RGA------------QLSG 567
Cdd:PRK15064 85 vimghTELWEVKQERDRIYALPEMSEED------GMKVADLEVKFAEmdGYTaeARAGEllLGVgipeeqhyglmsEVAP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 115533592 568 GQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNNvmKGRTVLIIAH 621
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNE--RNSTMIIISH 210
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
445-649 |
1.46e-06 |
|
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: 51.55 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 445 NLTLSIPAGQVVALCGPSGEGKSTITH--LLERFYEPKSGRVTLDGRDLRELNVEWLrGQVIgLISQEPV---------- 512
Cdd:TIGR00630 626 NITVSIPLGLFTCITGVSGSGKSTLINdtLYPALANRLNGAKTVPGRYTSIEGLEHL-DKVI-HIDQSPIgrtprsnpat 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 513 ----------LFATSVEE------------NIRYGR-----------------PDAT----------------------- 530
Cdd:TIGR00630 704 ytgvfdeireLFAETPEAkvrgytpgrfsfNVKGGRceacqgdgvikiemhflPDVYvpcevckgkrynretlevkykgk 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 531 ------DEEVREAAraahvdEFVSRFPS-------------GYSTVvGERGAQLSGGQKQRIAIARAILK---NPPILIL 588
Cdd:TIGR00630 784 niadvlDMTVEEAY------EFFEAVPSisrklqtlcdvglGYIRL-GQPATTLSGGEAQRIKLAKELSKrstGRTLYIL 856
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 589 DEATSALDSHSEHMVQEALNN-VMKGRTVLIIAHRLSTIRSAQmiYVI--------KDKKALESGTHEQL 649
Cdd:TIGR00630 857 DEPTTGLHFDDIKKLLEVLQRlVDKGNTVVVIEHNLDVIKTAD--YIIdlgpeggdGGGTVVASGTPEEV 924
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
425-657 |
1.54e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 51.94 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPGHTVfENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRElNVEWLRgQVI 504
Cdd:TIGR01257 1938 LRLNELTKVYSGTSSPAV-DRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVH-QNM 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 505 GLISQEPVL--FATSVEENIRYGRPDATDEEVREAARAAHVDEFvsrfpsGYSTVVGERGAQLSGGQKQRIAIARAILKN 582
Cdd:TIGR01257 2015 GYCPQFDAIddLLTGREHLYLYARLRGVPAEEIEKVANWSIQSL------GLSLYADRLAGTYSGGNKRKLSTAIALIGC 2088
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115533592 583 PPILILDEATSALDSHSEHMVQEALNNVMK-GRTVLIIAHRLSTIRSAQMIYVIKDKKALES-GTHEQLMAKKGSLY 657
Cdd:TIGR01257 2089 PPLVLLDEPTTGMDPQARRMLWNTIVSIIReGRAVVLTSHSMEECEALCTRLAIMVKGAFQClGTIQHLKSKFGDGY 2165
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
237-365 |
2.25e-06 |
|
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: 49.91 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 237 IGSLYFLSPTMTMYTVAVVPGIILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEKLESRLFDNELDK 316
Cdd:cd18586 130 LAVIFLIHPPLGWVALVGAPVLVGLAWLNHRATRKPLGEANEAQAARDALAAETLRNAETIKALGMLGNLRRRWEARHAE 209
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 115533592 317 ARAMQEQLGVGIGLFQAGTNLFLNGMILSVLYGGSNLISKGEMTPGALM 365
Cdd:cd18586 210 TLELQIRASDLAGAISAIGKTLRMALQSLILGVGAYLVIDGELTIGALI 258
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
447-621 |
2.34e-06 |
|
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: 49.33 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 447 TLSIPAG-----QVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDlrelnvewlrgqviglISQEPvlfatsveen 521
Cdd:cd03237 14 TLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT----------------VSYKP---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 522 iRYGRPDaTDEEVREAARAAHVDEFVSRF-------PSGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILILDEATSA 594
Cdd:cd03237 68 -QYIKAD-YEGTVRDLLSSITKDFYTHPYfkteiakPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAY 145
|
170 180
....*....|....*....|....*....
gi 115533592 595 LDSHSEHMVQEALNNVM--KGRTVLIIAH 621
Cdd:cd03237 146 LDVEQRLMASKVIRRFAenNEKTAFVVEH 174
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
444-636 |
2.44e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.98 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 444 ENLTLSIPAGQVVALCGPSGEGKS-----TITHLLERFYEPKS-----------GRVT-----LDGR------------- 489
Cdd:PRK00635 612 KDLTISLPLGRLTVVTGVSGSGKSslindTLVPAVEEFIEQGFcsnlsiqwgaiSRLVhitrdLPGRsqrsipltyikaf 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 490 -DLRELNVEWLRGQVIGLI--------------------------SQEPV--------LFATSVEEnIRYGRPDATDEEV 534
Cdd:PRK00635 692 dDLRELFAEQPRSKRLGLTkshfsfntplgacaecqglgsitttdNRTSIpcpsclgkRFLPQVLE-VRYKGKNIADILE 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 535 REAARAahvDEFVSRFPSGYSTV------------VGERGAQLSGGQKQRIAIARAIL---KNPPILILDEATSALDSHS 599
Cdd:PRK00635 771 MTAYEA---EKFFLDEPSIHEKIhalcslgldylpLGRPLSSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHD 847
|
250 260 270
....*....|....*....|....*....|....*...
gi 115533592 600 EHMVQEALNNVM-KGRTVLIIAHRLSTIRSAQmiYVIK 636
Cdd:PRK00635 848 IKALIYVLQSLThQGHTVVIIEHNMHVVKVAD--YVLE 883
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
444-667 |
4.15e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.63 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 444 ENLTLSIP-----AGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEwlrgQVIGLISQEPVLFAT-- 516
Cdd:PRK10938 15 DTKTLQLPsltlnAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFE----QLQKLVSDEWQRNNTdm 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 517 -SVEENiRYGRPDA--TDEEVREAARAAhvdEFVSRFpsGYSTVVGERGAQLSGGQKQRIAIARAILKNPPILILDEATS 593
Cdd:PRK10938 91 lSPGED-DTGRTTAeiIQDEVKDPARCE---QLAQQF--GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115533592 594 ALDSHSEHMVQEALNNVM-KGRTVLIIAHRLSTIRS-AQMIYVIKDKKALESGTHEQLMAKkgSLYRKLVEAHNVD 667
Cdd:PRK10938 165 GLDVASRQQLAELLASLHqSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ--ALVAQLAHSEQLE 238
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
450-626 |
9.44e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.65 E-value: 9.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 450 IPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGRdlrelnvewlrgqviglISQEPvlfatsveeniRYGRPDa 529
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK-----------------ISYKP-----------QYIKPD- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 530 TDEEVREAARAAHVD--------EFVSRF--PSGYSTVVGErgaqLSGGQKQRIAIARAILKNPPILILDEATSALDSHS 599
Cdd:PRK13409 413 YDGTVEDLLRSITDDlgssyyksEIIKPLqlERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQ 488
|
170 180
....*....|....*....|....*....
gi 115533592 600 EHMVQEALNNVMKGR--TVLIIAHRLSTI 626
Cdd:PRK13409 489 RLAVAKAIRRIAEEReaTALVVDHDIYMI 517
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
425-626 |
1.04e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.47 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRPghtVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYePK--SGRVTLDGRDLRELNVEWLRGQ 502
Cdd:PRK10938 261 IVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDH-PQgySNDLTLFGRRRGSGETIWDIKK 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 503 VIGLISQEPVL---FATSVEENIRYGRPDATD--EEVREAARAAhVDEFVSRFpsGYSTVVGERGAQ-LSGGQkQRIA-I 575
Cdd:PRK10938 337 HIGYVSSSLHLdyrVSTSVRNVILSGFFDSIGiyQAVSDRQQKL-AQQWLDIL--GIDKRTADAPFHsLSWGQ-QRLAlI 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115533592 576 ARAILKNPPILILDEATSALDSHSEHMVQEALNN-VMKGRTVLI------------IAHRLSTI 626
Cdd:PRK10938 413 VRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQLLfvshhaedapacITHRLEFV 476
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
396-596 |
1.22e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.39 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 396 GRVLqfSRLEPSIPMDTGVCIpyhslwgdIKFEDVSFSYPTRPGHTVFENLTLSIPAGQVVALCGPSGEGKS-TITHLLE 474
Cdd:PRK13549 241 GREL--TALYPREPHTIGEVI--------LEVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTeLVQCLFG 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 475 RFYEPKSGRVTLDGRDLRELNVEWLRGQVIGLISQE-------PVLfatSVEENI------RYGRPDATDEevreAARAA 541
Cdd:PRK13549 311 AYPGRWEGEIFIDGKPVKIRNPQQAIAQGIAMVPEDrkrdgivPVM---GVGKNItlaaldRFTGGSRIDD----AAELK 383
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 115533592 542 HVDEFVSRF----PSGYSTVvgergAQLSGGQKQRIAIARAILKNPPILILDEATSALD 596
Cdd:PRK13549 384 TILESIQRLkvktASPELAI-----ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
557-624 |
1.32e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 48.69 E-value: 1.32e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 557 VVGERGAQ-LSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEAL-NNVMKGRTVLIIAHRLS 624
Cdd:PLN03140 1011 IVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPS 1080
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
564-636 |
2.08e-05 |
|
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: 45.43 E-value: 2.08e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115533592 564 QLSGGQKQRIAIARAI----LKNPPILILDEATSALDSHSEHMVQEALN-NVMKGRTVLIIAHRLSTIRSAQMIYVIK 636
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILeHLVKGAQVIVITHLPELAELADKLIHIK 154
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
175-369 |
2.19e-05 |
|
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: 46.70 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 175 RMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFklcvsqgLRTFAQTI-------GCIGSLYFLSPTM 247
Cdd:cd18585 65 RLLSNLRVWFYRKLEPLAPARLQKYRSGDLLNRIVADIDTLDNLY-------LRVLSPPVvallvilATILFLAFFSPAL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 248 TMYTVA-------VVPGII-LAGSAIGAGLRQLsrRAQGQSATAsavsdEALTNIRTIRAF-AMEKLESRLFDNElDKAR 318
Cdd:cd18585 138 ALILLAglllagvVIPLLFyRLGKKIGQQLVQL--RAELRTELV-----DGLQGMAELLIFgALERQRQQLEQLS-DALI 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 115533592 319 AMQEQLGVGIGLFQAGTNLFLNGMILSVLYGGSNLISKGEMtPGALMSFLV 369
Cdd:cd18585 210 KEQRRLARLSGLSQALMILLSGLTVWLVLWLGAPLVQNGAL-DGALLAMLV 259
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
156-315 |
2.53e-05 |
|
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: 46.73 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 156 VAQSALTFLYITFLTVLGERMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFKLCVSQGLRTFAQTIG 235
Cdd:cd18580 50 LASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 236 CIGSLYFLSPtmtmYTVAVVPGIILAGSAIGAGLRQLSRRAQGQSATA-----SAVSdEALTNIRTIRAFAMEKLESRLF 310
Cdd:cd18580 130 SLIVIAIVSP----YFLIVLPPLLVVYYLLQRYYLRTSRQLRRLESESrsplySHFS-ETLSGLSTIRAFGWQERFIEEN 204
|
....*
gi 115533592 311 DNELD 315
Cdd:cd18580 205 LRLLD 209
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
424-651 |
2.97e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 46.72 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 424 DIKFEDVSFSYPTRPGHTVfENLTLSIPAGQVVALCGPSGEGKSTITHLL----ERFYEPKSGRVTLDGRDLRELNVEWL 499
Cdd:PRK15093 5 DIRNLTIEFKTSDGWVKAV-DRVSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtKDNWRVTADRMRFDDIDLLRLSPRER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 500 R---GQVIGLISQEP---VLFATSVEENIRYGRPDATDEE---VREAARAAHVDEFVSRFP-SGYSTVVGERGAQLSGGQ 569
Cdd:PRK15093 84 RklvGHNVSMIFQEPqscLDPSERVGRQLMQNIPGWTYKGrwwQRFGWRKRRAIELLHRVGiKDHKDAMRSFPYELTEGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 570 KQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALN--NVMKGRTVLIIAHRLSTIRS-AQMIYVIKDKKALESGTH 646
Cdd:PRK15093 164 CQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTrlNQNNNTTILLISHDLQMLSQwADKINVLYCGQTVETAPS 243
|
....*
gi 115533592 647 EQLMA 651
Cdd:PRK15093 244 KELVT 248
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
435-627 |
3.35e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.96 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 435 PTRPGHTVF--ENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVTLDGrdlrELNV----EWLRGQVIGLis 508
Cdd:PRK13546 30 PKHKNKTFFalDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----EVSViaisAGLSGQLTGI-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 509 qepvlfatsveENIRYG------RPDATDEEVREAARAAHVDEFVSRFPSGYSTvvgergaqlsgGQKQRIAIARAILKN 582
Cdd:PRK13546 104 -----------ENIEFKmlcmgfKRKEIKAMTPKIIEFSELGEFIYQPVKKYSS-----------GMRAKLGFSINITVN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 115533592 583 PPILILDEATSALDshsEHMVQEALNNVMK----GRTVLIIAHRLSTIR 627
Cdd:PRK13546 162 PDILVIDEALSVGD---QTFAQKCLDKIYEfkeqNKTIFFVSHNLGQVR 207
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
425-621 |
4.40e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.65 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 425 IKFEDVSFSYPTRpghTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLERFYEPKSGRVT----------------LDG 488
Cdd:PRK11819 325 IEAENLSKSFGDR---LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKigetvklayvdqsrdaLDP 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 489 rdlrELNVeWlrgQVI--GLisqepvlfatsveENIRYGRpdatdeevRE-AARAahvdeFVSRFpsgystvvGERGA-- 563
Cdd:PRK11819 402 ----NKTV-W---EEIsgGL-------------DIIKVGN--------REiPSRA-----YVGRF--------NFKGGdq 439
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115533592 564 -----QLSGGQKQRIAIARaILK---NppILILDEATSALDSHSEHMVQEALNNVmkGRTVLIIAH 621
Cdd:PRK11819 440 qkkvgVLSGGERNRLHLAK-TLKqggN--VLLLDEPTNDLDVETLRALEEALLEF--PGCAVVISH 500
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
565-626 |
4.65e-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: 44.49 E-value: 4.65e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115533592 565 LSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMVQEALNN-VMKG-RTVLIIAHRLSTI 626
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRlSEEGkKTALVVEHDLAVL 135
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
560-638 |
7.85e-05 |
|
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: 44.14 E-value: 7.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 560 ERGaQLSGGQKQ------RIAIARAILKNPPILILDEATSALDshSEHmVQEALNNVM------KGRTVLIIAHRLSTIR 627
Cdd:cd03240 112 MRG-RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLD--EEN-IEESLAEIIeerksqKNFQLIVITHDEELVD 187
|
90
....*....|..
gi 115533592 628 SAQMIY-VIKDK 638
Cdd:cd03240 188 AADHIYrVEKDG 199
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
564-633 |
1.08e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.82 E-value: 1.08e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115533592 564 QLSGGQKQRIAIAR--AILK-NP-PILILDEATSALD-SHSE---HMVQEalnnvMKGRT-VLIIAHRLSTIRSAQMIY 633
Cdd:TIGR02168 1089 LLSGGEKALTALALlfAIFKvKPaPFCILDEVDAPLDdANVErfaNLLKE-----FSKNTqFIVITHNKGTMEVADQLY 1162
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
148-371 |
1.38e-04 |
|
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: 44.46 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 148 ALHLMTLYVAQSALTFLYITFLTVLGERMATKMRSDLFQKLLHHDMAFFDSHKSGELSARL--NADVQEfkssfkLCVSQ 225
Cdd:cd18779 45 GLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLGFLEHLLRLPYRFFQQRSTGDLLMRLssNATIRE------LLTSQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 226 GLRTF---AQTIGCIGSLYFLSPTMtmytVAVVPGIILAGSAIGAGLRQLSRRAQGQSATASAVSD----EALTNIRTIR 298
Cdd:cd18779 119 TLSALldgTLVLGYLALLFAQSPLL----GLVVLGLAALQVALLLATRRRVRELMARELAAQAEAQsylvEALSGIETLK 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 115533592 299 AFAMEK--LE--SRLFDNELDKARAmQEQLGvgiGLFQAGTNLFLNGMILSVLYGGSNLISKGEMTPGALMSFLVSA 371
Cdd:cd18779 195 ASGAEDraLDrwSNLFVDQLNASLR-RGRLD---ALVDALLATLRLAAPLVLLWVGAWQVLDGQLSLGTMLALNALA 267
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
168-364 |
1.71e-04 |
|
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: 43.97 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 168 FLTVLGERMATKMRSDLFQKLLHHDMAFFDShKSGELSARLnadvQEFKSsfklcvsqgLRTF--AQTIGC--------- 236
Cdd:cd18587 65 FIDVAGKRADVILSSRLFERVLGLRLEARPA-SVGSFANNL----REFES---------VRDFftSATLTAlidlpfvll 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 237 -IGSLYFLSPTMTMYTVAVVPGIILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFAMEklesRLFDNELD 315
Cdd:cd18587 131 fLAVIALIGGPLALVPLVAIPLVLLYGLLLQKPLRRLVEESMRESAQKNALLVESLSGLETIKALGAE----GRMQRRWE 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 115533592 316 KARAMQEQLGVGIGLFQA----GTNLFLNGMILSVLYGGSNLISKGEMTPGAL 364
Cdd:cd18587 207 EAVAALARSSLKSRLLSSsatnFAQFVQQLVTVAIVIVGVYLISDGELTMGGL 259
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
455-621 |
2.13e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.08 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 455 VVALCGPSGEGKST----ITHLLE-------------RFYEPKSGRVTL----DGRDLRelnVEWLRGQVIGLISQEP-- 511
Cdd:COG0419 25 LNLIVGPNGAGKSTileaIRYALYgkarsrsklrsdlINVGSEEASVELefehGGKRYR---IERRQGEFAEFLEAKPse 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 512 ------VLFATSVEENIR---YGRPDATDEEVREAARAAHVDEFVSRFPSGYSTVvgergAQLSGGQKQRIAIARAILkn 582
Cdd:COG0419 102 rkealkRLLGLEIYEELKerlKELEEALESALEELAELQKLKQEILAQLSGLDPI-----ETLSGGERLRLALADLLS-- 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 115533592 583 ppiLILDeaTSALDSHSEHMVQEALnnvmkgRTVLIIAH 621
Cdd:COG0419 175 ---LILD--FGSLDEERLERLLDAL------EELAIITH 202
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
524-621 |
2.19e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 524 YGRPDATDEEVREAaRAAHVDEFVSRFPSgystVVGERGAQLSGGQKQRIAIARAILKNPPILILDEATSALDSHSEHMV 603
Cdd:PLN03073 309 YKRLELIDAYTAEA-RAASILAGLSFTPE----MQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWL 383
|
90
....*....|....*...
gi 115533592 604 QEALnnVMKGRTVLIIAH 621
Cdd:PLN03073 384 ETYL--LKWPKTFIVVSH 399
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
431-596 |
2.43e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.17 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 431 SFSYptrpgHTVFENLTLSIPAGQVVALCGPSGEGKSTITHLLerfyepkSGRVTLD-GRDLRELNVEWLR--------- 500
Cdd:PRK11147 12 SFSD-----APLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDdGRIIYEQDLIVARlqqdpprnv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 501 -GQVIGLISQEPVLFATSVEENIRYGRPDATDEEVREAARAAHVDEFVS-----RFPSGYSTVVGERG-------AQLSG 567
Cdd:PRK11147 80 eGTVYDFVAEGIEEQAEYLKRYHDISHLVETDPSEKNLNELAKLQEQLDhhnlwQLENRINEVLAQLGldpdaalSSLSG 159
|
170 180
....*....|....*....|....*....
gi 115533592 568 GQKQRIAIARAILKNPPILILDEATSALD 596
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
152-382 |
5.18e-04 |
|
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: 42.46 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 152 MTLYV----AQSALTFLYITFLTVLGERMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSfklcVSQGL 227
Cdd:cd18606 38 IGIYAglgvLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNE----LPDSL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 228 RTFAQTIGCIGSLYFLSPTMTMYTVAVVPGIILAGSAIGAGLRQLSR---R--AQGQSATASAVSdEALTNIRTIRAFAM 302
Cdd:cd18606 114 RMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYRASSRelkRleSILRSFVYANFS-ESLSGLSTIRAYGA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 303 EKLESRLFDNELDKAR-------AMQEQLGVGIGLFQAGTNLFLNgmILSVlyGGSNLISKGEMtpGALMSFLVS-AQTI 374
Cdd:cd18606 193 QDRFIKKNEKLIDNMNrayfltiANQRWLAIRLDLLGSLLVLIVA--LLCV--TRRFSISPSST--GLVLSYVLQiTQVL 266
|
....*...
gi 115533592 375 QRSLSQLS 382
Cdd:cd18606 267 SWLVRQFA 274
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
139-304 |
7.45e-04 |
|
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: 42.21 E-value: 7.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 139 SHFEQLKPSALHLMTLYVAQS----ALTFLYITFLTVLGERMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQE 214
Cdd:cd18602 40 TSSSLEDDEVSYYISVYAGLSlgavILSLVTNLAGELAGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 215 FKSSFKLCVSQGLRTFAQTIGCIG-----SLYFLsptmtmytVAVVPGIILA---GSAIGAGLRQLSRRaqgQSATASAV 286
Cdd:cd18602 120 IDQKLPTTLERLLRFLLLCLSAIIvnaivTPYFL--------IALIPIIIVYyflQKFYRASSRELQRL---DNITKSPV 188
|
170 180
....*....|....*....|.
gi 115533592 287 SD---EALTNIRTIRAFAMEK 304
Cdd:cd18602 189 FShfsETLGGLTTIRAFRQQA 209
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
553-635 |
1.09e-03 |
|
ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 41.09 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 553 GYSTVvgERGAQ-LSGGQKQRIAIARAILKN--PPILILDEATSALDSHSEHMVQEALNNVM-KGRTVLIIAHRLSTIRS 628
Cdd:cd03270 127 GYLTL--SRSAPtLSGGEAQRIRLATQIGSGltGVLYVLDEPSIGLHPRDNDRLIETLKRLRdLGNTVLVVEHDEDTIRA 204
|
....*..
gi 115533592 629 AQmiYVI 635
Cdd:cd03270 205 AD--HVI 209
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
565-633 |
1.30e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 40.53 E-value: 1.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 115533592 565 LSGGQKQRIAIAR--AILK-NP-PILILDEATSALDSHS----EHMVQEalnnvMKGRT-VLIIAHRLSTIRSAQMIY 633
Cdd:cd03278 114 LSGGEKALTALALlfAIFRvRPsPFCVLDEVDAALDDANverfARLLKE-----FSKETqFIVITHRKGTMEAADRLY 186
|
|
| APS_kinase |
pfam01583 |
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ... |
453-551 |
1.60e-03 |
|
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3'-phosphoadenylylsulfate. This domain contains an ATP binding P-loop motif.
Pssm-ID: 396247 [Multi-domain] Cd Length: 154 Bit Score: 39.61 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 453 GQVVALCGPSGEGKSTITHLLERFYEPKSGRVT-LDGRDLR-ELNVE-----------WLR-GQVIGLISQEPVLFATSV 518
Cdd:pfam01583 2 GCTIWLTGLSGAGKSTIANALERKLFEQGRSVYvLDGDNVRhGLNKDlgfseedrtenIRRiGEVAKLFADAGLIVITAF 81
|
90 100 110
....*....|....*....|....*....|....
gi 115533592 519 EENIRygrpdatdeEVREAARAAHVD-EFVSRFP 551
Cdd:pfam01583 82 ISPYR---------EDREQARELHEEgKFIEVFV 106
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
565-655 |
2.44e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.21 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 565 LSGGQKQRIAIARAILKNP---PILILDEATSALDSHSEHMVQEALNN-VMKGRTVLIIAHRLSTIRSAQmiYVIK---- 636
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLHFEDIRKLLEVLHRlVDKGNTVVVIEHNLDVIKTAD--WIIDlgpe 908
|
90 100
....*....|....*....|...
gi 115533592 637 --DK--KALESGTHEQLMAKKGS 655
Cdd:PRK00349 909 ggDGggEIVATGTPEEVAKVEAS 931
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
565-635 |
2.74e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.17 E-value: 2.74e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115533592 565 LSGGQKQRIAIARAILK--NPPIL-ILDEATSALDSHSEHMVQEALNN-VMKGRTVLIIAHRLSTIRSAQmiYVI 635
Cdd:COG0178 827 LSGGEAQRVKLASELSKrsTGKTLyILDEPTTGLHFHDIRKLLEVLHRlVDKGNTVVVIEHNLDVIKTAD--WII 899
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
553-596 |
3.11e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.48 E-value: 3.11e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 115533592 553 GYSTVVGergaQLSGGQKQRIAIARAILKNPPILILDEATSALD 596
Cdd:PRK10982 384 GHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
152-366 |
3.48e-03 |
|
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and similar proteins; This group includes the 6-TMD of an uncharacterized peptidase-containing ABC transporter of T1SS (type 1 secretion systems), similar to heterocyst differentiation protein HetC. HetC is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350015 [Multi-domain] Cd Length: 294 Bit Score: 40.12 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 152 MTLYVAQSALTFLYITFLTVLGERMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNaD---VQEFKSSfklcvsqglr 228
Cdd:cd18571 49 LVLFLGSTSIEFIRSWILLHISSRINISIISDFLIKLMRLPISFFDTKMTGDILQRIN-DhsrIESFLTS---------- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 229 TFAQTIGCIGSLYFLSPTMTMYTVaVVPGIILAGSAIGAG--LRQLSRR-----------AQGQSAT---ASAVSDEALT 292
Cdd:cd18571 118 SSLSILFSLLNLIVFSIVLAYYNL-TIFLIFLIGSVLYILwiLLFLKKRkkldykrfdlsSENQSKLielINGMQEIKLN 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115533592 293 NIRTIRAFAMEKLESRLFDNELDKARAMQEQlgvgiglfQAGTNLFLNGMILSVLYGGSNLISKGEMTPGALMS 366
Cdd:cd18571 197 NSERQKRWEWERIQAKLFKINIKSLKLDQYQ--------QIGALFINQLKNILITFLAAKLVIDGEITLGMMLA 262
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
443-632 |
3.51e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.08 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 443 FENLTLSIPAGQVVALC------------GPSGEGKSTITHLLERFYEPKSGRVTLDGRDLRELNVEWLR--GQVIGLIS 508
Cdd:PRK13541 4 LHQLQFNIEQKNLFDLSitflpsaityikGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTyiGHNLGLKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 509 QepvlfaTSVEENIRYGRPDATDEEVREAAraahvdefVSRFPSGYstVVGERGAQLSGGQKQRIAIARAILKNPPILIL 588
Cdd:PRK13541 84 E------MTVFENLKFWSEIYNSAETLYAA--------IHYFKLHD--LLDEKCYSLSSGMQKIVAIARLIACQSDLWLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 115533592 589 DEATSALDSHSEHMvqeaLNN--VMK---GRTVLIIAHRLSTIRSAQMI 632
Cdd:PRK13541 148 DEVETNLSKENRDL----LNNliVMKansGGIVLLSSHLESSIKSAQIL 192
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
560-656 |
4.04e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.38 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 560 ERGAQ-LSGGQKQRIAIARAI---LKNpPILILDEATSALDSHSEHMVQEALNNVMK-GRTVLIIAHRLSTIRSAQMIYV 634
Cdd:TIGR00630 483 SRAAGtLSGGEAQRIRLATQIgsgLTG-VLYVLDEPSIGLHQRDNRRLINTLKRLRDlGNTLIVVEHDEDTIRAADYVID 561
|
90 100
....*....|....*....|....*...
gi 115533592 635 IKDKKALE------SGTHEQLMAKKGSL 656
Cdd:TIGR00630 562 IGPGAGEHggevvaSGTPEEILANPDSL 589
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
142-394 |
5.22e-03 |
|
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: 39.19 E-value: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 142 EQLKPSALHLMTLYVAQSALTFLYITFLTVLGERMATKMRSDLFQKLLHHDMAFFDSHKSGELSARLNADVQEFKSSFKL 221
Cdd:cd18561 33 EDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 222 CVSQGLRTFAQTIGCIGSLYFLSPTMTMYTVAVVPGIILAGSAIGAGLRQLSRRAQGQSATASAVSDEALTNIRTIRAFA 301
Cdd:cd18561 113 YLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFG 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 302 MEKLESRLFDNELDKAR-AMQEQLGVGIgLFQAGTNLFLN-GMILSVLYGGSNLISkGEMTPGALMSFLVSAQTIQRSLS 379
Cdd:cd18561 193 ASKRRGNELAARAEDLRqATMKVLAVSL-LSSGIMGLATAlGTALALGVGALRVLG-GQLTLSSLLLILFLSREFFRPLR 270
|
250
....*....|....*
gi 115533592 380 QLSIIFGTAIKGWTA 394
Cdd:cd18561 271 DLGAYWHAGYQGISA 285
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
558-658 |
7.84e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.81 E-value: 7.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115533592 558 VGERGAQLSGGQKQRIAIARAIL---KNPPILILDEATSALDSHSEHMVQEALNN-VMKGRTVLIIAHRLSTIRSAQmiY 633
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTlVSLGHSVIYIDHDPALLKQAD--Y 1770
|
90 100 110
....*....|....*....|....*....|...
gi 115533592 634 VIK--------DKKALESGTHEQLMAKKGSLYR 658
Cdd:PRK00635 1771 LIEmgpgsgktGGKILFSGPPKDISASKDSLLK 1803
|
|
| |
