|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-492 |
1.05e-45 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 168.03 E-value: 1.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 6 YLKYFSLFSVLLLMK--VNLALPsYLIGQIINITSQSPKLEGLGNLLNYLLLSTLVTIIISPFFTYFFeQEVQINVETKS 83
Cdd:COG1132 19 YRGLLILALLLLLLSalLELLLP-LLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLL-ARLAQRVVADL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 84 RS-LFSQLIRKPFSHFKRLEIGSLASKFERGLGSYEQFINLSVSRGLPLTIELFALGCAIIFFSGWLT-FTLVVFVLMIA 161
Cdd:COG1132 97 RRdLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLAlIVLLVLPLLLL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 162 TMIktRIIRLRRPHISRVNEAEDEILDQIVGVFSGIRTIQSNRVEGFFEKRLGPFFENYRQATVSLAVSRSVFDGVAIAT 241
Cdd:COG1132 177 VLR--LFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 242 hSLISLSIITLFIFYLFPEQHSDAGQLVTALLLSASLTRAFTGLLDVYRLLDQSREDFSALKGILDHEEKLTGVSQVLN- 320
Cdd:COG1132 255 -GNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPDPPGAVPl 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 321 --------------------QVLEEL---AKPNvNTIAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSNYL 368
Cdd:COG1132 334 ppvrgeiefenvsfsypgdrPVLKDIsltIPPG-ETVALVGPSGSGKSTLVNLLLRFYDPTsgrilidgvDIRDLTLESL 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 369 -------EQNNFVFSGSVYENLSLGKK-MDNDWLTSQIDKVGLSSRLT-----LDSELQGNGQNLSGGEKRRLCFLRAYI 435
Cdd:COG1132 413 rrqigvvPQDTFLFSGTIRENIRYGRPdATDEEVEEAAKAAQAHEFIEalpdgYDTVVGERGVNLSGGQRQRIAIARALL 492
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2159016728 436 HSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTkLVVVTHDSSYLGHFDKVITLD 492
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERLMKGRT-TIVIAHRLSTIRNADRILVLD 548
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
11-492 |
8.20e-43 |
|
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: 161.54 E-value: 8.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 11 SLFSVLLlmkvNLALPsYLIGQIIN--ITSQSpkleglgnllnyllLSTLVTIIISPFFTYFFEQ-------------EV 75
Cdd:COG2274 165 SLLINLL----ALATP-LFTQVVIDrvLPNQD--------------LSTLWVLAIGLLLALLFEGllrllrsylllrlGQ 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 76 QINVETKSRsLFSQLIRKPFSHFKRLEIGSLASKFeRGLGSYEQFINlSVSRGLPLTIELFALGCAIIFFSGWlTFTLVV 155
Cdd:COG2274 226 RIDLRLSSR-FFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLT-GSLLTALLDLLFVLIFLIVLFFYSP-PLALVV 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 156 FVLMIATMIKTRII-RLRRPHISRVNEAEDEILDQIVGVFSGIRTIQSNRVEGFFEKRLGPFFENYRQATVSLAVSRSVF 234
Cdd:COG2274 302 LLLIPLYVLLGLLFqPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 235 DGVAIATHSLISLsIITLFIFYLFPEQHSDAGQLVTALLLSASLTRAFTGLLDVYRLLDQSREDFSALKGILDHE-EKLT 313
Cdd:COG2274 382 STLSGLLQQLATV-ALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPpEREE 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 314 GVSQVLNQVLE-------------ELAKP---NVN-------TIAVIGKSGQGKTILLDTLAGLLTPT---------PVS 361
Cdd:COG2274 461 GRSKLSLPRLKgdielenvsfrypGDSPPvldNISltikpgeRVAIVGRSGSGKSTLLKLLLGLYEPTsgrilidgiDLR 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 362 HLSSN-------YLEQNNFVFSGSVYENLSLGKK-MDNDWLTSQIDKVGLS---SRLT--LDSELQGNGQNLSGGEKRRL 428
Cdd:COG2274 541 QIDPAslrrqigVVLQDVFLFSGTIRENITLGDPdATDEEIIEAARLAGLHdfiEALPmgYDTVVGEGGSNLSGGQRQRL 620
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2159016728 429 CFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTkLVVVTHDSSYLGHFDKVITLD 492
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRT-VIIIAHRLSTIRLADRIIVLD 683
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
129-492 |
1.01e-38 |
|
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: 148.38 E-value: 1.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 129 LPLTIELFALGCAII---FFSGWLTFTLVVFVLMIATMIKTRIIRLRRPHISRVNEAEDEILDQIVGVFSGIRTIQSNRV 205
Cdd:COG4987 134 LPLLVALLVILAAVAflaFFSPALALVLALGLLLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGA 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 206 EGFFEKRLGPFFENYRQATVSLAVsrsvFDGVAIATHSLIS-LSIITLFIF--YLFPEQHSDAGQLVTALLLSASLTRAF 282
Cdd:COG4987 214 LDRALARLDAAEARLAAAQRRLAR----LSALAQALLQLAAgLAVVAVLWLaaPLVAAGALSGPLLALLVLAALALFEAL 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 283 TGLLDVYRLLDQSREdfSA--LKGILDHEE-----------------KLTGVS--------QVLNQVleELAKPNVNTIA 335
Cdd:COG4987 290 APLPAAAQHLGRVRA--AArrLNELLDAPPavtepaepapapggpslELEDVSfrypgagrPVLDGL--SLTLPPGERVA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 336 VIGKSGQGKTILLDTLAGLLTPT---------PVSHLSS-------NYLEQNNFVFSGSVYENLSLGKKM-DNDWLTSQI 398
Cdd:COG4987 366 IVGPSGSGKSTLLALLLRFLDPQsgsitlggvDLRDLDEddlrrriAVVPQRPHLFDTTLRENLRLARPDaTDEELWAAL 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 399 DKVGLSSRLT-----LDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTkLV 473
Cdd:COG4987 446 ERVGLGDWLAalpdgLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRT-VL 524
|
410
....*....|....*....
gi 2159016728 474 VVTHDSSYLGHFDKVITLD 492
Cdd:COG4987 525 LITHRLAGLERMDRILVLE 543
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
333-492 |
1.58e-31 |
|
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: 127.57 E-value: 1.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 333 TIAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSN-------YLEQNNFVFSGSVYENLSLGK-KMDNDWLT 395
Cdd:COG4988 365 RVALVGPSGAGKSTLLNLLLGFLPPYsgsilingvDLSDLDPAswrrqiaWVPQNPYLFAGTIRENLRLGRpDASDEELE 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 396 SQIDKVGLSSRLT-----LDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQT 470
Cdd:COG4988 445 AALEAAGLDEFVAalpdgLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRT 524
|
170 180
....*....|....*....|..
gi 2159016728 471 kLVVVTHDSSYLGHFDKVITLD 492
Cdd:COG4988 525 -VILITHRLALLAQADRILVLD 545
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
334-491 |
1.43e-28 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 112.83 E-value: 1.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSNYLEQ--NN---FVFSG-------SVYENLSL------- 385
Cdd:COG1136 37 VAIVGPSGSGKSTLLNILGGLDRPTsgevlidgqDISSLSERELARlrRRhigFVFQFfnllpelTALENVALplllagv 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 386 GKKMDNDWLTSQIDKVGLSSRLT-LDSELqgngqnlSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFS 464
Cdd:COG1136 117 SRKERRERARELLERVGLGDRLDhRPSQL-------SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRE 189
|
170 180
....*....|....*....|....*...
gi 2159016728 465 L-LEPQTKLVVVTHDSSYLGHFDKVITL 491
Cdd:COG1136 190 LnRELGTTIVMVTHDPELAARADRVIRL 217
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
334-491 |
2.45e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 108.75 E-value: 2.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSN-------YLEQNNFVFSGSVYENLSL-----GKKMDND 392
Cdd:COG4619 29 VAITGPSGSGKSTLLRALADLDPPTsgeiyldgkPLSAMPPPewrrqvaYVPQEPALWGGTVRDNLPFpfqlrERKFDRE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 393 WLTSQIDKVGLSSRLtldseLQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLL-EPQTK 471
Cdd:COG4619 109 RALELLERLGLPPDI-----LDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLaEEGRA 183
|
170 180
....*....|....*....|.
gi 2159016728 472 LVVVTHDSSYLGHF-DKVITL 491
Cdd:COG4619 184 VLWVSHDPEQIERVaDRVLTL 204
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
333-492 |
5.60e-27 |
|
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: 106.70 E-value: 5.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 333 TIAVIGKSGQGKTILLDTLAGLLTPT--------------PVSHLSSN--YLEQNNFVFSGSVYENLslgkkmdndwlts 396
Cdd:cd03228 30 KVAIVGPSGSGKSTLLKLLLRLYDPTsgeilidgvdlrdlDLESLRKNiaYVPQDPFLFSGTIRENI------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 397 qidkvglssrltldselqgngqnLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTkLVVVT 476
Cdd:cd03228 97 -----------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKGKT-VIVIA 152
|
170
....*....|....*.
gi 2159016728 477 HDSSYLGHFDKVITLD 492
Cdd:cd03228 153 HRLSTIRDADRIIVLD 168
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
334-491 |
9.94e-27 |
|
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: 107.58 E-value: 9.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSNYL-----EQNNFVFSG-------SVYENLSLG------ 386
Cdd:cd03255 33 VAIVGPSGSGKSTLLNILGGLDRPTsgevrvdgtDISKLSEKELaafrrRHIGFVFQSfnllpdlTALENVELPlllagv 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 387 -KKMDNDWLTSQIDKVGLSSRLTLdselqgNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSL 465
Cdd:cd03255 113 pKKERRERAEELLERVGLGDRLNH------YPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLREL 186
|
170 180
....*....|....*....|....*..
gi 2159016728 466 LEPQ-TKLVVVTHDSSYLGHFDKVITL 491
Cdd:cd03255 187 NKEAgTTIVVVTHDPELAEYADRIIEL 213
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
221-478 |
1.70e-25 |
|
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: 109.37 E-value: 1.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 221 RQATVSLAVSRSVFDGVAIATHSLIS--LSIITLFIFYLFPEQHSDAgqlVTALLLSA-SLTRAFTGLLDVYRLLDQSRE 297
Cdd:TIGR02868 240 GAALTLLAAGLAVLGALWAGGPAVADgrLAPVTLAVLVLLPLAAFEA---FAALPAAAqQLTRVRAAAERIVEVLDAAGP 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 298 dfsalKGILDHEEKLTGVSQVLNQVLEEL---------AKPNVN-------TIAVIGKSGQGKTILLDTLAGLLTP---- 357
Cdd:TIGR02868 317 -----VAEGSAPAAGAVGLGKPTLELRDLsagypgappVLDGVSldlppgeRVAILGPSGSGKSTLLATLAGLLDPlqge 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 358 -----TPVSHLSSN-------YLEQNNFVFSGSVYENLSLGKK-MDNDWLTSQIDKVGLSSRLT-----LDSELQGNGQN 419
Cdd:TIGR02868 392 vtldgVPVSSLDQDevrrrvsVCAQDAHLFDTTVRENLRLARPdATDEELWAALERVGLADWLRalpdgLDTVLGEGGAR 471
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2159016728 420 LSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKlVVVTHD 478
Cdd:TIGR02868 472 LSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTV-VLITHH 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
334-492 |
8.05e-25 |
|
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: 102.28 E-value: 8.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT--------------PVSHLSSN--YLEQNNFVFSGSVYENLSLGKKMDNDWLTSQ 397
Cdd:cd03245 33 VAIIGRVGSGKSTLLKLLAGLYKPTsgsvlldgtdirqlDPADLRRNigYVPQDVTLFYGTLRDNITLGAPLADDERILR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 398 IDKVGLSSRLT------LDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTk 471
Cdd:cd03245 113 AAELAGVTDFVnkhpngLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKT- 191
|
170 180
....*....|....*....|.
gi 2159016728 472 LVVVTHDSSYLGHFDKVITLD 492
Cdd:cd03245 192 LIIITHRPSLLDLVDRIIVMD 212
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
334-492 |
4.08e-23 |
|
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: 95.39 E-value: 4.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPTpvshlssnyleqnnfvfSGSVYENlslGKKMDNDWLTSQIDKVGLSSrltldsel 413
Cdd:cd00267 28 VALVGPNGSGKSTLLRAIAGLLKPT-----------------SGEILID---GKDIAKLPLEELRRRIGYVP-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 414 qgngQnLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVVVTHDSSYLGHF-DKVITLD 492
Cdd:cd00267 80 ----Q-LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAaDRVIVLK 154
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
334-491 |
3.26e-22 |
|
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: 99.67 E-value: 3.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSN-------YLEQNNFVFSGSVYENLSLGKK-MDNDWLTS 396
Cdd:TIGR02857 351 VALVGPSGAGKSTLLNLLLGFVDPTegsiavngvPLADADADswrdqiaWVPQHPFLFAGTIAENIRLARPdASDAEIRE 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 397 QIDKVGLSS-----RLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTk 471
Cdd:TIGR02857 431 ALERAGLDEfvaalPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRT- 509
|
170 180
....*....|....*....|
gi 2159016728 472 LVVVTHDSSYLGHFDKVITL 491
Cdd:TIGR02857 510 VLLVTHRLALAALADRIVVL 529
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
334-492 |
1.48e-21 |
|
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: 92.53 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSN-------YLEQN--NFVFSGSVYE-------NLSLGKK 388
Cdd:cd03225 30 VLIVGPNGSGKSTLLRLLNGLLGPTsgevlvdgkDLTKLSLKelrrkvgLVFQNpdDQFFGPTVEEevafgleNLGLPEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 389 MDNDWLTSQIDKVGLSSRLTLDSelqgngQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEP 468
Cdd:cd03225 110 EIEERVEEALELVGLEGLRDRSP------FTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE 183
|
170 180
....*....|....*....|....*
gi 2159016728 469 QTKLVVVTHDSSYL-GHFDKVITLD 492
Cdd:cd03225 184 GKTIIIVTHDLDLLlELADRVIVLE 208
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
335-478 |
7.07e-21 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 91.28 E-value: 7.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 335 AVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSNYLE------QNNFVFSG-SVYENLSL---GKKMDNDWLT 395
Cdd:COG1131 30 GLLGPNGAGKTTTIRMLLGLLRPTsgevrvlgeDVARDPAEVRRrigyvpQEPALYPDlTVRENLRFfarLYGLPRKEAR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 396 SQIDKvgLSSRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVVV 475
Cdd:COG1131 110 ERIDE--LLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLS 187
|
...
gi 2159016728 476 THD 478
Cdd:COG1131 188 THY 190
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
332-478 |
1.15e-20 |
|
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: 90.70 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 332 NTI-AVIGKSGQGKTILLDTLAGLLTPTP--------------VSHLSSNYLE---------QNNFVFSGSVYENLSLGK 387
Cdd:cd03260 26 GEItALIGPSGCGKSTLLRLLNRLNDLIPgapdegevlldgkdIYDLDVDVLElrrrvgmvfQKPNPFPGSIYDNVAYGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 388 K---MDNDWLTSQIDKVGLSsRLTLDSEL--QGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEII 462
Cdd:cd03260 106 RlhgIKLKEELDERVEEALR-KAALWDEVkdRLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELI 184
|
170
....*....|....*.
gi 2159016728 463 FSLLEPQTkLVVVTHD 478
Cdd:cd03260 185 AELKKEYT-IVIVTHN 199
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
336-492 |
1.16e-20 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 90.50 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 336 VIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSN---YLEQN-NFVFSG-------SVYENLSL-----GKKMD 390
Cdd:COG2884 33 LTGPSGAGKSTLLKLLYGEERPTsgqvlvngqDLSRLKRReipYLRRRiGVVFQDfrllpdrTVYENVALplrvtGKSRK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 391 ------NDWLtsqiDKVGLSSRLTLdselqgNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFS 464
Cdd:COG2884 113 eirrrvREVL----DLVGLSDKAKA------LPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEE 182
|
170 180
....*....|....*....|....*....
gi 2159016728 465 LLEPQTKLVVVTHDSSYLGHFDK-VITLD 492
Cdd:COG2884 183 INRRGTTVLIATHDLELVDRMPKrVLELE 211
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
334-492 |
1.73e-20 |
|
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: 89.45 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPTP--VSHLSS-NYLEQNNFVFSGSVYENLSLGKKMDNDWLTSQIDKVGLSSRLTL- 409
Cdd:cd03250 34 VAIVGPVGSGKSSLLSALLGELEKLSgsVSVPGSiAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEIl 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 410 ----DSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWE-IIFSLLEPQTKLVVVTHDSSYLGH 484
Cdd:cd03250 114 pdgdLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEnCILGLLLNNKTRILVTHQLQLLPH 193
|
....*...
gi 2159016728 485 FDKVITLD 492
Cdd:cd03250 194 ADQIVVLD 201
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
334-492 |
1.84e-20 |
|
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: 90.08 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSN-------YLEQN--NFVFSGSVYENLSLG---KKMDND 392
Cdd:COG1122 30 VAIIGPNGSGKSTLLRLLNGLLKPTsgevlvdgkDITKKNLRelrrkvgLVFQNpdDQLFAPTVEEDVAFGpenLGLPRE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 393 WLTSQIDK----VGLSSRLTLDSelqgngQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEP 468
Cdd:COG1122 110 EIRERVEEalelVGLEHLADRPP------HELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE 183
|
170 180
....*....|....*....|....*
gi 2159016728 469 QTKLVVVTHDSSYL-GHFDKVITLD 492
Cdd:COG1122 184 GKTVIIVTHDLDLVaELADRVIVLD 208
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
335-492 |
4.16e-20 |
|
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: 89.53 E-value: 4.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 335 AVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSN------YLEQNNFVFSG-SVYENLSL---GKKMDNDWLT 395
Cdd:COG4555 31 GLLGPNGAGKTTLLRMLAGLLKPDsgsilidgeDVRKEPREarrqigVLPDERGLYDRlTVRENIRYfaeLYGLFDEELK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 396 SQIDKvgLSSRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVVV 475
Cdd:COG4555 111 KRIEE--LIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFS 188
|
170
....*....|....*...
gi 2159016728 476 THDSSYLGH-FDKVITLD 492
Cdd:COG4555 189 SHIMQEVEAlCDRVVILH 206
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
334-491 |
7.94e-20 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 87.67 E-value: 7.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGL-------------LTPTPVSHLSSN-------YLEQN-NFVFSGSVYENLSLG------ 386
Cdd:TIGR03608 27 YAIIGESGSGKSTLLNIIGLLekfdsgqvylngqETPPLNSKKASKfrreklgYLFQNfALIENETVEENLDLGlkykkl 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 387 -KKMDNDWLTSQIDKVGLSSRL-TLDSELqgngqnlSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFS 464
Cdd:TIGR03608 107 sKKEKREKKKEALEKVGLNLKLkQKIYEL-------SGGEQQRVALARAILKPPPLILADEPTGSLDPKNRDEVLDLLLE 179
|
170 180
....*....|....*....|....*..
gi 2159016728 465 LLEPQTKLVVVTHDSSYLGHFDKVITL 491
Cdd:TIGR03608 180 LNDEGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
334-492 |
8.40e-20 |
|
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: 86.60 E-value: 8.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTP---------TPVSHLSSN------YLEQNNFVFSGSVYENLslgkkmdndwltsqi 398
Cdd:cd03247 31 IALLGRSGSGKSTLLQLLTGDLKPqqgeitldgVPVSDLEKAlsslisVLNQRPYLFDTTLRNNL--------------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 399 dkvglssrltldselqgnGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTkLVVVTHD 478
Cdd:cd03247 96 ------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKT-LIWITHH 156
|
170
....*....|....
gi 2159016728 479 SSYLGHFDKVITLD 492
Cdd:cd03247 157 LTGIEHMDKILFLE 170
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
305-492 |
9.53e-20 |
|
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: 86.47 E-value: 9.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 305 ILDHEEKLTGVSQVLNQVleELAKPNVNTIAVIGKSGQGKTILLDTLAGLLTPT------------------PVSHLSSN 366
Cdd:cd03229 2 ELKNVSKRYGQKTVLNDV--SLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDsgsilidgedltdledelPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 367 YLEQNNFVFSG-SVYENLSLGkkmdndwltsqidkvglssrltldselqgngqnLSGGEKRRLCFLRAYIHSPELLLLDE 445
Cdd:cd03229 80 MVFQDFALFPHlTVLENIALG---------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2159016728 446 PTTGLDSETGQGLWEIIFSLLE-PQTKLVVVTHDSSYLGHF-DKVITLD 492
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAqLGITVVLVTHDLDEAARLaDRVVVLR 175
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
333-492 |
2.49e-19 |
|
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: 86.72 E-value: 2.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 333 TIAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSNYL-----EQNNFVF-------SGSVYENLSL------ 385
Cdd:COG4181 40 SVAIVGASGSGKSTLLGLLAGLDRPTsgtvrlagqDLFALDEDARarlraRHVGFVFqsfqllpTLTALENVMLplelag 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 386 ---GKKMDNDWLtsqiDKVGLSSRLT-LDSELqgngqnlSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEI 461
Cdd:COG4181 120 rrdARARARALL----ERVGLGHRLDhYPAQL-------SGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDL 188
|
170 180 190
....*....|....*....|....*....|..
gi 2159016728 462 IFSLLEPQ-TKLVVVTHDSSYLGHFDKVITLD 492
Cdd:COG4181 189 LFELNRERgTTLVLVTHDPALAARCDRVLRLR 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
334-492 |
2.67e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 90.65 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLA-------G--LLTPTPVSHLSSNYL-------EQNNFVFSGSVYENLSLGKKMDND-WLTS 396
Cdd:PRK11160 369 VALLGRTGCGKSTLLQLLTrawdpqqGeiLLNGQPIADYSEAALrqaisvvSQRVHLFSATLRDNLLLAAPNASDeALIE 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 397 QIDKVGLSSRLT----LDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTkL 472
Cdd:PRK11160 449 VLQQVGLEKLLEddkgLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKT-V 527
|
170 180
....*....|....*....|
gi 2159016728 473 VVVTHDSSYLGHFDKVITLD 492
Cdd:PRK11160 528 LMITHRLTGLEQFDRICVMD 547
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
333-448 |
3.27e-19 |
|
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: 84.24 E-value: 3.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 333 TIAVIGKSGQGKTILLDTLAGLLTPT--------------PVSHLSSN--YLEQNNFVFSG-SVYENLSLGKKM------ 389
Cdd:pfam00005 13 ILALVGPNGAGKSTLLKLIAGLLSPTegtilldgqdltddERKSLRKEigYVFQDPQLFPRlTVRENLRLGLLLkglskr 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 390 -DNDWLTSQIDKVGLSsrLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTT 448
Cdd:pfam00005 93 eKDARAEEALEKLGLG--DLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
334-478 |
3.58e-19 |
|
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: 84.76 E-value: 3.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPTpvshlssnyleqnnfvfSGSVYenlSLGKKMDNDWLTSQ------IDKVGLSSRL 407
Cdd:cd03230 29 YGLLGPNGAGKTTLIKIILGLLKPD-----------------SGEIK---VLGKDIKKEPEEVKrrigylPEEPSLYENL 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2159016728 408 TLDSELQgngqnLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVVVTHD 478
Cdd:cd03230 89 TVRENLK-----LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHI 154
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
333-492 |
3.63e-19 |
|
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: 86.13 E-value: 3.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 333 TIAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSNYLE-------QNNFVFSGSVYENLSLGKkmdndwLTS 396
Cdd:cd03254 31 TVAIVGPTGAGKTTLINLLMRFYDPQkgqilidgiDIRDISRKSLRsmigvvlQDTFLFSGTIMENIRLGR------PNA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 397 QIDKVGLSSRLT------------LDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFS 464
Cdd:cd03254 105 TDEEVIEAAKEAgahdfimklpngYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEK 184
|
170 180
....*....|....*....|....*...
gi 2159016728 465 LLEPQTkLVVVTHDSSYLGHFDKVITLD 492
Cdd:cd03254 185 LMKGRT-SIIIAHRLSTIKNADKILVLD 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
334-492 |
5.68e-19 |
|
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: 85.28 E-value: 5.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSN--YLEQN---NFVFSGSVYENLSLG-----------KK 388
Cdd:cd03235 28 LAIVGPNGAGKSTLLKAILGLLKPTsgsirvfgkPLEKERKRigYVPQRrsiDRDFPISVRDVVLMGlyghkglfrrlSK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 389 MDNDWLTSQIDKVGLS----SRLTldselqgngqNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFS 464
Cdd:cd03235 108 ADKAKVDEALERVGLSeladRQIG----------ELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRE 177
|
170 180
....*....|....*....|....*....
gi 2159016728 465 LLEPQTKLVVVTHD-SSYLGHFDKVITLD 492
Cdd:cd03235 178 LRREGMTILVVTHDlGLVLEYFDRVLLLN 206
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
336-491 |
1.72e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 84.38 E-value: 1.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 336 VIGKSGQGKTILLDTLAGLLTPT---------PVSHLSS-------NYLEQNNFVFSGSVYENLSL-----GKKMDNDWL 394
Cdd:PRK10247 38 ITGPSGCGKSTLLKIVASLISPTsgtllfegeDISTLKPeiyrqqvSYCAQTPTLFGDTVYDNLIFpwqirNQQPDPAIF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 395 TSQIDKVGLSsrltlDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVV 474
Cdd:PRK10247 118 LDDLERFALP-----DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVL 192
|
170
....*....|....*...
gi 2159016728 475 -VTHDSSYLGHFDKVITL 491
Cdd:PRK10247 193 wVTHDKDEINHADKVITL 210
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
301-480 |
3.57e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 83.96 E-value: 3.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 301 ALKGIldheEKLTGVSQVLNQVleELAKPNVNTIAVIGKSGQGKTILLDTLAGLLTPTPVSHLS-----SNYLEQNNFVF 375
Cdd:PRK11247 14 LLNAV----SKRYGERTVLNQL--DLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAgtaplAEAREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 376 SG-------SVYENLSLGKKmdNDWLTSQ---IDKVGLSSRLTldsELQGNgqnLSGGEKRRLCFLRAYIHSPELLLLDE 445
Cdd:PRK11247 88 QDarllpwkKVIDNVGLGLK--GQWRDAAlqaLAAVGLADRAN---EWPAA---LSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 2159016728 446 PTTGLDSETGQGLWEIIFSLLEPQTKLVV-VTHDSS 480
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLWQQHGFTVLlVTHDVS 195
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
333-491 |
5.78e-18 |
|
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: 81.49 E-value: 5.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 333 TIAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSN-------YLEQNNFVFSGSVYENLslgkkmdndwlts 396
Cdd:cd03246 30 SLAIIGPSGSGKSTLARLILGLLRPTsgrvrldgaDISQWDPNelgdhvgYLPQDDELFSGSIAENI------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 397 qidkvglssrltldselqgngqnLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVVVT 476
Cdd:cd03246 97 -----------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIA 153
|
170
....*....|....*
gi 2159016728 477 HDSSYLGHFDKVITL 491
Cdd:cd03246 154 HRPETLASADRILVL 168
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
333-478 |
1.22e-17 |
|
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: 82.16 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 333 TIAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSN----------YLEQNNFVFSG-SVYENLS-------- 384
Cdd:cd03261 28 ILAIIGPSGSGKSTLLRLIVGLLRPDsgevlidgeDISGLSEAelyrlrrrmgMLFQSGALFDSlTVFENVAfplrehtr 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 385 LGKKMDNDWLTSQIDKVGLSSRLTL-DSELqgngqnlSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIF 463
Cdd:cd03261 108 LSEEEIREIVLEKLEAVGLRGAEDLyPAEL-------SGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIR 180
|
170
....*....|....*.
gi 2159016728 464 SL-LEPQTKLVVVTHD 478
Cdd:cd03261 181 SLkKELGLTSIMVTHD 196
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
334-492 |
2.31e-17 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 81.29 E-value: 2.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSN--YLEQNNFV---FSGSVYENLSLG-----------KK 388
Cdd:COG1121 35 VAIVGPNGAGKSTLLKAILGLLPPTsgtvrlfgkPPRRARRRigYVPQRAEVdwdFPITVRDVVLMGrygrrglfrrpSR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 389 MDNDWLTSQIDKVGLSSRLtlDSELqgnGQnLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEP 468
Cdd:COG1121 115 ADREAVDEALERVGLEDLA--DRPI---GE-LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE 188
|
170 180
....*....|....*....|....*
gi 2159016728 469 QTKLVVVTHD-SSYLGHFDKVITLD 492
Cdd:COG1121 189 GKTILVVTHDlGAVREYFDRVLLLN 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
334-491 |
2.50e-17 |
|
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: 79.90 E-value: 2.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPTPVShlssnyleqnnfvfsGSVYENlslGKKMDNDWLTSQIDKVG--------LSS 405
Cdd:cd03213 38 TAIMGPSGAGKSTLLNALAGRRTGLGVS---------------GEVLIN---GRPLDKRSFRKIIGYVPqddilhptLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 406 RLTLD--SELQGngqnLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVVVTHDSSYL- 482
Cdd:cd03213 100 RETLMfaAKLRG----LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEi 175
|
170
....*....|
gi 2159016728 483 -GHFDKVITL 491
Cdd:cd03213 176 fELFDKLLLL 185
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
334-478 |
3.71e-17 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 81.29 E-value: 3.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSNYLeqnnFVFSG-------SVYENLSLG-------KKMD 390
Cdd:COG1116 40 VALVGPSGCGKSTLLRLIAGLEKPTsgevlvdgkPVTGPGPDRG----VVFQEpallpwlTVLDNVALGlelrgvpKAER 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 391 NDWLTSQIDKVGLSSRLT-LDSELqgngqnlSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQ 469
Cdd:COG1116 116 RERARELLELVGLAGFEDaYPHQL-------SGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQET 188
|
170
....*....|
gi 2159016728 470 TKLVV-VTHD 478
Cdd:COG1116 189 GKTVLfVTHD 198
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
63-492 |
4.16e-17 |
|
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: 84.00 E-value: 4.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 63 ISPFFTYFFEQEVQINVETKSR-SLFSQLIRKPFSHFKRLEIGSLASKF----ERGLGSYEQFINLSVSRGLpLTIELFA 137
Cdd:TIGR02203 69 ICSFVSTYLLSWVSNKVVRDIRvRMFEKLLGLPVSFFDRQPTGTLLSRItfdsEQVASAATDAFIVLVRETL-TVIGLFI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 138 lgcaIIFFSGWlTFTLVVFVLMIATMIKTRIIRLRRPHISR--------VNEAEDEILD--QIVGVFSGirtiqsnrvEG 207
Cdd:TIGR02203 148 ----VLLYYSW-QLTLIVVVMLPVLSILMRRVSKRLRRISKeiqnsmgqVTTVAEETLQgyRVVKLFGG---------QA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 208 FFEKRLGPFFENYRQATVSLAVSRSVFDGVaiaTHSLISLSIITLFIFYLFPEQHS--DAGQLV---TALLL-------- 274
Cdd:TIGR02203 214 YETRRFDAVSNRNRRLAMKMTSAGSISSPI---TQLIASLALAVVLFIALFQAQAGslTAGDFTafiTAMIAlirplksl 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 275 ---SASLTRAFTGLLDVYRLLDQSREdfsALKGILdHEEKLTGVSQVLN----------QVLEE---LAKPNvNTIAVIG 338
Cdd:TIGR02203 291 tnvNAPMQRGLAAAESLFTLLDSPPE---KDTGTR-AIERARGDVEFRNvtfrypgrdrPALDSislVIEPG-ETVALVG 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 339 KSGQGKTILLDTLAGLLTPT---------PVSHLSSNYLE-------QNNFVFSGSVYENLSLGKKMDND---------- 392
Cdd:TIGR02203 366 RSGSGKSTLVNLIPRFYEPDsgqilldghDLADYTLASLRrqvalvsQDVVLFNDTIANNIAYGRTEQADraeieralaa 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 393 -WLTSQIDKvglsSRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTK 471
Cdd:TIGR02203 446 aYAQDFVDK----LPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTT 521
|
490 500
....*....|....*....|.
gi 2159016728 472 LvVVTHDSSYLGHFDKVITLD 492
Cdd:TIGR02203 522 L-VIAHRLSTIEKADRIVVMD 541
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
334-492 |
4.18e-17 |
|
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: 79.83 E-value: 4.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSN------YLEQNNFVFSG-SVYENLSL-----GKKMDND 392
Cdd:COG4133 31 LALTGPNGSGKTTLLRILAGLLPPSagevlwngePIRDAREDyrrrlaYLGHADGLKPElTVRENLRFwaalyGLRADRE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 393 WLTSQIDKVGLSSRLTLDselqgnGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKL 472
Cdd:COG4133 111 AIDEALEAVGLAGLADLP------VRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAV 184
|
170 180
....*....|....*....|
gi 2159016728 473 VVVTHDSSYLgHFDKVITLD 492
Cdd:COG4133 185 LLTTHQPLEL-AAARVLDLG 203
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
330-480 |
6.65e-17 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 79.26 E-value: 6.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 330 NVNTIAVIGKSGQGKTILLDTLAGLLTPT--------------------PVSHLSSNYLEQNNFVFSG-SVYENLSLG-K 387
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDggtivlngtvlfdsrkkinlPPQQRKIGLVFQQYALFPHlNVRENLAFGlK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 388 KMDNDWLTSQIDKvgLSSRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQglwEIIFSLLE 467
Cdd:cd03297 102 RKRNREDRISVDE--LLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL---QLLPELKQ 176
|
170
....*....|....*..
gi 2159016728 468 PQTKL----VVVTHDSS 480
Cdd:cd03297 177 IKKNLnipvIFVTHDLS 193
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
333-478 |
7.08e-17 |
|
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: 80.02 E-value: 7.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 333 TIAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSN----------YLEQNNFVFSG-SVYENLSLGKKMDND 392
Cdd:COG1127 33 ILAIIGGSGSGKSVLLKLIIGLLRPDsgeilvdgqDITGLSEKelyelrrrigMLFQGGALFDSlTVFENVAFPLREHTD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 393 WLTSQIDK--------VGLSSrlTLD---SELqgngqnlSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEI 461
Cdd:COG1127 113 LSEAEIRElvleklelVGLPG--AADkmpSEL-------SGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDEL 183
|
170 180
....*....|....*....|.
gi 2159016728 462 IFSLlepQTKL----VVVTHD 478
Cdd:COG1127 184 IREL---RDELgltsVVVTHD 201
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
334-478 |
2.18e-16 |
|
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: 77.90 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSN--YLEQNNFVFS-GSVYENLSLGKKMdNDWLTSQ---- 397
Cdd:cd03293 33 VALVGPSGCGKSTLLRIIAGLERPTsgevlvdgePVTGPGPDrgYVFQQDALLPwLTVLDNVALGLEL-QGVPKAEarer 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 398 ----IDKVGLSsrltlDSELQGNGQnLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLV 473
Cdd:cd03293 112 aeelLELVGLS-----GFENAYPHQ-LSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTV 185
|
....*.
gi 2159016728 474 V-VTHD 478
Cdd:cd03293 186 LlVTHD 191
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
86-460 |
2.24e-16 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 82.08 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 86 LFSQLIRKPFSHFKRLEIGSLASKfergLGSYEQfinlSVSRGLPLTIELF--ALGCAI--IFFSGWLTF--TLVVFVLM 159
Cdd:TIGR00958 240 LFRSLLRQDLGFFDENKTGELTSR----LSSDTQ----TMSRSLSLNVNVLlrNLVMLLglLGFMLWLSPrlTMVTLINL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 160 IATMIKTRIIRLRRPHIS-RVNEAEDEILDQIVGVFSGIRTIQSNRVEGFFEKRLGPFFENYRQATVSLAVSRSVFdgva 238
Cdd:TIGR00958 312 PLVFLAEKVFGKRYQLLSeELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGY---- 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 239 IATHSLISLSIITLFIFY---LFPEQHSDAGQLVTALLLSASLTRAFTGLLDVYRLLDQS------------REDFSALK 303
Cdd:TIGR00958 388 LWTTSVLGMLIQVLVLYYggqLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAvgasekvfeyldRKPNIPLT 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 304 GILdHEEKLTGV-----------SQVLNQVLEELA---KPNvNTIAVIGKSGQGKTILLDTLAGLLTPT---------PV 360
Cdd:TIGR00958 468 GTL-APLNLEGLiefqdvsfsypNRPDVPVLKGLTftlHPG-EVVALVGPSGSGKSTVAALLQNLYQPTggqvlldgvPL 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 361 SHLSSNYLE-------QNNFVFSGSVYENLSLG-KKMDNDWLTSQIDKVGLSSRLT-----LDSELQGNGQNLSGGEKRR 427
Cdd:TIGR00958 546 VQYDHHYLHrqvalvgQEPVLFSGSVRENIAYGlTDTPDEEIMAAAKAANAHDFIMefpngYDTEVGEKGSQLSGGQKQR 625
|
410 420 430
....*....|....*....|....*....|...
gi 2159016728 428 LCFLRAYIHSPELLLLDEPTTGLDSETGQGLWE 460
Cdd:TIGR00958 626 IAIARALVRKPRVLILDEATSALDAECEQLLQE 658
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
333-478 |
6.10e-16 |
|
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: 76.40 E-value: 6.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 333 TIAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSsnyLEQNN--FVFSG-------SVYENLSLGKKMDNDWL 394
Cdd:cd03259 28 FLALLGPSGCGKTTLLRLIAGLERPDsgeilidgrDVTGVP---PERRNigMVFQDyalfphlTVAENIAFGLKLRGVPK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 395 TSQIDKVGLSSRLT-LDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLL-EPQTKL 472
Cdd:cd03259 105 AEIRARVRELLELVgLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQrELGITT 184
|
....*.
gi 2159016728 473 VVVTHD 478
Cdd:cd03259 185 IYVTHD 190
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
333-483 |
9.44e-16 |
|
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: 75.76 E-value: 9.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 333 TIAVIGKSGQGKTILLDTLAGLLTPT--------PVSHL-----SSNYLEQN---NFvFSGSVYENLSLGKKMDNDwltS 396
Cdd:cd03226 28 IIALTGKNGAGKTTLAKILAGLIKESsgsillngKPIKAkerrkSIGYVMQDvdyQL-FTDSVREELLLGLKELDA---G 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 397 QIDKVGLSSRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVVVT 476
Cdd:cd03226 104 NEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVIT 183
|
....*..
gi 2159016728 477 HDSSYLG 483
Cdd:cd03226 184 HDYEFLA 190
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
336-492 |
1.34e-15 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 75.75 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 336 VIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSNYLEQ-----------NNFVFSGSVYENLSL-----GKKmD 390
Cdd:TIGR02673 33 LTGPSGAGKTTLLKLLYGALTPSrgqvriageDVNRLRGRQLPLlrrrigvvfqdFRLLPDRTVYENVALplevrGKK-E 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 391 NDW---LTSQIDKVGLSSRLtldselQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLE 467
Cdd:TIGR02673 112 REIqrrVGAALRQVGLEHKA------DAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDLSERILDLLKRLNK 185
|
170 180
....*....|....*....|....*.
gi 2159016728 468 PQTKLVVVTHDSSYLGHFDK-VITLD 492
Cdd:TIGR02673 186 RGTTVIVATHDLSLVDRVAHrVIILD 211
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
314-450 |
1.49e-15 |
|
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: 75.55 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 314 GVSQVLNQVleELAKPNVNTIAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSN--------YLEQNNFVFS 376
Cdd:cd03224 11 GKSQILFGV--SLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRsgsirfdgrDITGLPPHeraragigYVPEGRRIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 377 G-SVYENLSLG----KKMDNDWltsQIDKV-GLSSRLtldSELQGN-GQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTG 449
Cdd:cd03224 89 ElTVEENLLLGayarRRAKRKA---RLERVyELFPRL---KERRKQlAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
|
.
gi 2159016728 450 L 450
Cdd:cd03224 163 L 163
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
94-492 |
4.37e-15 |
|
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: 77.86 E-value: 4.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 94 PFSHFKRLEIGSLASKFERGLGSYEQFINLSVSRGLPLTIELfalgcAIIFFSGWLTFTLVVFVLmIATMIKTRIIRLRR 173
Cdd:TIGR01193 243 PMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILV-----IVGLFLVRQNMLLFLLSL-LSIPVYAVIIILFK 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 174 PHISRVN----EAEDEILDQIVGVFSGIRTIQSNRVEGFFEKRLGPFFENYRQATVSLAVSRSVfdGVAIATHSLISLSI 249
Cdd:TIGR01193 317 RTFNKLNhdamQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQG--QQAIKAVTKLILNV 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 250 ITLFI-FYLFPEQHSDAGQLVTALLLSASLTRAFTGLLDVYRLLDQSREDFSALKGIL--DHEEKLTGVSQVLNQ----- 321
Cdd:TIGR01193 395 VILWTgAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYlvDSEFINKKKRTELNNlngdi 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 322 --------------VLEE--LAKPNVNTIAVIGKSGQGKTILLDTLAG---------LLTPTPVSHLSS-------NYLE 369
Cdd:TIGR01193 475 vindvsysygygsnILSDisLTIKMNSKTTIVGMSGSGKSTLAKLLVGffqarsgeiLLNGFSLKDIDRhtlrqfiNYLP 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 370 QNNFVFSGSVYENLSLGKK----MDNDWLT---SQIDKVGLSSRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLL 442
Cdd:TIGR01193 555 QEPYIFSGSILENLLLGAKenvsQDEIWAAceiAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLI 634
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2159016728 443 LDEPTTGLDSETGQglwEIIFSLLEPQTK-LVVVTHDSSYLGHFDKVITLD 492
Cdd:TIGR01193 635 LDESTSNLDTITEK---KIVNNLLNLQDKtIIFVAHRLSVAKQSDKIIVLD 682
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
312-479 |
4.39e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 74.43 E-value: 4.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 312 LTGVsqvlnqvleELAKPNVNTIAVIGKSGQGKTILLDTLAGL---------LTPTPVSHLSSN---YLEQNN--FVFSG 377
Cdd:PRK10584 26 LTGV---------ELVVKRGETIALIGESGSGKSTLLAILAGLddgssgevsLVGQPLHQMDEEaraKLRAKHvgFVFQS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 378 -------SVYENLSLGKKM----DNDwltSQIDKVGLSSRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEP 446
Cdd:PRK10584 97 fmliptlNALENVELPALLrgesSRQ---SRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190
....*....|....*....|....*....|....
gi 2159016728 447 TTGLDSETGQGLWEIIFSL-LEPQTKLVVVTHDS 479
Cdd:PRK10584 174 TGNLDRQTGDKIADLLFSLnREHGTTLILVTHDL 207
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
334-478 |
7.29e-15 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 72.84 E-value: 7.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSNYLEQNNFV-----------FSGSVYENLSLGKK---MD 390
Cdd:TIGR01166 21 LALLGANGAGKSTLLLHLNGLLRPQsgavlidgePLDYSRKGLLERRQRVglvfqdpddqlFAADVDQDVAFGPLnlgLS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 391 NDWLTSQIDKV-------GLSSRLTldselqgngQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIF 463
Cdd:TIGR01166 101 EAEVERRVREAltavgasGLRERPT---------HCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGREQMLAILR 171
|
170
....*....|....*
gi 2159016728 464 SLLEPQTKLVVVTHD 478
Cdd:TIGR01166 172 RLRAEGMTVVISTHD 186
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
334-492 |
7.59e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 76.81 E-value: 7.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLtPTPVS------------------HLSsnYLEQNNFVFSGSVYENLSLGKK-MDNDWL 394
Cdd:PRK11174 379 IALVGPSGAGKTSLLNALLGFL-PYQGSlkingielreldpeswrkHLS--WVGQNPQLPHGTLRDNVLLGNPdASDEQL 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 395 TSQIDKVGLS---SRLT--LDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQ 469
Cdd:PRK11174 456 QQALENAWVSeflPLLPqgLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQ 535
|
170 180
....*....|....*....|...
gi 2159016728 470 TKLvVVTHDSSYLGHFDKVITLD 492
Cdd:PRK11174 536 TTL-MVTHQLEDLAQWDQIWVMQ 557
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
333-492 |
7.63e-15 |
|
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: 77.10 E-value: 7.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 333 TIAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSN-------YLEQNNFVFSGSVYENLSlgkKMDNdwLTS 396
Cdd:COG4618 360 VLGVIGPSGSGKSTLARLLVGVWPPTagsvrldgaDLSQWDREelgrhigYLPQDVELFDGTIAENIA---RFGD--ADP 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 397 qiDKVGLSSR--------LTL----DSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFS 464
Cdd:COG4618 435 --EKVVAAAKlagvhemiLRLpdgyDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRA 512
|
170 180
....*....|....*....|....*...
gi 2159016728 465 LLEPQTKLVVVTHDSSYLGHFDKVITLD 492
Cdd:COG4618 513 LKARGATVVVITHRPSLLAAVDKLLVLR 540
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
332-492 |
8.38e-15 |
|
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: 73.46 E-value: 8.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 332 NTIAVIGKSGQGKTILLDTLAGLLTPTPVS-------------HL---SSNYLEQNNFVFSG-SVYE------NLSLGKK 388
Cdd:cd03234 34 QVMAILGSSGSGKTTLLDAISGRVEGGGTTsgqilfngqprkpDQfqkCVAYVRQDDILLPGlTVREtltytaILRLPRK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 389 MDNdwltSQIDKVGLSSRLTL--DSELQGNG-QNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIfSL 465
Cdd:cd03234 114 SSD----AIRKKRVEDVLLRDlaLTRIGGNLvKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTL-SQ 188
|
170 180 190
....*....|....*....|....*....|
gi 2159016728 466 LEPQTKLVVVT-HD--SSYLGHFDKVITLD 492
Cdd:cd03234 189 LARRNRIVILTiHQprSDLFRLFDRILLLS 218
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
336-492 |
1.23e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 76.38 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 336 VIGKSGQGKTILLDTLAGL--------LTPTPVSHLssnYLEQNNFVFSGSVYENLS---LGKKMDNDWLTSQIDKVGLS 404
Cdd:COG4178 394 ITGPSGSGKSTLLRAIAGLwpygsgriARPAGARVL---FLPQRPYLPLGTLREALLypaTAEAFSDAELREALEAVGLG 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 405 SRLT-LDSELQGnGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLePQTKLVVVTHDSSYLG 483
Cdd:COG4178 471 HLAErLDEEADW-DQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREEL-PGTTVISVGHRSTLAA 548
|
....*....
gi 2159016728 484 HFDKVITLD 492
Cdd:COG4178 549 FHDRVLELT 557
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
335-491 |
1.63e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 71.88 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 335 AVIGKSGQGKTILLDTLAGLLTPTP-----VSHLSSNYLEQNNFV---FSGSVYENLSLGK-----------KMDNDWLT 395
Cdd:NF040873 22 AVVGPNGSGKSTLLKVLAGVLRPTSgtvrrAGGARVAYVPQRSEVpdsLPLTVRDLVAMGRwarrglwrrltRDDRAAVD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 396 SQIDKVGLS--SRLTLDSelqgngqnLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLV 473
Cdd:NF040873 102 DALERVGLAdlAGRQLGE--------LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHARGATVV 173
|
170
....*....|....*...
gi 2159016728 474 VVTHDSSYLGHFDKVITL 491
Cdd:NF040873 174 VVTHDLELVRRADPCVLL 191
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
334-492 |
1.91e-14 |
|
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: 72.90 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSNYLE-------QNNFVFSGSVYENLSLGKK-MDNDWLTS 396
Cdd:cd03252 31 VGIVGRSGSGKSTLTKLIQRFYVPEngrvlvdghDLALADPAWLRrqvgvvlQENVLFNRSIRDNIALADPgMSMERVIE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 397 QIDKVG-----LSSRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTk 471
Cdd:cd03252 111 AAKLAGahdfiSELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRT- 189
|
170 180
....*....|....*....|.
gi 2159016728 472 LVVVTHDSSYLGHFDKVITLD 492
Cdd:cd03252 190 VIIIAHRLSTVKNADRIIVME 210
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
336-491 |
3.31e-14 |
|
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: 71.67 E-value: 3.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 336 VIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSN---YLEQN-NFVFSGS-------VYENLSL-------GKK 388
Cdd:cd03292 32 LVGPSGAGKSTLLKLIYKEELPTsgtirvngqDVSDLRGRaipYLRRKiGVVFQDFrllpdrnVYENVAFalevtgvPPR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 389 MDNDWLTSQIDKVGLSSRL-TLDSELqgngqnlSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLE 467
Cdd:cd03292 112 EIRKRVPAALELVGLSHKHrALPAEL-------SGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINK 184
|
170 180
....*....|....*....|....*
gi 2159016728 468 PQTKLVVVTHDSS-YLGHFDKVITL 491
Cdd:cd03292 185 AGTTVVVATHAKElVDTTRHRVIAL 209
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
333-492 |
3.78e-14 |
|
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: 71.88 E-value: 3.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 333 TIAVIGKSGQGKTILLDTLAGLLTPTP---------VSHLSSNYL-------EQNNFVFSGSVYENLSLGK--------- 387
Cdd:cd03251 30 TVALVGPSGSGKSTLVNLIPRFYDVDSgrilidghdVRDYTLASLrrqiglvSQDVFLFNDTVAENIAYGRpgatreeve 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 388 ---KMDNdwLTSQIDKVGLSsrltLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFS 464
Cdd:cd03251 110 eaaRAAN--AHEFIMELPEG----YDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALER 183
|
170 180
....*....|....*....|....*...
gi 2159016728 465 LLEPQTKLvVVTHDSSYLGHFDKVITLD 492
Cdd:cd03251 184 LMKNRTTF-VIAHRLSTIENADRIVVLE 210
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
335-478 |
6.30e-14 |
|
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: 71.21 E-value: 6.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 335 AVIGKSGQGKTILLDTLAGLLTP------------TPVSHLSSN--YLEQNNFVFSG-SVYENLSLG-KKMDNDwlTSQI 398
Cdd:cd03299 29 VILGPTGSGKSVLLETIAGFIKPdsgkillngkdiTNLPPEKRDisYVPQNYALFPHmTVYKNIAYGlKKRKVD--KKEI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 399 DK--VGLSSRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEII-FSLLEPQTKLVVV 475
Cdd:cd03299 107 ERkvLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELkKIRKEFGVTVLHV 186
|
...
gi 2159016728 476 THD 478
Cdd:cd03299 187 THD 189
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
334-492 |
1.48e-13 |
|
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: 69.83 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSNYLE-------QNNFVFSGSVYENL-SLGKKMDNDwLTS 396
Cdd:cd03244 33 VGIVGRTGSGKSSLLLALFRLVELSsgsilidgvDISKIGLHDLRsrisiipQDPVLFSGTIRSNLdPFGEYSDEE-LWQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 397 QIDKVGLSSRL-----TLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLePQTK 471
Cdd:cd03244 112 ALERVGLKEFVeslpgGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAF-KDCT 190
|
170 180
....*....|....*....|.
gi 2159016728 472 LVVVTHDSSYLGHFDKVITLD 492
Cdd:cd03244 191 VLTIAHRLDTIIDSDRILVLD 211
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
334-492 |
1.69e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 72.77 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTP------------TPVS----HLSSNYLEQNN-FVFSGSVYENL--SLGKKMDNDWL 394
Cdd:TIGR00955 54 LAVMGSSGAGKTTLMNALAFRSPKgvkgsgsvllngMPIDakemRAISAYVQQDDlFIPTLTVREHLmfQAHLRMPRRVT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 395 TSQ--------IDKVGLSSRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLL 466
Cdd:TIGR00955 134 KKEkrervdevLQALGLRKCANTRIGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLA 213
|
170 180
....*....|....*....|....*...
gi 2159016728 467 EPQTKLVVVTHDSSY--LGHFDKVITLD 492
Cdd:TIGR00955 214 QKGKTIICTIHQPSSelFELFDKIILMA 241
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
317-478 |
4.52e-13 |
|
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: 68.33 E-value: 4.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 317 QVLNQVLEELAKPNVntIAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSNYLE---QNNFVFSG------- 377
Cdd:cd03262 14 HVLKGIDLTVKKGEV--VVIIGPSGSGKSTLLRCINLLEEPDsgtiiidglKLTDDKKNINElrqKVGMVFQQfnlfphl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 378 SVYENLSLG----KKMDNDWLTSQ----IDKVGLSSRLTldselqGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTG 449
Cdd:cd03262 92 TVLENITLApikvKGMSKAEAEERalelLEKVGLADKAD------AYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSA 165
|
170 180
....*....|....*....|....*....
gi 2159016728 450 LDSETGQGLWEIIFSLLEPQTKLVVVTHD 478
Cdd:cd03262 166 LDPELVGEVLDVMKDLAEEGMTMVVVTHE 194
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
316-492 |
4.53e-13 |
|
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: 68.65 E-value: 4.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 316 SQVLNQVLEELaKPNVNTiAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSNYLE-------QNNFVFSGSV 379
Cdd:cd03248 27 TLVLQDVSFTL-HPGEVT-ALVGPSGSGKSTVVALLENFYQPQggqvlldgkPISQYEHKYLHskvslvgQEPVLFARSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 380 YENLSLG-KKMDNDWLTSQIDKVGLSSRLTL-----DSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSE 453
Cdd:cd03248 105 QDNIAYGlQSCSFECVKEAAQKAHAHSFISElasgyDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190
....*....|....*....|....*....|....*....
gi 2159016728 454 TGQGLWEIIFSLLEPQTKLvVVTHDSSYLGHFDKVITLD 492
Cdd:cd03248 185 SEQQVQQALYDWPERRTVL-VIAHRLSTVERADQILVLD 222
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
138-491 |
6.25e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.55 E-value: 6.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 138 LGCAIIFFSgwltftLVVFVLM-IATMIKTRIIRLRRPHISRVNE---AEDEILD--QIVGVFSGIRTIQSnRVEGFFEK 211
Cdd:PLN03232 439 LGVASLFGS------LILFLLIpLQTLIVRKMRKLTKEGLQWTDKrvgIINEILAsmDTVKCYAWEKSFES-RIQGIRNE 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 212 RLGPFfenyRQATVSLAVSRSVFDGVAIAThSLISLSIITLFIFYLFPEQHSDAGQLVTAL---------LLS------A 276
Cdd:PLN03232 512 ELSWF----RKAQLLSAFNSFILNSIPVVV-TLVSFGVFVLLGGDLTPARAFTSLSLFAVLrsplnmlpnLLSqvvnanV 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 277 SLTRAFTGLLDVYRLLDQSREDFSALKGILDHEEKLTGVSQVLNQVLEE--LAKPNVNTIAVIGKSGQGKTILLDTLAGL 354
Cdd:PLN03232 587 SLQRIEELLLSEERILAQNPPLQPGAPAISIKNGYFSWDSKTSKPTLSDinLEIPVGSLVAIVGGTGEGKTSLISAMLGE 666
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 355 LTPTPVSHL----SSNYLEQNNFVFSGSVYENLSLGKKMDNDWLTSQIDKVGLSSRLTL-----DSELQGNGQNLSGGEK 425
Cdd:PLN03232 667 LSHAETSSVvirgSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLlpgrdLTEIGERGVNISGGQK 746
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2159016728 426 RRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWE-IIFSLLEPQTKlVVVTHDSSYLGHFDKVITL 491
Cdd:PLN03232 747 QRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDsCMKDELKGKTR-VLVTNQLHFLPLMDRIILV 812
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
325-491 |
6.56e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 70.90 E-value: 6.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 325 ELAKPNVNTIAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSNYL-------EQNNFVFSGSVYENLSLGKK 388
Cdd:PRK10790 361 NLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTegeirldgrPLSSLSHSVLrqgvamvQQDPVVLADTFLANVTLGRD 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 389 MDNDWLTSQIDKVGLSSRLT-----LDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIf 463
Cdd:PRK10790 441 ISEEQVWQALETVQLAELARslpdgLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAL- 519
|
170 180
....*....|....*....|....*...
gi 2159016728 464 SLLEPQTKLVVVTHDSSYLGHFDKVITL 491
Cdd:PRK10790 520 AAVREHTTLVVIAHRLSTIVEADTILVL 547
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
333-462 |
9.96e-13 |
|
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: 67.53 E-value: 9.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 333 TIAVIGKSGQGKTILLDTLAGLLTPTP----VSHLSSN-----------YLEQNNFVFSG-SVYENLSL----------G 386
Cdd:cd03263 30 IFGLLGHNGAGKTTTLKMLTGELRPTSgtayINGYSIRtdrkaarqslgYCPQFDALFDElTVREHLRFyarlkglpksE 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2159016728 387 KKMDNDWLtsqIDKVGLSSRLTLDSelqgngQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEII 462
Cdd:cd03263 110 IKEEVELL---LRVLGLTDKANKRA------RTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLI 176
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
333-492 |
1.03e-12 |
|
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: 67.91 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 333 TIAVIGKSGQGKTILLDTLAGLLTPT---------PVSH-LSSNYLEQNNFVF---SGS------VYENLS-----LGKK 388
Cdd:COG1124 33 SFGLVGESGSGKSTLLRALAGLERPWsgevtfdgrPVTRrRRKAFRRRVQMVFqdpYASlhprhtVDRILAeplriHGLP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 389 MDNDWLTSQIDKVGLSSRLtldseLQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETgQGlwEIIfSLL-- 466
Cdd:COG1124 113 DREERIAELLEQVGLPPSF-----LDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSV-QA--EIL-NLLkd 183
|
170 180 190
....*....|....*....|....*....|
gi 2159016728 467 ---EPQTKLVVVTHDSSYLGHF-DKVITLD 492
Cdd:COG1124 184 lreERGLTYLFVSHDLAVVAHLcDRVAVMQ 213
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
334-478 |
1.19e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.09 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTP-----TPVSHLSSNYLEQNNFVFSG--SVYENLSLGKKMDNDWLTSQI-------- 398
Cdd:COG0488 344 IGLIGPNGAGKSTLLKLLAGELEPdsgtvKLGETVKIGYFDQHQEELDPdkTVLDELRDGAPGGTEQEVRGYlgrflfsg 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 399 ----DKVGlssrltldselqgngqNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETgqgLwEIIFSLLE--PQTkL 472
Cdd:COG0488 424 ddafKPVG----------------VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET---L-EALEEALDdfPGT-V 482
|
....*.
gi 2159016728 473 VVVTHD 478
Cdd:COG0488 483 LLVSHD 488
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
335-477 |
1.42e-12 |
|
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: 67.01 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 335 AVIGKSGQGKTILLDTLAGLLTPTPVSHL------SSNYLE--QNNFVFSGS--VYENLSL-----------GKKMDNdw 393
Cdd:cd03266 35 GLLGPNGAGKTTTLRMLAGLLEPDAGFATvdgfdvVKEPAEarRRLGFVSDStgLYDRLTArenleyfaglyGLKGDE-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 394 LTSQIDKvgLSSRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLV 473
Cdd:cd03266 113 LTARLEE--LADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCIL 190
|
....
gi 2159016728 474 VVTH 477
Cdd:cd03266 191 FSTH 194
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
334-492 |
1.77e-12 |
|
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: 66.36 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT--------------PVSHLSSNYLEQNNFVFSG-SVYENLSLGKKMDNDWLTSQI 398
Cdd:cd03298 27 TAIVGPSGSGKSTLLNLIAGFETPQsgrvlingvdvtaaPPADRPVSMLFQENNLFAHlTVEQNVGLGLSPGLKLTAEDR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 399 DKV-GLSSRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSL-LEPQTKLVVVT 476
Cdd:cd03298 107 QAIeVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhAETKMTVLMVT 186
|
170
....*....|....*....
gi 2159016728 477 H---DSSYLghFDKVITLD 492
Cdd:cd03298 187 HqpeDAKRL--AQRVVFLD 203
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
334-478 |
1.84e-12 |
|
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: 67.38 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSN-------YLEQNNFV-FSGSVYENLSLG---------- 386
Cdd:COG1120 30 TALLGPNGSGKSTLLRALAGLLKPSsgevlldgrDLASLSRRelarriaYVPQEPPApFGLTVRELVALGryphlglfgr 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 387 -KKMDNDWLTSQIDKVGLSS---RLtLDSelqgngqnLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLD----SEtgqgL 458
Cdd:COG1120 110 pSAEDREAVEEALERTGLEHladRP-VDE--------LSGGERQRVLIARALAQEPPLLLLDEPTSHLDlahqLE----V 176
|
170 180
....*....|....*....|.
gi 2159016728 459 WEIIFSLLEPQTKLVV-VTHD 478
Cdd:COG1120 177 LELLRRLARERGRTVVmVLHD 197
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
333-492 |
2.23e-12 |
|
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: 66.38 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 333 TIAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSNYLE----------QN-----NFVFS--GSVYENLSLG 386
Cdd:cd03257 33 TLGLVGESGSGKSTLARAILGLLKPTsgsiifdgkDLLKLSRRLRKirrkeiqmvfQDpmsslNPRMTigEQIAEPLRIH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 387 KKMDNDWLTSQI-----DKVGLSSRLtLDS---ELqgngqnlSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETgQgl 458
Cdd:cd03257 113 GKLSKKEARKEAvllllVGVGLPEEV-LNRyphEL-------SGGQRQRVAIARALALNPKLLIADEPTSALDVSV-Q-- 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2159016728 459 WEIIfSLL-----EPQTKLVVVTHDSSYLGHF-DKVITLD 492
Cdd:cd03257 182 AQIL-DLLkklqeELGLTLLFITHDLGVVAKIaDRVAVMY 220
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
333-478 |
2.30e-12 |
|
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: 66.24 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 333 TIAVIGKSGQGKTILLDTLAGLLTPTP---------VSHLSSNYLEQNNFVFSGSV-------YENLSLGKKM---DNDW 393
Cdd:cd03265 28 IFGLLGPNGAGKTTTIKMLTTLLKPTSgratvaghdVVREPREVRRRIGIVFQDLSvddeltgWENLYIHARLygvPGAE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 394 LTSQIDK----VGL---SSRLTldselqgngQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLL 466
Cdd:cd03265 108 RRERIDElldfVGLleaADRLV---------KTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLK 178
|
170
....*....|...
gi 2159016728 467 EPQ-TKLVVVTHD 478
Cdd:cd03265 179 EEFgMTILLTTHY 191
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
329-491 |
3.25e-12 |
|
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: 69.20 E-value: 3.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 329 PNVNTIAVIGKSGQGKTILLDTLAGLLTPTPvSHL----SSNYLEQNNFVFSGSVYENLSLGKKMDNDWLTSQIDKVGLS 404
Cdd:TIGR00957 662 PEGALVAVVGQVGCGKSSLLSALLAEMDKVE-GHVhmkgSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACALL 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 405 SRLTL-----DSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIF---SLLEPQTKlVVVT 476
Cdd:TIGR00957 741 PDLEIlpsgdRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIgpeGVLKNKTR-ILVT 819
|
170
....*....|....*
gi 2159016728 477 HDSSYLGHFDKVITL 491
Cdd:TIGR00957 820 HGISYLPQVDVIIVM 834
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
333-478 |
3.40e-12 |
|
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: 68.39 E-value: 3.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 333 TIAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSNYLEQNN----FVF---------SGSVYENLSLG---- 386
Cdd:COG1123 293 TLGLVGESGSGKSTLARLLLGLLRPTsgsilfdgkDLTKLSRRSLRELRrrvqMVFqdpysslnpRMTVGDIIAEPlrlh 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 387 KKMDNDWLTSQI----DKVGLSSRLtldseLQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDsETGQglWEII 462
Cdd:COG1123 373 GLLSRAERRERVaellERVGLPPDL-----ADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALD-VSVQ--AQIL 444
|
170 180
....*....|....*....|
gi 2159016728 463 FSLLEPQTKL----VVVTHD 478
Cdd:COG1123 445 NLLRDLQRELgltyLFISHD 464
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
314-477 |
3.40e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 66.47 E-value: 3.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 314 GVSQVLNQVleELAKPNVNTIAVIGKSGQGKTILLDTLAGLLTPTPVSHLSSNYLEQNNFVF------------------ 375
Cdd:PRK14247 14 GQVEVLDGV--NLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIFkmdvielrrrvqmvfqip 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 376 ----SGSVYENLSLGKKMdNDWLTSqidKVGLSSRL-----------TLDSELQGNGQNLSGGEKRRLCFLRAYIHSPEL 440
Cdd:PRK14247 92 npipNLSIFENVALGLKL-NRLVKS---KKELQERVrwalekaqlwdEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEV 167
|
170 180 190
....*....|....*....|....*....|....*..
gi 2159016728 441 LLLDEPTTGLDSETGQGLwEIIFSLLEPQTKLVVVTH 477
Cdd:PRK14247 168 LLADEPTANLDPENTAKI-ESLFLELKKDMTIVLVTH 203
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
334-478 |
4.58e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 65.61 E-value: 4.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSS-NYLEQNN----FVFSG-------SVYENLSL-----GK 387
Cdd:PRK11629 38 MAIVGSSGSGKSTLLHLLGGLDTPTsgdvifngqPMSKLSSaAKAELRNqklgFIYQFhhllpdfTALENVAMplligKK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 388 KMD--NDWLTSQIDKVGLSSRLtldselQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSL 465
Cdd:PRK11629 118 KPAeiNSRALEMLAAVGLEHRA------NHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGEL 191
|
170
....*....|....
gi 2159016728 466 LEPQ-TKLVVVTHD 478
Cdd:PRK11629 192 NRLQgTAFLVVTHD 205
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
333-492 |
5.59e-12 |
|
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: 65.33 E-value: 5.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 333 TIAVIGKSGQGKTILL-------DTLAG--LLTPTPVSHLSSNYLE-------QNNFVFSGSVYENLSLGK------KMD 390
Cdd:cd03253 29 KVAIVGPSGSGKSTILrllfrfyDVSSGsiLIDGQDIREVTLDSLRraigvvpQDTVLFNDTIGYNIRYGRpdatdeEVI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 391 NDWLTSQIDKVGLSSRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQT 470
Cdd:cd03253 109 EAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRT 188
|
170 180
....*....|....*....|..
gi 2159016728 471 kLVVVTHDSSYLGHFDKVITLD 492
Cdd:cd03253 189 -TIVIAHRLSTIVNADKIIVLK 209
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
334-478 |
5.67e-12 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 66.64 E-value: 5.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPTPVSHLSSNY---------LEQNNFVF-SGSVYENLSlgkKMDNDWLTSQIdkVGL 403
Cdd:TIGR01188 22 FGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYdvvreprkvRRSIGIVPqYASVDEDLT---GRENLEMMGRL--YGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 404 SSRLT-------LDS-ELQGNGQNL----SGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTK 471
Cdd:TIGR01188 97 PKDEAeeraeelLELfELGEAADRPvgtySGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYIRALKEEGVT 176
|
....*..
gi 2159016728 472 LVVVTHD 478
Cdd:TIGR01188 177 ILLTTHY 183
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
335-478 |
6.39e-12 |
|
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: 65.15 E-value: 6.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 335 AVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSNylE----------QNNFVFSG-SVYENLSLG-------- 386
Cdd:cd03219 30 GLIGPNGAGKTTLFNLISGFLRPTsgsvlfdgeDITGLPPH--EiarlgigrtfQIPRLFPElTVLENVMVAaqartgsg 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 387 ---------KKMDNDWLTSQIDKVGLSSRLtldSELQGNgqnLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQG 457
Cdd:cd03219 108 lllararreEREARERAEELLERVGLADLA---DRPAGE---LSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEE 181
|
170 180
....*....|....*....|.
gi 2159016728 458 LWEIIFSLLEPQTKLVVVTHD 478
Cdd:cd03219 182 LAELIRELRERGITVLLVEHD 202
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
317-492 |
7.61e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 65.54 E-value: 7.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 317 QVLNQVLEELAKPNVntIAVIGKSGQGKTILLDTLAGLLTPT---------------PVSH---LSSNYLEQNNFVFSG- 377
Cdd:PRK11264 17 TVLHGIDLEVKPGEV--VAIIGPSGSGKTTLLRCINLLEQPEagtirvgditidtarSLSQqkgLIRQLRQHVGFVFQNf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 378 ------SVYENLSLG----KKMDNDWLTSQ----IDKVGLSSRLTldselqGNGQNLSGGEKRRLCFLRAYIHSPELLLL 443
Cdd:PRK11264 95 nlfphrTVLENIIEGpvivKGEPKEEATARarelLAKVGLAGKET------SYPRRLSGGQQQRVAIARALAMRPEVILF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2159016728 444 DEPTTGLDSETGQGLWEIIFSLLEPQTKLVVVTHDSSYLGHF-DKVITLD 492
Cdd:PRK11264 169 DEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVaDRAIFMD 218
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
334-490 |
9.50e-12 |
|
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: 62.47 E-value: 9.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPTP--VSHLSSN---YLEQnnfvfsgsvyenlslgkkmdndwltsqidkvglssrlt 408
Cdd:cd03221 29 IGLVGRNGAGKSTLLKLIAGELEPDEgiVTWGSTVkigYFEQ-------------------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 409 ldselqgngqnLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEiifSLLEPQTKLVVVTHDSSYLghfDKV 488
Cdd:cd03221 71 -----------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEE---ALKEYPGTVILVSHDRYFL---DQV 133
|
..
gi 2159016728 489 IT 490
Cdd:cd03221 134 AT 135
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
329-491 |
1.23e-11 |
|
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: 64.27 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 329 PNVNTIAVIGKSGQGKT-ILLDTLAGLLTPTPVSHLSSN-------------------YLEQNNFVFSGSVYENLSLGKK 388
Cdd:cd03290 25 PTGQLTMIVGQVGCGKSsLLLAILGEMQTLEGKVHWSNKnesepsfeatrsrnrysvaYAAQKPWLLNATVEENITFGSP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 389 MDNDWLTSQIDKVGLSSRLTL-----DSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWE--I 461
Cdd:cd03290 105 FNKQRYKAVTDACSLQPDIDLlpfgdQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQegI 184
|
170 180 190
....*....|....*....|....*....|
gi 2159016728 462 IFSLLEPQTKLVVVTHDSSYLGHFDKVITL 491
Cdd:cd03290 185 LKFLQDDKRTLVLVTHKLQYLPHADWIIAM 214
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
334-489 |
1.52e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 67.07 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPTPVSHL----SSNYLEQNNFVFSGSVYENLSLGKKMDNDWLTSQIDKVGLSSRLTL 409
Cdd:PLN03130 646 VAIVGSTGEGKTSLISAMLGELPPRSDASVvirgTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDL 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 410 -----DSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWE-IIFSLLEPQTKlVVVTHDSSYLG 483
Cdd:PLN03130 726 lpggdLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDkCIKDELRGKTR-VLVTNQLHFLS 804
|
....*.
gi 2159016728 484 HFDKVI 489
Cdd:PLN03130 805 QVDRII 810
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
333-454 |
1.58e-11 |
|
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: 64.10 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 333 TIAVIGKSGQGKTilldTLAGLL----TPT--------------PVSHLSSN--YLEQNNFVFSGSVYENLSLGKkmdND 392
Cdd:cd03249 31 TVALVGSSGCGKS----TVVSLLerfyDPTsgeilldgvdirdlNLRWLRSQigLVSQEPVLFDGTIAENIRYGK---PD 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2159016728 393 WLTSQIDKVGLSSRL---------TLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSET 454
Cdd:cd03249 104 ATDEEVEEAAKKANIhdfimslpdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAES 174
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
420-477 |
1.58e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 65.62 E-value: 1.58e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2159016728 420 LSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVVVTH 477
Cdd:PRK13536 173 LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTH 230
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
334-490 |
2.53e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 65.86 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT--PVShLSSN----YLEQNNFVFSG-SVYENLSLGKK-------------MDNDW 393
Cdd:COG0488 27 IGLVGRNGAGKSTLLKILAGELEPDsgEVS-IPKGlrigYLPQEPPLDDDlTVLDTVLDGDAelraleaeleeleAKLAE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 394 LTSQIDKVG-LSSRL------TLDSE----LQGNG----------QNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDS 452
Cdd:COG0488 106 PDEDLERLAeLQEEFealggwEAEARaeeiLSGLGfpeedldrpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2159016728 453 ETgqglweIIFslLE------PQTkLVVVTHDSSYLghfDKVIT 490
Cdd:COG0488 186 ES------IEW--LEeflknyPGT-VLVVSHDRYFL---DRVAT 217
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
409-477 |
2.96e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 64.44 E-value: 2.96e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2159016728 409 LDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVVVTH 477
Cdd:PRK13537 128 LENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTH 196
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
329-451 |
4.95e-11 |
|
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: 63.98 E-value: 4.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 329 PNVNTIAVIGKSGQGKTILLDTLAGLLTPtPVSHLSSN---------------------YLEQNNFVFSG-SVYENLSLG 386
Cdd:TIGR02142 21 PGQGVTAIFGRSGSGKTTLIRLIAGLTRP-DEGEIVLNgrtlfdsrkgiflppekrrigYVFQEARLFPHlSVRGNLRYG 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2159016728 387 -KKMDNDWLTSQIDKVglSSRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLD 451
Cdd:TIGR02142 100 mKRARPSERRISFERV--IELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
10-255 |
5.67e-11 |
|
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: 63.34 E-value: 5.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 10 FSLFSVLLLMKVNLALPsYLIGQIINITSQSPKLEGLGNLLNYLLLSTLVTIIISPFFTYF---FEQEVQINVETKsrsL 86
Cdd:cd07346 3 LALLLLLLATALGLALP-LLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLaarLGQRVVFDLRRD---L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 87 FSQLIRKPFSHFKRLEIGSLASKFERGLGSYEQFINLSVSRGLPLTIELFALGCAIIFFSGWLTF-TLVVFVLMIATMik 165
Cdd:cd07346 79 FRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLvALLLLPLYVLIL-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 166 TRIIRLRRPHISRVNEAEDEILDQIVGVFSGIRTIQSNRVEGFFEKRLGPFFENYRQATVSLAVSRSVFDGVAIAthsLI 245
Cdd:cd07346 157 RYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGL---LT 233
|
250
....*....|
gi 2159016728 246 SLSIITLFIF 255
Cdd:cd07346 234 ALGTALVLLY 243
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
334-478 |
7.99e-11 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 63.58 E-value: 7.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSNylEQN-NFVF-SG------SVYENLSLG---KKMD--- 390
Cdd:COG3842 34 VALLGPSGCGKTTLLRMIAGFETPDsgrilldgrDVTGLPPE--KRNvGMVFqDYalfphlTVAENVAFGlrmRGVPkae 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 391 -----NDWLtsqiDKVGLS---SRLTldselqgngQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEII 462
Cdd:COG3842 112 irarvAELL----ELVGLEglaDRYP---------HQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREEL 178
|
170
....*....|....*...
gi 2159016728 463 FSLLEpQTKL--VVVTHD 478
Cdd:COG3842 179 RRLQR-ELGItfIYVTHD 195
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
420-477 |
1.00e-10 |
|
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: 62.02 E-value: 1.00e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2159016728 420 LSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSL-LEPQTKLVVVTH 477
Cdd:COG1119 143 LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaAEGAPTLVLVTH 201
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
417-492 |
1.50e-10 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 59.86 E-value: 1.50e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2159016728 417 GQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLepqTKLVVVTHDSSYLGHFDKVITLD 492
Cdd:cd03223 89 DDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELG---ITVISVGHRPSLWKFHDRVLDLD 161
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
334-480 |
1.52e-10 |
|
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: 61.10 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSNYlEQNNFVFSG-------SVYENLSLG---KKMDNDWL 394
Cdd:cd03300 29 FTLLGPSGCGKTTLLRLIAGFETPTsgeilldgkDITNLPPHK-RPVNTVFQNyalfphlTVFENIAFGlrlKKLPKAEI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 395 TSQIDKVglsSRLT-LDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQglwEIIFSLLEPQTKL- 472
Cdd:cd03300 108 KERVAEA---LDLVqLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRK---DMQLELKRLQKELg 181
|
170
....*....|.
gi 2159016728 473 ---VVVTHDSS 480
Cdd:cd03300 182 itfVFVTHDQE 192
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
320-477 |
1.53e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 61.40 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 320 NQVLE--ELAKPNVNTIAVIGKSGQGKTILLDTLAGLLTPTPVSHLSSN--------YLEQNN---------FVFSG--- 377
Cdd:PRK14267 17 NHVIKgvDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEvrlfgrniYSPDVDpievrrevgMVFQYpnp 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 378 ----SVYENLSLGKKMdNDWLTSQ--IDKV---GLSSRLTLD---SELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDE 445
Cdd:PRK14267 97 fphlTIYDNVAIGVKL-NGLVKSKkeLDERvewALKKAALWDevkDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDE 175
|
170 180 190
....*....|....*....|....*....|..
gi 2159016728 446 PTTGLDSETGQGLWEIIFSLLEPQTkLVVVTH 477
Cdd:PRK14267 176 PTANIDPVGTAKIEELLFELKKEYT-IVLVTH 206
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
306-478 |
2.17e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 62.02 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 306 LDHEEKLTGVSQVLNQVleELAKPNVNTIAVIGKSGQGKTILLDTLAGL---------LTPTPVSHLSSNYlEQNNFVFS 376
Cdd:PRK10851 5 IANIKKSFGRTQVLNDI--SLDIPSGQMVALLGPSGSGKTTLLRIIAGLehqtsghirFHGTDVSRLHARD-RKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 377 G-------SVYENLSLGKKM-------DNDWLTSQIDKvgLSSRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLL 442
Cdd:PRK10851 82 HyalfrhmTVFDNIAFGLTVlprrerpNAAAIKAKVTQ--LLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILL 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 2159016728 443 LDEPTTGLDSETGQGLWEIIFSLLEpQTKL--VVVTHD 478
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLRQLHE-ELKFtsVFVTHD 196
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
302-478 |
2.47e-10 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 60.80 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 302 LKGIldheEKLTGVSQVLNQVleELAKPNVNTIAVIGKSGQGKTILLDTLAGLLTPTpvshlsSNYLE--QNNFVFSGSV 379
Cdd:COG4161 5 LKNI----NCFYGSHQALFDI--NLECPSGETLVLLGPSGAGKSSLLRVLNLLETPD------SGQLNiaGHQFDFSQKP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 380 YEN--LSLGKK----------------MDNdwLTSQIDKV-GLS------------SRLTLDSELQGNGQNLSGGEKRRL 428
Cdd:COG4161 73 SEKaiRLLRQKvgmvfqqynlwphltvMEN--LIEAPCKVlGLSkeqarekamkllARLRLTDKADRFPLHLSGGQQQRV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2159016728 429 CFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVVVTHD 478
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHE 200
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
334-492 |
2.92e-10 |
|
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: 60.66 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSNYL-----------EQNNFVFSGSVYEN--------LSL 385
Cdd:cd03256 30 VALIGPSGAGKSTLLRCLNGLVEPTsgsvlidgtDINKLKGKALrqlrrqigmifQQFNLIERLSVLENvlsgrlgrRST 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 386 GKKMDNdWLTSQ--------IDKVGLssrltLDSELQGNGQnLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGqg 457
Cdd:cd03256 110 WRSLFG-LFPKEekqralaaLERVGL-----LDKAYQRADQ-LSGGQQQRVAIARALMQQPKLILADEPVASLDPASS-- 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2159016728 458 lwEIIFSLL-----EPQTKLVVVTHDSSY-LGHFDKVITLD 492
Cdd:cd03256 181 --RQVMDLLkrinrEEGITVIVSLHQVDLaREYADRIVGLK 219
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
333-450 |
3.61e-10 |
|
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: 60.00 E-value: 3.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 333 TIAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSN--------YLEQNNFVFSG-SVYENLSLG--KKMDND 392
Cdd:COG0410 31 IVALLGRNGAGKTTLLKAISGLLPPRsgsirfdgeDITGLPPHriarlgigYVPEGRRIFPSlTVEENLLLGayARRDRA 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 393 WLTSQIDKV-GLSSRLtldSELQGN-GQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGL 450
Cdd:COG0410 111 EVRADLERVyELFPRL---KERRRQrAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL 167
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
334-478 |
4.34e-10 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 59.77 E-value: 4.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT-------------------PVSHLSsnyleQNNFVFSG-SVYENLSLGkkmdndw 393
Cdd:COG3840 28 VAILGPSGAGKSTLLNLIAGFLPPDsgrilwngqdltalppaerPVSMLF-----QENNLFPHlTVAQNIGLG------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 394 ltsqidkvgLSSRLTLDSE-------------LQGNGQ----NLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDsetgQ 456
Cdd:COG3840 96 ---------LRPGLKLTAEqraqveqalervgLAGLLDrlpgQLSGGQRQRVALARCLVRKRPILLLDEPFSALD----P 162
|
170 180
....*....|....*....|....*..
gi 2159016728 457 GLWEIIFSLL-----EPQTKLVVVTHD 478
Cdd:COG3840 163 ALRQEMLDLVdelcrERGLTVLMVTHD 189
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
334-478 |
4.36e-10 |
|
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: 60.04 E-value: 4.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT----------PVSHlSSNYLEQNNFVFSG--------SVYENLSLGKKM---DND 392
Cdd:cd03267 50 VGFIGPNGAGKTTTLKILSGLLQPTsgevrvaglvPWKR-RKKFLRRIGVVFGQktqlwwdlPVIDSFYLLAAIydlPPA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 393 WLTSQIDKvgLSSRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLL-EPQTK 471
Cdd:cd03267 129 RFKKRLDE--LSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNrERGTT 206
|
....*..
gi 2159016728 472 LVVVTHD 478
Cdd:cd03267 207 VLLTSHY 213
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
334-478 |
4.92e-10 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 59.48 E-value: 4.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPTPVS-HLSSN----------YLEQNN---FVFSGSVYENLSLGKKMDNDWL----- 394
Cdd:TIGR03771 9 LGLLGPNGAGKTTLLRAILGLIPPAKGTvKVAGAspgkgwrhigYVPQRHefaWDFPISVAHTVMSGRTGHIGWLrrpcv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 395 ------TSQIDKVGLSsrltldsELQGN--GQnLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLL 466
Cdd:TIGR03771 89 adfaavRDALRRVGLT-------ELADRpvGE-LSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIELA 160
|
170
....*....|..
gi 2159016728 467 EPQTKLVVVTHD 478
Cdd:TIGR03771 161 GAGTAILMTTHD 172
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
84-282 |
7.39e-10 |
|
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: 59.58 E-value: 7.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 84 RSLFSQLIRKPFSHFKRLEIGSLASKFERGLGSYEQFINLSVSRGLPLTIELFAlGCAIIFFSGWlTFTLVVFVLMIATM 163
Cdd:pfam00664 78 RKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVG-GIIVMFYYGW-KLTLVLLAVLPLYI 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 164 IktrIIRLRRPHISRVNEAEDEILDQIVGVF----SGIRTIQSNRVEGFFEKRLGPFFENYRQATVSLAVSRSVFDGVAI 239
Cdd:pfam00664 156 L---VSAVFAKILRKLSRKEQKAVAKASSVAeeslSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQ 232
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2159016728 240 AThSLISLSIITLFIFYLFPEQHSDAGQLVTALLLSASLTRAF 282
Cdd:pfam00664 233 FI-GYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
334-478 |
7.48e-10 |
|
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: 58.22 E-value: 7.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPTpvshlssnyleqnnfvfSGSVY-ENLSLgKKMDNDWLTSQI-------DKVGLSS 405
Cdd:cd03214 28 VGILGPNGAGKSTLLKTLAGLLKPS-----------------SGEILlDGKDL-ASLSPKELARKIayvpqalELLGLAH 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2159016728 406 rlTLDSELQgngqNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVV-VTHD 478
Cdd:cd03214 90 --LADRPFN----ELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVmVLHD 157
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
314-478 |
9.39e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 58.95 E-value: 9.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 314 GVSQVLNQVLEELAKPNVntIAVIGKSGQGKTILLDTLAGLLTPTP----VSHLSSN---------------YLEQNNFV 374
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEV--VVIIGPSGSGKSTLLRCINKLEEITSgdliVDGLKVNdpkvderlirqeagmVFQQFYLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 375 FSGSVYENLSLG-------KKMDNDWLTSQI-DKVGLSSRLT-LDSELqgngqnlSGGEKRRLCFLRAYIHSPELLLLDE 445
Cdd:PRK09493 90 PHLTALENVMFGplrvrgaSKEEAEKQARELlAKVGLAERAHhYPSEL-------SGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190
....*....|....*....|....*....|...
gi 2159016728 446 PTTGLDSETGQGLWEIIFSLLEPQTKLVVVTHD 478
Cdd:PRK09493 163 PTSALDPELRHEVLKVMQDLAEEGMTMVIVTHE 195
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
374-478 |
9.80e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 59.28 E-value: 9.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 374 VFSGSVYENLSLGKKMDNDWLTSQIDKVGLSSRLTLD------SELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPT 447
Cdd:PRK14258 99 LFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADlwdeikHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPC 178
|
90 100 110
....*....|....*....|....*....|..
gi 2159016728 448 TGLDSETGQGLWEIIFSL-LEPQTKLVVVTHD 478
Cdd:PRK14258 179 FGLDPIASMKVESLIQSLrLRSELTMVIVSHN 210
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
336-477 |
9.83e-10 |
|
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: 58.75 E-value: 9.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 336 VIGKSGQGKTILLDTLAGLLTPTP---------VSHLSSNYLE----------QN-NFVFSGSVYENLSLGKKMDNdWLT 395
Cdd:cd03258 36 IIGRSGAGKSTLIRCINGLERPTSgsvlvdgtdLTLLSGKELRkarrrigmifQHfNLLSSRTVFENVALPLEIAG-VPK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 396 SQIDK--------VGLSSRLtldselQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQglwEIIFSLLE 467
Cdd:cd03258 115 AEIEErvlellelVGLEDKA------DAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQ---SILALLRD 185
|
170
....*....|....
gi 2159016728 468 PQTKL----VVVTH 477
Cdd:cd03258 186 INRELgltiVLITH 199
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
314-478 |
1.03e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 58.87 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 314 GVSQVLNQVleELAKPNVNTIAVIGKSGQGKTILLDTLAGLLTPtpvshlSSNYLE--QNNFVFSG-------------- 377
Cdd:PRK11124 13 GAHQALFDI--TLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMP------RSGTLNiaGNHFDFSKtpsdkairelrrnv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 378 -------------SVYENLS------LGkkMDNDWLTSQIDKvgLSSRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSP 438
Cdd:PRK11124 85 gmvfqqynlwphlTVQQNLIeapcrvLG--LSKDQALARAEK--LLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2159016728 439 ELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVVVTHD 478
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHE 200
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
334-478 |
1.27e-09 |
|
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: 58.04 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPTP----VSHLSSNYLEQNN----FVFSG-------SVYENLSLG---KKMDNDWLT 395
Cdd:cd03301 29 VVLLGPSGCGKTTTLRMIAGLEEPTSgriyIGGRDVTDLPPKDrdiaMVFQNyalyphmTVYDNIAFGlklRKVPKDEID 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 396 SQIDKVglSSRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETG-QGLWEIIFSLLEPQTKLVV 474
Cdd:cd03301 109 ERVREV--AELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRvQMRAELKRLQQRLGTTTIY 186
|
....
gi 2159016728 475 VTHD 478
Cdd:cd03301 187 VTHD 190
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
334-480 |
1.33e-09 |
|
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: 57.97 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT---------PV--------SHLSsnYLEQNNFVFSG-SVYENL---SLGKKMDND 392
Cdd:cd03264 28 YGLLGPNGAGKTTLMRILATLTPPSsgtiridgqDVlkqpqklrRRIG--YLPQEFGVYPNfTVREFLdyiAWLKGIPSK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 393 WLTSQID----KVGLSSRLtlDSELQGngqnLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEp 468
Cdd:cd03264 106 EVKARVDevleLVNLGDRA--KKKIGS----LSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGE- 178
|
170
....*....|...
gi 2159016728 469 qTKLVVV-THDSS 480
Cdd:cd03264 179 -DRIVILsTHIVE 190
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
375-478 |
1.38e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 58.64 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 375 FSGSVYENLSLGKKMdNDWLTSQIDKVGLSSRLT-----LDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTG 449
Cdd:PRK14243 103 FPKSIYDNIAYGARI-NGYKGDMDELVERSLRQAalwdeVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSA 181
|
90 100
....*....|....*....|....*....
gi 2159016728 450 LDSETGQGLWEIIFSLLEpQTKLVVVTHD 478
Cdd:PRK14243 182 LDPISTLRIEELMHELKE-QYTIIIVTHN 209
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
334-491 |
1.77e-09 |
|
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: 60.31 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT--PVSHLSS-NYLEQNNFVFSGSVYENLSLGKKMDNDWLTSQIDKVGLSSRLTLD 410
Cdd:TIGR01271 455 LAVAGSTGSGKSSLLMMIMGELEPSegKIKHSGRiSFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALF 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 411 SE-----LQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVVVTHDSSYLGHF 485
Cdd:TIGR01271 535 PEkdktvLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKA 614
|
....*.
gi 2159016728 486 DKVITL 491
Cdd:TIGR01271 615 DKILLL 620
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
335-477 |
1.83e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 58.25 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 335 AVIGKSGQGKTILLDTL--AGLLTPTPVSHLSSNYLEQNNFV---------------------FSGSVYENLSLGKKM-- 389
Cdd:PRK14239 35 ALIGPSGSGKSTLLRSInrMNDLNPEVTITGSIVYNGHNIYSprtdtvdlrkeigmvfqqpnpFPMSIYENVVYGLRLkg 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 390 --DNDWLTSQIDK--VGLSSRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSL 465
Cdd:PRK14239 115 ikDKQVLDEAVEKslKGASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL 194
|
170
....*....|..
gi 2159016728 466 LEPQTkLVVVTH 477
Cdd:PRK14239 195 KDDYT-MLLVTR 205
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
335-478 |
1.87e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 58.71 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 335 AVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSNYLE-----------QNNFVFSGSVYENLSLGK---KMDN 391
Cdd:PRK13636 36 AILGGNGAGKSTLFQNLNGILKPSsgrilfdgkPIDYSRKGLMKlresvgmvfqdPDNQLFSASVYQDVSFGAvnlKLPE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 392 DWLTSQIDKVglSSRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSetgQGLWEIIFSLLEPQTK 471
Cdd:PRK13636 116 DEVRKRVDNA--LKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP---MGVSEIMKLLVEMQKE 190
|
170
....*....|.
gi 2159016728 472 L----VVVTHD 478
Cdd:PRK13636 191 LgltiIIATHD 201
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
319-477 |
2.39e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 60.03 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 319 LNQVLEELAKPNVNTI----------AVIGKSGQGKTILLDTLAGLLTPTPVSHL---------------SSNYLEQNNF 373
Cdd:TIGR01257 934 LVKIFEPSGRPAVDRLnitfyenqitAFLGHNGAGKTTTLSILTGLLPPTSGTVLvggkdietnldavrqSLGMCPQHNI 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 374 VFSG-SVYENLSLGKKMD-NDWLTSQIDKVGLSSRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLD 451
Cdd:TIGR01257 1014 LFHHlTVAEHILFYAQLKgRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
170 180
....*....|....*....|....*.
gi 2159016728 452 SETGQGLWEIIFSLLEPQTkLVVVTH 477
Cdd:TIGR01257 1094 PYSRRSIWDLLLKYRSGRT-IIMSTH 1118
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
334-491 |
2.43e-09 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 57.42 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLD-------------TLAGLLTpTPVSHLSS--------NYLEQN-NFVFSGSVYENLSLGKKMDN 391
Cdd:NF038007 34 VSIMGPSGSGKSTLLNiigmfdsldsgslTLAGKEV-TNLSYSQKiilrreliGYIFQSfNLIPHLSIFDNVALPLKYRG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 392 DWLTSQIDKVG-LSSRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQT 470
Cdd:NF038007 113 VAKKERIERVNqVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSKNARAVLQQLKYINQKGT 192
|
170 180
....*....|....*....|.
gi 2159016728 471 KLVVVTHDSSYLGHFDKVITL 491
Cdd:NF038007 193 TIIMVTHSDEASTYGNRIINM 213
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
334-478 |
3.53e-09 |
|
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: 57.09 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPTPvshlSSNYLE---------------QNNFVFSG-SVYENLSLG-KKMDNDWLTS 396
Cdd:TIGR01184 14 ISLIGHSGCGKSTLLNLISGLAQPTS----GGVILEgkqitepgpdrmvvfQNYSLLPWlTVRENIALAvDRVLPDLSKS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 397 Q--------IDKVGLSsrltlDSELQGNGQnLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLL-E 467
Cdd:TIGR01184 90 ErraiveehIALVGLT-----EAADKRPGQ-LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIWeE 163
|
170
....*....|.
gi 2159016728 468 PQTKLVVVTHD 478
Cdd:TIGR01184 164 HRVTVLMVTHD 174
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
334-478 |
3.81e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.75 E-value: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPTpvshlssnyleqnnfvfSGSV--YENLSLG-------KKMDND-----WLtSQID 399
Cdd:PRK15064 348 LAIIGENGVGKTTLLRTLVGELEPD-----------------SGTVkwSENANIGyyaqdhaYDFENDltlfdWM-SQWR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 400 KVG---LSSRLTL------DSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETgqglweiIFSL---LE 467
Cdd:PRK15064 410 QEGddeQAVRGTLgrllfsQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMES-------IESLnmaLE 482
|
170
....*....|...
gi 2159016728 468 --PQTkLVVVTHD 478
Cdd:PRK15064 483 kyEGT-LIFVSHD 494
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
334-477 |
4.22e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 56.42 E-value: 4.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT-------------PVSHLSSNYLEQNNFVFSG-SVYENLSLGKKMDNDWLTS--- 396
Cdd:PRK13539 31 LVLTGPNGSGKTTLLRLIAGLLPPAagtikldggdiddPDVAEACHYLGHRNAMKPAlTVAENLEFWAAFLGGEELDiaa 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 397 QIDKVGLSSRLTLDselqgnGQNLSGGEKRRLCFLRAYI-HSPeLLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVVV 475
Cdd:PRK13539 111 ALEAVGLAPLAHLP------FGYLSAGQKRRVALARLLVsNRP-IWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAA 183
|
..
gi 2159016728 476 TH 477
Cdd:PRK13539 184 TH 185
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
334-482 |
4.94e-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: 58.41 E-value: 4.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTP-----TPVSHLSSNYLEQ-----NNFVFSGSVYENLSLGKKM-------------- 389
Cdd:TIGR03719 34 IGVLGLNGAGKSTLLRIMAGVDKDfngeaRPQPGIKVGYLPQepqldPTKTVRENVEEGVAEIKDAldrfneisakyaep 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 390 DNDW---------LTSQIDKVGLssrLTLDSELQ------------GNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTT 448
Cdd:TIGR03719 114 DADFdklaaeqaeLQEIIDAADA---WDLDSQLEiamdalrcppwdADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTN 190
|
170 180 190
....*....|....*....|....*....|....
gi 2159016728 449 GLDSETgqGLWEIIFsLLEPQTKLVVVTHDSSYL 482
Cdd:TIGR03719 191 HLDAES--VAWLERH-LQEYPGTVVAVTHDRYFL 221
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
335-478 |
7.47e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 57.54 E-value: 7.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 335 AVIGKSGQGKTILLDTLAGLLTPTP---------VSHLSSnYLEQNNFVFSG-------SVYENLSLGKKMDndwltsQI 398
Cdd:PRK11607 49 ALLGASGCGKSTLLRMLAGFEQPTAgqimldgvdLSHVPP-YQRPINMMFQSyalfphmTVEQNIAFGLKQD------KL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 399 DKVGLSSR----LTLDSELQGNGQ---NLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEP-QT 470
Cdd:PRK11607 122 PKAEIASRvnemLGLVHMQEFAKRkphQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERvGV 201
|
....*...
gi 2159016728 471 KLVVVTHD 478
Cdd:PRK11607 202 TCVMVTHD 209
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
317-478 |
8.33e-09 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 56.16 E-value: 8.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 317 QVLNQVLEELAKPNVntIAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSNYLEQNN---FVFSG------- 377
Cdd:COG1126 15 EVLKGISLDVEKGEV--VVIIGPSGSGKSTLLRCINLLEEPDsgtitvdgeDLTDSKKDINKLRRkvgMVFQQfnlfphl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 378 SVYENLSLG----KKMDND--------WLtsqiDKVGLSSRLtldselqgN---GQnLSGGEKRRLCFLRAYIHSPELLL 442
Cdd:COG1126 93 TVLENVTLApikvKKMSKAeaeerameLL----ERVGLADKA--------DaypAQ-LSGGQQQRVAIARALAMEPKVML 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 2159016728 443 LDEPTTGLDSETGQGLWEIIFSLLEPQTKLVVVTHD 478
Cdd:COG1126 160 FDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHE 195
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
12-289 |
8.83e-09 |
|
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: 56.80 E-value: 8.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 12 LFSVLLLMKVNLALPsYLIGQIINITSQSPKLEGLGNLLNYLLLSTLVTIIISPFFTYFFE--QEvQINVETKSRsLFSQ 89
Cdd:cd18557 2 LLFLLISSAAQLLLP-YLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNiaGE-RIVARLRRD-LFSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 90 LIRKPFSHFKRLEIGSLASKFERGLGSYEQFINLSVSRGL--PLTielFALGCAIIFFSGW-LTFTLVVFV--LMIATMI 164
Cdd:cd18557 79 LLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLrnILQ---VIGGLIILFILSWkLTLVLLLVIplLLIASKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 165 KTRIIRLRRPHISRVNEAEDEILDQivgVFSGIRTIQSNRVEGFFEKRlgpfFENYRQATVSLAVSRSVFDGVAIATHSL 244
Cdd:cd18557 156 YGRYIRKLSKEVQDALAKAGQVAEE---SLSNIRTVRSFSAEEKEIRR----YSEALDRSYRLARKKALANALFQGITSL 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2159016728 245 ISLSIITLFIFY---LFPEQHSDAGQLVTALLLSASLTRAFTGLLDVY 289
Cdd:cd18557 229 LIYLSLLLVLWYggyLVLSGQLTVGELTSFILYTIMVASSVGGLSSLL 276
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
333-492 |
9.00e-09 |
|
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: 57.61 E-value: 9.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 333 TIAVIGKSGQGKTILLDTLAGLLTPT-----------------PVSHLSS-------NYLEQNNFVFSGS----VYENLS 384
Cdd:COG1123 34 TVALVGESGSGKSTLALALMGLLPHGgrisgevlldgrdllelSEALRGRrigmvfqDPMTQLNPVTVGDqiaeALENLG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 385 LGKKMDNDWLTSQIDKVGLSSRLTLDSelqgngQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFS 464
Cdd:COG1123 114 LSRAEARARVLELLEAVGLERRLDRYP------HQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRE 187
|
170 180 190
....*....|....*....|....*....|
gi 2159016728 465 LL-EPQTKLVVVTHDSSYLGHF-DKVITLD 492
Cdd:COG1123 188 LQrERGTTVLLITHDLGVVAEIaDRVVVMD 217
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
368-492 |
9.86e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.12 E-value: 9.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 368 LEQNNFVFSGSVYENLSLGKK------MDNDWLTSQIDKVGLSSRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELL 441
Cdd:PTZ00265 1301 VSQEPMLFNMSIYENIKFGKEdatredVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKIL 1380
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2159016728 442 LLDEPTTGLDSETGQGLWEIIFSLLEPQTK-LVVVTHDSSYLGHFDKVITLD 492
Cdd:PTZ00265 1381 LLDEATSSLDSNSEKLIEKTIVDIKDKADKtIITIAHRIASIKRSDKIVVFN 1432
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
334-492 |
1.00e-08 |
|
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: 55.50 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT--------------PVSHLSSNY--LEQNNFVFSGSVYENLSLGKKMDNDWLTSQ 397
Cdd:cd03369 37 IGIVGRTGAGKSTLILALFRFLEAEegkieidgidistiPLEDLRSSLtiIPQDPTLFSGTIRSNLDPFDEYSDEEIYGA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 398 IdkvglssrltldsELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTkLVVVTH 477
Cdd:cd03369 117 L-------------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNST-ILTIAH 182
|
170
....*....|....*
gi 2159016728 478 DSSYLGHFDKVITLD 492
Cdd:cd03369 183 RLRTIIDYDKILVMD 197
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
335-478 |
1.06e-08 |
|
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: 56.20 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 335 AVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSNylE----------QNNFVFSG-SVYENLSLG--KKMDND 392
Cdd:COG0411 34 GLIGPNGAGKTTLFNLITGFYRPTsgrilfdgrDITGLPPH--RiarlgiartfQNPRLFPElTVLENVLVAahARLGRG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 393 WLTS--------------------QIDKVGLSSRLtldSELQGNgqnLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDS 452
Cdd:COG0411 112 LLAAllrlprarreereareraeeLLERVGLADRA---DEPAGN---LSYGQQRRLEIARALATEPKLLLLDEPAAGLNP 185
|
170 180
....*....|....*....|....*..
gi 2159016728 453 ETGQGLWEIIFSLLEPQTK-LVVVTHD 478
Cdd:COG0411 186 EETEELAELIRRLRDERGItILLIEHD 212
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
334-451 |
1.07e-08 |
|
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: 55.63 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT--------------PV---SHLSSNYLEQNNFVFSG-SVYENLSLGKKMDNDWLT 395
Cdd:cd03218 29 VGLLGPNGAGKTTTFYMIVGLVKPDsgkilldgqditklPMhkrARLGIGYLPQEASIFRKlTVEENILAVLEIRGLSKK 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2159016728 396 SQIDKV-GLSSRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLD 451
Cdd:cd03218 109 EREEKLeELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVD 165
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
334-492 |
1.29e-08 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 55.49 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPTPVSHLSSN--------YLEQNnfvFSGSVYENLSlgkKMDNDWLTSQIDKVGLSS 405
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdtvsykpqYIKAD---YEGTVRDLLS---SITKDFYTHPYFKTEIAK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 406 RLTLDSELQGNGQNLSGGEKRR----LCFLRayihSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLV-VVTHD-- 478
Cdd:cd03237 102 PLQIEQILDREVPELSGGELQRvaiaACLSK----DADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAfVVEHDii 177
|
170
....*....|....*
gi 2159016728 479 -SSYLGhfDKVITLD 492
Cdd:cd03237 178 mIDYLA--DRLIVFE 190
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
335-477 |
1.56e-08 |
|
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: 54.98 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 335 AVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSN---YL-EQNNFVFSGSVYENL-------SLGKKMDNDWL 394
Cdd:cd03269 30 GLLGPNGAGKTTTIRMILGIILPDsgevlfdgkPLDIAARNrigYLpEERGLYPKMKVIDQLvylaqlkGLKKEEARRRI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 395 TSQIDKVGLSSRLTLDSElqgngqNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVV 474
Cdd:cd03269 110 DEWLERLELSEYANKRVE------ELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVIL 183
|
...
gi 2159016728 475 VTH 477
Cdd:cd03269 184 STH 186
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
332-477 |
1.62e-08 |
|
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: 54.67 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 332 NTIAVIGKSGQGKTILLDTLAGLLTP---------TPVSHLSSNYLEQNNFV--FSG-----SVYENLS----LGKKMDN 391
Cdd:TIGR01189 27 EALQVTGPNGIGKTTLLRILAGLLRPdsgevrwngTPLAEQRDEPHENILYLghLPGlkpelSALENLHfwaaIHGGAQR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 392 DWLTSqIDKVGLSSRLTLDSelqgngQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTK 471
Cdd:TIGR01189 107 TIEDA-LAAVGLTGFEDLPA------AQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGI 179
|
....*.
gi 2159016728 472 LVVVTH 477
Cdd:TIGR01189 180 VLLTTH 185
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
334-491 |
1.78e-08 |
|
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: 55.63 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPTP--VSHLSS-NYLEQNNFVFSGSVYENLSLGKKMDNDWLTSQIDKVGLSSRLTLD 410
Cdd:cd03291 66 LAITGSTGSGKTSLLMLILGELEPSEgkIKHSGRiSFSSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKF 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 411 SE-----LQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVVVTHDSSYLGHF 485
Cdd:cd03291 146 PEkdntvLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTRILVTSKMEHLKKA 225
|
....*.
gi 2159016728 486 DKVITL 491
Cdd:cd03291 226 DKILIL 231
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
383-484 |
1.90e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 55.36 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 383 LSLGKKMDNDWLTSQIDKVGLSSRLTLDSELqgngqNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEII 462
Cdd:PRK10619 121 LGLSKQEARERAVKYLAKVGIDERAQGKYPV-----HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIM 195
|
90 100
....*....|....*....|..
gi 2159016728 463 FSLLEPQTKLVVVTHDSSYLGH 484
Cdd:PRK10619 196 QQLAEEGKTMVVVTHEMGFARH 217
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
295-480 |
1.97e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 55.88 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 295 SREDFSALKGIldheEKLTGVSQVLNQVleELAKPNVNTIAVIGKSGQGKTILLDTLAGLLTPTP---------VSHLSs 365
Cdd:PRK11432 2 TQKNFVVLKNI----TKRFGSNTVIDNL--NLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEgqifidgedVTHRS- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 366 nyLEQNN--FVFSG-------SVYENLSLGKKMDNDWLTSQIDKVGLSSRLTldsELQGNGQ----NLSGGEKRRLCFLR 432
Cdd:PRK11432 75 --IQQRDicMVFQSyalfphmSLGENVGYGLKMLGVPKEERKQRVKEALELV---DLAGFEDryvdQISGGQQQRVALAR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2159016728 433 AYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLlepQTKLVV----VTHDSS 480
Cdd:PRK11432 150 ALILKPKVLLFDEPLSNLDANLRRSMREKIREL---QQQFNItslyVTHDQS 198
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
334-451 |
1.97e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 54.97 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTP--------------TPVSHLSSNYLEQNNFVFSG-SVYENLSLGK----KMDNDW- 393
Cdd:PRK10771 28 VAILGPSGAGKSTLLNLIAGFLTPasgsltlngqdhttTPPSRRPVSMLFQENNLFSHlTVAQNIGLGLnpglKLNAAQr 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2159016728 394 --LTSQIDKVGLSSRLT-LDSElqgngqnLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLD 451
Cdd:PRK10771 108 ekLHAIARQMGIEDLLArLPGQ-------LSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
336-451 |
2.29e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 54.94 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 336 VIGKSGQGKTILLDTLAGLLT--------PTPVSHLSSN-------YL-EQNNFVFSGSV--YENLSLGKKMDNDWLTSQ 397
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAGLLPgsgsiqfaGQPLEAWSAAelarhraYLsQQQTPPFAMPVfqYLTLHQPDKTRTEAVASA 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2159016728 398 IDKVglSSRLTLDSELQGNGQNLSGGEKRRL----CFLRayIHS---PE--LLLLDEPTTGLD 451
Cdd:PRK03695 107 LNEV--AEALGLDDKLGRSVNQLSGGEWQRVrlaaVVLQ--VWPdinPAgqLLLLDEPMNSLD 165
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
11-289 |
2.58e-08 |
|
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: 55.18 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 11 SLFSVLLLMKVNLALPsYLIGQIINITSQSPKLEGLGNLLNYLLLSTLVTIIISPFFTYFFEQEVQINVETKSRSLFSQL 90
Cdd:cd18576 1 GLILLLLSSAIGLVFP-LLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 91 IRKPFSHFKRLEIGSLASKFERGLGSYEQFINLSVSRGLPLTIELfaLGCAIIFFSGWLTFTLVVFVLMIATMIKTRII- 169
Cdd:cd18576 80 QRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTL--IGGVVLLFFISWKLTLLMLATVPVVVLVAVLFg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 170 -RLRRphISRvnEAEDEILDQIVGV---FSGIRTIQSNRVEGFFEKRlgpfFENYRQATVSLAVSRSVFDGVAIATHSLI 245
Cdd:cd18576 158 rRIRK--LSK--KVQDELAEANTIVeetLQGIRVVKAFTREDYEIER----YRKALERVVKLALKRARIRALFSSFIIFL 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2159016728 246 SLSIITLFIFY---LFPEQHSDAGQLVTALLLSASLTRAFTGLLDVY 289
Cdd:cd18576 230 LFGAIVAVLWYggrLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLY 276
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
419-478 |
2.65e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.28 E-value: 2.65e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2159016728 419 NLSGGEKRR--LCflRAYIHSPELLLLDEPTTGLDSETgqGLWeiifslLE------PQTkLVVVTHD 478
Cdd:PRK11819 163 KLSGGERRRvaLC--RLLLEKPDMLLLDEPTNHLDAES--VAW------LEqflhdyPGT-VVAVTHD 219
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
310-478 |
2.76e-08 |
|
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: 54.65 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 310 EKLTGVSQVLNQVleELAKPNVNTIAVIGKSGQGKTILLDTLAGLLTPTP---------VSHLSsnyLEQNN--FVFSG- 377
Cdd:cd03296 9 SKRFGDFVALDDV--SLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSgtilfggedATDVP---VQERNvgFVFQHy 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 378 ------SVYENLSLG---KKMDNDWLTSQIDK--VGLSSRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEP 446
Cdd:cd03296 84 alfrhmTVFDNVAFGlrvKPRSERPPEAEIRAkvHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEP 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 2159016728 447 TTGLDSETGQGL--WeiifsLLEPQTKL----VVVTHD 478
Cdd:cd03296 164 FGALDAKVRKELrrW-----LRRLHDELhvttVFVTHD 196
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
334-490 |
2.80e-08 |
|
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: 56.10 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT-------PVSHLSsnYLEQNNFVFSG--SVYENLSLGkkmdNDWLtsQIDKVGLS 404
Cdd:TIGR03719 351 VGVIGPNGAGKSTLFRMITGQEQPDsgtieigETVKLA--YVDQSRDALDPnkTVWEEISGG----LDII--KLGKREIP 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 405 SRLTLDS-ELQGNGQ-----NLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEiifSLLEPQTKLVVVTHD 478
Cdd:TIGR03719 423 SRAYVGRfNFKGSDQqkkvgQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEE---ALLNFAGCAVVISHD 499
|
170
....*....|..
gi 2159016728 479 SSYLghfDKVIT 490
Cdd:TIGR03719 500 RWFL---DRIAT 508
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
79-474 |
2.98e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 56.18 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 79 VETKSRSLFSQLIRKPFSHFKRLEIGSLASKFerglgSY--EQFIN------LSVSRGLPLTIELFALgcaiIFFSGW-L 149
Cdd:PRK11176 97 VMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRI-----TYdsEQVASsssgalITVVREGASIIGLFIM----MFYYSWqL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 150 TFTLVVFVLMIATMIKTRIIRLRRphISR--------VNEAEDEILD--QIVGVFSGirtiqsNRVEgffEKRLGPFFEN 219
Cdd:PRK11176 168 SLILIVIAPIVSIAIRVVSKRFRN--ISKnmqntmgqVTTSAEQMLKghKEVLIFGG------QEVE---TKRFDKVSNR 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 220 YRQATVSLAVSRSVFDGVAiathSLISlSIITLFIFYL--FPEqhsdagqlVTALLLSASLTRAFTGLLDVYRLLD---- 293
Cdd:PRK11176 237 MRQQGMKMVSASSISDPII----QLIA-SLALAFVLYAasFPS--------VMDTLTAGTITVVFSSMIALMRPLKsltn 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 294 ---QSREDFSA---LKGILDHE-EKLTGVSQV--------LNQVL------EELAKPNVN-------TIAVIGKSGQGKT 345
Cdd:PRK11176 304 vnaQFQRGMAAcqtLFAILDLEqEKDEGKRVIerakgdieFRNVTftypgkEVPALRNINfkipagkTVALVGRSGSGKS 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 346 ----------------ILLD-------TLAGLLTPTPVshlssnyLEQNNFVFSGSVYENLSLGKKmdNDWLTSQIDK-- 400
Cdd:PRK11176 384 tianlltrfydidegeILLDghdlrdyTLASLRNQVAL-------VSQNVHLFNDTIANNIAYART--EQYSREQIEEaa 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 401 -----VGLSSRLT--LDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLV 473
Cdd:PRK11176 455 rmayaMDFINKMDngLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLV 534
|
.
gi 2159016728 474 V 474
Cdd:PRK11176 535 I 535
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
336-478 |
3.06e-08 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 54.87 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 336 VIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSNyleqNNFVFSG-------SVYENLSLGKKmdndwltsqID 399
Cdd:COG4525 38 ALGASGCGKTTLLNLIAGFLAPSsgeitldgvPVTGPGAD----RGVVFQKdallpwlNVLDNVAFGLR---------LR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 400 KVGLSSRLTLDSE------LQGNGQ----NLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQ 469
Cdd:COG4525 105 GVPKAERRARAEEllalvgLADFARrriwQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRT 184
|
170
....*....|
gi 2159016728 470 TKLV-VVTHD 478
Cdd:COG4525 185 GKGVfLITHS 194
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
334-478 |
3.42e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 54.84 E-value: 3.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPTPVS------HLSSNYLEQN----------------NFVFSGSVYENLSLGKKmdN 391
Cdd:PRK13641 36 VALVGHTGSGKSTLMQHFNALLKPSSGTitiagyHITPETGNKNlkklrkkvslvfqfpeAQLFENTVLKDVEFGPK--N 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 392 DWLTSQ---------IDKVGLSSRLTLDSELQgngqnLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEII 462
Cdd:PRK13641 114 FGFSEDeakekalkwLKKVGLSEDLISKSPFE-----LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLF 188
|
170
....*....|....*.
gi 2159016728 463 FSLLEPQTKLVVVTHD 478
Cdd:PRK13641 189 KDYQKAGHTVILVTHN 204
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
336-478 |
3.66e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 54.32 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 336 VIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSNyleqnnfvfSGSVYEN---LSLGKKMDNDWLTSQIDKVGL 403
Cdd:PRK11248 32 VLGPSGCGKTTLLNLIAGFVPYQhgsitldgkPVEGPGAE---------RGVVFQNeglLPWRNVQDNVAFGLQLAGVEK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 404 SSRLTLDSE------LQGNGQ----NLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLV 473
Cdd:PRK11248 103 MQRLEIAHQmlkkvgLEGAEKryiwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQV 182
|
....*.
gi 2159016728 474 -VVTHD 478
Cdd:PRK11248 183 lLITHD 188
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
334-489 |
3.74e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 55.89 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPTP---------VSHLSSNYL-----EQNNFVFS----------------GSVYENL 383
Cdd:PRK10535 37 VAIVGASGSGKSTLMNILGCLDKPTSgtyrvagqdVATLDADALaqlrrEHFGFIFQryhllshltaaqnvevPAVYAGL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 384 SLGKKMDNdwltsqidKVGLSSRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIF 463
Cdd:PRK10535 117 ERKQRLLR--------AQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILH 188
|
170 180
....*....|....*....|....*.
gi 2159016728 464 SLLEPQTKLVVVTHDSSYLGHFDKVI 489
Cdd:PRK10535 189 QLRDRGHTVIIVTHDPQVAAQAERVI 214
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
335-477 |
4.32e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 54.74 E-value: 4.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 335 AVIGKSGQGKTILLDTLAGLLTPT---------------------PV-SHLSSNYLEQNNFVFSGSVYENLSLG------ 386
Cdd:PRK13643 36 ALIGHTGSGKSTLLQHLNGLLQPTegkvtvgdivvsstskqkeikPVrKKVGVVFQFPESQLFEETVLKDVAFGpqnfgi 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 387 -KKMDNDWLTSQIDKVGLSSRLTLDSELQgngqnLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSL 465
Cdd:PRK13643 116 pKEKAEKIAAEKLEMVGLADEFWEKSPFE-----LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESI 190
|
170
....*....|..
gi 2159016728 466 LEPQTKLVVVTH 477
Cdd:PRK13643 191 HQSGQTVVLVTH 202
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
421-477 |
4.98e-08 |
|
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: 55.79 E-value: 4.98e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2159016728 421 SGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVVVTH 477
Cdd:TIGR01257 2072 SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSH 2128
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
334-477 |
5.39e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 54.26 E-value: 5.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT---------------------------------PVSHLSSNYLE-------QNnf 373
Cdd:PRK13634 36 VAIIGHTGSGKSTLLQHLNGLLQPTsgtvtigervitagkknkklkplrkkvgivfqfPEHQLFEETVEkdicfgpMN-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 374 vFSGSVYENLSLGKKMdndwltsqIDKVGLSSRLTLDSELQgngqnLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSE 453
Cdd:PRK13634 114 -FGVSEEDAKQKAREM--------IELVGLPEELLARSPFE-----LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180
....*....|....*....|....*
gi 2159016728 454 TGQGLWEIIFSL-LEPQTKLVVVTH 477
Cdd:PRK13634 180 GRKEMMEMFYKLhKEKGLTTVLVTH 204
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
413-477 |
5.62e-08 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 53.89 E-value: 5.62e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2159016728 413 LQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTkLVVVTH 477
Cdd:COG1117 148 LKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYT-IVIVTH 211
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
273-491 |
7.21e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 54.89 E-value: 7.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 273 LLSASLTRAFTGLLDV-YRL-LDQSREDFSALKGILDHEEKLTGVSQ------VLNQVlEELAKPNvNTIAVIGKSGQGK 344
Cdd:PLN03211 30 LLLSSCYPITLKFMDVcYRVkFENMKNKGSNIKRILGHKPKISDETRqiqertILNGV-TGMASPG-EILAVLGPSGSGK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 345 TILLDTLAGLL--------------TPTPVSHLSSNYLEQNNFVFSG-SVYENL----------SLGKKMDNDWLTSQID 399
Cdd:PLN03211 108 STLLNALAGRIqgnnftgtilannrKPTKQILKRTGFVTQDDILYPHlTVRETLvfcsllrlpkSLTKQEKILVAESVIS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 400 KVGLSSrltLDSELQGNG--QNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVVVTH 477
Cdd:PLN03211 188 ELGLTK---CENTIIGNSfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
|
250
....*....|....*.
gi 2159016728 478 --DSSYLGHFDKVITL 491
Cdd:PLN03211 265 qpSSRVYQMFDSVLVL 280
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
334-491 |
8.35e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 53.48 E-value: 8.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLT--PTPVSHLS----------------------SNYL-EQNNFVFSGSVYENLSLGK- 387
Cdd:PRK09984 33 VALLGPSGSGKSTLLRHLSGLITgdKSAGSHIEllgrtvqregrlardirksranTGYIfQQFNLVNRLSVLENVLIGAl 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 388 ------KMDNDWLTSQIDKVGLS--SRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLW 459
Cdd:PRK09984 113 gstpfwRTCFSWFTREQKQRALQalTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVM 192
|
170 180 190
....*....|....*....|....*....|....
gi 2159016728 460 EIIFSLLEPQTKLVVVT-HDSSY-LGHFDKVITL 491
Cdd:PRK09984 193 DTLRDINQNDGITVVVTlHQVDYaLRYCERIVAL 226
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
334-456 |
1.01e-07 |
|
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: 54.92 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTP---TPVSHLSSN------------YLEQNNFVFSGSVYENLSLGKKMDNDWLTSQI 398
Cdd:TIGR01271 1248 VGLLGRTGSGKSTLLSALLRLLSTegeIQIDGVSWNsvtlqtwrkafgVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVA 1327
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2159016728 399 DKVGLSSRL-----TLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQ 456
Cdd:TIGR01271 1328 EEVGLKSVIeqfpdKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQ 1390
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
317-465 |
1.02e-07 |
|
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: 52.22 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 317 QVLNQVLEELAKPNVntIAVIGKSGQGKTILLDTLAGLLTPT----------------PVSHLSSnYLEQNNFVFSGSVY 380
Cdd:cd03268 14 RVLDDISLHVKKGEI--YGFLGPNGAGKTTTMKIILGLIKPDsgeitfdgksyqknieALRRIGA-LIEAPGFYPNLTAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 381 ENLSLGKKM---DNDWLTSQIDKVGLSsrltlDSELQGNGQnLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQG 457
Cdd:cd03268 91 ENLRLLARLlgiRKKRIDEVLDVVGLK-----DSAKKKVKG-FSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKE 164
|
....*...
gi 2159016728 458 LWEIIFSL 465
Cdd:cd03268 165 LRELILSL 172
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
336-478 |
1.14e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 52.57 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 336 VIGKSGQGKTILLDTLAGLLTPTP---------VSHLSSN-----------YLEQNNFVFSGSVYENLSL-----GKKMD 390
Cdd:PRK10908 33 LTGHSGAGKSTLLKLICGIERPSAgkiwfsghdITRLKNRevpflrrqigmIFQDHHLLMDRTVYDNVAIpliiaGASGD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 391 N--DWLTSQIDKVGLssrltLDSELQGNGQnLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEP 468
Cdd:PRK10908 113 DirRRVSAALDKVGL-----LDKAKNFPIQ-LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRV 186
|
170
....*....|
gi 2159016728 469 QTKLVVVTHD 478
Cdd:PRK10908 187 GVTVLMATHD 196
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
420-478 |
1.21e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 53.18 E-value: 1.21e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2159016728 420 LSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTkLVVVTHD 478
Cdd:PRK14271 164 LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLT-VIIVTHN 221
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
314-478 |
1.42e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 52.42 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 314 GVSQVLNQVLEELAKPNVNTIavIGKSGQGKTILLDTLAGLLTPTpvshlsSNYLEQNNFVFSGSVYENLSL-------- 385
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTL--LGPNGAGKSTLVRVVLGLVAPD------EGVIKRNGKLRIGYVPQKLYLdttlpltv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 386 GKKMDNDWLTSQIDKVGLSSRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSL 465
Cdd:PRK09544 87 NRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQL 166
|
170
....*....|....
gi 2159016728 466 L-EPQTKLVVVTHD 478
Cdd:PRK09544 167 RrELDCAVLMVSHD 180
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
332-451 |
1.50e-07 |
|
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: 51.72 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 332 NTIAVIGKSGQGKTILLDTLAGLLTPT---------------PVSHLSSNYL-EQNNFVFSGSVYENLSLGKKM-DNDWL 394
Cdd:cd03231 27 EALQVTGPNGSGKTTLLRILAGLSPPLagrvllnggpldfqrDSIARGLLYLgHAPGIKTTLSVLENLRFWHADhSDEQV 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2159016728 395 TSQIDKVGLSSrltldSELQGNGQnLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLD 451
Cdd:cd03231 107 EEALARVGLNG-----FEDRPVAQ-LSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
334-478 |
1.52e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.80 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPTPVS-----HLSSNYLEQNNFVF--SGSVYENLSLGKKmdndwltsqidkvglssr 406
Cdd:PRK11147 348 IALIGPNGCGKTTLLKLMLGQLQADSGRihcgtKLEVAYFDQHRAELdpEKTVMDNLAEGKQ------------------ 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 407 ltldsELQGNGQN-----------------------LSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIF 463
Cdd:PRK11147 410 -----EVMVNGRPrhvlgylqdflfhpkramtpvkaLSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLD 484
|
170
....*....|....*
gi 2159016728 464 SLlepQTKLVVVTHD 478
Cdd:PRK11147 485 SY---QGTVLLVSHD 496
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
329-462 |
1.53e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 52.88 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 329 PNVNTIAVIGKSGQGKTILLDTLAGLLTPTPVSHL-------SSNYLEQNNFV-----------FSGSVYENLSLGK--- 387
Cdd:PRK13652 28 PRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLirgepitKENIREVRKFVglvfqnpddqiFSPTVEQDIAFGPinl 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2159016728 388 KMDNDWLTSQIDKVglSSRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSetgQGLWEII 462
Cdd:PRK13652 108 GLDEETVAHRVSSA--LHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP---QGVKELI 177
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
334-453 |
1.66e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.66 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPTPVSHLSS-------NYLEQNnfvFSGSVYENL-SLGKKMDNDWLTSQIDKvglss 405
Cdd:PRK13409 368 IGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisykpQYIKPD---YDGTVEDLLrSITDDLGSSYYKSEIIK----- 439
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2159016728 406 RLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSE 453
Cdd:PRK13409 440 PLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 487
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
334-478 |
1.75e-07 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 53.31 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSNYLEQ--------NNFVFSGSVYENLSLGKKMDndwlTS 396
Cdd:PRK09536 32 VGLVGPNGAGKTTLLRAINGTLTPTagtvlvagdDVEALSARAASRrvasvpqdTSLSFEFDVRQVVEMGRTPH----RS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 397 QIDKVGLSSRLTLDSELQGNG---------QNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLE 467
Cdd:PRK09536 108 RFDTWTETDRAAVERAMERTGvaqfadrpvTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVD 187
|
170
....*....|.
gi 2159016728 468 PQTKLVVVTHD 478
Cdd:PRK09536 188 DGKTAVAAIHD 198
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
334-451 |
1.86e-07 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 53.03 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPTP---------VSHLSSnylEQN--NFVFSG-------SVYENLSLGKKMdndwlt 395
Cdd:PRK09452 43 LTLLGPSGCGKTTVLRLIAGFETPDSgrimldgqdITHVPA---ENRhvNTVFQSyalfphmTVFENVAFGLRM------ 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2159016728 396 SQIDKVGLSSRLT-------LDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLD 451
Cdd:PRK09452 114 QKTPAAEITPRVMealrmvqLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
334-451 |
2.52e-07 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 51.70 E-value: 2.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSNYL--------EQNNFVFSGSVYE-------NLSLGKKM 389
Cdd:PRK13548 31 VAILGPNGAGKSTLLRALSGELSPDsgevrlngrPLADWSPAELarrravlpQHSSLSFPFTVEEvvamgraPHGLSRAE 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2159016728 390 DNDWLTSQIDKVG---LSSRLTldselqgngQNLSGGEKRR------LCFLRAYIHSPELLLLDEPTTGLD 451
Cdd:PRK13548 111 DDALVAAALAQVDlahLAGRDY---------PQLSGGEQQRvqlarvLAQLWEPDGPPRWLLLDEPTSALD 172
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
334-467 |
2.81e-07 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 51.51 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTP---------TPVSHLSSN--------YLEQNNFVFSG-SVYEN----LSLGKKMDN 391
Cdd:TIGR04406 30 VGLLGPNGAGKTTSFYMIVGLVRPdagkilidgQDITHLPMHerarlgigYLPQEASIFRKlTVEENimavLEIRKDLDR 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2159016728 392 DWLTSQIDKvgLSSRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLE 467
Cdd:TIGR04406 110 AEREERLEA--LLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVGDIKKIIKHLKE 183
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
314-480 |
3.55e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 51.42 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 314 GVSQVLNQVLEELAKPNVNTIavIGKSGQGKTILLDTLAGL--------------LTPTPVSHLSSNYLE---QNNFVFS 376
Cdd:PRK11614 16 GKIQALHEVSLHINQGEIVTL--IGANGAGKTTLLGTLCGDpratsgrivfdgkdITDWQTAKIMREAVAivpEGRRVFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 377 G-SVYENLSLGKKM-DNDWLTSQIDKV-GLSSRLtLDSELQGNGqNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSE 453
Cdd:PRK11614 94 RmTVEENLAMGGFFaERDQFQERIKWVyELFPRL-HERRIQRAG-TMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPI 171
|
170 180
....*....|....*....|....*..
gi 2159016728 454 TGQGLWEIIFSLLEPQTKLVVVTHDSS 480
Cdd:PRK11614 172 IIQQIFDTIEQLREQGMTIFLVEQNAN 198
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
333-478 |
3.60e-07 |
|
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: 51.15 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 333 TIAVIGKSGQGKTILLDTLAGLLTPT--------------PVSHLSSN--YLEQNNFVFSG-SVYENLSLGKKMdNDWLT 395
Cdd:cd03295 29 FLVLIGPSGSGKTTTMKMINRLIEPTsgeifidgedireqDPVELRRKigYVIQQIGLFPHmTVEENIALVPKL-LKWPK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 396 SQIDK--------VGLSSRLTLD---SELqgngqnlSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFS 464
Cdd:cd03295 108 EKIREradellalVGLDPAEFADrypHEL-------SGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKR 180
|
170
....*....|....*
gi 2159016728 465 LLEPQTKLVV-VTHD 478
Cdd:cd03295 181 LQQELGKTIVfVTHD 195
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
336-489 |
4.23e-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: 51.21 E-value: 4.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 336 VIGKSGQGKTILLDTLAGLLTP------------TPVSHLSSNYLeQNNF----------------------VFSGSVYE 381
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPnlgkfddppdwdEILDEFRGSEL-QNYFtkllegdvkvivkpqyvdlipkAVKGKVGE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 382 NLSlgKKMDNDWLTSQIDkvglssRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEI 461
Cdd:cd03236 110 LLK--KKDERGKLDELVD------QLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARL 181
|
170 180
....*....|....*....|....*...
gi 2159016728 462 IFSLLEPQTKLVVVTHDSSYLGHFDKVI 489
Cdd:cd03236 182 IRELAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
320-456 |
4.79e-07 |
|
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: 51.39 E-value: 4.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 320 NQVLEEL---AKPNvNTIAVIGKSGQGKTILLDTLAGLLT---PTPVSHLSSN------------YLEQNNFVFSGSVYE 381
Cdd:cd03289 17 NAVLENIsfsISPG-QRVGLLGRTGSGKSTLLSAFLRLLNtegDIQIDGVSWNsvplqkwrkafgVIPQKVFIFSGTFRK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 382 NLSLGKKMDNDWLTSQIDKVGLSSRL-----TLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQ 456
Cdd:cd03289 96 NLDPYGKWSDEEIWKVAEEVGLKSVIeqfpgQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQ 175
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
398-478 |
5.04e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 51.24 E-value: 5.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 398 IDKVGLSsrltlDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSetgQGLWEI--IFSLLEPQTKLVV- 474
Cdd:PRK13651 149 IELVGLD-----ESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDP---QGVKEIleIFDNLNKQGKTIIl 220
|
....
gi 2159016728 475 VTHD 478
Cdd:PRK13651 221 VTHD 224
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
335-451 |
5.21e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 51.80 E-value: 5.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 335 AVIGKSGQGKTILLDTLAGLLTP----------TPVSHLSSNYL--EQNN--FVFSG-------SVYENLSLG--KKMDn 391
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPqkgrivlngrVLFDAEKGICLppEKRRigYVFQDarlfphyKVRGNLRYGmaKSMV- 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2159016728 392 dwltSQIDK-VGLssrLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLD 451
Cdd:PRK11144 107 ----AQFDKiVAL---LGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
336-491 |
5.60e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.47 E-value: 5.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 336 VIGKSGQGKTILLDTLaglLTPTPVSH------LSSNYLEQNNFVFSGSVYENLSLGKKMDNDWLTSQIDKVGLSSRLT- 408
Cdd:PTZ00243 691 VLGATGSGKSTLLQSL---LSQFEISEgrvwaeRSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAq 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 409 ----LDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLW-EIIFSLLEPQTKlVVVTHDSSYLG 483
Cdd:PTZ00243 768 lgggLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVeECFLGALAGKTR-VLATHQVHVVP 846
|
....*...
gi 2159016728 484 HFDKVITL 491
Cdd:PTZ00243 847 RADYVVAL 854
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
327-492 |
6.32e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 51.89 E-value: 6.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 327 AKPNvNTIAVIGKSGQGKTILLDTLAGLLTP---------TPVSHLSSNYLEQNNFV-------FSGSVYENLSLGKK-- 388
Cdd:PRK13657 358 AKPG-QTVAIVGPTGAGKSTLINLLQRVFDPqsgrilidgTDIRTVTRASLRRNIAVvfqdaglFNRSIEDNIRVGRPda 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 389 ------------MDNDWLTSQIDKvglssrltLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQ 456
Cdd:PRK13657 437 tdeemraaaeraQAHDFIERKPDG--------YDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEA 508
|
170 180 190
....*....|....*....|....*....|....*.
gi 2159016728 457 GLWEIIFSLLEPQTKLvVVTHDSSYLGHFDKVITLD 492
Cdd:PRK13657 509 KVKAALDELMKGRTTF-IIAHRLSTVRNADRILVFD 543
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
336-492 |
6.33e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 51.39 E-value: 6.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 336 VIGKSGQGKTILLDTLAGLLTPT--------------PVSHLSSNYLEQ---NNF-----------------VFSGSVYE 381
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKygtiqvgdiyigdkKNNHELITNPYSkkiKNFkelrrrvsmvfqfpeyqLFKDTIEK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 382 NLSLG------KKMDNDWLTS-QIDKVGLSsrltlDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSET 454
Cdd:PRK13631 137 DIMFGpvalgvKKSEAKKLAKfYLNKMGLD-----DSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKG 211
|
170 180 190
....*....|....*....|....*....|....*....
gi 2159016728 455 GQGLWEIIFSLLEPQTKLVVVTHD-SSYLGHFDKVITLD 492
Cdd:PRK13631 212 EHEMMQLILDAKANNKTVFVITHTmEHVLEVADEVIVMD 250
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
317-492 |
7.79e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 50.46 E-value: 7.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 317 QVLNQVleELAKPNVNTIAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSNylEQNNF------VFS---GS 378
Cdd:PRK10419 26 TVLNNV--SLSLKSGETVALLGRSGCGKSTLARLLVGLESPSqgnvswrgePLAKLNRA--QRKAFrrdiqmVFQdsiSA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 379 VYENLSLGKKMDNDW--LTSqIDKVGLSSRLT-------LDSE-LQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTT 448
Cdd:PRK10419 102 VNPRKTVREIIREPLrhLLS-LDKAERLARASemlravdLDDSvLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2159016728 449 GLDSEtgqgLWEIIFSLLEP-----QTKLVVVTHDSSYLGHF-DKVITLD 492
Cdd:PRK10419 181 NLDLV----LQAGVIRLLKKlqqqfGTACLFITHDLRLVERFcQRVMVMD 226
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
334-451 |
8.23e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 50.47 E-value: 8.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLS----SNYLEQnnfVF---------SGSVYENLSL----GK 387
Cdd:COG1101 35 VTVIGSNGAGKSTLLNAIAGSLPPDsgsilidgkDVTKLPeykrAKYIGR---VFqdpmmgtapSMTIEENLALayrrGK 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2159016728 388 KMdndWLTSQIDK--------------VGLSSRLTLDSELqgngqnLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLD 451
Cdd:COG1101 112 RR---GLRRGLTKkrrelfrellatlgLGLENRLDTKVGL------LSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
421-478 |
9.42e-07 |
|
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: 49.74 E-value: 9.42e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2159016728 421 SGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVVVTHD 478
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHD 211
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
334-451 |
9.58e-07 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 50.84 E-value: 9.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSnylEQNN--FVF-------SGSVYENLSLG---KKMDND 392
Cdd:COG3839 32 LVLLGPSGCGKSTLLRMIAGLEDPTsgeiliggrDVTDLPP---KDRNiaMVFqsyalypHMTVYENIAFPlklRKVPKA 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2159016728 393 wltsQID-KVG-LSSRLTLDSELQGNGQNLSGGEKRR--LCflRAYIHSPELLLLDEPTTGLD 451
Cdd:COG3839 109 ----EIDrRVReAAELLGLEDLLDRKPKQLSGGQRQRvaLG--RALVREPKVFLLDEPLSNLD 165
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
419-477 |
1.20e-06 |
|
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: 49.06 E-value: 1.20e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2159016728 419 NLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVVVTH 477
Cdd:cd03217 104 GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITH 162
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
335-478 |
1.20e-06 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 50.46 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 335 AVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSNYLEQN----NFVF-------SGSVYENLSLGKKMDNdWL 394
Cdd:COG1135 35 GIIGYSGAGKSTLIRCINLLERPTsgsvlvdgvDLTALSERELRAArrkiGMIFqhfnllsSRTVAENVALPLEIAG-VP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 395 TSQIDK--------VGLSSRltldselqgnGQ----NLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGlweiI 462
Cdd:COG1135 114 KAEIRKrvaellelVGLSDK----------ADaypsQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRS----I 179
|
170 180
....*....|....*....|.
gi 2159016728 463 FSLL-EPQTKL----VVVTHD 478
Cdd:COG1135 180 LDLLkDINRELgltiVLITHE 200
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
420-462 |
1.24e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.28 E-value: 1.24e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2159016728 420 LSGGEKRRL---CflrAYIHSPELLLLDEPTTGLDSETGQGLWEII 462
Cdd:NF033858 137 LSGGMKQKLglcC---ALIHDPDLLILDEPTTGVDPLSRRQFWELI 179
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
334-492 |
1.37e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 49.60 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPTP---------VSHLSSNYLEQ----------NNFVFSgSVYENLSLG---KKMDN 391
Cdd:PRK13632 38 VAILGHNGSGKSTISKILTGLLKPQSgeikidgitISKENLKEIRKkigiifqnpdNQFIGA-TVEDDIAFGlenKKVPP 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 392 DWLTSQIDKvgLSSRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTK 471
Cdd:PRK13632 117 KKMKDIIDD--LAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKK 194
|
170 180
....*....|....*....|..
gi 2159016728 472 -LVVVTHDSSYLGHFDKVITLD 492
Cdd:PRK13632 195 tLISITHDMDEAILADKVIVFS 216
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
334-478 |
1.44e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.01 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPTPVSHLSSNYLEQNnfVFSGSVYENLSLGKK-----------MDNDWLTSQIDKVG 402
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMA--VFSQHHVDGLDLSSNpllymmrcfpgVPEQKLRAHLGSFG 615
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2159016728 403 LSSRLTLDSELqgngqNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLweiIFSLLEPQTKLVVVTHD 478
Cdd:PLN03073 616 VTGNLALQPMY-----TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEAL---IQGLVLFQGGVLMVSHD 683
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
317-462 |
1.54e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.88 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 317 QVLNQVlEELAKPNVNTiAVIGKSGQGKTILLDTLAGLLTPTPVSH---------------LSSNYLEQNN--------- 372
Cdd:TIGR00956 777 VILNNV-DGWVKPGTLT-ALMGASGAGKTTLLNVLAERVTTGVITGgdrlvngrpldssfqRSIGYVQQQDlhlptstvr 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 373 --FVFSGSVYENLSLGKKMDNDWLTSQIDKVGLSSrlTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLL-LDEPTTG 449
Cdd:TIGR00956 855 esLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMES--YADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSG 932
|
170
....*....|...
gi 2159016728 450 LDSETGqglWEII 462
Cdd:TIGR00956 933 LDSQTA---WSIC 942
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
391-482 |
1.58e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.72 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 391 NDW-LTSQIDKVGLSSRLTLDSELQgngqNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIifsLLEPQ 469
Cdd:PRK11147 131 NLWqLENRINEVLAQLGLDPDAALS----SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGF---LKTFQ 203
|
90
....*....|...
gi 2159016728 470 TKLVVVTHDSSYL 482
Cdd:PRK11147 204 GSIIFISHDRSFI 216
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
334-453 |
1.61e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.55 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPTPVShLSSN--------YLEQNnfvFSGSVYENLS--LGKKMDNDWLTSQIDKvgl 403
Cdd:COG1245 369 LGIVGPNGIGKTTFAKILAGVLKPDEGE-VDEDlkisykpqYISPD---YDGTVEEFLRsaNTDDFGSSYYKTEIIK--- 441
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2159016728 404 ssRLTLDSELQGNGQNLSGGEKRRL----CFLRayihSPELLLLDEPTTGLDSE 453
Cdd:COG1245 442 --PLGLEKLLDKNVKDLSGGELQRVaiaaCLSR----DADLYLLDEPSAHLDVE 489
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
334-492 |
1.79e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 49.60 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPTPVSHLSSNyLEQNNFV-------FSGSVYENLS---LGKKMDNDW---------- 393
Cdd:PRK13644 31 IGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG-IDTGDFSklqgirkLVGIVFQNPEtqfVGRTVEEDLafgpenlclp 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 394 ---LTSQIDKVglSSRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQT 470
Cdd:PRK13644 110 pieIRKRVDRA--LAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGK 187
|
170 180
....*....|....*....|..
gi 2159016728 471 KLVVVTHDSSYLGHFDKVITLD 492
Cdd:PRK13644 188 TIVYITHNLEELHDADRIIVMD 209
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
421-478 |
1.83e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.55 E-value: 1.83e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2159016728 421 SGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEiifSLLEPQTKLVVVTHD 478
Cdd:PRK10636 432 SGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTE---ALIDFEGALVVVSHD 486
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
335-478 |
2.10e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 49.39 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 335 AVIGKSGQGKTILLDTLAGLLTPT----PVSHLSSNYLEQNNFV------------------FSGSVYENLSLGKK---M 389
Cdd:PRK13646 37 AIVGQTGSGKSTLIQNINALLKPTtgtvTVDDITITHKTKDKYIrpvrkrigmvfqfpesqlFEDTVEREIIFGPKnfkM 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 390 DNDWLTSQIDKV----GLSSRLTLDSELQgngqnLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSL 465
Cdd:PRK13646 117 NLDEVKNYAHRLlmdlGFSRDVMSQSPFQ-----MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSL 191
|
170
....*....|....
gi 2159016728 466 LEPQTK-LVVVTHD 478
Cdd:PRK13646 192 QTDENKtIILVSHD 205
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
328-492 |
2.25e-06 |
|
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: 48.01 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 328 KPNVNTiAVIGKSGQGKTILLDTLAGLLT-------------PTPVSHL-SSNYLEQNNFVFSGS-VYENLSLGKKMDnd 392
Cdd:cd03232 31 KPGTLT-ALMGESGAGKTTLLDVLAGRKTagvitgeilingrPLDKNFQrSTGYVEQQDVHSPNLtVREALRFSALLR-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 393 wltsqidkvGLS----SRLTLDSELQGNgqnlsggekrrlcflrayihsPELLLLDEPTTGLDSETGQGLWEIIFSLLEP 468
Cdd:cd03232 108 ---------GLSveqrKRLTIGVELAAK---------------------PSILFLDEPTSGLDSQAAYNIVRFLKKLADS 157
|
170 180
....*....|....*....|....*.
gi 2159016728 469 QTKLVVVTH--DSSYLGHFDKVITLD 492
Cdd:cd03232 158 GQAILCTIHqpSASIFEKFDRLLLLK 183
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
317-478 |
2.42e-06 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 49.37 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 317 QVLNQVleELAKPNVNTIAVIGKSGQGKTILLDTLAGLLTPTP----------VSHLSSnylEQNN--FVFSG------- 377
Cdd:COG1118 16 TLLDDV--SLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSgrivlngrdlFTNLPP---RERRvgFVFQHyalfphm 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 378 SVYENLSLG-----------KKMDNDWLtsqiDKVGLSsrltldsELqGN---GQnLSGGEKRRLCFLRAYIHSPELLLL 443
Cdd:COG1118 91 TVAENIAFGlrvrppskaeiRARVEELL----ELVQLE-------GL-ADrypSQ-LSGGQRQRVALARALAVEPEVLLL 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 2159016728 444 DEPTTGLDSETGQGLWEIIFSLLEpQTKLVV--VTHD 478
Cdd:COG1118 158 DEPFGALDAKVRKELRRWLRRLHD-ELGGTTvfVTHD 193
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
334-477 |
2.47e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 48.42 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPTPVShlSSNYLEQNNFVFSGSVYENLslGKKMDNDWLTSQIDKVGLSSRLTLDSEL 413
Cdd:COG2401 59 VLIVGASGSGKSTLLRLLAGALKGTPVA--GCVDVPDNQFGREASLIDAI--GRKGDFKDAVELLNAVGLSDAVLWLRRF 134
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2159016728 414 QgngqNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLL-EPQTKLVVVTH 477
Cdd:COG2401 135 K----ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLArRAGITLVVATH 195
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
337-451 |
2.64e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 49.32 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 337 IGKSGQGKTILLDTLAGLLTPT----------PVSHlSSNYLEQNNFVFsG---------SVYENLSLGKKM---DNDWL 394
Cdd:COG4586 54 IGPNGAGKSTTIKMLTGILVPTsgevrvlgyvPFKR-RKEFARRIGVVF-GqrsqlwwdlPAIDSFRLLKAIyriPDAEY 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2159016728 395 TSQIDKvgLSSRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLD 451
Cdd:COG4586 132 KKRLDE--LVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLD 186
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
370-492 |
2.84e-06 |
|
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: 50.33 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 370 QNNFVFSGSVYENLS-LGKKMDND-WLTSQIDKV-GLSSRL--TLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLD 444
Cdd:TIGR00957 1367 QDPVLFSGSLRMNLDpFSQYSDEEvWWALELAHLkTFVSALpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLD 1446
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2159016728 445 EPTTGLDSETGQGLWEIIFSLLEPQTKLvVVTHDSSYLGHFDKVITLD 492
Cdd:TIGR00957 1447 EATAAVDLETDNLIQSTIRTQFEDCTVL-TIAHRLNTIMDYTRVIVLD 1493
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
334-478 |
3.08e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 48.92 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSNYLE---------QN--NFVFSGSVYEN-----LSLGKK 388
Cdd:PRK13639 31 VALLGPNGAGKSTLFLHFNGILKPTsgevlikgePIKYDKKSLLEvrktvgivfQNpdDQLFAPTVEEDvafgpLNLGLS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 389 MDN--DWLTSQIDKVGLSsrltlDSElQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLL 466
Cdd:PRK13639 111 KEEveKRVKEALKAVGME-----GFE-NKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLN 184
|
170
....*....|..
gi 2159016728 467 EPQTKLVVVTHD 478
Cdd:PRK13639 185 KEGITIIISTHD 196
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
337-492 |
3.42e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 49.26 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 337 IGKSGQGKTILLDTLAGLLTPTP----VSHLSSNYLEQNN----FVFSG-------SVYENLSLGKKMdndwltSQIDKV 401
Cdd:PRK11000 35 VGPSGCGKSTLLRMIAGLEDITSgdlfIGEKRMNDVPPAErgvgMVFQSyalyphlSVAENMSFGLKL------AGAKKE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 402 GLSSR-------LTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETG-QGLWEIifSLLEPQTK-- 471
Cdd:PRK11000 109 EINQRvnqvaevLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRvQMRIEI--SRLHKRLGrt 186
|
170 180
....*....|....*....|..
gi 2159016728 472 LVVVTHDS-SYLGHFDKVITLD 492
Cdd:PRK11000 187 MIYVTHDQvEAMTLADKIVVLD 208
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
375-489 |
3.80e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.96 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 375 FSGSvyENLSL-GKKMDNDWLTSQIDKVGLSSRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSE 453
Cdd:NF000106 101 FSGR--ENLYMiGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPR 178
|
90 100 110
....*....|....*....|....*....|....*....
gi 2159016728 454 TGQGLWEIIFSLLEPQTKLVVVTH---DSSYLGHFDKVI 489
Cdd:NF000106 179 TRNEVWDEVRSMVRDGATVLLTTQymeEAEQLAHELTVI 217
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
334-491 |
4.44e-06 |
|
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: 47.98 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTIL-------LDTLAGLL-------TPTPVSHLSS--NYLEQNNFVFSGSVYENLSLGKKMDNDWLTSQ 397
Cdd:cd03288 50 VGICGRTGSGKSSLslaffrmVDIFDGKIvidgidiSKLPLHTLRSrlSIILQDPILFSGSIRFNLDPECKCTDDRLWEA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 398 IDKVGLSSRLT-----LDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTkL 472
Cdd:cd03288 130 LEIAQLKNMVKslpggLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRT-V 208
|
170
....*....|....*....
gi 2159016728 473 VVVTHDSSYLGHFDKVITL 491
Cdd:cd03288 209 VTIAHRVSTILDADLVLVL 227
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
329-478 |
4.75e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 48.12 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 329 PNVNTIAVIGKSGQGKTILLDTLAGLL-------------------------------------TPTPVSHLSsnyleqn 371
Cdd:PRK14246 34 PNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskikvdgkvlyfgkdifqidaiklrkevgmvfqQPNPFPHLS------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 372 nfVFSGSVYENLSLG---KKMDNDWLTSQIDKVGLSSRLTldSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTT 448
Cdd:PRK14246 107 --IYDNIAYPLKSHGikeKREIKKIVEECLRKVGLWKEVY--DRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190
....*....|....*....|....*....|
gi 2159016728 449 GLDSETGQGLwEIIFSLLEPQTKLVVVTHD 478
Cdd:PRK14246 183 MIDIVNSQAI-EKLITELKNEIAIVIVSHN 211
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
335-477 |
5.12e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 48.20 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 335 AVIGKSGQGKTILLDTLAGLLTPTP----VSHLSSNYLEQN------------------NFVFSGSVYENLSLGKKmdnD 392
Cdd:PRK13649 37 AFIGHTGSGKSTIMQLLNGLHVPTQgsvrVDDTLITSTSKNkdikqirkkvglvfqfpeSQLFEETVLKDVAFGPQ---N 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 393 WLTSQIDKVGLS-SRLTL----DSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLE 467
Cdd:PRK13649 114 FGVSQEEAEALArEKLALvgisESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQ 193
|
170
....*....|
gi 2159016728 468 PQTKLVVVTH 477
Cdd:PRK13649 194 SGMTIVLVTH 203
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
336-478 |
5.78e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.96 E-value: 5.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 336 VIGKSGQGKTILLDTLAGLLTPT-------PVSHLSsnYLEQNNFVFSG--SVYENLSLGkkmdNDWLtsQIDKVGLSSR 406
Cdd:PRK11819 355 IIGPNGAGKSTLFKMITGQEQPDsgtikigETVKLA--YVDQSRDALDPnkTVWEEISGG----LDII--KVGNREIPSR 426
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2159016728 407 LTLDS-ELQGNGQ-----NLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEiifSLLEPQTKLVVVTHD 478
Cdd:PRK11819 427 AYVGRfNFKGGDQqkkvgVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEE---ALLEFPGCAVVISHD 501
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
333-451 |
6.40e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.55 E-value: 6.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 333 TIAVIGKSGQGKTILLDTLAGLLTPTPVSHLSSNYLEQNNFVFSGS--------------------------------VY 380
Cdd:PRK15134 37 TLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGESLLHASeqtlrgvrgnkiamifqepmvslnplhtlekqLY 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2159016728 381 ENLSLGKKMDNDWLTSQI----DKVGL---SSRLTlDSELQgngqnLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLD 451
Cdd:PRK15134 117 EVLSLHRGMRREAARGEIlnclDRVGIrqaAKRLT-DYPHQ-----LSGGERQRVMIAMALLTRPELLIADEPTTALD 188
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
336-451 |
7.77e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 46.72 E-value: 7.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 336 VIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSNYLEqnNFVFSG---------SVYENL----SLGKKMDNDW 393
Cdd:PRK13538 32 IEGPNGAGKTSLLRILAGLARPDagevlwqgePIRRQRDEYHQ--DLLYLGhqpgiktelTALENLrfyqRLHGPGDDEA 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2159016728 394 LTSQIDKVGLSSRLTLDSElqgngqNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLD 451
Cdd:PRK13538 110 LWEALAQVGLAGFEDVPVR------QLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
420-451 |
8.80e-06 |
|
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: 47.74 E-value: 8.80e-06
10 20 30
....*....|....*....|....*....|..
gi 2159016728 420 LSGGEKRRLCFLRAYIHSPELLLLDEPTTGLD 451
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALD 182
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
84-288 |
9.70e-06 |
|
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: 47.47 E-value: 9.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 84 RSLFSQLIRKPFSHFKRLEIGSLASKFERGLgsyeQFINLSVSRGLPLTIELFAL---GCAIIFFSGWLtFTLVVF---- 156
Cdd:cd18577 84 KRYLKALLRQDIAWFDKNGAGELTSRLTSDT----NLIQDGIGEKLGLLIQSLSTfiaGFIIAFIYSWK-LTLVLLatlp 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 157 VLMIATMIKTRIIRlrrPHISRVNEAEDE---ILDQivgVFSGIRTIQSNRVEGFFEKRlgpfFENYRQATVSLAVSRSV 233
Cdd:cd18577 159 LIAIVGGIMGKLLS---KYTKKEQEAYAKagsIAEE---ALSSIRTVKAFGGEEKEIKR----YSKALEKARKAGIKKGL 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2159016728 234 FDGVAIATHSLISLSIITL-FIF--YLFPEQHSDAGQLVTA----LLLSASLTRAFTGLLDV 288
Cdd:cd18577 229 VSGLGLGLLFFIIFAMYALaFWYgsRLVRDGEISPGDVLTVffavLIGAFSLGQIAPNLQAF 290
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
335-489 |
1.13e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 45.78 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 335 AVIGKSGQGK-TILLDTLAGLLTPTPVSHLSSNYleQNNFVFSGSVyenlslgkkmdndwltSQIDKVGLSSrLTLDSEL 413
Cdd:cd03238 25 VVTGVSGSGKsTLVNEGLYASGKARLISFLPKFS--RNKLIFIDQL----------------QFLIDVGLGY-LTLGQKL 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2159016728 414 QgngqNLSGGEKRRL---CFLRAYIHsPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVVVTHDSSYLGHFDKVI 489
Cdd:cd03238 86 S----TLSGGELQRVklaSELFSEPP-GTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWII 159
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
57-297 |
1.16e-05 |
|
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: 47.20 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 57 TLVTIIISPFFTYFF-EQEVQINVETKSRsLFSQLIRKPFSHFKRLEIGSLASKFeRGLGSYEQFInlsVSRGLPLTIE- 134
Cdd:cd18782 52 ALLEAVLTALRTYLFtDTANRIDLELGGT-IIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFL---TGTALTTLLDv 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 135 LFALGCAIIFFSGWLTFTLVVFV---LMIATMIKtrIIRLRRPHISRVNEAEDEILDQIVGVFSGIRTIQSNRVEGFFEK 211
Cdd:cd18782 127 LFSVIYIAVLFSYSPLLTLVVLAtvpLQLLLTFL--FGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARW 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 212 RLGPFFENYRQATVSLAVSRSVFDGVAiathSLISLSIITLFIF---YLFPEQHSDAGQLVTALLLSASLTRA---FTGL 285
Cdd:cd18782 205 RWQNRYARSLGEGFKLTVLGTTSGSLS----QFLNKLSSLLVLWvgaYLVLRGELTLGQLIAFRILSGYVTGPilrLSTL 280
|
250
....*....|..
gi 2159016728 286 LDVYRLLDQSRE 297
Cdd:cd18782 281 WQQFQELRVSLE 292
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
311-451 |
1.19e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 46.96 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 311 KLTGVSQVLNQ--VLEELAKPNVNT-------IAVIGKSGQGKTILLDTLAGLLTPTPVS-------------HLSS--- 365
Cdd:PRK13637 4 KIENLTHIYMEgtPFEKKALDNVNIeiedgefVGLIGHTGSGKSTLIQHLNGLLKPTSGKiiidgvditdkkvKLSDirk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 366 ------NYLEQNnfVFSGSVYE-------NLSLGKKMDNDWLTSQIDKVGLSSRLTLD-SELQgngqnLSGGEKRRLCFL 431
Cdd:PRK13637 84 kvglvfQYPEYQ--LFEETIEKdiafgpiNLGLSEEEIENRVKRAMNIVGLDYEDYKDkSPFE-----LSGGQKRRVAIA 156
|
170 180
....*....|....*....|
gi 2159016728 432 RAYIHSPELLLLDEPTTGLD 451
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLD 176
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
338-451 |
1.45e-05 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 46.18 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 338 GKSGQGKTILLDTLAGLLTPT---------PVSHLSSN--------YLEQNNFVFSG-SVYENL-------SLGKKMDND 392
Cdd:COG1137 36 GPNGAGKTTTFYMIVGLVKPDsgrifldgeDITHLPMHkrarlgigYLPQEASIFRKlTVEDNIlavlelrKLSKKEREE 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2159016728 393 WLTSQIDKVGLSSRLtlDSelqgNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLD 451
Cdd:COG1137 116 RLEELLEEFGITHLR--KS----KAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
334-480 |
1.75e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 46.14 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSNYLE--------QNNFVF-SGSVYENL------------ 383
Cdd:PRK11300 34 VSLIGPNGAGKTTVFNCLTGFYKPTggtillrgqHIEGLPGHQIArmgvvrtfQHVRLFrEMTVIENLlvaqhqqlktgl 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 384 ------------SLGKKMDN--DWLtsqiDKVGLssrLTLDSELQGNgqnLSGGEKRRLCFLRAYIHSPELLLLDEPTTG 449
Cdd:PRK11300 114 fsgllktpafrrAESEALDRaaTWL----ERVGL---LEHANRQAGN---LAYGQQRRLEIARCMVTQPEILMLDEPAAG 183
|
170 180 190
....*....|....*....|....*....|..
gi 2159016728 450 LDSETGQGLWEIIFSLL-EPQTKLVVVTHDSS 480
Cdd:PRK11300 184 LNPKETKELDELIAELRnEHNVTVLLIEHDMK 215
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
367-451 |
2.10e-05 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 46.04 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 367 YLEQNNFVFSG-SVYENLSLGKKMDNDWLTSQidKVGLSSRLTLD---SELQGN-GQNLSGGEKRRLCFLRAYIHSPELL 441
Cdd:PRK10895 82 YLPQEASIFRRlSVYDNLMAVLQIRDDLSAEQ--REDRANELMEEfhiEHLRDSmGQSLSGGERRRVEIARALAANPKFI 159
|
90
....*....|
gi 2159016728 442 LLDEPTTGLD 451
Cdd:PRK10895 160 LLDEPFAGVD 169
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
420-479 |
2.22e-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: 44.66 E-value: 2.22e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2159016728 420 LSGGEKRR--LCF---LRAYIHSPeLLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVVVTHDS 479
Cdd:cd03227 78 LSGGEKELsaLALilaLASLKPRP-LYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLP 141
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
418-492 |
2.49e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 45.95 E-value: 2.49e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2159016728 418 QNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLL-EPQTKLVVVTHDSSYLGHFDKVITLD 492
Cdd:PRK13640 142 ANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkKNNLTVISITHDIDEANMADQVLVLD 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
398-477 |
3.46e-05 |
|
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: 46.33 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 398 IDKVGLSSRLTLDSelqgngQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGqglwEIIFSLLEPQTK-----L 472
Cdd:TIGR03269 153 IEMVQLSHRITHIA------RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTA----KLVHNALEEAVKasgisM 222
|
....*
gi 2159016728 473 VVVTH 477
Cdd:TIGR03269 223 VLTSH 227
|
|
| Rad50_Sulf |
NF041034 |
DNA double-strand break repair ATPase Rad50; |
292-491 |
3.52e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 468963 [Multi-domain] Cd Length: 872 Bit Score: 46.63 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 292 LDQSREDFSALKGILdhEEKLTGVSQVLNQvLEELaKPNVNTIAVIGKSgqgktilLDTLAGLLtptpvSHLSSNYLEqn 371
Cdd:NF041034 658 LNRIEQEISKLEGKI--EALENDIDNLNSE-LEKI-KEKLNKIPKLENA-------IKKLEKLR-----EDLSGSGLQ-- 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 372 NFVFSgsvyenlSLGKKMDNDwLTSQIDKVGLS-SRLTLDSELQGNGQN-------------------LSGGEK------ 425
Cdd:NF041034 720 NYIIS-------NVKSKIENN-LNDILSKFDLSfSRVEIDFEIGGKTKKgkseikayntagqdldvnaLSGGERisiala 791
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2159016728 426 RRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVVVTHDSSYLGHFDKVITL 491
Cdd:NF041034 792 LRLAIAKSLMDEIGFMILDEPTVHLDEERKKELIDIIRSSMEIVPQIIVVTHDEELKEISDYIISV 857
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
387-478 |
3.69e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 45.48 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 387 KKMDnDWLtsqiDKVGLSSRLtlDSELQgngqNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLL 466
Cdd:COG4152 108 RRAD-EWL----ERLGLGDRA--NKKVE----ELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELA 176
|
90
....*....|..
gi 2159016728 467 EPQTKLVVVTHD 478
Cdd:COG4152 177 AKGTTVIFSSHQ 188
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
420-491 |
4.34e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 4.34e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2159016728 420 LSGGEKRRL---CFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVVVTHDSSYLGHFDKVITL 491
Cdd:PRK00635 810 LSGGEIQRLklaYELLAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLEL 884
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
335-451 |
4.55e-05 |
|
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: 45.48 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 335 AVIGKSGQGKTILLDTLAGLLTPtPVSHLSSN-----------YL--EQNN--FVFSG-------SVYENLSLGKKmdnd 392
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERP-DSGRIRLGgevlqdsargiFLppHRRRigYVFQEarlfphlSVRGNLLYGRK---- 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2159016728 393 wltsqiDKVGLSSRLTLDS--ELQGNG-------QNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLD 451
Cdd:COG4148 104 ------RAPRAERRISFDEvvELLGIGhlldrrpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
381-491 |
4.57e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.18 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 381 ENLSLGKK-MDNDWLTSQIDKvglssrltLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLW 459
Cdd:PTZ00265 548 EVVDVSKKvLIHDFVSALPDK--------YETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
|
90 100 110
....*....|....*....|....*....|...
gi 2159016728 460 EIIFSLLEPQTKL-VVVTHDSSYLGHFDKVITL 491
Cdd:PTZ00265 620 KTINNLKGNENRItIIIAHRLSTIRYANTIFVL 652
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
336-479 |
4.84e-05 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 44.39 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 336 VIGKSGQGKTILLDTLAGLLTP------------TPVSHLSSN-----YLEQNNFVFSG-SVYENLSLGkkMDNDWLTSQ 397
Cdd:COG4136 32 LMGPSGSGKSTLLAAIAGTLSPafsasgevllngRRLTALPAEqrrigILFQDDLLFPHlSVGENLAFA--LPPTIGRAQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 398 --------IDKVGLSSRLTLDSElqgngqNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEpQ 469
Cdd:COG4136 110 rrarveqaLEEAGLAGFADRDPA------TLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIR-Q 182
|
170
....*....|..
gi 2159016728 470 TKL--VVVTHDS 479
Cdd:COG4136 183 RGIpaLLVTHDE 194
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
333-492 |
5.19e-05 |
|
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: 44.80 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 333 TIAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSN----YLEQNNFVFS---GSVYENLS----LGKKMDNd 392
Cdd:TIGR02769 39 TVGLLGRSGCGKSTLARLLLGLEKPAqgtvsfrgqDLYQLDRKqrraFRRDVQLVFQdspSAVNPRMTvrqiIGEPLRH- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 393 wLTSQ------------IDKVGLSsrltlDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWE 460
Cdd:TIGR02769 118 -LTSLdeseqkariaelLDMVGLR-----SEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILE 191
|
170 180 190
....*....|....*....|....*....|....
gi 2159016728 461 IIFSL-LEPQTKLVVVTHDSSYLGHF-DKVITLD 492
Cdd:TIGR02769 192 LLRKLqQAFGTAYLFITHDLRLVQSFcQRVAVMD 225
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
421-477 |
5.43e-05 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 44.56 E-value: 5.43e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2159016728 421 SGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVVVTH 477
Cdd:TIGR01978 146 SGGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITH 202
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
420-478 |
5.71e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 45.12 E-value: 5.71e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2159016728 420 LSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSeTGQGlwEIIFSLLEPQTK----LVVVTHD 478
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDV-TIQA--QIIELLLELQQKenmaLVLITHD 213
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
336-454 |
7.33e-05 |
|
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: 43.79 E-value: 7.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 336 VIGKSGQGKTILLDTLAGlltptpvsHLSSNYLEQNNFVFSGsvYENLSLGKKMDNDWLTSQIDKV---GLSSRLTLDSE 412
Cdd:cd03233 38 VLGRPGSGCSTLLKALAN--------RTEGNVSVEGDIHYNG--IPYKEFAEKYPGEIIYVSEEDVhfpTLTVRETLDFA 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2159016728 413 LQGNGQN----LSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSET 454
Cdd:cd03233 108 LRCKGNEfvrgISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
334-478 |
7.78e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 44.15 E-value: 7.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT--------------PVSHLSS-----------NYLEQN-------NFVFSGSVYE 381
Cdd:PRK11701 35 LGIVGESGSGKTTLLNALSARLAPDagevhyrmrdgqlrDLYALSEaerrrllrtewGFVHQHprdglrmQVSAGGNIGE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 382 NL-SLGKK-------MDNDWLtsqidkvglsSRLTLD-SELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDS 452
Cdd:PRK11701 115 RLmAVGARhygdiraTAGDWL----------ERVEIDaARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDV 184
|
170 180
....*....|....*....|....*..
gi 2159016728 453 ETGQGLWEIIFSLL-EPQTKLVVVTHD 478
Cdd:PRK11701 185 SVQARLLDLLRGLVrELGLAVVIVTHD 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
418-492 |
8.56e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 44.36 E-value: 8.56e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2159016728 418 QNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSL-LEPQTKLVVVTHDSSYLGHFDKVITLD 492
Cdd:PRK13648 141 NALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVkSEHNITIISITHDLSEAMEADHVIVMN 216
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
407-482 |
9.09e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.24 E-value: 9.09e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2159016728 407 LTLDSELQGNGQN-LSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETgqGLWEIIFSLLEPQTkLVVVTHDSSYL 482
Cdd:PLN03073 331 LSFTPEMQVKATKtFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA--VLWLETYLLKWPKT-FIVVSHAREFL 404
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
12-270 |
9.18e-05 |
|
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: 44.32 E-value: 9.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 12 LFSVLLLMKVNLA--LPSYLIGQIIN-ITSQSPKLEGLGNLLNYLllstLVTIIISPFFTYF-----FEQEVQINVETKS 83
Cdd:cd18541 2 LLGILFLILVDLLqlLIPRIIGRAIDaLTAGTLTASQLLRYALLI----LLLALLIGIFRFLwryliFGASRRIEYDLRN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 84 RsLFSQLIRKPFSHFKRLEIGSLASKFERGLgsyeQFINLSVSRGLPLTIELFALGCAIIFF----SGWLT-FTLVVFVL 158
Cdd:cd18541 78 D-LFAHLLTLSPSFYQKNRTGDLMARATNDL----NAVRMALGPGILYLVDALFLGVLVLVMmftiSPKLTlIALLPLPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 159 MIATMIK-TRIIRLRrphISRVNEAEDEILDQIVGVFSGIRTIQSNRVEGFFEKRLGPFFENYRQATVSLAVSRSVFDgv 237
Cdd:cd18541 153 LALLVYRlGKKIHKR---FRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFF-- 227
|
250 260 270
....*....|....*....|....*....|....*
gi 2159016728 238 aIATHSLISLSIITLFIF--YLFPEQHSDAGQLVT 270
Cdd:cd18541 228 -PLIGLLIGLSFLIVLWYggRLVIRGTITLGDLVA 261
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
335-477 |
1.28e-04 |
|
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: 42.42 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 335 AVIGKSGQGKTILLDTLAGLLTPTpvshlssnyleqnnfvfSGSVYENlslGKKMDNdwltsqidkvgLSSRltlDSELQ 414
Cdd:cd03216 30 ALLGENGAGKSTLMKILSGLYKPD-----------------SGEILVD---GKEVSF-----------ASPR---DARRA 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2159016728 415 GNG---QnLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVVVTH 477
Cdd:cd03216 76 GIAmvyQ-LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISH 140
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
83-233 |
1.51e-04 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 43.64 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 83 SRSLFSQLIRKPFS-HFKRlEIGSLASKFERGLGSYEQFINLSVSRGLPLTIElFALGCAIIFFS-GWlTFTLVVFVLMI 160
Cdd:cd18582 74 ALRVFRHLHSLSLRfHLSR-KTGALSRAIERGTRGIEFLLRFLLFNILPTILE-LLLVCGILWYLyGW-SYALITLVTVA 150
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2159016728 161 ATMIKTRII-RLRRPHISRVNEAEDEILDQIVGVFSGIRTIQSNRVEGFFEKRLGPFFENYRQATVSLAVSRSV 233
Cdd:cd18582 151 LYVAFTIKVtEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLAL 224
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
419-489 |
1.77e-04 |
|
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: 42.59 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 419 NLSGGEKR------RLCFLRAYIHSPELLLLDEPTTGLDSET-GQGLWEIIFSLLE---PQtkLVVVTHDSSYLGHFDKV 488
Cdd:cd03240 115 RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENiEESLAEIIEERKSqknFQ--LIVITHDEELVDAADHI 192
|
.
gi 2159016728 489 I 489
Cdd:cd03240 193 Y 193
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
334-465 |
2.21e-04 |
|
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: 42.03 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSNYLEQNNFVF------------SGSVYENLSLGkkmdnd 392
Cdd:cd03215 29 VGIAGLVGNGQTELAEALFGLRPPAsgeitldgkPVTRRSPRDAIRAGIAYvpedrkreglvlDLSVAENIALS------ 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2159016728 393 wltsqidkvglssrltldselqgngQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSL 465
Cdd:cd03215 103 -------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIREL 150
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
307-478 |
2.22e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 43.19 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 307 DHEEKLTGVSqvlnqvleeLAKPNVNTIAVIGKSGQGKTILLDTLAGLLTPT--PVSHLSSNYLEQNNF----------- 373
Cdd:PRK13647 16 DGTKALKGLS---------LSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQrgRVKVMGREVNAENEKwvrskvglvfq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 374 -----VFSGSVYE-------NLSLGKKMDNDWLTSQIDKVGLSsrltldsELQGNG-QNLSGGEKRRLCFLRAYIHSPEL 440
Cdd:PRK13647 87 dpddqVFSSTVWDdvafgpvNMGLDKDEVERRVEEALKAVRMW-------DFRDKPpYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 2159016728 441 LLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVVVTHD 478
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHD 197
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
335-475 |
2.33e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 43.46 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 335 AVIGKSGQGKTILLDTLAGLLTP---------TPVSHLSsnyLEQNNFVFSGSVYENlslgkkmDNDWLTSQIDKVGLSS 405
Cdd:PRK10938 33 AFVGANGSGKSALARALAGELPLlsgerqsqfSHITRLS---FEQLQKLVSDEWQRN-------NTDMLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 406 RLTLDSELQGNG-------------------QNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLL 466
Cdd:PRK10938 103 AEIIQDEVKDPArceqlaqqfgitalldrrfKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLH 182
|
....*....
gi 2159016728 467 EPQTKLVVV 475
Cdd:PRK10938 183 QSGITLVLV 191
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
421-451 |
2.35e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 43.54 E-value: 2.35e-04
10 20 30
....*....|....*....|....*....|.
gi 2159016728 421 SGGEKRRLCFLRAYIHSPELLLLDEPTTGLD 451
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
418-478 |
2.73e-04 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 42.69 E-value: 2.73e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2159016728 418 QNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVVVTHD 478
Cdd:PRK13638 135 QCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHD 195
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
420-477 |
2.74e-04 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 42.36 E-value: 2.74e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2159016728 420 LSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVVVTH 477
Cdd:COG0396 141 FSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITH 198
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
420-478 |
2.79e-04 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 42.56 E-value: 2.79e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2159016728 420 LSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVVVTHD 478
Cdd:PRK15056 143 LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHN 201
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
86-285 |
3.46e-04 |
|
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: 42.41 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 86 LFSQLIRKPFSHFKRLEIGSLASKFerglgSYE-QFINLSVSRGLpltIELFALGCAIIFFSGWL-----TFTLVVFVLM 159
Cdd:cd18552 78 LFDKLLRLPLSFFDRNSSGDLISRI-----TNDvNQVQNALTSAL---TVLVRDPLTVIGLLGVLfyldwKLTLIALVVL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 160 IATMIKTRII--RLRRpHISRVNEAEDEILDQIVGVFSGIRTIQSNRVEGFFEKRLGPFFENYRQATVSLAVSRSVFDGV 237
Cdd:cd18552 150 PLAALPIRRIgkRLRK-ISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPL 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2159016728 238 aiaTHSLISLSIITLFIF--YLFPEQHSDAGQLV---TALLLSA----SLTRAFTGL 285
Cdd:cd18552 229 ---MELLGAIAIALVLWYggYQVISGELTPGEFIsfiTALLLLYqpikRLSNVNANL 282
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
370-454 |
4.85e-04 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 42.78 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 370 QNNFVFSGSVYENLSLGKKmdnDWLTSQIDKVG-LSS------RLT--LDSELQGNGQNLSGGEKRRLCFLRAYIHSPEL 440
Cdd:PRK10789 396 QTPFLFSDTVANNIALGRP---DATQQEIEHVArLASvhddilRLPqgYDTEVGERGVMLSGGQKQRISIARALLLNAEI 472
|
90
....*....|....
gi 2159016728 441 LLLDEPTTGLDSET 454
Cdd:PRK10789 473 LILDDALSAVDGRT 486
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
336-478 |
6.59e-04 |
|
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: 41.48 E-value: 6.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 336 VIGKSGQGKTILLDTLAGLLTPT---------PVSHLSSNYLEQ-----NNFVFSG-------SVYENLSLG-------K 387
Cdd:cd03294 55 IMGLSGSGKSTLLRCINRLIEPTsgkvlidgqDIAAMSRKELRElrrkkISMVFQSfallphrTVLENVAFGlevqgvpR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 388 KMDNDWLTSQIDKVGLSsrltlDSELQGNGQnLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEiifSLLE 467
Cdd:cd03294 135 AEREERAAEALELVGLE-----GWEHKYPDE-LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQD---ELLR 205
|
170
....*....|....*
gi 2159016728 468 PQTKL----VVVTHD 478
Cdd:cd03294 206 LQAELqktiVFITHD 220
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
420-454 |
6.61e-04 |
|
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: 42.11 E-value: 6.61e-04
10 20 30
....*....|....*....|....*....|....*
gi 2159016728 420 LSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSET 454
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRT 529
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
417-478 |
7.08e-04 |
|
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: 41.45 E-value: 7.08e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2159016728 417 GQN---LSGGEKRRL---CFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVVVTHD 478
Cdd:cd03271 164 GQPattLSGGEAQRIklaKELSKRSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHN 231
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
420-489 |
8.49e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 8.49e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2159016728 420 LSGGEK------RRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVVVTHDSSYLGHFDKVI 489
Cdd:PRK03918 789 LSGGERialglaFRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIMERYLRKIPQVIIVSHDEELKDAADYVI 864
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
336-477 |
8.49e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 40.60 E-value: 8.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 336 VIGKSGQGKTILLDTLAGLLTPTP---------------------VSHLSSnyLEQNNfvfsgSVYENLSL--------G 386
Cdd:PRK13543 42 VQGDNGAGKTTLLRVLAGLLHVESgqiqidgktatrgdrsrfmayLGHLPG--LKADL-----STLENLHFlcglhgrrA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 387 KKMDNDWLTSqidkVGLSsrltlDSElQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLL 466
Cdd:PRK13543 115 KQMPGSALAI----VGLA-----GYE-DTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHL 184
|
170
....*....|.
gi 2159016728 467 EPQTKLVVVTH 477
Cdd:PRK13543 185 RGGGAALVTTH 195
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
84-289 |
8.83e-04 |
|
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: 41.37 E-value: 8.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 84 RSLFSQLIRKPFSHFKRLEIGSLASKfergLGSYEQfinlSVSRGLPLTIELFA----LGCAIIFFSGWLTF--TLVVFV 157
Cdd:cd18572 73 RDLFRSLLRQDIAFFDATKTGELTSR----LTSDCQ----KVSDPLSTNLNVFLrnlvQLVGGLAFMFSLSWrlTLLAFI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 158 LMIATMIKTRII--------RLRRPHISRVNEAEDEildqivgVFSGIRTIQS----NRVEGFFEKRLgpffenyrQATV 225
Cdd:cd18572 145 TVPVIALITKVYgryyrklsKEIQDALAEANQVAEE-------ALSNIRTVRSfateEREARRYERAL--------DKAL 209
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2159016728 226 SLAVSRSVFDGVAIATHSLISLSIITLFIFY---LFPEQHSDAGQLVTALLLSASLTRAFTGLLDVY 289
Cdd:cd18572 210 KLSVRQALAYAGYVAVNTLLQNGTQVLVLFYgghLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVF 276
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
118-288 |
9.15e-04 |
|
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: 41.40 E-value: 9.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 118 EQFINLSVSRGLPLTIELfaLGCAIIFF--SGWLT-FTLVVFVLMIATMIktRIIRLRRPHISRVNEAEDEILDQIVGVF 194
Cdd:cd18565 125 ERFLDDGANSIIRVVVTV--LGIGAILFylNWQLAlVALLPVPLIIAGTY--WFQRRIEPRYRAVREAVGDLNARLENNL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 195 SGIRTIQSNRVEGFFEKRLGPFFENYRQATVSLAVSRSVFDGVaiaTHSLISLSIITLFIF---------YLFPEQHSdA 265
Cdd:cd18565 201 SGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAFFPV---IRLVAGAGFVATFVVggywvldgpPLFTGTLT-V 276
|
170 180
....*....|....*....|...
gi 2159016728 266 GQLVTALLLSASLTRAFTGLLDV 288
Cdd:cd18565 277 GTLVTFLFYTQRLLWPLTRLGDL 299
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
423-465 |
1.66e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.26 E-value: 1.66e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2159016728 423 GEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSL 465
Cdd:NF033858 401 GIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIEL 443
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
420-491 |
1.80e-03 |
|
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: 40.96 E-value: 1.80e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2159016728 420 LSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVVVTHD-SSYLGHFDKVITL 491
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSElAEVLGLSDRVLVI 476
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
420-451 |
1.88e-03 |
|
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: 40.82 E-value: 1.88e-03
10 20 30
....*....|....*....|....*....|..
gi 2159016728 420 LSGGEKRRLCFLRAYIHSPELLLLDEPTTGLD 451
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALD 457
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
334-492 |
1.92e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 41.11 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPTPVSHLSSNY----------------LEQNNFVFSGSVYENLS-LGKKMDND-WLT 395
Cdd:PLN03232 1265 VGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCdvakfgltdlrrvlsiIPQSPVLFSGTVRFNIDpFSEHNDADlWEA 1344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 396 ---SQIDKVGLSSRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKL 472
Cdd:PLN03232 1345 lerAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTML 1424
|
170 180
....*....|....*....|
gi 2159016728 473 vVVTHDSSYLGHFDKVITLD 492
Cdd:PLN03232 1425 -VIAHRLNTIIDCDKILVLS 1443
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
421-491 |
2.34e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 40.09 E-value: 2.34e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2159016728 421 SGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSeTGQGLweiIFSLL-----EPQTKLVVVTHDSSYL-GHFDKVITL 491
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDV-TVQAQ---IMTLLnelkrEFNTAIIMITHDLGVVaGICDKVLVM 235
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
335-477 |
2.52e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 40.15 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 335 AVIGKSGQGKTILLDTLAGLLTPTP----VSHLSSNYLEQNNFVFSG--------------SVYENLSLGKKMDN----- 391
Cdd:PRK09700 35 ALLGENGAGKSTLMKVLSGIHEPTKgtitINNINYNKLDHKLAAQLGigiiyqelsvidelTVLENLYIGRHLTKkvcgv 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 392 ---DWLTSQIDKVGLSSRLTLDSELQGNGQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEP 468
Cdd:PRK09700 115 niiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE 194
|
....*....
gi 2159016728 469 QTKLVVVTH 477
Cdd:PRK09700 195 GTAIVYISH 203
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
420-491 |
2.65e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 39.61 E-value: 2.65e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2159016728 420 LSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTK-LVVVTHD-SSYLGHFDKVITL 491
Cdd:PRK13645 151 LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKrIIMVTHNmDQVLRIADEVIVM 224
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
394-477 |
2.90e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 39.63 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 394 LTSQIDKVGLSSRLtldseLQGN-GQNLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKL 472
Cdd:CHL00131 130 INEKLKLVGMDPSF-----LSRNvNEGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSI 204
|
....*
gi 2159016728 473 VVVTH 477
Cdd:CHL00131 205 ILITH 209
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
421-477 |
2.94e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.39 E-value: 2.94e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 2159016728 421 SGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVVVTH 477
Cdd:PRK09580 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
417-477 |
3.09e-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: 3.09e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2159016728 417 GQN---LSGGEKRRL---CFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVVVTH 477
Cdd:TIGR00630 824 GQPattLSGGEAQRIklaKELSKRSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEH 890
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
387-477 |
3.59e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 39.61 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 387 KKMDNDWLtsqiDKVGLSSRLTlDSELQGngqnLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLL 466
Cdd:PRK10938 378 QKLAQQWL----DILGIDKRTA-DAPFHS----LSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLI 448
|
90
....*....|..
gi 2159016728 467 -EPQTKLVVVTH 477
Cdd:PRK10938 449 sEGETQLLFVSH 460
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
401-489 |
3.85e-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: 38.78 E-value: 3.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 401 VGLSsRLTLDSElqgnGQNLSGGEKRRLcFLRAYIHSP---ELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVVVTH 477
Cdd:cd03270 124 VGLG-YLTLSRS----APTLSGGEAQRI-RLATQIGSGltgVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEH 197
|
90
....*....|..
gi 2159016728 478 DSSYLGHFDKVI 489
Cdd:cd03270 198 DEDTIRAADHVI 209
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
335-451 |
3.98e-03 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 39.00 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 335 AVIGKSGQGKTILLDTL-------AG--LLTPTPVSHLSSN-------YLEQNNFVFSG-SVYENLSLGK---------- 387
Cdd:PRK10575 41 GLIGHNGSGKSTLLKMLgrhqppsEGeiLLDAQPLESWSSKafarkvaYLPQQLPAAEGmTVRELVAIGRypwhgalgrf 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2159016728 388 -KMDNDWLTSQIDKVGL---SSRLtLDSelqgngqnLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLD 451
Cdd:PRK10575 121 gAADREKVEEAISLVGLkplAHRL-VDS--------LSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
87-287 |
4.88e-03 |
|
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: 38.97 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 87 FSQLIRKPFSHFKRLEIGSLASKFERGLGSYEQFINLSVSRGLPLTIELFALGcaIIFFSGWLTFTLVVFVLMIATMIkt 166
Cdd:cd18570 82 FKHLLKLPLSFFETRKTGEIISRFNDANKIREAISSTTISLFLDLLMVIISGI--ILFFYNWKLFLITLLIIPLYILI-- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 167 rIIRLRRPHIS---RVNEAEDEILDQIVGVFSGIRTIQSNRVEGFFEKRLGPFFENYRQATVSLAVSRSVFDGVAIATHS 243
Cdd:cd18570 158 -ILLFNKPFKKknrEVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISL 236
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2159016728 244 LISLSIITLFIFYLFPEQHSdAGQLVTALLLSASLTRAFTGLLD 287
Cdd:cd18570 237 IGSLLILWIGSYLVIKGQLS-LGQLIAFNALLGYFLGPIENLIN 279
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
334-492 |
5.35e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 39.18 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 334 IAVIGKSGQGKTILLDTLAGLLTPT---------PVshlSSNYLEQNNFVFSgSVYENLSL--------GKKMDNDWLTS 396
Cdd:PRK10522 352 LFLIGGNGSGKSTLAMLLTGLYQPQsgeilldgkPV---TAEQPEDYRKLFS-AVFTDFHLfdqllgpeGKPANPALVEK 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 397 QIDKVGLSSRLTLDSELQGNGQnLSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSLLEPQTKLVV-V 475
Cdd:PRK10522 428 WLERLKMAHKLELEDGRISNLK-LSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFaI 506
|
170
....*....|....*..
gi 2159016728 476 THDSSYLGHFDKVITLD 492
Cdd:PRK10522 507 SHDDHYFIHADRLLEMR 523
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
420-478 |
6.07e-03 |
|
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: 39.02 E-value: 6.07e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 420 LSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWE-IIFSLLEPQTKLVVVTHD 478
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHD 487
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
420-486 |
6.61e-03 |
|
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: 38.96 E-value: 6.61e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2159016728 420 LSGGEKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIifsLLEPQTKLVVVTHDSS------YLGHFD 486
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRL---CREFGITLFSVSHRKSlwkyheYLLYMD 652
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
84-285 |
6.97e-03 |
|
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: 38.57 E-value: 6.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 84 RSLFSQLIRKPFSHFKRLEIGSLASKfergLGSYEQFINLSVSRGLP-LTIELFALGCAII--FFSGWLTFTLVVFVLMI 160
Cdd:cd18551 73 RRLWRRLLRLPVSFFDRRRSGDLVSR----VTNDTTLLRELITSGLPqLVTGVLTVVGAVVlmFLLDWVLTLVTLAVVPL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 161 ATMIKTRIIRLRRPHISRVNEAEDEILDQIVGVFSGIRTIQSNRVEGFFEKRLGPFFENYRQATVSLAVSRSV------- 233
Cdd:cd18551 149 AFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALigplmgl 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2159016728 234 -----------FDGVAIATHSLiSLSIITLFIFYLFpeqhsdagQLVTALllsASLTRAFTGL 285
Cdd:cd18551 229 avqlallvvlgVGGARVASGAL-TVGTLVAFLLYLF--------QLITPL---SQLSSFFTQL 279
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
287-478 |
9.03e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 38.48 E-value: 9.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 287 DVYRLL-DQSREDFSALKGILDHEEKLTGVSQVLNQVLEELAKPNVNTIAVIGKSGQGKTILLDTLAGLLTPT------- 358
Cdd:PRK10070 9 NLYKIFgEHPQRAFKYIEQGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTrgqvlid 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 359 --PVSHLSSNYLEQNNFVFSGSVYENLSLGKKM---DNDWLTSQIDKVGLSSR----------LTLDSELQGNGQNLSGG 423
Cdd:PRK10070 89 gvDIAKISDAELREVRRKKIAMVFQSFALMPHMtvlDNTAFGMELAGINAEERrekaldalrqVGLENYAHSYPDELSGG 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2159016728 424 EKRRLCFLRAYIHSPELLLLDEPTTGLDSETGQGLWEIIFSL-LEPQTKLVVVTHD 478
Cdd:PRK10070 169 MRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHD 224
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
83-256 |
9.51e-03 |
|
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: 37.95 E-value: 9.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 83 SRSLFSQLIRKPFSHFKRLEIGSLASKfergLGSYEQFINLSVSRGLPLTIEL------FALgcaIIFFSGWLTFTLVVF 156
Cdd:cd18566 78 SNAAFEHLLSLPLSFFEREPSGAHLER----LNSLEQIREFLTGQALLALLDLpfvlifLGL---IWYLGGKLVLVPLVL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159016728 157 VLMIATMIKTRIIRLRRpHISRVNEAEDEILDQIVGVFSGIRTIQSNRVEGFFEKRlgpfFENYrQATVSLAVSR-SVFD 235
Cdd:cd18566 151 LGLFVLVAILLGPILRR-ALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRR----YERL-QANAAYAGFKvAKIN 224
|
170 180
....*....|....*....|.
gi 2159016728 236 GVAIATHSLISLSIITLFIFY 256
Cdd:cd18566 225 AVAQTLGQLFSQVSMVAVVAF 245
|
|
| |
