|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
2-268 |
0e+00 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 559.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 2 IETLLEVRNLSKTFRYRTGWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFG 81
Cdd:PRK15112 1 VETLLEVRNLSKTFRYRTGWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 82 DYSFRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTNLEPEQRRKQIIETMRMVGLLPDHVSYYPHMLAPGQKQRLGL 161
Cdd:PRK15112 81 DYSYRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 162 ARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVLAS 241
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLAS 240
|
250 260
....*....|....*....|....*..
gi 446495558 242 PLHELTKRLIAGHFGEALTADAWRKDR 268
Cdd:PRK15112 241 PLHELTKRLIAGHFGEALTADAWRKDR 267
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
3-266 |
0e+00 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 536.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 3 ETLLEVRNLSKTFRYRTGWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD 82
Cdd:COG4167 2 SALLEVRNLSKTFKYRTGLFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 83 YSFRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTNLEPEQRRKQIIETMRMVGLLPDHVSYYPHMLAPGQKQRLGLA 162
Cdd:COG4167 82 YKYRCKHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQKQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 163 RALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVLASP 242
Cdd:COG4167 162 RALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANP 241
|
250 260
....*....|....*....|....
gi 446495558 243 LHELTKRLIAGHFGEALTADAWRK 266
Cdd:COG4167 242 QHEVTKRLIESHFGEALTADAWRR 265
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-252 |
4.79e-106 |
|
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: 316.85 E-value: 4.79e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 3 ETLLEVRNLSKTFRYRtgwfRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH--- 79
Cdd:COG1123 258 EPLLEVRNLSKRYPVR----GKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTkls 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 80 FGDYSFRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTNLEPEQRRKQIIETMRMVGLLPDHVSYYPHMLAPGQKQRL 159
Cdd:COG1123 334 RRSLRELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRV 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 160 GLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVL 239
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVF 493
|
250
....*....|...
gi 446495558 240 ASPLHELTKRLIA 252
Cdd:COG1123 494 ANPQHPYTRALLA 506
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-252 |
2.00e-102 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 301.27 E-value: 2.00e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 1 MIETLLEVRNLSKTFRYRTGWFRRQ--TVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL 78
Cdd:COG4608 3 MAEPLLEVRDLKKHFPVRGGLFGRTvgVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 79 HFGDYS----FRsQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTNLEPEQRRKQIIETMRMVGLLPDHVSYYPHMLAPG 154
Cdd:COG4608 83 TGLSGRelrpLR-RRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEFSGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 155 QKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGS 234
Cdd:COG4608 162 QRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAP 241
|
250
....*....|....*...
gi 446495558 235 TADVLASPLHELTKRLIA 252
Cdd:COG4608 242 RDELYARPLHPYTQALLS 259
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-252 |
4.23e-93 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 277.62 E-value: 4.23e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 1 MIETLLEVRNLSKTFRYRTGWFR-RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAgMIE-PTSGELLIDDHPL 78
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPVKRGLFKpERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLT-MIEtPTGGELYYQGQDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 79 HFGDYS---FRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTNLEPEQRRKQIIETMRMVGLLPDHVSYYPHMLAPGQ 155
Cdd:PRK11308 80 LKADPEaqkLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 156 KQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGST 235
Cdd:PRK11308 160 RQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTK 239
|
250
....*....|....*..
gi 446495558 236 ADVLASPLHELTKRLIA 252
Cdd:PRK11308 240 EQIFNNPRHPYTQALLS 256
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-252 |
3.12e-92 |
|
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: 275.01 E-value: 3.12e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 5 LLEVRNLSKTFRYRTGWFRrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEP---TSGELLIDDHPL-HF 80
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVK-----AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLlKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 81 GD---YSFRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTNLEPEQRRKQIIETMRMVGLLP--DHVSYYPHMLAPGQ 155
Cdd:COG0444 76 SEkelRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDpeRRLDRYPHELSGGM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 156 KQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGST 235
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPV 235
|
250
....*....|....*..
gi 446495558 236 ADVLASPLHELTKRLIA 252
Cdd:COG0444 236 EELFENPRHPYTRALLS 252
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-252 |
1.85e-89 |
|
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: 274.64 E-value: 1.85e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 3 ETLLEVRNLSKTFRYRTGWFRRQT--VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIePTSGELLIDDHPLH- 79
Cdd:COG4172 273 PPLLEARDLKVWFPIKRGLFRRTVghVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDg 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 80 FGDYSFRSQRIRM--IFQDPSTSLNPRQRISQILDFPLRL-NTNLEPEQRRKQIIETMRMVGLLPDHVSYYPHMLAPGQK 156
Cdd:COG4172 352 LSRRALRPLRRRMqvVFQDPFGSLSPRMTVGQIIAEGLRVhGPGLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQR 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 157 QRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTA 236
Cdd:COG4172 432 QRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTE 511
|
250
....*....|....*.
gi 446495558 237 DVLASPLHELTKRLIA 252
Cdd:COG4172 512 QVFDAPQHPYTRALLA 527
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-233 |
4.52e-87 |
|
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: 258.59 E-value: 4.52e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 5 LLEVRNLSKTFRYRTGWfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 84
Cdd:cd03257 1 LLEVKNLSVSFPTGGGS-----VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 85 FRSQR---IRMIFQDPSTSLNPRQRISQILDFPLRLNTNL-EPEQRRKQIIETMRMVGLLPDHVSYYPHMLAPGQKQRLG 160
Cdd:cd03257 76 LRKIRrkeIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLsKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446495558 161 LARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERG 233
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-252 |
6.03e-87 |
|
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: 258.96 E-value: 6.03e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 5 LLEVRNLSKTFRYRtgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 84
Cdd:COG1124 1 MLEVRNLSVSYGQG-----GRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 85 FRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTNLEPEQRrkqIIETMRMVGLLPDHVSYYPHMLAPGQKQRLGLARA 164
Cdd:COG1124 76 AFRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHGLPDREER---IAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 165 LILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVLASPLH 244
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
....*...
gi 446495558 245 ELTKRLIA 252
Cdd:COG1124 233 PYTRELLA 240
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
5-252 |
9.48e-75 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 230.75 E-value: 9.48e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 5 LLEVRNLSKTFRYRTG----WFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELL-IDDHPLH 79
Cdd:PRK15079 8 LLEVADLKVHFDIKDGkqwfWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwLGKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 80 FGDYSFRSQR--IRMIFQDPSTSLNPRQRISQILDFPLRL-NTNLEPEQRRKQIIETMRMVGLLPDHVSYYPHMLAPGQK 156
Cdd:PRK15079 88 MKDDEWRAVRsdIQMIFQDPLASLNPRMTIGEIIAEPLRTyHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQC 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 157 QRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTA 236
Cdd:PRK15079 168 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYD 247
|
250
....*....|....*.
gi 446495558 237 DVLASPLHELTKRLIA 252
Cdd:PRK15079 248 EVYHNPLHPYTKALMS 263
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-242 |
9.34e-64 |
|
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: 207.83 E-value: 9.34e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 3 ETLLEVRNLSktFRYRTGWfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPT---SGELLIDDHPLH 79
Cdd:COG1123 2 TPLLEVRDLS--VRYPGGD-----VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 80 FGDYSFRSQRIRMIFQDPSTSLNPRQRISQIlDFPLRlNTNLEPEQRRKQIIETMRMVGLlPDHVSYYPHMLAPGQKQRL 159
Cdd:COG1123 75 ELSEALRGRRIGMVFQDPMTQLNPVTVGDQI-AEALE-NLGLSRAEARARVLELLEAVGL-ERRLDRYPHQLSGGQRQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 160 GLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVL 239
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEIL 231
|
...
gi 446495558 240 ASP 242
Cdd:COG1123 232 AAP 234
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-252 |
1.09e-62 |
|
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: 205.30 E-value: 1.09e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 1 MIETLLEVRNLSKTFRYRTGwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKS--TLAKM--LAGMIEPTSGELLIDDH 76
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGG-----TVEAVKGVSFDIAAGETLALVGESGSGKSvtALSILrlLPDPAAHPSGSILFDGQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 77 PL-HFGDYSFRS---QRIRMIFQDPSTSLNPRQRISQILDFPLRLNTNLEPEQRRKQIIETMRMVGLlPD---HVSYYPH 149
Cdd:COG4172 77 DLlGLSERELRRirgNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGI-PDperRLDAYPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 150 MLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEV 229
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEI 235
|
250 260
....*....|....*....|...
gi 446495558 230 VERGSTADVLASPLHELTKRLIA 252
Cdd:COG4172 236 VEQGPTAELFAAPQHPYTRKLLA 258
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-252 |
2.59e-60 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 199.16 E-value: 2.59e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 3 ETLLEVRNLSKTFRYRTGWFRRQTVE--AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIePTSGELLIDDHPLHF 80
Cdd:PRK15134 273 SPLLDVEQLQVAFPIRKGILKRTVDHnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 81 GD----YSFRSqRIRMIFQDPSTSLNPRQRISQILDFPLRLN-TNLEPEQRRKQIIETMRMVGLLPDHVSYYPHMLAPGQ 155
Cdd:PRK15134 352 LNrrqlLPVRH-RIQVVFQDPNSSLNPRLNVLQIIEEGLRVHqPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQ 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 156 KQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGST 235
Cdd:PRK15134 431 RQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDC 510
|
250
....*....|....*..
gi 446495558 236 ADVLASPLHELTKRLIA 252
Cdd:PRK15134 511 ERVFAAPQQEYTRQLLA 527
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-252 |
3.80e-59 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 198.16 E-value: 3.80e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 3 ETLLEVRNLSKTFRYRTGWFRRQT--VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH- 79
Cdd:PRK10261 311 EPILQVRNLVTRFPLRSGLLNRVTreVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDt 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 80 FGDYSFRSQR--IRMIFQDPSTSLNPRQRISQILDFPLRLNTNLEPEQRRKQIIETMRMVGLLPDHVSYYPHMLAPGQKQ 157
Cdd:PRK10261 391 LSPGKLQALRrdIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQ 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 158 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTAD 237
Cdd:PRK10261 471 RICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRA 550
|
250
....*....|....*
gi 446495558 238 VLASPLHELTKRLIA 252
Cdd:PRK10261 551 VFENPQHPYTRKLMA 565
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-240 |
6.61e-57 |
|
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: 181.76 E-value: 6.61e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSktFRYRTGwfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSF 85
Cdd:COG1122 1 IELENLS--FSYPGG------TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RSQRIRMIFQDPStslnprqriSQILD--------FPLRlNTNLEPEQRRKQIIETMRMVGLLpDHVSYYPHMLAPGQKQ 157
Cdd:COG1122 73 LRRKVGLVFQNPD---------DQLFAptveedvaFGPE-NLGLPREEIRERVEEALELVGLE-HLADRPPHELSGGQKQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 158 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTAD 237
Cdd:COG1122 142 RVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLN-KEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPRE 220
|
...
gi 446495558 238 VLA 240
Cdd:COG1122 221 VFS 223
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
4-241 |
1.37e-55 |
|
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: 179.62 E-value: 1.37e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 4 TLLEVRNLSKtfRYRTGWF--RRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFG 81
Cdd:TIGR02769 1 SLLEVRDVTH--TYRTGGLfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 82 DysfRSQR------IRMIFQDPSTSLNPRQRISQILDFPLRLNTNLEPEQRRKQIIETMRMVGLLPDHVSYYPHMLAPGQ 155
Cdd:TIGR02769 79 D---RKQRrafrrdVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 156 KQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGST 235
Cdd:TIGR02769 156 LQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDV 235
|
....*.
gi 446495558 236 ADVLAS 241
Cdd:TIGR02769 236 AQLLSF 241
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-240 |
1.83e-54 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 176.80 E-value: 1.83e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 4 TLLEVRNLSKtfRYRTGWF--RRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFG 81
Cdd:PRK10419 2 TLLNVSGLSH--HYAHGGLsgKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 82 DYS----FRsQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTNLEPEQRRKQIIETMRMVGLLPDHVSYYPHMLAPGQKQ 157
Cdd:PRK10419 80 NRAqrkaFR-RDIQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 158 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTAD 237
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGD 238
|
...
gi 446495558 238 VLA 240
Cdd:PRK10419 239 KLT 241
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-252 |
1.31e-52 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 174.11 E-value: 1.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 1 MIEtlleVRNLSKTFRYRTGwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhf 80
Cdd:COG1135 1 MIE----LENLSKTFPTKGG-----PVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDL-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 81 GDYS------FRsQRIRMIFQDPS--TSLNPRQRISqildFPLRLnTNLEPEQRRKQIIETMRMVGlLPDHVSYYPHMLA 152
Cdd:COG1135 70 TALSerelraAR-RKIGMIFQHFNllSSRTVAENVA----LPLEI-AGVPKAEIRKRVAELLELVG-LSDKADAYPSQLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 153 PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVER 232
Cdd:COG1135 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQ 222
|
250 260
....*....|....*....|
gi 446495558 233 GSTADVLASPLHELTKRLIA 252
Cdd:COG1135 223 GPVLDVFANPQSELTRRFLP 242
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-233 |
1.64e-51 |
|
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: 167.31 E-value: 1.64e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFRyrtgwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSF 85
Cdd:cd03259 1 LELKGLSKTYG---------SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT--GVPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RSQRIRMIFQDPStsLNPRQRISQILDFPLRLNTNLEPEQRRKqIIETMRMVGLlPDHVSYYPHMLAPGQKQRLGLARAL 165
Cdd:cd03259 70 ERRNIGMVFQDYA--LFPHLTVAENIAFGLKLRGVPKAEIRAR-VRELLELVGL-EGLLNRYPHELSGGQQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446495558 166 ILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERG 233
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-262 |
3.38e-51 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 167.96 E-value: 3.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 3 ETLLEVRNLSKTFRYRTGwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFgd 82
Cdd:COG1116 5 APALELRGVSKRFPTGGG-----GVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 83 ysfRSQRIRMIFQDPStsLNPRQRISQILDFPLRLnTNLEPEQRRKQIIETMRMVGLLpDHVSYYPHMLAPGQKQRLGLA 162
Cdd:COG1116 78 ---PGPDRGVVFQEPA--LLPWLTVLDNVALGLEL-RGVPKAERRERARELLELVGLA-GFEDAYPHQLSGGMRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 163 RALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTqhigmmkH-------ISDQVLVM--HQGEVVE-- 231
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVT-------HdvdeavfLADRVVVLsaRPGRIVEei 223
|
250 260 270
....*....|....*....|....*....|....*..
gi 446495558 232 -----RGSTADVLASP-LHELTKRLIAGHFGEALTAD 262
Cdd:COG1116 224 dvdlpRPRDRELRTSPeFAALRAEILDLLREEAERAA 260
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-242 |
1.04e-50 |
|
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: 166.31 E-value: 1.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 1 MIETLLEVRNLSKTFRyrtgwfrRQTVeaVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF 80
Cdd:COG1127 1 MSEPMIEVRNLTKSFG-------DRVV--LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 81 GD----YSFRsQRIRMIFQDPS--TSLNPRQRISqildFPLRLNTNLEPEQRRKQIIETMRMVGlLPDHVSYYPHMLAPG 154
Cdd:COG1127 72 LSekelYELR-RRIGMLFQGGAlfDSLTVFENVA----FPLREHTDLSEAEIRELVLEKLELVG-LPGAADKMPSELSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 155 QKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGS 234
Cdd:COG1127 146 MRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGT 225
|
....*...
gi 446495558 235 TADVLASP 242
Cdd:COG1127 226 PEELLASD 233
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-242 |
1.60e-50 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 169.12 E-value: 1.60e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 1 MIETLLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-- 78
Cdd:COG3842 1 MAMPALELENVSKRY---------GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVtg 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 79 ---HfgdysfrsQR-IRMIFQD----PStsLNPRQRISqildFPLRLNtNLEPEQRRKQIIETMRMVGLlPDHVSYYPHM 150
Cdd:COG3842 72 lppE--------KRnVGMVFQDyalfPH--LTVAENVA----FGLRMR-GVPKAEIRARVAELLELVGL-EGLADRYPHQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 151 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTqhigmmkH-------ISDQVLV 223
Cdd:COG3842 136 LSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVT-------HdqeealaLADRIAV 208
|
250
....*....|....*....
gi 446495558 224 MHQGEVVERGSTADVLASP 242
Cdd:COG3842 209 MNDGRIEQVGTPEEIYERP 227
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-242 |
2.70e-50 |
|
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: 164.98 E-value: 2.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFRYRTGWfrrqtveavKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH----FG 81
Cdd:cd03261 1 IELRGLTKSFGGRTVL---------KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglseAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 82 DYSFRsQRIRMIFQDPS--TSLNPRQRISqildFPLRLNTNLEPEQRRKQIIETMRMVGLLPDHvSYYPHMLAPGQKQRL 159
Cdd:cd03261 72 LYRLR-RRMGMLFQSGAlfDSLTVFENVA----FPLREHTRLSEEEIREIVLEKLEAVGLRGAE-DLYPAELSGGMKKRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 160 GLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVL 239
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
...
gi 446495558 240 ASP 242
Cdd:cd03261 226 ASD 228
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
30-179 |
7.50e-50 |
|
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: 160.89 E-value: 7.50e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 30 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSFRSQRIRMIFQDPstSLNPRQRISQ 109
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDP--QLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446495558 110 ILDFPLRL--NTNLEPEQRRKQIIETMRMVGLLPDHVSYYPHMLAPGQKQRLGLARALILRPKVIIADEALA 179
Cdd:pfam00005 79 NLRLGLLLkgLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-246 |
7.95e-50 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 163.70 E-value: 7.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFRyrtgwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSF 85
Cdd:COG1131 1 IEVRGLTKRYG---------DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RsQRIRMIFQDPstSLNPRQRISQILDFPLRLNtNLEPEQRRKQIIETMRMVGLLP---DHVSYYPHmlapGQKQRLGLA 162
Cdd:COG1131 72 R-RRIGYVPQEP--ALYPDLTVRENLRFFARLY-GLPRKEARERIDELLELFGLTDaadRKVGTLSG----GMKQRLGLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 163 RALILRPKVIIADEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVLASP 242
Cdd:COG1131 144 LALLHDPELLILDEPTSGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
....
gi 446495558 243 LHEL 246
Cdd:COG1131 223 LEDV 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-242 |
1.25e-48 |
|
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: 160.82 E-value: 1.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 5 LLEVRNLSKTFRYRTGwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDY 83
Cdd:cd03258 1 MIELKNVSKVFGDTGG-----KVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtLLSGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 84 SFR--SQRIRMIFQDPS--TSLNPRQRISqildFPLRLnTNLEPEQRRKQIIETMRMVGLlPDHVSYYPHMLAPGQKQRL 159
Cdd:cd03258 76 ELRkaRRRIGMIFQHFNllSSRTVFENVA----LPLEI-AGVPKAEIEERVLELLELVGL-EDKADAYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 160 GLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVL 239
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVF 229
|
...
gi 446495558 240 ASP 242
Cdd:cd03258 230 ANP 232
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-228 |
2.63e-48 |
|
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: 159.17 E-value: 2.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 7 EVRNLSktFRYRTGwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSFR 86
Cdd:cd03225 1 ELKNLS--FSYPDG-----ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 87 SQRIRMIFQDPSTSL-NPRqrisqILD---FPLRlNTNLEPEQRRKQIIETMRMVGL--LPDHVsyyPHMLAPGQKQRLG 160
Cdd:cd03225 74 RRKVGLVFQNPDDQFfGPT-----VEEevaFGLE-NLGLPEEEIEERVEEALELVGLegLRDRS---PFTLSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446495558 161 LARALILRPKVIIADEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHIGMMKHISDQVLVMHQGE 228
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-231 |
2.29e-47 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 157.13 E-value: 2.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 3 ETLLEVRNLSKTfrYRTGwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgD 82
Cdd:COG1136 2 SPLLELRNLTKS--YGTG---EGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIS--S 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 83 YS------FRSQRIRMIFQD----PSTSlnprqrisqILD---FPLRLNtNLEPEQRRKQIIETMRMVGlLPDHVSYYPH 149
Cdd:COG1136 75 LSerelarLRRRHIGFVFQFfnllPELT---------ALEnvaLPLLLA-GVSRKERRERARELLERVG-LGDRLDHRPS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 150 MLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTqHIGMMKHISDQVLVMHQGEV 229
Cdd:COG1136 144 QLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVT-HDPELAARADRVIRLRDGRI 222
|
..
gi 446495558 230 VE 231
Cdd:COG1136 223 VS 224
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
3-251 |
8.44e-47 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 158.73 E-value: 8.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 3 ETLLEVRNLSKTFRYRTGwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEP---TSG-------ELL 72
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDG-----DVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGsatfngrEIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 73 -IDDHPLHfgdySFRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTNLE-----------------PEQRRKqiietM 134
Cdd:PRK09473 85 nLPEKELN----KLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSkaeafeesvrmldavkmPEARKR-----M 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 135 RMvgllpdhvsyYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMM 214
Cdd:PRK09473 156 KM----------YPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVV 225
|
250 260 270
....*....|....*....|....*....|....*..
gi 446495558 215 KHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLI 251
Cdd:PRK09473 226 AGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGLL 262
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-245 |
9.54e-47 |
|
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: 156.17 E-value: 9.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 5 LLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 84
Cdd:COG4555 1 MIEVENLSKKY---------GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 85 FRsQRIRMIFQDPstSLNPRQRISQILDFPLRLNtNLEPEQRRKQIIETMRMVGLLPDHVSYYpHMLAPGQKQRLGLARA 164
Cdd:COG4555 72 AR-RQIGVLPDER--GLYDRLTVRENIRYFAELY-GLFDEELKKRIEELIELLGLEEFLDRRV-GELSTGMKKKVALARA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 165 LILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVLASPLH 244
Cdd:COG4555 147 LVHDPKVLLLDEPTNGLDVMARRLLREILRALK-KEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGE 225
|
.
gi 446495558 245 E 245
Cdd:COG4555 226 E 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-232 |
1.99e-46 |
|
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: 154.55 E-value: 1.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFRyrtgwFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdySF 85
Cdd:cd03293 1 LEVRNVSKTYG-----GGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV-----TG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RSQRIRMIFQDPStsLNPRQRISQILDFPLRLNtNLEPEQRRKQIIETMRMVGLLpDHVSYYPHMLAPGQKQRLGLARAL 165
Cdd:cd03293 71 PGPDRGYVFQQDA--LLPWLTVLDNVALGLELQ-GVPKAEARERAEELLELVGLS-GFENAYPHQLSGGMRQRVALARAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446495558 166 ILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQ--GEVVER 232
Cdd:cd03293 147 AVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-242 |
3.85e-45 |
|
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: 151.62 E-value: 3.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFryrtGWFRrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSF 85
Cdd:cd03300 1 IELENVSKFY----GGFV-----ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT--NLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RSQRIRMIFQdpSTSLNPRQRISQILDFPLRLNtNLEPEQRRKQIIETMRMVGLLpDHVSYYPHMLAPGQKQRLGLARAL 165
Cdd:cd03300 70 HKRPVNTVFQ--NYALFPHLTVFENIAFGLRLK-KLPKAEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446495558 166 ILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVLASP 242
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEP 222
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-240 |
4.03e-45 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 152.58 E-value: 4.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSktFRYRtgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHplhfgDYSF 85
Cdd:TIGR04520 1 IEVENVS--FSYP-----ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGL-----DTLD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RS------QRIRMIFQDPSTslnprQRISQILD----FPLRlNTNLEPEQRRKQIIETMRMVGLLpDHVSYYPHMLAPGQ 155
Cdd:TIGR04520 69 EEnlweirKKVGMVFQNPDN-----QFVGATVEddvaFGLE-NLGVPREEMRKRVDEALKLVGME-DFRDREPHLLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 156 KQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTqHigMMKHI--SDQVLVMHQGEVVERG 233
Cdd:TIGR04520 142 KQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISIT-H--DMEEAvlADRVIVMNKGKIVAEG 218
|
....*..
gi 446495558 234 STADVLA 240
Cdd:TIGR04520 219 TPREIFS 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-229 |
7.07e-45 |
|
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: 150.72 E-value: 7.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTfrYRTGwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYS- 84
Cdd:cd03255 1 IELKNLSKT--YGGG---GEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIS--KLSe 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 85 -----FRSQRIRMIFQDPStsLNPRQRISQILDFPLRLnTNLEPEQRRKQIIETMRMVGLlPDHVSYYPHMLAPGQKQRL 159
Cdd:cd03255 74 kelaaFRRRHIGFVFQSFN--LLPDLTALENVELPLLL-AGVPKKERRERAEELLERVGL-GDRLNHYPSELSGGQQQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 160 GLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTqHIGMMKHISDQVLVMHQGEV 229
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVT-HDPELAEYADRIIELRDGKI 218
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-252 |
3.81e-44 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 157.71 E-value: 3.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 3 ETLLEVRNLSKTFRYRtgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH--- 79
Cdd:PRK10261 10 RDVLAVENLNIAFMQE-----QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRrrs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 80 --------FGDYSFRSQR---IRMIFQDPSTSLNPRQRISQILDFPLRLNTNLepeQRRKQIIETMRMVGL--LPDH--- 143
Cdd:PRK10261 85 rqvielseQSAAQMRHVRgadMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGA---SREEAMVEAKRMLDQvrIPEAqti 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 144 VSYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLV 223
Cdd:PRK10261 162 LSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLV 241
|
250 260
....*....|....*....|....*....
gi 446495558 224 MHQGEVVERGSTADVLASPLHELTKRLIA 252
Cdd:PRK10261 242 MYQGEAVETGSVEQIFHAPQHPYTRALLA 270
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-262 |
7.59e-44 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 151.49 E-value: 7.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 1 MIEtlleVRNLSKTFRYRTGWfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-H 79
Cdd:PRK11153 1 MIE----LKNISKVFPQGGRT-----IHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 80 FGDYSFRSQR--IRMIFQDPSTsLNPRQRISQILdFPLRLnTNLEPEQRRKQIIETMRMVGLlPDHVSYYPHMLAPGQKQ 157
Cdd:PRK11153 72 LSEKELRKARrqIGMIFQHFNL-LSSRTVFDNVA-LPLEL-AGTPKAEIKARVTELLELVGL-SDKADRYPAQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 158 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTAD 237
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSE 227
|
250 260
....*....|....*....|....*
gi 446495558 238 VLASPLHELTKRLIAGHFGEALTAD 262
Cdd:PRK11153 228 VFSHPKHPLTREFIQSTLHLDLPED 252
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-251 |
1.40e-43 |
|
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: 147.83 E-value: 1.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFRYRTgwfrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSF 85
Cdd:cd03295 1 IEFENVTKRYGGGK--------KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RSQRIRMIFQdpSTSLNPRQRISQILDFPLRLNtNLEPEQRRKQIIETMRMVGLLPDH-VSYYPHMLAPGQKQRLGLARA 164
Cdd:cd03295 73 LRRKIGYVIQ--QIGLFPHMTVEENIALVPKLL-KWPKEKIRERADELLALVGLDPAEfADRYPHELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 165 LILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVLASPLH 244
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPAN 229
|
....*..
gi 446495558 245 ELTKRLI 251
Cdd:cd03295 230 DFVAEFV 236
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-229 |
1.34e-42 |
|
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: 143.31 E-value: 1.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFRyrtgwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdysf 85
Cdd:cd03230 1 IEVRNLSKRYG---------KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 rsqrirmifqdpstslnprqrisqildfplrlntnlepeqrrKQIIETMRMVGLLPDHVSYYPHM-------LAPGQKQR 158
Cdd:cd03230 66 ------------------------------------------KEPEEVKRRIGYLPEEPSLYENLtvrenlkLSGGMKQR 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446495558 159 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHIGMMKHISDQVLVMHQGEV 229
Cdd:cd03230 104 LALAQALLHDPELLILDEPTSGLDPESRREFWELLRELK-KEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
5-251 |
1.94e-41 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 144.88 E-value: 1.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 5 LLEVRNLSKTFRYRTGWFRrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIE-P---TSGELLIDDHPLHF 80
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFR-----AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPgrvMAEKLEFNGQDLQR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 81 GDYSFRSQ----RIRMIFQDPSTSLNPRQRIS-QILDfPLRLNTNLEPEQRRKQIIETMRMVGLlPDHVS---YYPHMLA 152
Cdd:PRK11022 78 ISEKERRNlvgaEVAMIFQDPMTSLNPCYTVGfQIME-AIKVHQGGNKKTRRQRAIDLLNQVGI-PDPASrldVYPHQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 153 PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVER 232
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVET 235
|
250
....*....|....*....
gi 446495558 233 GSTADVLASPLHELTKRLI 251
Cdd:PRK11022 236 GKAHDIFRAPRHPYTQALL 254
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
6-253 |
7.25e-41 |
|
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: 141.63 E-value: 7.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFRYRT---------GWFRRQTVE------AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGE 70
Cdd:cd03294 1 IKIKGLYKIFGKNPqkafkllakGKSKEEILKktgqtvGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 71 LLIDDHPLHFGDYS----FRSQRIRMIFQdpSTSLNPRQRISQILDFPLRLNtNLEPEQRRKQIIETMRMVGLLPDHVSY 146
Cdd:cd03294 81 VLIDGQDIAAMSRKelreLRRKKISMVFQ--SFALLPHRTVLENVAFGLEVQ-GVPRAEREERAAEALELVGLEGWEHKY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 147 yPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQ 226
Cdd:cd03294 158 -PDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKD 236
|
250 260
....*....|....*....|....*..
gi 446495558 227 GEVVERGSTADVLASPLHELTKRLIAG 253
Cdd:cd03294 237 GRLVQVGTPEEILTNPANDYVREFFRG 263
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-246 |
7.28e-41 |
|
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: 140.78 E-value: 7.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFRyrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF-GDYS 84
Cdd:cd03256 1 IEVENLSKTYP--------NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlKGKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 85 FRSQR--IRMIFQDPStsLNPRQRISQILDFPlRLNT--------NLEPEQRRKQIIETMRMVGLLPDH---VSYyphmL 151
Cdd:cd03256 73 LRQLRrqIGMIFQQFN--LIERLSVLENVLSG-RLGRrstwrslfGLFPKEEKQRALAALERVGLLDKAyqrADQ----L 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 152 APGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVE 231
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVF 225
|
250
....*....|....*
gi 446495558 232 RGSTADVLASPLHEL 246
Cdd:cd03256 226 DGPPAELTDEVLDEI 240
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
6-242 |
8.99e-41 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 143.67 E-value: 8.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD------HPlh 79
Cdd:COG3839 4 LELENVSKSY---------GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGrdvtdlPP-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 80 fgdysfrSQR-IRMIFQD----PSTSLnpRQRISqildFPLRLNtNLEPEQRRKQIIETMRMVGLLP--DHvsyYPHMLA 152
Cdd:COG3839 73 -------KDRnIAMVFQSyalyPHMTV--YENIA----FPLKLR-KVPKAEIDRRVREAAELLGLEDllDR---KPKQLS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 153 PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVT--QHIGMMkhISDQVLVMHQGEVV 230
Cdd:COG3839 136 GGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVThdQVEAMT--LADRIAVMNDGRIQ 213
|
250
....*....|..
gi 446495558 231 ERGSTADVLASP 242
Cdd:COG3839 214 QVGTPEELYDRP 225
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-228 |
3.46e-40 |
|
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: 137.32 E-value: 3.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSF 85
Cdd:cd03229 1 LELKNVSKRYGQKT---------VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RSQR--IRMIFQDPStsLNPRQRISQILDFPLrlntnlepeqrrkqiietmrmvgllpdhvsyyphmlAPGQKQRLGLAR 163
Cdd:cd03229 72 PPLRrrIGMVFQDFA--LFPHLTVLENIALGL------------------------------------SGGQQQRVALAR 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446495558 164 ALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGE 228
Cdd:cd03229 114 ALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-252 |
3.65e-40 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 145.62 E-value: 3.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 1 MIETLLEVRNLSKTFRYRTgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLA-KMLAGMIEP----TSGELLIDD 75
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQ-----TVRTVVNDVSLQIEAGETLALVGESGSGKSVTAlSILRLLPSPpvvyPSGDIRFHG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 76 HPLHFGDYS----FRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTNLEPEQRRKQIIETMRMVGL--LPDHVSYYPH 149
Cdd:PRK15134 76 ESLLHASEQtlrgVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIrqAAKRLTDYPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 150 MLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEV 229
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRC 235
|
250 260
....*....|....*....|...
gi 446495558 230 VERGSTADVLASPLHELTKRLIA 252
Cdd:PRK15134 236 VEQNRAATLFSAPTHPYTQKLLN 258
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-240 |
7.20e-40 |
|
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: 146.52 E-value: 7.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSktFRYRtgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYS 84
Cdd:COG2274 474 IELENVS--FRYP-----GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLrQIDPAS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 85 FRSQrIRMIFQDP---STSlnprqrisqILDfplrlntNL---EPEQRRKQIIETMRMVGLLPDhVSYYPH--------- 149
Cdd:COG2274 547 LRRQ-IGVVLQDVflfSGT---------IRE-------NItlgDPDATDEEIIEAARLAGLHDF-IEALPMgydtvvgeg 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 150 --MLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELqeKQGISYIYVTQHIGMMKHiSDQVLVMHQG 227
Cdd:COG2274 609 gsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRLSTIRL-ADRIIVLDKG 685
|
250
....*....|...
gi 446495558 228 EVVERGSTADVLA 240
Cdd:COG2274 686 RIVEDGTHEELLA 698
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-256 |
1.60e-39 |
|
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: 137.87 E-value: 1.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 5 LLEVRNLSktfryrtgwFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYS 84
Cdd:COG1120 1 MLEAENLS---------VGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLA--SLS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 85 FR--SQRIRMIFQDPSTSLN------------PRQRISQILDfplrlntnlepEQRRKQIIETMRMVGLlpDHVSYYP-H 149
Cdd:COG1120 70 RRelARRIAYVPQEPPAPFGltvrelvalgryPHLGLFGRPS-----------AEDREAVEEALERTGL--EHLADRPvD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 150 MLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEV 229
Cdd:COG1120 137 ELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
250 260
....*....|....*....|....*..
gi 446495558 230 VERGSTADVlasplheLTKRLIAGHFG 256
Cdd:COG1120 217 VAQGPPEEV-------LTPELLEEVYG 236
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-228 |
3.11e-39 |
|
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: 134.43 E-value: 3.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSktFRYRTGwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSF 85
Cdd:cd03228 1 IEFKNVS--FSYPGR-----PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RSQRIRMIFQDPstslnprqrisQILDFPLRLNtnlepeqrrkqiietmrmvgllpdhvsyyphMLAPGQKQRLGLARAL 165
Cdd:cd03228 74 LRKNIAYVPQDP-----------FLFSGTIREN-------------------------------ILSGGQRQRIAIARAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446495558 166 ILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHIGMMKHiSDQVLVMHQGE 228
Cdd:cd03228 112 LRDPPILILDEATSALDPETEALILEALRALAKGKTV--IVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
5-259 |
5.82e-38 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 135.80 E-value: 5.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 5 LLEVRNLSKTFRYRTGWFRrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTsgeLLIDDHPLHFGD-- 82
Cdd:COG4170 3 LLDIRNLTIEIDTPQGRVK-----AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDN---WHVTADRFRWNGid 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 83 ---YSFRSQR------IRMIFQDPSTSLNPRQRISQILDFPLrLNTNLE------PEQRRKQIIETMRMVGLlPDHVSY- 146
Cdd:COG4170 75 llkLSPRERRkiigreIAMIFQEPSSCLDPSAKIGDQLIEAI-PSWTFKgkwwqrFKWRKKRAIELLHRVGI-KDHKDIm 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 147 --YPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVM 224
Cdd:COG4170 153 nsYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVL 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 446495558 225 HQGEVVERGSTADVLASPLHELTKRLI--AGHFGEAL 259
Cdd:COG4170 233 YCGQTVESGPTEQILKSPHHPYTKALLrsMPDFRQPL 269
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-241 |
6.58e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 133.96 E-value: 6.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 3 ETLLEVRNLSktFRYRTgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD 82
Cdd:PRK13632 5 SVMIKVENVS--FSYPN-----SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 83 YSFRSQRIRMIFQDPSTslnprQRI-SQILD---FPLRlNTNLEPEQRRKQIIETMRMVGLLpDHVSYYPHMLAPGQKQR 158
Cdd:PRK13632 78 LKEIRKKIGIIFQNPDN-----QFIgATVEDdiaFGLE-NKKVPPKKMKDIIDDLAKKVGME-DYLDKEPQNLSGGQKQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 159 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHigmMKHI--SDQVLVMHQGEVVERGSTA 236
Cdd:PRK13632 151 VAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHD---MDEAilADKVIVFSEGKLIAQGKPK 227
|
....*
gi 446495558 237 DVLAS 241
Cdd:PRK13632 228 EILNN 232
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
20-228 |
7.11e-38 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 130.44 E-value: 7.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 20 GWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSFRSQRIRMIFQdpst 99
Cdd:cd00267 5 LSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 100 slnprqrisqildfplrlntnlepeqrrkqiietmrmvgllpdhvsyyphmLAPGQKQRLGLARALILRPKVIIADEALA 179
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446495558 180 SLDMSMRSQLINLMLELQEkQGISYIYVTQHIGMMKHISDQVLVMHQGE 228
Cdd:cd00267 110 GLDPASRERLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-242 |
9.64e-38 |
|
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: 132.56 E-value: 9.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFryrtGWFRrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYS 84
Cdd:cd03219 1 LEVRGLTKRF----GGLV-----ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItGLPPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 85 FRSQRIRMIFQDPS------------TSLNPRQRISQILDFPLRlntnlEPEQRRKQIIETMRMVGLlpDHVSYYP-HML 151
Cdd:cd03219 72 IARLGIGRTFQIPRlfpeltvlenvmVAAQARTGSGLLLARARR-----EEREARERAEELLERVGL--ADLADRPaGEL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 152 APGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHIGMMKHISDQVLVMHQGEVVE 231
Cdd:cd03219 145 SYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSLADRVTVLDQGRVIA 223
|
250
....*....|.
gi 446495558 232 RGSTADVLASP 242
Cdd:cd03219 224 EGTPDEVRNNP 234
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-231 |
1.20e-37 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 132.10 E-value: 1.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 1 MIEtlleVRNLSKtfRYRTGwfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH- 79
Cdd:COG2884 1 MIR----FENVSK--RYPGG------REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSr 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 80 --FGDYSFRSQRIRMIFQDpsTSLNPRQRISQILDFPLRLnTNLEPEQRRKQIIETMRMVGLLpDHVSYYPHMLAPGQKQ 157
Cdd:COG2884 69 lkRREIPYLRRRIGVVFQD--FRLLPDRTVYENVALPLRV-TGKSRKEIRRRVREVLDLVGLS-DKAKALPHELSGGEQQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446495558 158 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVE 231
Cdd:COG2884 145 RVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-230 |
1.65e-37 |
|
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: 129.86 E-value: 1.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFRyrtgwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSf 85
Cdd:cd03216 1 LELRGITKRFG---------GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPR- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RSQR--IRMIFQdpstslnprqrisqildfplrlntnlepeqrrkqiietmrmvgllpdhvsyyphmLAPGQKQRLGLAR 163
Cdd:cd03216 71 DARRagIAMVYQ-------------------------------------------------------LSVGERQMVEIAR 95
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446495558 164 ALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHIGMMKHISDQVLVMHQGEVV 230
Cdd:cd03216 96 ALARNARLLILDEPTAALTPAEVERLFKVIRRLR-AQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-251 |
1.47e-36 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 129.49 E-value: 1.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLskTFRYRTGWFRrqtveavkpLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfGDYSF 85
Cdd:COG3840 2 LRLDDL--TYRYGDFPLR---------FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNG-----QDLTA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 R--SQR-IRMIFQDpsTSLNPRQRISQILDFPLRLNTNLEPEQRrKQIIETMRMVGLLpDHVSYYPHMLAPGQKQRLGLA 162
Cdd:COG3840 66 LppAERpVSMLFQE--NNLFPHLTVAQNIGLGLRPGLKLTAEQR-AQVEQALERVGLA-GLLDRLPGQLSGGQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 163 RALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVLASP 242
Cdd:COG3840 142 RCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
....*....
gi 446495558 243 LHELTKRLI 251
Cdd:COG3840 222 PPPALAAYL 230
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
3-242 |
2.01e-36 |
|
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: 129.77 E-value: 2.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 3 ETLLEVRNLSKTFryrtGwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL---- 78
Cdd:COG0411 2 DPLLEVRGLTKRF----G-----GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 79 -HfgdysfrsQRIRM----IFQDPS------------TSLNPRQRISqILDFPLRLNTNLEPEQR-RKQIIETMRMVGLL 140
Cdd:COG0411 73 pH--------RIARLgiarTFQNPRlfpeltvlenvlVAAHARLGRG-LLAALLRLPRARREEREaRERAEELLERVGLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 141 pDHVSYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQ 220
Cdd:COG0411 144 -DRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADR 222
|
250 260
....*....|....*....|..
gi 446495558 221 VLVMHQGEVVERGSTADVLASP 242
Cdd:COG0411 223 IVVLDFGRVIAEGTPAEVRADP 244
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-238 |
2.52e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 129.87 E-value: 2.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 3 ETLLEVRNLSktFRYRT-GWFrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFG 81
Cdd:PRK13648 5 NSIIVFKNVS--FQYQSdASF------TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 82 DYSFRSQRIRMIFQDPSTslnprQRISQIL--DFPLRLNTNLEPEQRRKQII-ETMRMVGLLpDHVSYYPHMLAPGQKQR 158
Cdd:PRK13648 77 NFEKLRKHIGIVFQNPDN-----QFVGSIVkyDVAFGLENHAVPYDEMHRRVsEALKQVDML-ERADYEPNALSGGQKQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 159 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHiSDQVLVMHQGEVVERGSTADV 238
Cdd:PRK13648 151 VAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-241 |
8.35e-36 |
|
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: 134.12 E-value: 8.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSktFRYRTGwfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSF 85
Cdd:COG4988 337 IELEDVS--FSYPGG------RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RSQRIRMIFQDPstslnprqRIsqildFPLRLNTNL---EPEQRRKQIIETMRMVGLLpDHVSYYPHMLA---------- 152
Cdd:COG4988 409 WRRQIAWVPQNP--------YL-----FAGTIRENLrlgRPDASDEELEAALEAAGLD-EFVAALPDGLDtplgeggrgl 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 153 -PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHIGMMKHiSDQVLVMHQGEVVE 231
Cdd:COG4988 475 sGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTV--ILITHRLALLAQ-ADRILVLDDGRIVE 551
|
250
....*....|
gi 446495558 232 RGSTADVLAS 241
Cdd:COG4988 552 QGTHEELLAK 561
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-229 |
1.23e-35 |
|
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: 126.49 E-value: 1.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFryrtGWFrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSF 85
Cdd:cd03262 1 IEIKNLHKSF----GDF-----HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RS--QRIRMIFQdpSTSLNPRQRISQILDFPLRLNTNLEPEQRRKQIIETMRMVGLLpDHVSYYPHMLAPGQKQRLGLAR 163
Cdd:cd03262 72 NElrQKVGMVFQ--QFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLA-DKADAYPAQLSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446495558 164 ALILRPKVIIADEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHIGMMKHISDQVLVMHQGEV 229
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAE-EGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-233 |
1.55e-35 |
|
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: 126.22 E-value: 1.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSF 85
Cdd:cd03301 1 VELENVTKRF---------GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RSQRIRMIFQdpSTSLNPRQRISQILDFPLRLNTNLEPE--QRRKQIIETMRMVGLLpdhvSYYPHMLAPGQKQRLGLAR 163
Cdd:cd03301 70 KDRDIAMVFQ--NYALYPHMTVYDNIAFGLKLRKVPKDEidERVREVAELLQIEHLL----DRKPKQLSGGQRQRVALGR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 164 ALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERG 233
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-238 |
1.95e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 132.06 E-value: 1.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 3 ETLLEVRNLSKTFRyrtgwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD 82
Cdd:COG1129 2 EPLLEMRGISKSFG---------GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 83 YSfRSQR--IRMIFQDPstSLNP-------------------------RQRISQILDfplRLNTNLEPEQRrkqiietmr 135
Cdd:COG1129 73 PR-DAQAagIAIIHQEL--NLVPnlsvaeniflgreprrgglidwramRRRARELLA---RLGLDIDPDTP--------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 136 mVGLLPdhvsyyphmlaPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHIGMMK 215
Cdd:COG1129 138 -VGDLS-----------VAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKA-QGVAIIYISHRLDEVF 204
|
250 260
....*....|....*....|...
gi 446495558 216 HISDQVLVMHQGEVVERGSTADV 238
Cdd:COG1129 205 EIADRVTVLRDGRLVGTGPVAEL 227
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
6-258 |
2.19e-35 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 129.45 E-value: 2.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHplhfgDYSF 85
Cdd:PRK11432 7 VVLKNITKRFGSNT---------VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGE-----DVTH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RS--QR-IRMIFQdpSTSLNPRQRISQILDFPLRLnTNLEPEQRRKQIIETMRMVGL--LPDHvsyYPHMLAPGQKQRLG 160
Cdd:PRK11432 73 RSiqQRdICMVFQ--SYALFPHMSLGENVGYGLKM-LGVPKEERKQRVKEALELVDLagFEDR---YVDQISGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 161 LARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVLA 240
Cdd:PRK11432 147 LARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYR 226
|
250
....*....|....*...
gi 446495558 241 SPlhelTKRLIAGHFGEA 258
Cdd:PRK11432 227 QP----ASRFMASFMGDA 240
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-241 |
4.09e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 127.05 E-value: 4.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 1 MIETLLEVRNLSktFRYRtgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF 80
Cdd:PRK13635 1 MKEEIIRVEHIS--FRYP-----DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 81 GDYSFRSQRIRMIFQDPSTslnprQRI-SQILD---FPLRlNTNLEPEQRRKQIIETMRMVGLLpDHVSYYPHMLAPGQK 156
Cdd:PRK13635 74 ETVWDVRRQVGMVFQNPDN-----QFVgATVQDdvaFGLE-NIGVPREEMVERVDQALRQVGME-DFLNREPHRLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 157 QRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHiSDQVLVMHQGEVVERGSTA 236
Cdd:PRK13635 147 QRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPE 225
|
....*
gi 446495558 237 DVLAS 241
Cdd:PRK13635 226 EIFKS 230
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
29-238 |
5.77e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 126.74 E-value: 5.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 29 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhpLHFGD----YSFRsQRIRMIFQDPSTslnpr 104
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDeenlWDIR-NKAGMVFQNPDN----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 105 QRISQILDFPLRL---NTNLEPEQRRKQIIETMRMVGLLpDHVSYYPHMLAPGQKQRLGLARALILRPKVIIADEALASL 181
Cdd:PRK13633 97 QIVATIVEEDVAFgpeNLGIPPEEIRERVDESLKKVGMY-EYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAML 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446495558 182 DMSMRSQLINLMLELQEKQGISYIYVTQHigMMKHI-SDQVLVMHQGEVVERGSTADV 238
Cdd:PRK13633 176 DPSGRREVVNTIKELNKKYGITIILITHY--MEEAVeADRIIVMDSGKVVMEGTPKEI 231
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-229 |
9.68e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 124.16 E-value: 9.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFRYRTGWfrrqtveavKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfGDYS- 84
Cdd:COG4619 1 LELEGLSFRVGGKPIL---------SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL--SAMPp 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 85 --FRSQrIRMIFQDPSTslnPRQRISQILDFPLRLNtnlEPEQRRKQIIETMRMVGLLPDHVSYYPHMLAPGQKQRLGLA 162
Cdd:COG4619 70 peWRRQ-VAYVPQEPAL---WGGTVRDNLPFPFQLR---ERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALI 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446495558 163 RALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEV 229
Cdd:COG4619 143 RALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-258 |
1.97e-34 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 130.28 E-value: 1.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSktFRYRTGwfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSF 85
Cdd:COG1132 340 IEFENVS--FSYPGD------RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIR--DLTL 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RS--QRIRMIFQDPstslnprqrisQILDFPLRlnTNL---EPEQRRKQIIETMRMVGL------LPD----HVSYYPHM 150
Cdd:COG1132 410 ESlrRQIGVVPQDT-----------FLFSGTIR--ENIrygRPDATDEEVEEAAKAAQAhefieaLPDgydtVVGERGVN 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 151 LAPGQKQRLGLARALILRPKVIIADEALASLD----MSMRSQLINLMlelqekQGISYIYVTQHIGMMKHiSDQVLVMHQ 226
Cdd:COG1132 477 LSGGQRQRIAIARALLKDPPILILDEATSALDteteALIQEALERLM------KGRTTIVIAHRLSTIRN-ADRILVLDD 549
|
250 260 270
....*....|....*....|....*....|..
gi 446495558 227 GEVVERGSTADVLASplHELTKRLIAGHFGEA 258
Cdd:COG1132 550 GRIVEQGTHEELLAR--GGLYARLYRLQFGEE 579
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-242 |
3.55e-34 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 126.03 E-value: 3.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhFGDYSF 85
Cdd:COG1118 3 IEVRNISKRFGSFT---------LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL-FTNLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RSQRIRMIFQDPStsLNP----RQRISqildFPLRlNTNLEPEQRRKQIIETMRMVGL--LPDHvsyYPHMLAPGQKQRL 159
Cdd:COG1118 73 RERRVGFVFQHYA--LFPhmtvAENIA----FGLR-VRPPSKAEIRARVEELLELVQLegLADR---YPSQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 160 GLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTqhigmmkH-------ISDQVLVMHQGEVVER 232
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVT-------HdqeealeLADRVVVMNQGRIEQV 215
|
250
....*....|
gi 446495558 233 GSTADVLASP 242
Cdd:COG1118 216 GTPDEVYDRP 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-233 |
3.55e-34 |
|
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: 121.77 E-value: 3.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 7 EVRNLSktfryrtgwFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdysfr 86
Cdd:cd03214 1 EVENLS---------VGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLA------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 87 sqrirmifqdpstSLNPRQRISQILDFPlrlntnlepeqrrkQIIETMRMVGLLPDHVSyyphMLAPGQKQRLGLARALI 166
Cdd:cd03214 65 -------------SLSPKELARKIAYVP--------------QALELLGLAHLADRPFN----ELSGGERQRVLLARALA 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446495558 167 LRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERG 233
Cdd:cd03214 114 QEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-235 |
4.75e-34 |
|
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: 122.67 E-value: 4.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSktfryrtgwFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIE-----PTSGELLIDDHPLHF 80
Cdd:cd03260 1 IELRDLN---------VYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 81 GDYSFRSQRIR--MIFQDPstslNP-RQRISQILDFPLRLNTNLEPEQRRKQIIETMRMVGLlPDHVS--YYPHMLAPGQ 155
Cdd:cd03260 72 LDVDVLELRRRvgMVFQKP----NPfPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAAL-WDEVKdrLHALGLSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 156 KQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHIGMMKHISDQVLVMHQGEVVERGST 235
Cdd:cd03260 147 QQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTI--VIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
6-230 |
9.56e-34 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 121.66 E-value: 9.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTfrYRTGWFRRQTVEAVkplSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSF 85
Cdd:TIGR02982 2 ISIRNLNHY--YGHGSLRKQVLFDI---NLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RSQ---RIRMIFQDPS--TSLNPRQRISQILDfplrLNTNLEPEQRRKQIIETMRMVGLlPDHVSYYPHMLAPGQKQRLG 160
Cdd:TIGR02982 77 LVQlrrRIGYIFQAHNllGFLTARQNVQMALE----LQPNLSYQEARERARAMLEAVGL-GDHLNYYPHNLSGGQKQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 161 LARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTqHIGMMKHISDQVLVMHQGEVV 230
Cdd:TIGR02982 152 IARALVHHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVT-HDNRILDVADRILQMEDGKLL 220
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-242 |
1.15e-33 |
|
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: 122.06 E-value: 1.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFryrtGWFRRQTVeavkplSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfGDYSF 85
Cdd:cd03299 1 LKVENLSKDW----KEFKLKNV------SLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI--TNLPP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RSQRIRMIFQDpsTSLNPRQRISQILDFPLRLNTNLEPEqRRKQIIETMRMVGLlpDHV-SYYPHMLAPGQKQRLGLARA 164
Cdd:cd03299 69 EKRDISYVPQN--YALFPHMTVYKNIAYGLKKRKVDKKE-IERKVLEIAEMLGI--DHLlNRKPETLSGGEQQRVAIARA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446495558 165 LILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVLASP 242
Cdd:cd03299 144 LVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-236 |
1.45e-33 |
|
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: 121.46 E-value: 1.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFRYRTgwfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSF 85
Cdd:cd03263 1 LQIRNLTKTYKKGT-------KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RsQRIRMIFQDPS--TSLNPRqrisQILDFPLRLnTNLEPEQRRKQIIETMRMVGLLpDHVSYYPHMLAPGQKQRLGLAR 163
Cdd:cd03263 74 R-QSLGYCPQFDAlfDELTVR----EHLRFYARL-KGLPKSEIKEEVELLLRVLGLT-DKANKRARTLSGGMKRKLSLAI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446495558 164 ALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHIGMMKHISDQVLVMHQGEVVERGSTA 236
Cdd:cd03263 147 ALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSI--ILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQ 217
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-242 |
1.49e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 122.12 E-value: 1.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 1 MIETLLEVRNLskTFRYRTgwfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHf 80
Cdd:COG1121 2 MMMPAIELENL--TVSYGG-------RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 81 gdysfrsqrirmifqdpstslNPRQRIS---QIL----DFPLR--------------LNTNLEPEQRRK--QIIETMRMV 137
Cdd:COG1121 72 ---------------------RARRRIGyvpQRAevdwDFPITvrdvvlmgrygrrgLFRRPSRADREAvdEALERVGLE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 138 GLLPDHVSyyphMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHIGMMKHI 217
Cdd:COG1121 131 DLADRPIG----ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELR-REGKTILVVTHDLGAVREY 205
|
250 260
....*....|....*....|....*
gi 446495558 218 SDQVLVMHQGeVVERGSTADVLASP 242
Cdd:COG1121 206 FDRVLLLNRG-LVAHGPPEEVLTPE 229
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-202 |
2.12e-33 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 120.66 E-value: 2.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 5 LLEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 84
Cdd:COG4133 2 MLEAENLSCRRGERL---------LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 85 FRSQrirMIFQDPSTSLNPRQRISQILDFPLRLNTNLEPEQRRKQIIETMRMVGLLpdHVsyYPHMLAPGQKQRLGLARA 164
Cdd:COG4133 73 YRRR---LAYLGHADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGLA--DL--PVRQLSAGQKRRVALARL 145
|
170 180 190
....*....|....*....|....*....|....*...
gi 446495558 165 LILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGI 202
Cdd:COG4133 146 LLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGA 183
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
6-253 |
2.77e-33 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 125.15 E-value: 2.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSK--------TFRY-RTGWFRRQTVE------AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGE 70
Cdd:PRK10070 5 LEIKNLYKifgehpqrAFKYiEQGLSKEQILEktglslGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 71 LLIDDHPL-HFGDYSFRSQR---IRMIFQdpSTSLNPRQRISQILDFPLRLnTNLEPEQRRKQIIETMRMVGLlPDHVSY 146
Cdd:PRK10070 85 VLIDGVDIaKISDAELREVRrkkIAMVFQ--SFALMPHMTVLDNTAFGMEL-AGINAEERREKALDALRQVGL-ENYAHS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 147 YPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQ 226
Cdd:PRK10070 161 YPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN 240
|
250 260
....*....|....*....|....*..
gi 446495558 227 GEVVERGSTADVLASPLHELTKRLIAG 253
Cdd:PRK10070 241 GEVVQVGTPDEILNNPANDYVRTFFRG 267
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
2-246 |
2.78e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 122.15 E-value: 2.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 2 IETLLEVRNLskTFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFG 81
Cdd:PRK13650 1 MSNIIEVKNL--TFKYKE----DQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 82 DYSFRSQRIRMIFQDPSTslnprQRISQILD----FPLRlNTNLEPEQRRKQIIETMRMVGLLpDHVSYYPHMLAPGQKQ 157
Cdd:PRK13650 75 NVWDIRHKIGMVFQNPDN-----QFVGATVEddvaFGLE-NKGIPHEEMKERVNEALELVGMQ-DFKEREPARLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 158 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKhISDQVLVMHQGEvVERGSTAD 237
Cdd:PRK13650 148 RVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQ-VESTSTPR 225
|
....*....
gi 446495558 238 VLASPLHEL 246
Cdd:PRK13650 226 ELFSRGNDL 234
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-253 |
4.01e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 121.17 E-value: 4.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIE-----PTSGELLIDDHPLHF 80
Cdd:PRK14247 4 IEIRDLKVSF---------GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 81 GDYSFRSQRIRMIFQDPSTSlnPRQRISQILDFPLRLN----TNLEPEQRRKQIIETMRMVGLLPDHVSYYPHMLAPGQK 156
Cdd:PRK14247 75 MDVIELRRRVQMVFQIPNPI--PNLSIFENVALGLKLNrlvkSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 157 QRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELqeKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTA 236
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTR 230
|
250
....*....|....*..
gi 446495558 237 DVLASPLHELTKRLIAG 253
Cdd:PRK14247 231 EVFTNPRHELTEKYVTG 247
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-231 |
4.15e-33 |
|
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: 120.62 E-value: 4.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 1 MIETLLEVRNLSKTFRYRTGwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF 80
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAG-----ELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 81 GD----YSFRSQRIRMIFQDpstslnprqriSQILD---------FPLRLNTNLEPEQRRKQIIETmrmVGL--LPDHvs 145
Cdd:COG4181 79 LDedarARLRARHVGFVFQS-----------FQLLPtltalenvmLPLELAGRRDARARARALLER---VGLghRLDH-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 146 yYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHiSDQVLVMH 225
Cdd:COG4181 143 -YPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLR 220
|
....*.
gi 446495558 226 QGEVVE 231
Cdd:COG4181 221 AGRLVE 226
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-240 |
5.51e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 121.49 E-value: 5.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 1 MIETLLEVRNLSktFRYRTGwfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhf 80
Cdd:PRK13636 1 MEDYILKVEELN--YNYSDG------THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 81 gDYSFRS-----QRIRMIFQDPSTSLNPRQrISQILDFPLrLNTNLEPEQRRKQIIETMRMVGLlpDHVSYYP-HMLAPG 154
Cdd:PRK13636 71 -DYSRKGlmklrESVGMVFQDPDNQLFSAS-VYQDVSFGA-VNLKLPEDEVRKRVDNALKRTGI--EHLKDKPtHCLSFG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 155 QKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGS 234
Cdd:PRK13636 146 QKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGN 225
|
....*.
gi 446495558 235 TADVLA 240
Cdd:PRK13636 226 PKEVFA 231
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-242 |
7.91e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 120.95 E-value: 7.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 5 LLEVRNLSktFRYRTGwfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgDYS 84
Cdd:PRK13639 1 ILETRDLK--YSYPDG------TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI---KYD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 85 FRS-----QRIRMIFQDPSTSL-NPrqRISQILDF-PlrLNTNLEPEQRRKQIIETMRMVGLLpDHVSYYPHMLAPGQKQ 157
Cdd:PRK13639 70 KKSllevrKTVGIVFQNPDDQLfAP--TVEEDVAFgP--LNLGLSKEEVEKRVKEALKAVGME-GFENKPPHHLSGGQKK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 158 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTAD 237
Cdd:PRK13639 145 RVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLN-KEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKE 223
|
....*
gi 446495558 238 VLASP 242
Cdd:PRK13639 224 VFSDI 228
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-242 |
1.28e-32 |
|
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: 119.37 E-value: 1.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFryrtGWFRrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfGDYSF 85
Cdd:cd03296 3 IEVRNVSKRF----GDFV-----ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA--TDVPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RSQRIRMIFQDpsTSLNPRQRISQILDFPLRLNTNLE--PEQR-RKQIIETMRMVGL--LPDHvsyYPHMLAPGQKQRLG 160
Cdd:cd03296 72 QERNVGFVFQH--YALFRHMTVFDNVAFGLRVKPRSErpPEAEiRAKVHELLKLVQLdwLADR---YPAQLSGGQRQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 161 LARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVLA 240
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
..
gi 446495558 241 SP 242
Cdd:cd03296 227 HP 228
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
6-240 |
2.38e-32 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 119.03 E-value: 2.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFR-YRTGWFR------------RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELL 72
Cdd:COG1134 5 IEVENVSKSYRlYHEPSRSlkelllrrrrtrREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 73 IDdhplhfGdysfrsqRIRMIFqDPSTSLNP----RQRI---SQILDFPLRlntnlEPEQRRKQIIEtmrMVGL-----L 140
Cdd:COG1134 85 VN------G-------RVSALL-ELGAGFHPeltgRENIylnGRLLGLSRK-----EIDEKFDEIVE---FAELgdfidQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 141 PdhVSYYPhmlaPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHIGMMKHISDQ 220
Cdd:COG1134 143 P--VKTYS----SGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRE-SGRTVIFVSHSMGAVRRLCDR 215
|
250 260
....*....|....*....|
gi 446495558 221 VLVMHQGEVVERGSTADVLA 240
Cdd:COG1134 216 AIWLEKGRLVMDGDPEEVIA 235
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
28-238 |
3.96e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 119.38 E-value: 3.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 28 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhpLHFGDYSFRSQRIR----MIFQDPSTSLNp 103
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG--VDITDKKVKLSDIRkkvgLVFQYPEYQLF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 104 RQRISQILDFPLRlNTNLEPEQRRKQIIETMRMVGLlpDHVSY---YPHMLAPGQKQRLGLARALILRPKVIIADEALAS 180
Cdd:PRK13637 98 EETIEKDIAFGPI-NLGLSEEEIENRVKRAMNIVGL--DYEDYkdkSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446495558 181 LDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADV 238
Cdd:PRK13637 175 LDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
6-240 |
2.31e-31 |
|
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: 121.80 E-value: 2.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSktFRYRTgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSF 85
Cdd:COG4987 334 LELEDVS--FRYPG-----AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RSQRIRMIFQDP---STSL--NprqrisqildfpLRL-NTNLEPEqrrkQIIETMRMVGL------LPD----HVSYYPH 149
Cdd:COG4987 407 LRRRIAVVPQRPhlfDTTLreN------------LRLaRPDATDE----ELWAALERVGLgdwlaaLPDgldtWLGEGGR 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 150 MLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHIGMMKHIsDQVLVMHQGEV 229
Cdd:COG4987 471 RLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTV--LLITHRLAGLERM-DRILVLEDGRI 547
|
250
....*....|.
gi 446495558 230 VERGSTADVLA 240
Cdd:COG4987 548 VEQGTHEELLA 558
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
7-241 |
3.84e-31 |
|
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: 115.40 E-value: 3.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 7 EVRNLSktFRYRTGwfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSFR 86
Cdd:cd03254 4 EFENVN--FSYDEK------KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIR--DISRK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 87 SQR--IRMIFQDP---STSlnprqrisqILDfPLRLNTnlePEQRRKQIIETMRMVGL------LPDHVSYYP----HML 151
Cdd:cd03254 74 SLRsmIGVVLQDTflfSGT---------IME-NIRLGR---PNATDEEVIEAAKEAGAhdfimkLPNGYDTVLgengGNL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 152 APGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEkqGISYIYVTQHIGMMKHiSDQVLVMHQGEVVE 231
Cdd:cd03254 141 SQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIE 217
|
250
....*....|
gi 446495558 232 RGSTADVLAS 241
Cdd:cd03254 218 EGTHDELLAK 227
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
4-242 |
5.38e-31 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 118.13 E-value: 5.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 4 TLLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfGDY 83
Cdd:PRK09452 13 PLVELRGISKSF---------DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI--THV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 84 SFRSQRIRMIFQdpSTSLNPRQRISQILDFPLRLNTNLEPEQRRKqIIETMRMVGLlPDHVSYYPHMLAPGQKQRLGLAR 163
Cdd:PRK09452 82 PAENRHVNTVFQ--SYALFPHMTVFENVAFGLRMQKTPAAEITPR-VMEALRMVQL-EEFAQRKPHQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 164 ALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTqH-----IGMmkhiSDQVLVMHQGEVVERGSTADV 238
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVT-HdqeeaLTM----SDRIVVMRDGRIEQDGTPREI 232
|
....
gi 446495558 239 LASP 242
Cdd:PRK09452 233 YEEP 236
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
34-242 |
5.84e-31 |
|
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: 117.89 E-value: 5.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 34 SFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdysFRSQ----------RIRMIFQDPStsLNP 103
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL------QDSArgiflpphrrRIGYVFQEAR--LFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 104 RQRISQILDFPLRLNTNLEPEQRRKQIIETMRMVGLLpDHvsyYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 183
Cdd:COG4148 91 HLSVRGNLLYGRKRAPRAERRISFDEVVELLGIGHLL-DR---RPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446495558 184 SMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVLASP 242
Cdd:COG4148 167 ARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-256 |
6.46e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 115.52 E-value: 6.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 3 ETLLEVRNLSktFRYRTgwfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIE--P---TSGELLIDDHP 77
Cdd:COG1117 9 EPKIEVRNLN--VYYGD-------KQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 78 LHFGD---YSFRsQRIRMIFQDPstslNPrqrisqildFP----------LRLNtNLEPEQRRKQIIET-MRMVGLlPDH 143
Cdd:COG1117 80 IYDPDvdvVELR-RRVGMVFQKP----NP---------FPksiydnvaygLRLH-GIKSKSELDEIVEEsLRKAAL-WDE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 144 VSYYPHM----LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTqHigMMKH--- 216
Cdd:COG1117 144 VKDRLKKsalgLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTI--VIVT-H--NMQQaar 218
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446495558 217 ISDQVLVMHQGEVVERGSTADVLASPLHELTKRLIAGHFG 256
Cdd:COG1117 219 VSDYTAFFYLGELVEFGPTEQIFTNPKDKRTEDYITGRFG 258
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-251 |
1.26e-30 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 117.24 E-value: 1.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 5 LLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDY 83
Cdd:PRK11607 19 LLEIRNLTKSF---------DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLsHVPPY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 84 sfrsQR-IRMIFQdpSTSLNPRQRISQILDFPLRLNtNLEPEQRRKQIIETMRMVGLLpDHVSYYPHMLAPGQKQRLGLA 162
Cdd:PRK11607 90 ----QRpINMMFQ--SYALFPHMTVEQNIAFGLKQD-KLPKAEIASRVNEMLGLVHMQ-EFAKRKPHQLSGGQRQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 163 RALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVLASP 242
Cdd:PRK11607 162 RSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
|
....*....
gi 446495558 243 LHELTKRLI 251
Cdd:PRK11607 242 TTRYSAEFI 250
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
26-261 |
1.76e-30 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 114.41 E-value: 1.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 26 TVEAVKPL----SFTLREGQTLAIIGENGSGKSTLAKMLAGMIEP----TSGELLIDDHPLHFGdySFRSQRIRMIFQDP 97
Cdd:PRK10418 11 ALQAAQPLvhgvSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPC--ALRGRKIATIMQNP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 98 STSLNPRQRISQILDFPLRLNTNLEPEQrrkQIIETMRMVGLLPDH--VSYYPHMLAPGQKQRLGLARALILRPKVIIAD 175
Cdd:PRK10418 89 RSAFNPLHTMHTHARETCLALGKPADDA---TLTAALEAVGLENAArvLKLYPFEMSGGMLQRMMIALALLCEAPFIIAD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 176 EALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLIAGH- 254
Cdd:PRK10418 166 EPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSAHl 245
|
....*....
gi 446495558 255 --FGEALTA 261
Cdd:PRK10418 246 alYGMELAS 254
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-242 |
2.80e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 114.51 E-value: 2.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 5 LLEVRNLSKTFRyrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 84
Cdd:PRK13652 3 LIETRDLCYSYS--------GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 85 FRSQRIRMIFQDPSTSLNPRQRISQILDFPLrlNTNLEPEQRRKQIIETMRMVGLlPDHVSYYPHMLAPGQKQRLGLARA 164
Cdd:PRK13652 75 EVRKFVGLVFQNPDDQIFSPTVEQDIAFGPI--NLGLDEETVAHRVSSALHMLGL-EELRDRVPHHLSGGEKKRVAIAGV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446495558 165 LILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVLASP 242
Cdd:PRK13652 152 IAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
33-233 |
3.01e-30 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 112.39 E-value: 3.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 33 LSFTLrEGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFG----DYSFRSQRIRMIFQDpsTSLNPRQRIS 108
Cdd:cd03297 17 IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSrkkiNLPPQQRKIGLVFQQ--YALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 109 QILDFPLRLNTNLEPEQRRKQIIETMRMvgllpDHVSY-YPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRS 187
Cdd:cd03297 94 ENLAFGLKRKRNREDRISVDELLDLLGL-----DHLLNrYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446495558 188 QLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERG 233
Cdd:cd03297 169 QLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-233 |
3.75e-30 |
|
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: 112.29 E-value: 3.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKtfRYRTGWfrrqtveAVKPLSFTLREGQTlAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSF 85
Cdd:cd03264 1 LQLENLTK--RYGKKR-------ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RsQRIRMIFQDPSTSlnPRQRISQILDFPLRLNtNLEPEQRRKQIIETMRMVGLLpDHVSYYPHMLAPGQKQRLGLARAL 165
Cdd:cd03264 71 R-RRIGYLPQEFGVY--PNFTVREFLDYIAWLK-GIPSKEVKARVDEVLELVNLG-DRAKKKIGSLSGGMRRRVGIAQAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446495558 166 ILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHIGMMKHISDQVLVMHQGEVVERG 233
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIV--ILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-252 |
4.44e-30 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 113.10 E-value: 4.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 1 MIETLLEVRNLSKTFRYRTGwFRRqtveavkpLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF 80
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKG-CRD--------VSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 81 GD-YSFRSQRIRMIF--------QDPSTSLnpRQRISQILDFPLRLntnLEPEQR-----RKQIIETMRMVGLLPDHVSY 146
Cdd:PRK11701 73 RDlYALSEAERRRLLrtewgfvhQHPRDGL--RMQVSAGGNIGERL---MAVGARhygdiRATAGDWLERVEIDAARIDD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 147 YPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQ 226
Cdd:PRK11701 148 LPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQ 227
|
250 260
....*....|....*....|....*.
gi 446495558 227 GEVVERGSTADVLASPLHELTKRLIA 252
Cdd:PRK11701 228 GRVVESGLTDQVLDDPQHPYTQLLVS 253
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-259 |
8.89e-30 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 114.13 E-value: 8.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 5 LLEVRNLSKTFRYRTGWfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMiepTSGELLIDDHPLHFGD-- 82
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGW-----VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV---TKDNWRVTADRMRFDDid 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 83 ---YSFRSQR------IRMIFQDPSTSLNPRQRISQ--ILDFP---------LRLNtnlepeQRRKQIIETMRMVGLlPD 142
Cdd:PRK15093 75 llrLSPRERRklvghnVSMIFQEPQSCLDPSERVGRqlMQNIPgwtykgrwwQRFG------WRKRRAIELLHRVGI-KD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 143 H---VSYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISD 219
Cdd:PRK15093 148 HkdaMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWAD 227
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 446495558 220 QVLVMHQGEVVERGSTADVLASPLHELTKRLIAG--HFGEAL 259
Cdd:PRK15093 228 KINVLYCGQTVETAPSKELVTTPHHPYTQALIRAipDFGSAM 269
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
33-242 |
1.89e-29 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 111.26 E-value: 1.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 33 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF----GDYSFRS--QRIRMIFQdpSTSLNPRQR 106
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFsktpSDKAIRElrRNVGMVFQ--QYNLWPHLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 107 ISQIL-DFPLRLN--TNLEPEQRRKQIIETMRmvglLPDHVSYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 183
Cdd:PRK11124 99 VQQNLiEAPCRVLglSKDQALARAEKLLERLR----LKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446495558 184 SMRSQLINLMLELQEkQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGsTADVLASP 242
Cdd:PRK11124 175 EITAQIVSIIRELAE-TGITQVIVTHEVEVARKTASRVVYMENGHIVEQG-DASCFTQP 231
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
33-233 |
2.45e-29 |
|
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: 110.28 E-value: 2.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 33 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSFRSqrIRMIFQDpsTSLNPRQRISQILD 112
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP--VSMLFQE--NNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 113 FPLRLNTNLEPEQRRKqIIETMRMVGLlPDHVSYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINL 192
Cdd:cd03298 93 LGLSPGLKLTAEDRQA-IEVALARVGL-AGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446495558 193 MLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERG 233
Cdd:cd03298 171 VLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-253 |
5.49e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 110.52 E-value: 5.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 30 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSFRSQRIR------MIFQDPSTSlnP 103
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAIKlrkevgMVFQQPNPF--P 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 104 RQRISQILDFPLRLNTNLEPEQRRKQIIETMRMVGL---LPDHVSYYPHMLAPGQKQRLGLARALILRPKVIIADEALAS 180
Cdd:PRK14246 104 HLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwkeVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446495558 181 LDMSMRSQLINLMLELqeKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLIAG 253
Cdd:PRK14246 184 IDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYVIG 254
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-240 |
1.39e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 110.56 E-value: 1.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 7 EVRNLSKTFRYR----------TGWFRRQ--TVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLID 74
Cdd:COG4586 3 EVENLSKTYRVYekepglkgalKGLFRREyrEVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 75 DH-PlhfgdysFRSQ-----RIRMIFQdpstslnprQRiSQIL-DFP----LRLNT---NLEPE---QRRKQIIETMRMV 137
Cdd:COG4586 83 GYvP-------FKRRkefarRIGVVFG---------QR-SQLWwDLPaidsFRLLKaiyRIPDAeykKRLDELVELLDLG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 138 GLLPDHVsyypHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHI 217
Cdd:COG4586 146 ELLDTPV----RQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEAL 221
|
250 260
....*....|....*....|...
gi 446495558 218 SDQVLVMHQGEVVERGSTADVLA 240
Cdd:COG4586 222 CDRVIVIDHGRIIYDGSLEELKE 244
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
2-241 |
1.47e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 109.80 E-value: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 2 IETLLEVRNLskTFRYRtgwfRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFG 81
Cdd:PRK13642 1 MNKILEVENL--VFKYE----KESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 82 DYSFRSQRIRMIFQDPSTSLnPRQRISQILDFPLRlNTNLEPEQRRKQIIETMRMVGLLpDHVSYYPHMLAPGQKQRLGL 161
Cdd:PRK13642 75 NVWNLRRKIGMVFQNPDNQF-VGATVEDDVAFGME-NQGIPREEMIKRVDEALLAVNML-DFKTREPARLSGGQKQRVAV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 162 ARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHiSDQVLVMHQGEVVERGSTADVLAS 241
Cdd:PRK13642 152 AGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFAT 230
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-240 |
2.10e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 109.33 E-value: 2.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 21 WFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgDYSFRS-----QRIRMIFQ 95
Cdd:PRK13638 8 WFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL---DYSKRGllalrQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 96 DPSTSLNpRQRISQILDFPLRlNTNLEPEQRRKQIIETMRMVGllPDHVSYYP-HMLAPGQKQRLGLARALILRPKVIIA 174
Cdd:PRK13638 85 DPEQQIF-YTDIDSDIAFSLR-NLGVPEAEITRRVDEALTLVD--AQHFRHQPiQCLSHGQKKRVAIAGALVLQARYLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446495558 175 DEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVLA 240
Cdd:PRK13638 161 DEPTAGLDPAGRTQMIAIIRRIVA-QGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-233 |
2.76e-28 |
|
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: 107.30 E-value: 2.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgdysf 85
Cdd:cd03268 1 LKTNDLTKTY---------GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG---------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 rsqrirmifQDPSTSLNPRQRISQILDFP-----------LRLNTNLePEQRRKQIIETMRMVGLlpdhvSYYPHMLAP- 153
Cdd:cd03268 62 ---------KSYQKNIEALRRIGALIEAPgfypnltarenLRLLARL-LGIRKKRIDEVLDVVGL-----KDSAKKKVKg 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 154 ---GQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISyIYVTQHI-GMMKHISDQVLVMHQGEV 229
Cdd:cd03268 127 fslGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLR-DQGIT-VLISSHLlSEIQKVADRIGIINKGKL 204
|
....
gi 446495558 230 VERG 233
Cdd:cd03268 205 IEEG 208
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
22-230 |
3.28e-28 |
|
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: 106.96 E-value: 3.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 22 FRRQTvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDysfRSQRIRMIFQDPStsl 101
Cdd:cd03226 9 YKKGT-EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIGYVMQDVD--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 102 npRQRISQILDFPLRLNTNL--EPEQRRKQIIETMRMVGLLPDHvsyyPHMLAPGQKQRLGLARALILRPKVIIADEALA 179
Cdd:cd03226 82 --YQLFTDSVREELLLGLKEldAGNEQAETVLKDLDLYALKERH----PLSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446495558 180 SLDM-SMRSqLINLMLELQeKQGISYIYVTQHIGMMKHISDQVLVMHQGEVV 230
Cdd:cd03226 156 GLDYkNMER-VGELIRELA-AQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-229 |
4.35e-28 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 107.84 E-value: 4.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 4 TLLEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGdy 83
Cdd:PRK11247 11 TPLLLNAVSKRYGERT---------VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 84 sfrSQRIRMIFQDpsTSLNPRQRIsqILDFPLRLNTNLEPEQRrkqiiETMRMVGLlPDHVSYYPHMLAPGQKQRLGLAR 163
Cdd:PRK11247 80 ---REDTRLMFQD--ARLLPWKKV--IDNVGLGLKGQWRDAAL-----QALAAVGL-ADRANEWPAALSGGQKQRVALAR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446495558 164 ALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEV 229
Cdd:PRK11247 147 ALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
28-241 |
5.49e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 108.33 E-value: 5.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 28 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFG--DYSFRS--QRIRMIFQDPSTSLNP 103
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkDKYIRPvrKRIGMVFQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 104 RQRISQILDFPLRLNTNLEpeQRRKQIIETMRMVGLLPDHVSYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 183
Cdd:PRK13646 101 DTVEREIIFGPKNFKMNLD--EVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446495558 184 SMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVLAS 241
Cdd:PRK13646 179 QSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-233 |
6.12e-28 |
|
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: 106.21 E-value: 6.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFRyrtgwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSf 85
Cdd:cd03269 1 LEVENVTKRFG---------RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARN- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 rsqriRMIFQDPSTSLNPRQRISQILDFPLRLNtNLEPEQRRKQIIETMRMVGlLPDHVSYYPHMLAPGQKQRLGLARAL 165
Cdd:cd03269 71 -----RIGYLPEERGLYPKMKVIDQLVYLAQLK-GLKKEEARRRIDEWLERLE-LSEYANKRVEELSKGNQQKVQFIAAV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446495558 166 ILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHIGMMKHISDQVLVMHQGEVVERG 233
Cdd:cd03269 144 IHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
21-224 |
6.49e-28 |
|
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: 106.46 E-value: 6.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 21 WFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGdysfrSQRIRMIFQdpSTS 100
Cdd:cd03235 6 TVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVPQ--RRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 101 LNPRQRISqILDF-------PLRLNTNLEPEQRRKqIIETMRMVGLLpdHVSYYP-HMLAPGQKQRLGLARALILRPKVI 172
Cdd:cd03235 79 IDRDFPIS-VRDVvlmglygHKGLFRRLSKADKAK-VDEALERVGLS--ELADRQiGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446495558 173 IADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHIGMMKHISDQVLVM 224
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-238 |
8.29e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 111.27 E-value: 8.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 1 MIETLLEVRNLSKTFryrtGwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF 80
Cdd:COG3845 1 MMPPALELRGITKRF----G-----GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 81 GDYSF-RSQRIRMIFQDPS--TSLNPRQRIsqILDFPLRLNTNLEPEQRRKQIIETMRMVGL--LPD-HVsyypHMLAPG 154
Cdd:COG3845 72 RSPRDaIALGIGMVHQHFMlvPNLTVAENI--VLGLEPTKGGRLDRKAARARIRELSERYGLdvDPDaKV----EDLSVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 155 QKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGS 234
Cdd:COG3845 146 EQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAA-EGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVD 224
|
....
gi 446495558 235 TADV 238
Cdd:COG3845 225 TAET 228
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-240 |
1.15e-27 |
|
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: 111.05 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 3 ETLLEVRNLSKtfRYRTgwFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEL--LIDDHPLHF 80
Cdd:TIGR03269 277 EPIIKVRNVSK--RYIS--VDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvRVGDEWVDM 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 81 GDYSF----RSQR-IRMIFQD----PSTSL--NPRQRISqiLDFPLRLntnlepeQRRKQIIeTMRMVGLLPDH----VS 145
Cdd:TIGR03269 353 TKPGPdgrgRAKRyIGILHQEydlyPHRTVldNLTEAIG--LELPDEL-------ARMKAVI-TLKMVGFDEEKaeeiLD 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 146 YYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMH 225
Cdd:TIGR03269 423 KYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMR 502
|
250
....*....|....*
gi 446495558 226 QGEVVERGSTADVLA 240
Cdd:TIGR03269 503 DGKIVKIGDPEEIVE 517
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-233 |
1.17e-27 |
|
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: 105.91 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 5 LLEVRNLSKTFRyrtgwFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdYS 84
Cdd:cd03266 1 MITADALTKRFR-----DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV---KE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 85 FRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNtNLEP---EQRRKQIIETMRMVGLLPDHVSyyphMLAPGQKQRLGL 161
Cdd:cd03266 73 PAEARRRLGFVSDSTGLYDRLTARENLEYFAGLY-GLKGdelTARLEELADRLGMEELLDRRVG----GFSTGMRQKVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446495558 162 ARALILRPKVIIADEALASLDMsMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERG 233
Cdd:cd03266 148 ARALVHDPPVLLLDEPTTGLDV-MATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
30-241 |
1.25e-27 |
|
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: 110.99 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 30 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDysfRSQRIRMIF---QDPstSLNP--- 103
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWD---REELGRHIGylpQDV--ELFDgti 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 104 RQRISqildfplRLnTNLEPEqrrkQIIETMRMVGL------LPD----HVSYYPHMLAPGQKQRLGLARALILRPKVII 173
Cdd:COG4618 423 AENIA-------RF-GDADPE----KVVAAAKLAGVhemilrLPDgydtRIGEGGARLSGGQRQRIGLARALYGDPRLVV 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446495558 174 ADEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHIGMMKHiSDQVLVMHQGEVVERGSTADVLAS 241
Cdd:COG4618 491 LDEPNSNLDDEGEAALAAAIRALKA-RGATVVVITHRPSLLAA-VDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-235 |
1.28e-27 |
|
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: 105.91 E-value: 1.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHplhfgDYSF 85
Cdd:cd03265 1 IEVENLVKKY---------GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGH-----DVVR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RSQRIR----MIFQDPstSLNPRQRISQILDFPLRLnTNLEPEQRRKQIIETMRMVGLLP---DHVSYYphmlAPGQKQR 158
Cdd:cd03265 67 EPREVRrrigIVFQDL--SVDDELTGWENLYIHARL-YGVPGAERRERIDELLDFVGLLEaadRLVKTY----SGGMRRR 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446495558 159 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGST 235
Cdd:cd03265 140 LEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
10-241 |
2.51e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 106.63 E-value: 2.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 10 NLSKTFRYRTGW-FRrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSFRS- 87
Cdd:PRK13645 11 NVSYTYAKKTPFeFK-----ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 88 QRIR----MIFQDPSTSLNpRQRISQILDF-PLRLNTNlePEQRRKQIIETMRMVGLLPDHVSYYPHMLAPGQKQRLGLA 162
Cdd:PRK13645 86 KRLRkeigLVFQFPEYQLF-QETIEKDIAFgPVNLGEN--KQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446495558 163 RALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVLAS 241
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-242 |
2.68e-27 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 105.56 E-value: 2.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 5 LLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhpLHFGDYS 84
Cdd:PRK09493 1 MIEFKNVSKHF---------GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 85 FRSQRIR----MIFQdpSTSLNPRQRISQILDF-PLRLNtNLEPEQRRKQIIETMRMVGLlPDHVSYYPHMLAPGQKQRL 159
Cdd:PRK09493 70 VDERLIRqeagMVFQ--QFYLFPHLTALENVMFgPLRVR-GASKEEAEKQARELLAKVGL-AERAHHYPSELSGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 160 GLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVL 239
Cdd:PRK09493 146 AIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAE-EGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLI 224
|
...
gi 446495558 240 ASP 242
Cdd:PRK09493 225 KNP 227
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
9-242 |
3.39e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 106.26 E-value: 3.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 9 RNLSKTFRYRTGWFRRqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSFRSQ 88
Cdd:PRK13634 6 QKVEHRYQYKTPFERR----ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 89 RIR----MIFQDPSTSLNPRQRISQILDFPLrlNTNLEPEQRRKQIIETMRMVGLLPDHVSYYPHMLAPGQKQRLGLARA 164
Cdd:PRK13634 82 PLRkkvgIVFQFPEHQLFEETVEKDICFGPM--NFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446495558 165 LILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVLASP 242
Cdd:PRK13634 160 LAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
7-240 |
4.98e-27 |
|
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: 104.54 E-value: 4.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 7 EVRNLSktFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSFR 86
Cdd:cd03249 2 EFKNVS--FRYPS----RPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 87 SQRIRMIFQDPstslnprqrisQILDFPLRLNTNL-EPEQRRKQIIETMRMVGL------LPD----HVSYYPHMLAPGQ 155
Cdd:cd03249 76 RSQIGLVSQEP-----------VLFDGTIAENIRYgKPDATDEEVEEAAKKANIhdfimsLPDgydtLVGERGSQLSGGQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 156 KQRLGLARALILRPKVIIADEALASLDmSMRSQLINLMLElQEKQGISYIYVTQHIGMMKHiSDQVLVMHQGEVVERGST 235
Cdd:cd03249 145 KQRIAIARALLRNPKILLLDEATSALD-AESEKLVQEALD-RAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTH 221
|
....*
gi 446495558 236 ADVLA 240
Cdd:cd03249 222 DELMA 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-229 |
7.32e-27 |
|
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: 102.29 E-value: 7.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSktFRYRTGwfrRQTVeaVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdysf 85
Cdd:cd03246 1 LEVENVS--FRYPGA---EPPV--LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIS------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 rsqrirmifqdpstslnprqrisqildfplrlntNLEPEQRRKQIIETMRMVGLLPDHVSyyPHMLAPGQKQRLGLARAL 165
Cdd:cd03246 68 ----------------------------------QWDPNELGDHVGYLPQDDELFSGSIA--ENILSGGQRQRLGLARAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446495558 166 ILRPKVIIADEALASLDmSMRSQLINLMLELQEKQGISYIYVTQHIGMMKhISDQVLVMHQGEV 229
Cdd:cd03246 112 YGNPRILVLDEPNSHLD-VEGERALNQAIAALKAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
6-233 |
1.14e-26 |
|
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: 103.57 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFRYRT----------GWFRR--QTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLI 73
Cdd:cd03267 1 IEVSNLSKSYRVYSkepgligslkSLFKRkyREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 74 DDhplhFGDYSFRSQRIRMIfqdpstSLNPRQRISQILDFP----LRLNT---NLEPEQRRKQIIETMRMVGLlpDHVSY 146
Cdd:cd03267 81 AG----LVPWKRRKKFLRRI------GVVFGQKTQLWWDLPvidsFYLLAaiyDLPPARFKKRLDELSELLDL--EELLD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 147 YP-HMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMH 225
Cdd:cd03267 149 TPvRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVID 228
|
....*...
gi 446495558 226 QGEVVERG 233
Cdd:cd03267 229 KGRLLYDG 236
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
14-241 |
1.44e-26 |
|
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: 103.33 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 14 TFRYRTgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSFRSQRIRMI 93
Cdd:cd03252 7 RFRYKP-----DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 94 FQDpstslnprqriSQILDFPLRLNTNL-EPEQRRKQIIETMRMVGL------LPDHvsyYPHM-------LAPGQKQRL 159
Cdd:cd03252 82 LQE-----------NVLFNRSIRDNIALaDPGMSMERVIEAAKLAGAhdfiseLPEG---YDTIvgeqgagLSGGQRQRI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 160 GLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEkqGISYIYVTQHIGMMKHiSDQVLVMHQGEVVERGSTADVL 239
Cdd:cd03252 148 AIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELL 224
|
..
gi 446495558 240 AS 241
Cdd:cd03252 225 AE 226
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-241 |
1.45e-26 |
|
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: 103.63 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 3 ETLLEVRNLSktfryrtgwFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSG-ELLIDDHPlhFG 81
Cdd:COG1119 1 DPLLELRNVT---------VRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGER--RG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 82 DYSFRSQRIRMIFQDPSTSLNPRQRISqILD------FP-LRLNTNLEPEQRRK--QIIETMRMVGLLpDHvsyYPHMLA 152
Cdd:COG1119 70 GEDVWELRKRIGLVSPALQLRFPRDET-VLDvvlsgfFDsIGLYREPTDEQRERarELLELLGLAHLA-DR---PFGTLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 153 PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIG-MMKHISdQVLVMHQGEVVE 231
Cdd:COG1119 145 QGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeIPPGIT-HVLLLKDGRVVA 223
|
250
....*....|
gi 446495558 232 RGSTADVLAS 241
Cdd:COG1119 224 AGPKEEVLTS 233
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
5-221 |
2.28e-26 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 102.97 E-value: 2.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 5 LLEVRNLSKtfRYRTGwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH----F 80
Cdd:PRK11629 5 LLQCDNLCK--RYQEG---SVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSklssA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 81 GDYSFRSQRIRMIFQdpSTSLNPRQRISQILDFPLrLNTNLEPEQRRKQIIETMRMVGLlpDHVSYY-PHMLAPGQKQRL 159
Cdd:PRK11629 80 AKAELRNQKLGFIYQ--FHHLLPDFTALENVAMPL-LIGKKKPAEINSRALEMLAAVGL--EHRANHrPSELSGGERQRV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446495558 160 GLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQV 221
Cdd:PRK11629 155 AIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-233 |
2.28e-26 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 107.89 E-value: 2.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 2 IETLLEVRNLSktFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFG 81
Cdd:TIGR00958 475 LEGLIEFQDVS--FSYPN----RPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQY 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 82 DYSFRSQRIRMIFQDPST-SLNPRQRISQILDF-PLRLNTNLEPEQRRKQIIetMRMVGLLPDHVSYYPHMLAPGQKQRL 159
Cdd:TIGR00958 549 DHHYLHRQVALVGQEPVLfSGSVRENIAYGLTDtPDEEIMAAAKAANAHDFI--MEFPNGYDTEVGEKGSQLSGGQKQRI 626
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446495558 160 GLARALILRPKVIIADEALASLDmsmrSQLINLMLELQEKQGISYIYVTQHIGMMKHiSDQVLVMHQGEVVERG 233
Cdd:TIGR00958 627 AIARALVRKPRVLILDEATSALD----AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMG 695
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-240 |
2.57e-26 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 102.51 E-value: 2.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKtfRYRTgwfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdySF 85
Cdd:cd03224 1 LEVENLNA--GYGK-------SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT----GL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RSQRI-----------RMIFQD------------PSTSLNPRQRISQILD-FPlRLntnlepEQRRKQiietmrMVGLlp 141
Cdd:cd03224 68 PPHERaragigyvpegRRIFPEltveenlllgayARRRAKRKARLERVYElFP-RL------KERRKQ------LAGT-- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 142 dhvsyyphmLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHIGMMKHISDQV 221
Cdd:cd03224 133 ---------LSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRD-EGVTILLVEQNARFALEIADRA 202
|
250
....*....|....*....
gi 446495558 222 LVMHQGEVVERGSTADVLA 240
Cdd:cd03224 203 YVLERGRVVLEGTAAELLA 221
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-234 |
4.34e-26 |
|
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: 101.80 E-value: 4.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSktFRYRTGwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYS 84
Cdd:cd03244 3 IEFKNVS--LRYRPN-----LPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDIsKIGLHD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 85 FRSqRIRMIFQDPstslnprqrisQILDFPLRLntNLEPEQRR--KQIIETMRMVGLLpDHVSYYPHML----------- 151
Cdd:cd03244 76 LRS-RISIIPQDP-----------VLFSGTIRS--NLDPFGEYsdEELWQALERVGLK-EFVESLPGGLdtvveeggenl 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 152 APGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLmleLQEK-QGISYIYVTQHIGMMKHiSDQVLVMHQGEVV 230
Cdd:cd03244 141 SVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKT---IREAfKDCTVLTIAHRLDTIID-SDRILVLDKGRVV 216
|
....
gi 446495558 231 ERGS 234
Cdd:cd03244 217 EFDS 220
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-250 |
5.21e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 102.96 E-value: 5.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 1 MIETLLEVRNLSKTFRyrtgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGE---LLIDDHP 77
Cdd:PRK13640 1 MKDNIVEFKHVSFTYP-------DSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGIT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 78 LHFGDYSFRSQRIRMIFQDPSTslnprQRISQIL--DFPLRLNTNLEPEQRRKQII-ETMRMVGLLpDHVSYYPHMLAPG 154
Cdd:PRK13640 74 LTAKTVWDIREKVGIVFQNPDN-----QFVGATVgdDVAFGLENRAVPRPEMIKIVrDVLADVGML-DYIDSEPANLSGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 155 QKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHiSDQVLVMHQGEVVERGS 234
Cdd:PRK13640 148 QKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGS 226
|
250
....*....|....*.
gi 446495558 235 TADVLASPlhELTKRL 250
Cdd:PRK13640 227 PVEIFSKV--EMLKEI 240
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-240 |
9.45e-26 |
|
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: 105.57 E-value: 9.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 2 IETLLEVRNLskTFRYRTgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfg 81
Cdd:TIGR02203 327 ARGDVEFRNV--TFRYPG-----RDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLA-- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 82 DYSFRSQR--IRMIFQDpstslnprqrisqILDFPLRLNTNL---EPEQ-RRKQIIETMRMVGLLpDHVSYYPH------ 149
Cdd:TIGR02203 398 DYTLASLRrqVALVSQD-------------VVLFNDTIANNIaygRTEQaDRAEIERALAAAYAQ-DFVDKLPLgldtpi 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 150 -----MLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQekQGISYIYVTQHIGMMKHiSDQVLVM 224
Cdd:TIGR02203 464 gengvLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLM--QGRTTLVIAHRLSTIEK-ADRIVVM 540
|
250
....*....|....*.
gi 446495558 225 HQGEVVERGSTADVLA 240
Cdd:TIGR02203 541 DDGRIVERGTHNELLA 556
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-239 |
1.14e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 101.39 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 4 TLLEVRNLSktfrYRTGwfRRQTVEAVkplSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDY 83
Cdd:PRK13548 1 AMLEARNLS----VRLG--GRTLLDDV---SLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLA--DW 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 84 SFR--SQRIRMIFQDPStslnprqrisqiLDFPLR--------LNTNLEPEQRRKQIIET-MRMVGLLPDHVSYYPHmLA 152
Cdd:PRK13548 70 SPAelARRRAVLPQHSS------------LSFPFTveevvamgRAPHGLSRAEDDALVAAaLAQVDLAHLAGRDYPQ-LS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 153 PGQKQRLGLARALI------LRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQ 226
Cdd:PRK13548 137 GGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQ 216
|
250
....*....|...
gi 446495558 227 GEVVERGSTADVL 239
Cdd:PRK13548 217 GRLVADGTPAEVL 229
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-233 |
1.80e-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: 99.97 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSktFRYRTgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSF 85
Cdd:cd03245 3 IEFRNVS--FSYPN-----QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RSQRIRMIFQDPStslnprqrisqiLDF-PLRLNTNL-EPEQRRKQIIETMRMVGL---LPDHVSYYPHM-------LAP 153
Cdd:cd03245 76 LRRNIGYVPQDVT------------LFYgTLRDNITLgAPLADDERILRAAELAGVtdfVNKHPNGLDLQigergrgLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 154 GQKQRLGLARALILRPKVIIADEALASLDMSMRSQLI-NLMLELQEKqgiSYIYVTQHIGMMKhISDQVLVMHQGEVVER 232
Cdd:cd03245 144 GQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKeRLRQLLGDK---TLIIITHRPSLLD-LVDRIIVMDSGRIVAD 219
|
.
gi 446495558 233 G 233
Cdd:cd03245 220 G 220
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-229 |
2.37e-25 |
|
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: 99.85 E-value: 2.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 2 IETLLEVRNLskTFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFG 81
Cdd:cd03248 8 LKGIVKFQNV--TFAYPT----RPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 82 DYSFRSQRIRMIFQDP---STSLnpRQRISQIL-DFPLRLNTNLEPEQRRKQIIETMRMvGLLPDhVSYYPHMLAPGQKQ 157
Cdd:cd03248 82 EHKYLHSKVSLVGQEPvlfARSL--QDNIAYGLqSCSFECVKEAAQKAHAHSFISELAS-GYDTE-VGEKGSQLSGGQKQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446495558 158 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQgiSYIYVTQHIGMMKHiSDQVLVMHQGEV 229
Cdd:cd03248 158 RVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
32-240 |
2.90e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 100.04 E-value: 2.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 32 PLSFTL--REGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLID--DHplhfgDYSFRSQR-IRMIFQDPS--TSLNPR 104
Cdd:PRK10771 15 PMRFDLtvERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNgqDH-----TTTPPSRRpVSMLFQENNlfSHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 105 QRISQILDFPLRLNtnlepEQRRKQIIETMRMVGLLpDHVSYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMS 184
Cdd:PRK10771 90 QNIGLGLNPGLKLN-----AAQREKLHAIARQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446495558 185 MRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVLA 240
Cdd:PRK10771 164 LRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
29-242 |
3.58e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 100.83 E-value: 3.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 29 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhpLHFGDYSfRSQRIR----MIFQDPSTSLNPR 104
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFS-KLQGIRklvgIVFQNPETQFVGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 105 QrISQILDFPLRlNTNLEPEQRRKQIIETMRMVGlLPDHVSYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMS 184
Cdd:PRK13644 94 T-VEEDLAFGPE-NLCLPPIEIRKRVDRALAEIG-LEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446495558 185 MRSQLINLMLELQEKqGISYIYVTQHIGMMkHISDQVLVMHQGEVVERGSTADVLASP 242
Cdd:PRK13644 171 SGIAVLERIKKLHEK-GKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
30-238 |
7.14e-25 |
|
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: 98.69 E-value: 7.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 30 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdysfRSQRIRMI-FQDPSTS--LNPRQR 106
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT------EPGPDRMVvFQNYSLLpwLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 107 ISQILDfplRLNTNLEPEQRRKQIIETMRMVGLlPDHVSYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR 186
Cdd:TIGR01184 75 IALAVD---RVLPDLSKSERRAIVEEHIALVGL-TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446495558 187 SQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADV 238
Cdd:TIGR01184 151 GNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
4-251 |
9.85e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 99.05 E-value: 9.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 4 TLLEVRNLSKTFRyrtgwfrRQTVeaVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfGDY 83
Cdd:PRK11264 2 SAIEVKNLVKKFH-------GQTV--LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITID-TAR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 84 SFRSQR--IR-------MIFQdpSTSLNP-RQRISQILDFPLRLNTnlEP-EQRRKQIIETMRMVGLLPDHVSYyPHMLA 152
Cdd:PRK11264 72 SLSQQKglIRqlrqhvgFVFQ--NFNLFPhRTVLENIIEGPVIVKG--EPkEEATARARELLAKVGLAGKETSY-PRRLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 153 PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLEL-QEKQgiSYIYVTQHIGMMKHISDQVLVMHQGEVVE 231
Cdd:PRK11264 147 GGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLaQEKR--TMVIVTHEMSFARDVADRAIFMDQGRIVE 224
|
250 260
....*....|....*....|
gi 446495558 232 RGSTADVLASPLHELTKRLI 251
Cdd:PRK11264 225 QGPAKALFADPQQPRTRQFL 244
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-240 |
1.01e-24 |
|
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: 98.46 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLskTFRYRTGwfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDY-- 83
Cdd:cd03253 1 IEFENV--TFAYDPG------RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIR--EVtl 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 84 -SFRSQrIRMIFQDpsTSL-------NPR--------------QRISQILDFPLRLntnlePEQRRKQIIETmrmvGLlp 141
Cdd:cd03253 71 dSLRRA-IGVVPQD--TVLfndtigyNIRygrpdatdeevieaAKAAQIHDKIMRF-----PDGYDTIVGER----GL-- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 142 dhvsyyphMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELqeKQGISYIYVTQHIGMMKHiSDQV 221
Cdd:cd03253 137 --------KLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDV--SKGRTTIVIAHRLSTIVN-ADKI 205
|
250
....*....|....*....
gi 446495558 222 LVMHQGEVVERGSTADVLA 240
Cdd:cd03253 206 IVLKDGRIVERGTHEELLA 224
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
6-233 |
2.08e-24 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 97.22 E-value: 2.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFRY-------------RTGWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELL 72
Cdd:cd03220 1 IELENVSKSYPTykggssslkklgiLGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 73 IddhplhfgdysfrsqrirmifqdpstslnpRQRISQILDfplrLNTNLEPEQR-RKQIIETMRMVGLLPD--------- 142
Cdd:cd03220 81 V------------------------------RGRVSSLLG----LGGGFNPELTgRENIYLNGRLLGLSRKeidekidei 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 143 ------------HVSYYphmlAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISyIYVTQH 210
Cdd:cd03220 127 iefselgdfidlPVKTY----SSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTV-ILVSHD 201
|
250 260
....*....|....*....|...
gi 446495558 211 IGMMKHISDQVLVMHQGEVVERG 233
Cdd:cd03220 202 PSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
28-253 |
2.30e-24 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 98.12 E-value: 2.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 28 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-----------FGDYSFRSQRIR--MIF 94
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvADKNQLRLLRTRltMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 95 QDPSTsLNPRQRISQILDFPLRLnTNLEPEQRRKQIIETMRMVGLLPDHVSYYPHMLAPGQKQRLGLARALILRPKVIIA 174
Cdd:PRK10619 99 QHFNL-WSHMTVLENVMEAPIQV-LGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLF 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446495558 175 DEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLIAG 253
Cdd:PRK10619 177 DEPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLKG 254
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-229 |
4.05e-24 |
|
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: 95.58 E-value: 4.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 3 ETLLEVRNLSktfryrtgwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD 82
Cdd:cd03215 2 EPVLEVRGLS-------------VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 83 YS-FRSQRIRMIFQDpstslnpRQRISQILDFPLRLNTNLepeqrrkqiietmrmvgllpdhvsyyPHMLAPGQKQRLGL 161
Cdd:cd03215 69 PRdAIRAGIAYVPED-------RKREGLVLDLSVAENIAL--------------------------SSLLSGGNQQKVVL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446495558 162 ARALILRPKVIIADEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHIGMMKHISDQVLVMHQGEV 229
Cdd:cd03215 116 ARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAD-AGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-230 |
4.14e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 97.46 E-value: 4.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFRYRTGWFRRqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYS 84
Cdd:COG1101 2 LELKNLSKTFNPGTVNEKR----ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtKLPEYK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 85 fRSQRIRMIFQDPSTSLNPRQRISQIL--------DFPLRLNTNlepEQRRKQIIETMRMVGL-LPDHVSYYPHMLAPGQ 155
Cdd:COG1101 78 -RAKYIGRVFQDPMMGTAPSMTIEENLalayrrgkRRGLRRGLT---KKRRELFRELLATLGLgLENRLDTKVGLLSGGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446495558 156 KQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHigmMKH---ISDQVLVMHQGEVV 230
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHN---MEQaldYGNRLIMMHEGRII 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
33-242 |
4.31e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 97.98 E-value: 4.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 33 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSFRSQRIR----MIFQDPSTSLNPRQRIS 108
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLRkkvsLVFQFPEAQLFENTVLK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 109 QILDFPlrLNTNLEPEQRRKQIIETMRMVGLLPDHVSYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQ 188
Cdd:PRK13641 106 DVEFGP--KNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKE 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446495558 189 LINLMLELQeKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVLASP 242
Cdd:PRK13641 184 MMQLFKDYQ-KAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-233 |
1.80e-23 |
|
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: 93.53 E-value: 1.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSktFRYRtgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSF 85
Cdd:cd03247 1 LSINNVS--FSYP-----EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RSQrIRMIFQDPstslnprqrisQILDFPLRLNtnlepeqrrkqiietmrmVGLlpdhvsyyphMLAPGQKQRLGLARAL 165
Cdd:cd03247 74 SSL-ISVLNQRP-----------YLFDTTLRNN------------------LGR----------RFSGGERQRLALARIL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446495558 166 ILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHIGMMKHIsDQVLVMHQGEVVERG 233
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTL--IWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-224 |
1.81e-23 |
|
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: 98.90 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSktFRYRTGWfrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSF 85
Cdd:TIGR02857 322 LEFSGVS--VAYPGRR------PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RSQRIRMIFQDPstslnprqrisQILDFPLRLNTNL-EPEQRRKQIIETMRMVGL------LPDH----VSYYPHMLAPG 154
Cdd:TIGR02857 394 WRDQIAWVPQHP-----------FLFAGTIAENIRLaRPDASDAEIREALERAGLdefvaaLPQGldtpIGEGGAGLSGG 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 155 QKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELqeKQGISYIYVTQHIGMMkHISDQVLVM 224
Cdd:TIGR02857 463 QAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL--AQGRTVLLVTHRLALA-ALADRIVVL 529
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
26-229 |
2.59e-23 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 94.40 E-value: 2.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 26 TVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHP---LHFGDYSFRSQRIRMIFQDpsTSLN 102
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdLRGRAIPYLRRKIGVVFQD--FRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 103 PRQRISQILDFPLRLnTNLEPEQRRKQIIETMRMVGLLPDHVSyYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD 182
Cdd:cd03292 91 PDRNVYENVAFALEV-TGVPPREIRKRVPAALELVGLSHKHRA-LPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446495558 183 MSMRSQLINLMLELQeKQGISYIYVTQHIGMMKHISDQVLVMHQGEV 229
Cdd:cd03292 169 PDTTWEIMNLLKKIN-KAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
28-240 |
3.85e-23 |
|
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: 98.27 E-value: 3.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 28 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSFRSQRIRMIFQDP---STSlnpr 104
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPyifSGS---- 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 105 qrisqILD-FPLRLNTNLEPEQRRKQI--------IETMRMvGLLPDhVSYYPHMLAPGQKQRLGLARALILRPKVIIAD 175
Cdd:TIGR01193 564 -----ILEnLLLGAKENVSQDEIWAACeiaeikddIENMPL-GYQTE-LSEEGSSISGGQKQRIALARALLTDSKVLILD 636
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446495558 176 EALASLDMSMRSQLINLMLELQEKqgiSYIYVTQHIGMMKHiSDQVLVMHQGEVVERGSTADVLA 240
Cdd:TIGR01193 637 ESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELLD 697
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-242 |
6.56e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 95.30 E-value: 6.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 5 LLEVRNLSKTFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD-----HPLH 79
Cdd:PRK13631 21 ILRVKNLYCVFDEKQ----ENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdKKNN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 80 FGDYSFRSQR-----------IRMIFQDPSTSLNPRQRISQILDFPLRLN-TNLEPEQRRKQIIETMrmvGLLPDHVSYY 147
Cdd:PRK13631 97 HELITNPYSKkiknfkelrrrVSMVFQFPEYQLFKDTIEKDIMFGPVALGvKKSEAKKLAKFYLNKM---GLDDSYLERS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 148 PHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLElQEKQGISYIYVTQHIGMMKHISDQVLVMHQG 227
Cdd:PRK13631 174 PFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKG 252
|
250
....*....|....*
gi 446495558 228 EVVERGSTADVLASP 242
Cdd:PRK13631 253 KILKTGTPYEIFTDQ 267
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
6-234 |
6.89e-23 |
|
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: 92.86 E-value: 6.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSktFRYRTgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYS 84
Cdd:cd03369 7 IEVENLS--VRYAP-----DLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIsTIPLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 85 FRSqRIRMIFQDPStslnprqrisqILDFPLRLNTNLEPEQRRKQIIETMRmvgllpdhVSYYPHMLAPGQKQRLGLARA 164
Cdd:cd03369 80 LRS-SLTIIPQDPT-----------LFSGTIRSNLDPFDEYSDEEIYGALR--------VSEGGLNLSQGQRQLLCLARA 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 165 LILRPKVIIADEALASLDMSMRSQLINLMLElqEKQGISYIYVTQHIGMMKHIsDQVLVMHQGEVVERGS 234
Cdd:cd03369 140 LLKRPRVLVLDEATASIDYATDALIQKTIRE--EFTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDH 206
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
9-256 |
7.18e-23 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 95.87 E-value: 7.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 9 RNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSFRSq 88
Cdd:PRK11000 7 RNVTKAY---------GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 89 rIRMIFQdpSTSLNPRQRISQILDFPLRLN--TNLEPEQRRKQIIETMRMVGLLPDHvsyyPHMLAPGQKQRLGLARALI 166
Cdd:PRK11000 77 -VGMVFQ--SYALYPHLSVAENMSFGLKLAgaKKEEINQRVNQVAEVLQLAHLLDRK----PKALSGGQRQRVAIGRTLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 167 LRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQhigmmkhisDQVLVMHQGE---VVERGSTADVlASPL 243
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTH---------DQVEAMTLADkivVLDAGRVAQV-GKPL 219
|
250
....*....|....*.
gi 446495558 244 ---HELTKRLIAGHFG 256
Cdd:PRK11000 220 elyHYPANRFVAGFIG 235
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
6-241 |
9.05e-23 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 97.10 E-value: 9.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSktFRYRTGWFRRQTVE-AVKPLSFtlregqtLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 84
Cdd:PRK10790 341 IDIDNVS--FAYRDDNLVLQNINlSVPSRGF-------VALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 85 FRSQRIRMIFQDPStslnprqrisqILDFPLRLNTNLE---PEQRRKQIIETMRMVGL---LPD----HVSYYPHMLAPG 154
Cdd:PRK10790 412 VLRQGVAMVQQDPV-----------VLADTFLANVTLGrdiSEEQVWQALETVQLAELarsLPDglytPLGEQGNNLSVG 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 155 QKQRLGLARALILRPKVIIADEALASLDmSMRSQLINLMLELQEKQgiSYIYVTQHigMMKHI--SDQVLVMHQGEVVER 232
Cdd:PRK10790 481 QKQLLALARVLVQTPQILILDEATANID-SGTEQAIQQALAAVREH--TTLVVIAH--RLSTIveADTILVLHRGQAVEQ 555
|
....*....
gi 446495558 233 GSTADVLAS 241
Cdd:PRK10790 556 GTHQQLLAA 564
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-224 |
9.59e-23 |
|
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: 92.88 E-value: 9.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 3 ETLLEVRNLSKTFR-YRTGwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfg 81
Cdd:COG4778 2 TTLLEVENLSKTFTlHLQG---GKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRH------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 82 dysfRSQRIRMIFQDPSTSLNPRQR----ISQILDF------------PLRLN--TNLEPEQRRKQIIETMRmvglLPDH 143
Cdd:COG4778 73 ----DGGWVDLAQASPREILALRRRtigyVSQFLRViprvsaldvvaePLLERgvDREEARARARELLARLN----LPER 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 144 V-SYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHIGMMKHISDQVL 222
Cdd:COG4778 145 LwDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAK-ARGTAIIGIFHDEEVREAVADRVV 223
|
..
gi 446495558 223 VM 224
Cdd:COG4778 224 DV 225
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-241 |
1.11e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 94.41 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYsf 85
Cdd:COG4152 2 LELKGLTKRF---------GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDR-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 rsQRI------RmifqdpstSLNPRQRISQILDFPLRLNtNLEPEQRRKQI---IETMRMVGLLPDHVsyypHMLAPGQK 156
Cdd:COG4152 71 --RRIgylpeeR--------GLYPKMKVGEQLVYLARLK-GLSKAEAKRRAdewLERLGLGDRANKKV----EELSKGNQ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 157 QRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTqHIgmMKH---ISDQVLVMHQGEVVERG 233
Cdd:COG4152 136 QKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSS-HQ--MELveeLCDRIVIINKGRKVLSG 211
|
....*...
gi 446495558 234 STADVLAS 241
Cdd:COG4152 212 SVDEIRRQ 219
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-238 |
1.45e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 96.39 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 1 MIETLLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF 80
Cdd:PRK09700 1 MATPYISMAGIGKSF---------GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 81 GDYSFRSQR-IRMIFQDPS-----TSLNP----RQRISQILDFPLrlntnLEPEQRRKQIIETMRMVGLLPDhVSYYPHM 150
Cdd:PRK09700 72 LDHKLAAQLgIGIIYQELSvidelTVLENlyigRHLTKKVCGVNI-----IDWREMRVRAAMMLLRVGLKVD-LDEKVAN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 151 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHIGMMKHISDQVLVMHQGEVV 230
Cdd:PRK09700 146 LSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLR-KEGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
|
....*...
gi 446495558 231 ERGSTADV 238
Cdd:PRK09700 225 CSGMVSDV 232
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-256 |
1.49e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 93.37 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 28 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIE-----PTSGELLIDDHPLHFGDYS---FRsQRIRMIFQDPST 99
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDpieVR-REVGMVFQYPNP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 100 SlnPRQRISQILDFPLRLNTNLEPEQRRKQIIE-TMRMVGL---LPDHVSYYPHMLAPGQKQRLGLARALILRPKVIIAD 175
Cdd:PRK14267 97 F--PHLTIYDNVAIGVKLNGLVKSKKELDERVEwALKKAALwdeVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 176 EALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLIAGHF 255
Cdd:PRK14267 175 EPTANIDPVGTAKIEELLFELKKEYTI--VLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYVTGAL 252
|
.
gi 446495558 256 G 256
Cdd:PRK14267 253 G 253
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
5-265 |
1.90e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 96.33 E-value: 1.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 5 LLEVRNLSKTfrYRTGwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLI--------DDH 76
Cdd:PRK10535 4 LLELKDIRRS--YPSG---EEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVagqdvatlDAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 77 PL------HFGdysfrsqrirMIFQdpSTSLNPRQRISQILDFPlRLNTNLEPEQRRKQIIETMRMVGLlPDHVSYYPHM 150
Cdd:PRK10535 79 ALaqlrreHFG----------FIFQ--RYHLLSHLTAAQNVEVP-AVYAGLERKQRLLRAQELLQRLGL-EDRVEYQPSQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 151 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEkQGISYIYVTqHIGMMKHISDQVLVMHQGEVV 230
Cdd:PRK10535 145 LSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRD-RGHTVIIVT-HDPQVAAQAERVIEIRDGEIV 222
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 446495558 231 ERG---STADVLASPLHELTK----RLIAGHFGEALTAdAWR 265
Cdd:PRK10535 223 RNPpaqEKVNVAGGTEPVVNTasgwRQFVSGFREALTM-AWR 263
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
14-240 |
1.17e-21 |
|
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: 90.37 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 14 TFRYRtgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSFRSQR--IR 91
Cdd:cd03251 7 TFRYP-----GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVR--DYTLASLRrqIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 92 MIFQDPstslnprqrisqILdfplrLNTNLE-------PEQRRKQIIETMRMVGL------LPDHvsyYPHM-------L 151
Cdd:cd03251 80 LVSQDV------------FL-----FNDTVAeniaygrPGATREEVEEAARAANAhefimeLPEG---YDTVigergvkL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 152 APGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEkqGISYIYVTQHIGMMKHiSDQVLVMHQGEVVE 231
Cdd:cd03251 140 SGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVE 216
|
....*....
gi 446495558 232 RGSTADVLA 240
Cdd:cd03251 217 RGTHEELLA 225
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-256 |
1.33e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 90.61 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 1 MIETLLEVRNLSKTFRYRtgwfrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGM--IEP---TSGELLIDD 75
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKK---------KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 76 HPLhfgdYSFRS------QRIRMIFQDPstslNP-RQRISQILDFPLRLNtNLEPEQRRKQIIETMRMVGLLPDHVSYYP 148
Cdd:PRK14239 72 HNI----YSPRTdtvdlrKEIGMVFQQP----NPfPMSIYENVVYGLRLK-GIKDKQVLDEAVEKSLKGASIWDEVKDRL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 149 H----MLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHIGMMKHISDQVLVM 224
Cdd:PRK14239 143 HdsalGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTM--LLVTRSMQQASRISDRTGFF 220
|
250 260 270
....*....|....*....|....*....|..
gi 446495558 225 HQGEVVERGSTADVLASPLHELTKRLIAGHFG 256
Cdd:PRK14239 221 LDGDLIEYNDTKQMFMNPKHKETEDYISGKFG 252
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-208 |
2.05e-21 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 89.45 E-value: 2.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 3 ETLLEVRNLSKtfryRTGWFRRQtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD 82
Cdd:PRK10584 4 ENIVEVHHLKK----SVGQGEHE-LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 83 ----YSFRSQRIRMIFQdpSTSLNPRQRISQILDFPLRLNTNLEpEQRRKQIIETMRMVGlLPDHVSYYPHMLAPGQKQR 158
Cdd:PRK10584 79 eearAKLRAKHVGFVFQ--SFMLIPTLNALENVELPALLRGESS-RQSRNGAKALLEQLG-LGKRLDHLPAQLSGGEQQR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446495558 159 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVT 208
Cdd:PRK10584 155 VALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVT 204
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
28-230 |
2.79e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 89.16 E-value: 2.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 28 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHP---LHFGDYSFRSQRIRMIFQDPSTSLNpr 104
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrLKNREVPFLRRQIGMIFQDHHLLMD-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 105 QRISQILDFPLRLnTNLEPEQRRKQIIETMRMVGLLpDHVSYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMS 184
Cdd:PRK10908 94 RTVYDNVAIPLII-AGASGDDIRRRVSAALDKVGLL-DKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446495558 185 MRSQLINLMLELQeKQGISYIYVTQHIGMMKHISDQVLVMHQGEVV 230
Cdd:PRK10908 172 LSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
6-238 |
3.76e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 89.80 E-value: 3.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFRYRTGWFRRqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSF 85
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEGR----ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RSQRIR----MIFQDPSTSLNPRQRISQILDFPlrLNTNLEPEQRRKQIIETMRMVGLLPDHVSYYPHMLAPGQKQRLGL 161
Cdd:PRK13649 79 DIKQIRkkvgLVFQFPESQLFEETVLKDVAFGP--QNFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446495558 162 ARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADV 238
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-233 |
3.84e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 89.79 E-value: 3.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 2 IETLLEVRNLskTFRYRTGwfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFG 81
Cdd:PRK13647 1 MDNIIEVEDL--HFRYKDG------TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 82 DYSFRSQRIRMIFQDPSTSLNPRQRISQILDFPLrlNTNLEPEQRRKQIIETMRMVGLLpDHVSYYPHMLAPGQKQRLGL 161
Cdd:PRK13647 73 NEKWVRSKVGLVFQDPDDQVFSSTVWDDVAFGPV--NMGLDKDEVERRVEEALKAVRMW-DFRDKPPYHLSYGQKKRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446495558 162 ARALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERG 233
Cdd:PRK13647 150 AGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLH-NQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
33-243 |
4.70e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 89.30 E-value: 4.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 33 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYSFrSQRIRMIFQDPST--SLNPRQRI-- 107
Cdd:PRK11231 21 LSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIsMLSSRQL-ARRLALLPQHHLTpeGITVRELVay 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 108 --SQILDFPLRLNTnlEPEQRRKQIIETMRMVGLLPDHVSyyphMLAPGQKQRLGLARALILRPKVIIADEALASLDMSM 185
Cdd:PRK11231 100 grSPWLSLWGRLSA--EDNARVNQAMEQTRINHLADRRLT----DLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINH 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446495558 186 RSQLINLMLELQEkQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVLASPL 243
Cdd:PRK11231 174 QVELMRLMRELNT-QGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGL 230
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-243 |
5.56e-21 |
|
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: 88.37 E-value: 5.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH-----PLHf 80
Cdd:cd03218 1 LRAENLSKRYGKRK---------VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklPMH- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 81 gdysfrsQRIRM----IFQDPST--SLNPRQRISQILDFplrlnTNLEPEQRRKQIIETMRMVGL--LPDHVSYYphmLA 152
Cdd:cd03218 71 -------KRARLgigyLPQEASIfrKLTVEENILAVLEI-----RGLSKKEREEKLEELLEEFHIthLRKSKASS---LS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 153 PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISyIYVTQH-----IGmmkhISDQVLVMHQG 227
Cdd:cd03218 136 GGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDR-GIG-VLITDHnvretLS----ITDRAYIIYEG 209
|
250
....*....|....*.
gi 446495558 228 EVVERGSTADVLASPL 243
Cdd:cd03218 210 KVLAEGTPEEIAANEL 225
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-258 |
8.22e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 88.51 E-value: 8.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 1 MIETLLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHf 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRF---------GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 81 GDYSFRSQRIRMI--FQdpstslNPR--QRISQILDF----PLRLNTNL------EPEQRRK------QIIETMRMVGLL 140
Cdd:PRK11300 71 GLPGHQIARMGVVrtFQ------HVRlfREMTVIENLlvaqHQQLKTGLfsgllkTPAFRRAesealdRAATWLERVGLL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 141 pDHVSYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQ 220
Cdd:PRK11300 145 -EHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDR 223
|
250 260 270
....*....|....*....|....*....|....*...
gi 446495558 221 VLVMHQGEVVERGSTADVLASPlheltkRLIAGHFGEA 258
Cdd:PRK11300 224 IYVVNQGTPLANGTPEEIRNNP------DVIKAYLGEA 255
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
15-182 |
1.13e-20 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 91.24 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 15 FRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD-HPLHFGDYSFRSQRIRMI 93
Cdd:PTZ00265 390 FHYDT----RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDsHNLKDINLKWWRSKIGVV 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 94 FQDP-----------------------------------STSLNPRQ--RISQILDFPLRLNTNLEPE--QRRK--QIIE 132
Cdd:PTZ00265 466 SQDPllfsnsiknnikyslyslkdlealsnyynedgndsQENKNKRNscRAKCAGDLNDMSNTTDSNEliEMRKnyQTIK 545
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446495558 133 TMRMVG-----LLPDHVSYYP-----------HMLAPGQKQRLGLARALILRPKVIIADEALASLD 182
Cdd:PTZ00265 546 DSEVVDvskkvLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-210 |
2.12e-20 |
|
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: 90.11 E-value: 2.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSktFRYRTGwfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSF 85
Cdd:TIGR02868 335 LELRDLS--AGYPGA------PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RSQRIRMIFQDPstslnprqrisQILDFPLRLNTNL-EPEQRRKQIIETMRMVGLLpDHVSYYPH-----------MLAP 153
Cdd:TIGR02868 407 VRRRVSVCAQDA-----------HLFDTTVRENLRLaRPDATDEELWAALERVGLA-DWLRALPDgldtvlgeggaRLSG 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446495558 154 GQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMleLQEKQGISYIYVTQH 210
Cdd:TIGR02868 475 GERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-237 |
2.34e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 90.11 E-value: 2.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 5 LLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 84
Cdd:PRK15439 11 LLCARSISKQY---------SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 85 FRSQR-IRMIFQDPstSLNPRQRISQ-ILdfpLRLNTNLEPEQRRKQIIETMrmvgllpdHVSYYPHMLAP----GQKQR 158
Cdd:PRK15439 82 KAHQLgIYLVPQEP--LLFPNLSVKEnIL---FGLPKRQASMQKMKQLLAAL--------GCQLDLDSSAGslevADRQI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446495558 159 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTAD 237
Cdd:PRK15439 149 VEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLA-QGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTAD 226
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
6-240 |
3.22e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 87.83 E-value: 3.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFRYRTGWfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGE---LLIDDHPLHFGD 82
Cdd:PRK13651 3 IKVKNIVKIFNKKLPT----ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTiewIFKDEKNKKKTK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 83 ySFRSQRIRMIFQDPSTSL-----NPRQRISQILDF-----------------PLRLNTN-LEPEQRRKQIIEtmrMVGL 139
Cdd:PRK13651 79 -EKEKVLEKLVIQKTRFKKikkikEIRRRVGVVFQFaeyqlfeqtiekdiifgPVSMGVSkEEAKKRAAKYIE---LVGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 140 LPDHVSYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHIGMMKHISD 219
Cdd:PRK13651 155 DESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDNVLEWTK 233
|
250 260
....*....|....*....|.
gi 446495558 220 QVLVMHQGEVVERGSTADVLA 240
Cdd:PRK13651 234 RTIFFKDGKIIKDGDTYDILS 254
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-242 |
3.29e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 88.60 E-value: 3.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFRyrtgwfRRQTVEAVkplSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELliddhPLHFGDYS- 84
Cdd:PRK10851 3 IEIANIKKSFG------RTQVLNDI---SLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHI-----RFHGTDVSr 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 85 --FRSQRIRMIFQDpsTSLNPRQRISQILDFPLRLntnLEPEQR------RKQIIETMRMVGLlpDHVS-YYPHMLAPGQ 155
Cdd:PRK10851 69 lhARDRKVGFVFQH--YALFRHMTVFDNIAFGLTV---LPRRERpnaaaiKAKVTQLLEMVQL--AHLAdRYPAQLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 156 KQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVT--QHIGMmkHISDQVLVMHQGEVVERG 233
Cdd:PRK10851 142 KQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVThdQEEAM--EVADRVVVMSQGNIEQAG 219
|
....*....
gi 446495558 234 STADVLASP 242
Cdd:PRK10851 220 TPDQVWREP 228
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
44-243 |
6.37e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 87.62 E-value: 6.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 44 AIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdysFRSQ----------RIRMIFQDpstslnprQRIsqildF 113
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVL------FDAEkgiclppekrRIGYVFQD--------ARL-----F 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 114 P-LRLNTNLEPEQRRKQIIETMRMVGLL--PDHVSYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLI 190
Cdd:PRK11144 89 PhYKVRGNLRYGMAKSMVAQFDKIVALLgiEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446495558 191 NLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVLASPL 243
Cdd:PRK11144 169 PYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
6-202 |
6.38e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.93 E-value: 6.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKtfryrtgwfRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSF 85
Cdd:PRK13539 3 LEGEDLAC---------VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RSQRIrmifqDPSTSLNPRQRISQILDFPLRLNTNLEPeqrrkQIIETMRMVGLlpDHVSYYP-HMLAPGQKQRLGLARA 164
Cdd:PRK13539 74 ACHYL-----GHRNAMKPALTVAENLEFWAAFLGGEEL-----DIAAALEAVGL--APLAHLPfGYLSAGQKRRVALARL 141
|
170 180 190
....*....|....*....|....*....|....*...
gi 446495558 165 LILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGI 202
Cdd:PRK13539 142 LVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGI 179
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
29-259 |
7.52e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 86.71 E-value: 7.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 29 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSFRSQRIR----MIFQDPSTSLNPR 104
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRkkvgVVFQFPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 105 QRISQILDFPLrlNTNLEPEQRRKQIIETMRMVGLLPDHVSYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMS 184
Cdd:PRK13643 101 TVLKDVAFGPQ--NFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446495558 185 MRSQLINLmLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVLAS----PLHELTKRLiAGHFGEAL 259
Cdd:PRK13643 179 ARIEMMQL-FESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEvdflKAHELGVPK-ATHFADQL 255
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
31-241 |
1.06e-19 |
|
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: 88.34 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 31 KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfGDYSFRSQR--IRMIFQDpsTSL------- 101
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI--RDVTQASLRaaIGIVPQD--TVLfndtiay 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 102 -----NP-------RQ--RISQILDFPLRLntnlePEQrrkqiIETM---RmvGLlpdhvsyyphMLAPGQKQRLGLARA 164
Cdd:COG5265 451 niaygRPdaseeevEAaaRAAQIHDFIESL-----PDG-----YDTRvgeR--GL----------KLSGGEKQRVAIART 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 165 LILRPKVIIADEALASLDmSMRSQLInlMLELQEkqgisyiyVTQHigmmkHIS-------------DQVLVMHQGEVVE 231
Cdd:COG5265 509 LLKNPPILIFDEATSALD-SRTERAI--QAALRE--------VARG-----RTTlviahrlstivdaDEILVLEAGRIVE 572
|
250
....*....|
gi 446495558 232 RGSTADVLAS 241
Cdd:COG5265 573 RGTHAELLAQ 582
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-242 |
1.28e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.20 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSF 85
Cdd:PRK09536 4 IDVSDLSVEF---------GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RSQRIRMIFQDPSTSLNPRQRisQILDF---PLRLNTNLEPEQRRKQIIETMRMVGLlpDHVSYYP-HMLAPGQKQRLGL 161
Cdd:PRK09536 75 ASRRVASVPQDTSLSFEFDVR--QVVEMgrtPHRSRFDTWTETDRAAVERAMERTGV--AQFADRPvTSLSGGERQRVLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 162 ARALILRPKVIIADEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVLAS 241
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVD-DGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTA 229
|
.
gi 446495558 242 P 242
Cdd:PRK09536 230 D 230
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-242 |
1.37e-19 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 85.59 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 3 ETLLEVRNLSktfryrtgwFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDdhplhfGD 82
Cdd:PRK11831 5 ANLVDMRGVS---------FTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFD------GE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 83 ----------YSFRsQRIRMIFQDPS--TSLNPRQRISqildFPLRLNTNLEPEQRRKQIIETMRMVGlLPDHVSYYPHM 150
Cdd:PRK11831 70 nipamsrsrlYTVR-KRMSMLFQSGAlfTDMNVFDNVA----YPLREHTQLPAPLLHSTVMMKLEAVG-LRGAAKLMPSE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 151 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVV 230
Cdd:PRK11831 144 LSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIV 223
|
250
....*....|..
gi 446495558 231 ERGSTADVLASP 242
Cdd:PRK11831 224 AHGSAQALQANP 235
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-211 |
3.42e-19 |
|
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: 82.79 E-value: 3.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSktfryrtgwFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGdysf 85
Cdd:TIGR01189 1 LAARNLA---------CSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RSQRIR-MIFQDPSTSLNPRQRISQILDFplrLNTNLEPEQRrkQIIETMRMVGLlpDHVSYYP-HMLAPGQKQRLGLAR 163
Cdd:TIGR01189 68 RDEPHEnILYLGHLPGLKPELSALENLHF---WAAIHGGAQR--TIEDALAAVGL--TGFEDLPaAQLSAGQQRRLALAR 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446495558 164 ALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHI 211
Cdd:TIGR01189 141 LWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGI--VLLTTHQ 186
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
30-210 |
3.99e-19 |
|
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: 81.82 E-value: 3.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 30 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELlidDHPLHfGDYSFRSQRIRMifqdPSTSLnprqrisq 109
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMPEG-EDLLFLPQRPYL----PLGTL-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 110 ildfplrlntnlepeqrRKQIIetmrmvgllpdhvsyYP--HMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRS 187
Cdd:cd03223 81 -----------------REQLI---------------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170 180
....*....|....*....|...
gi 446495558 188 QlinlMLELQEKQGISYIYVTQH 210
Cdd:cd03223 129 R----LYQLLKELGITVISVGHR 147
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
6-242 |
5.94e-19 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 84.89 E-value: 5.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTfrYRTGwfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfGDYSF 85
Cdd:PRK11650 4 LKLQAVRKS--YDGK------TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV--NELEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RSQRIRMIFQDpsTSLNPRQRISQILDFPLRlNTNLEPEQRRKQIIETMRMVGLLPdhvsyY----PHMLAPGQKQRLGL 161
Cdd:PRK11650 74 ADRDIAMVFQN--YALYPHMSVRENMAYGLK-IRGMPKAEIEERVAEAARILELEP-----LldrkPRELSGGQRQRVAM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 162 ARALILRPKVIIADEALASLDMSMRSQlinlM-LELQEKQ---GISYIYVT--QHIGMMkhISDQVLVMHQGEVVERGST 235
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLDAKLRVQ----MrLEIQRLHrrlKTTSLYVThdQVEAMT--LADRVVVMNGGVAEQIGTP 219
|
....*..
gi 446495558 236 ADVLASP 242
Cdd:PRK11650 220 VEVYEKP 226
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
30-227 |
6.80e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 85.63 E-value: 6.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 30 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHplhfGDYSFRSQRIRMifqdPSTSLnprqRisQ 109
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAG----ARVLFLPQRPYL----PLGTL----R--E 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 110 ILDFPlrlntNLEPEQRRKQIIETMRMVGLlPDHVSYY------PHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 183
Cdd:COG4178 445 ALLYP-----ATAEAFSDAELREALEAVGL-GHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446495558 184 SMRSQLINLMLElqEKQGISYIYVTQHIGMMKHiSDQVLVMHQG 227
Cdd:COG4178 519 ENEAALYQLLRE--ELPGTTVISVGHRSTLAAF-HDRVLELTGD 559
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-240 |
7.98e-19 |
|
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: 85.62 E-value: 7.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGM--IEPTSGELLID--------- 74
Cdd:TIGR03269 1 IEVKNLTKKF---------DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcgy 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 75 -DHPLHFGDY------SFRSQRIRMIFQDPSTSLNPRQRISQILD--FPL----RLNTNL---------EPEQRRKQIIE 132
Cdd:TIGR03269 72 vERPSKVGEPcpvcggTLEPEEVDFWNLSDKLRRRIRKRIAIMLQrtFALygddTVLDNVlealeeigyEGKEAVGRAVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 133 TMRMVGLlpDH-VSYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDmSMRSQLI-NLMLELQEKQGISYIYVTQH 210
Cdd:TIGR03269 152 LIEMVQL--SHrITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLD-PQTAKLVhNALEEAVKASGISMVLTSHW 228
|
250 260 270
....*....|....*....|....*....|
gi 446495558 211 IGMMKHISDQVLVMHQGEVVERGSTADVLA 240
Cdd:TIGR03269 229 PEVIEDLSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
14-245 |
9.03e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 83.30 E-value: 9.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 14 TFRYRTGWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYSFRSQRIRM 92
Cdd:PRK10575 11 TFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeSWSSKAFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 93 IFQDPSTSLNPRQRISQILDFPLRLNTNLEPEQRRKQIIETMRMVGLLPdHVSYYPHMLAPGQKQRLGLARALILRPKVI 172
Cdd:PRK10575 91 PQQLPAAEGMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSRCL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446495558 173 IADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVLASPLHE 245
Cdd:PRK10575 170 LLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLE 242
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
6-231 |
1.01e-18 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 85.41 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLskTFRYRTGWFrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD-YS 84
Cdd:PRK10522 323 LELRNV--TFAYQDNGF------SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQpED 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 85 FRSQrIRMIFQD---------PSTSLNPRQRISQILDFpLRLNTNLEPEQRRkqiIETMRmvgllpdhvsyyphmLAPGQ 155
Cdd:PRK10522 395 YRKL-FSAVFTDfhlfdqllgPEGKPANPALVEKWLER-LKMAHKLELEDGR---ISNLK---------------LSKGQ 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446495558 156 KQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTqHIGMMKHISDQVLVMHQGEVVE 231
Cdd:PRK10522 455 KKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAIS-HDDHYFIHADRLLEMRNGQLSE 529
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
6-240 |
1.09e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 85.07 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLskTFRYRTgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSF 85
Cdd:PRK11176 342 IEFRNV--TFTYPG-----KEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLR--DYTL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RSQR--IRMIFQdpstslnprqrisQILDFPLRLNTNL----EPEQRRKQIIETMRMVGLLpDHVSYYPH---------- 149
Cdd:PRK11176 413 ASLRnqVALVSQ-------------NVHLFNDTIANNIayarTEQYSREQIEEAARMAYAM-DFINKMDNgldtvigeng 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 150 -MLAPGQKQRLGLARALILRPKVIIADEALASLDM-SMRSqlINLMLELQEKQGISyiYVTQHIGMMKHISDQVLVMHQG 227
Cdd:PRK11176 479 vLLSGGQRQRIAIARALLRDSPILILDEATSALDTeSERA--IQAALDELQKNRTS--LVIAHRLSTIEKADEILVVEDG 554
|
250
....*....|...
gi 446495558 228 EVVERGSTADVLA 240
Cdd:PRK11176 555 EIVERGTHAELLA 567
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
29-232 |
1.46e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 82.44 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 29 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfGDYSFRSqrirMIFQDpsTSLNPRQRIS 108
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE-GPGAERG----VVFQN--EGLLPWRNVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 109 QILDFPLRLnTNLEPEQRRKQIIETMRMVGLLPDHvSYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQ 188
Cdd:PRK11248 89 DNVAFGLQL-AGVEKMQRLEIAHQMLKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446495558 189 LINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMH--QGEVVER 232
Cdd:PRK11248 167 MQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVER 212
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
44-261 |
1.85e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 82.45 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 44 AIIGENGSGKSTLAKMLAGMIEPTSGE------LLIDDHPLHFGDYSFRSQRIRMIFQDPstslNPrqrisqildFPLRL 117
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdvLLGGRSIFNYRDVLEFRRRVGMLFQRP----NP---------FPMSI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 118 NTN---------LEPEQRRKQIIET-MRMVGL---LPDHVSYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMS 184
Cdd:PRK14271 118 MDNvlagvrahkLVPRKEFRGVAQArLTEVGLwdaVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPT 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446495558 185 MRSQLINLMLELQEKqgISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLIAGHFGEALTA 261
Cdd:PRK14271 198 TTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGLSGDVKDA 272
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
30-242 |
5.21e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 83.36 E-value: 5.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 30 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIePTSGELLIDDHPLHFGDYSFRSQRIRMIFQDPSTslnPRQRISQ 109
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQL---PHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 110 ILdfpLRLNTNLEPEQ-----RRKQIIEtmrMVGLLPDHVSYYPH----MLAPGQKQRLGLARALILRPKVIIADEALAS 180
Cdd:PRK11174 442 NV---LLGNPDASDEQlqqalENAWVSE---FLPLLPQGLDTPIGdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTAS 515
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446495558 181 LDmsMRS-QLINLMLElQEKQGISYIYVTQHIGMMKHIsDQVLVMHQGEVVERGSTADVLASP 242
Cdd:PRK11174 516 LD--AHSeQLVMQALN-AASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
6-233 |
5.22e-18 |
|
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: 79.52 E-value: 5.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFRYRTGWFRRQTVeavKPLSFTLREGQTLAIIGENGSGKSTLAKMLAG--MIEPTSGELLIDDHPLHfgDY 83
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGKQLL---KNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLD--KR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 84 SFRSqRIRMIFQDpsTSLNPRQRISQILDFPLRLntnlepeqRRkqiietmrmvgllpdhvsyyphmLAPGQKQRLGLAR 163
Cdd:cd03213 79 SFRK-IIGYVPQD--DILHPTLTVRETLMFAAKL--------RG-----------------------LSGGERKRVSIAL 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446495558 164 ALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVT-QHIGMMKHISDQVLVMHQGEVVERG 233
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLA-DTGRTIICSIhQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-228 |
5.47e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 83.05 E-value: 5.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 1 MIETLLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGmIEPT---SGELLIDDHP 77
Cdd:PRK13549 1 MMEYLLEMKNITKTF---------GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 78 LHFgdYSFR-SQR--IRMIFQDpsTSLNPRQRISQildfplrlNTNLEPEQRRKQIIETMRMV----GLLPD-HVSYYPH 149
Cdd:PRK13549 71 LQA--SNIRdTERagIAIIHQE--LALVKELSVLE--------NIFLGNEITPGGIMDYDAMYlraqKLLAQlKLDINPA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 150 M----LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHIGMMKHISDQVLVMH 225
Cdd:PRK13549 139 TpvgnLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIR 217
|
...
gi 446495558 226 QGE 228
Cdd:PRK13549 218 DGR 220
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-256 |
5.90e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 80.85 E-value: 5.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSktFRYRTgwfrRQTVEAVkplSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEpTSGELLIDDHPLHFGD--Y 83
Cdd:PRK14258 8 IKVNNLS--FYYDT----QKILEGV---SMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRVEFFNQniY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 84 SFR------SQRIRMIFQDPSTslnprqrisqildFPLRLNTNL---------EPEQRRKQIIETMRMVGLLPDHVSYYP 148
Cdd:PRK14258 78 ERRvnlnrlRRQVSMVHPKPNL-------------FPMSVYDNVaygvkivgwRPKLEIDDIVESALKDADLWDEIKHKI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 149 HM----LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVM 224
Cdd:PRK14258 145 HKsaldLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFF 224
|
250 260 270
....*....|....*....|....*....|....*..
gi 446495558 225 HQ-----GEVVERGSTADVLASPLHELTKRLIAGHFG 256
Cdd:PRK14258 225 KGnenriGQLVEFGLTKKIFNSPHDSRTREYVLSRLG 261
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-260 |
9.39e-18 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 82.14 E-value: 9.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 5 LLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGmIEPT---SGELLIDDHPLHFG 81
Cdd:NF040905 1 ILEMRGITKTF---------PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDGEVCRFK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 82 DYSFRSQR-IRMIFQDpsTSLNPRQRISQildfplrlNTNLEPEQRRKQII----------ETMRMVGLLPDHVSYYPHm 150
Cdd:NF040905 71 DIRDSEALgIVIIHQE--LALIPYLSIAE--------NIFLGNERAKRGVIdwnetnrrarELLAKVGLDESPDTLVTD- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 151 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHIGMMKHISDQVLVMHQGEVV 230
Cdd:NF040905 140 IGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKA-QGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
250 260 270
....*....|....*....|....*....|
gi 446495558 231 ErgsTADVLASPLHEltKRLIAGHFGEALT 260
Cdd:NF040905 219 E---TLDCRADEVTE--DRIIRGMVGRDLE 243
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
29-261 |
1.39e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 81.93 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 29 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhpLHFGDYSFRSQR--IRMIFQDP-----STSL 101
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDG--TDIRTVTRASLRrnIAVVFQDAglfnrSIED 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 102 NPR--------------QRISQILDF----PLRLNTNLEpEQRRkqiietmrmvgllpdhvsyyphMLAPGQKQRLGLAR 163
Cdd:PRK13657 428 NIRvgrpdatdeemraaAERAQAHDFierkPDGYDTVVG-ERGR----------------------QLSGGERQRLAIAR 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 164 ALILRPKVIIADEALASLDMSMRSQLiNLMLELQEKQGISYIyVTQHIGMMKHiSDQVLVMHQGEVVERGSTADVLASpl 243
Cdd:PRK13657 485 ALLKDPPILILDEATSALDVETEAKV-KAALDELMKGRTTFI-IAHRLSTVRN-ADRILVFDNGRVVESGSFDELVAR-- 559
|
250
....*....|....*...
gi 446495558 244 heltkrliAGHFGEALTA 261
Cdd:PRK13657 560 --------GGRFAALLRA 569
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
33-211 |
1.48e-17 |
|
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: 78.69 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 33 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSFRSQRIRMIFQDP-STSLNPRQRisqiL 111
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGiKTTLSVLEN----L 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 112 DFPLRLNTnlepeqrRKQIIETMRMVGLLP-DHVSYypHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLI 190
Cdd:cd03231 95 RFWHADHS-------DEQVEEALARVGLNGfEDRPV--AQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFA 165
|
170 180
....*....|....*....|.
gi 446495558 191 NLMLELQEKQGIsyIYVTQHI 211
Cdd:cd03231 166 EAMAGHCARGGM--VVLTTHQ 184
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-233 |
1.64e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 79.34 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSktfryrtgwFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAG--MIEPTSGELLIDDHPLhfGDY 83
Cdd:COG0396 1 LEIKNLH---------VSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLDGEDI--LEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 84 SF--RSQR-IRMIFQDPstslnprQRIS--QILDFpLR--LNTNLEPEQR----RKQIIETMRMVGLLPDHVSYYPHM-L 151
Cdd:COG0396 70 SPdeRARAgIFLAFQYP-------VEIPgvSVSNF-LRtaLNARRGEELSarefLKLLKEKMKELGLDEDFLDRYVNEgF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 152 APGQKQRLGLARALILRPKVIIADEALASLDM-SMR--SQLINLMLElqekQGISYIYVTQHIGMMKHIS-DQVLVMHQG 227
Cdd:COG0396 142 SGGEKKRNEILQMLLLEPKLAILDETDSGLDIdALRivAEGVNKLRS----PDRGILIITHYQRILDYIKpDFVHVLVDG 217
|
....*.
gi 446495558 228 EVVERG 233
Cdd:COG0396 218 RIVKSG 223
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
6-249 |
1.80e-17 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 81.54 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLskTFRYRTGwfRRQTVEAVkplSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSF 85
Cdd:TIGR03797 452 IEVDRV--TFRYRPD--GPLILDDV---SLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQA 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RSQRIRMIFQDpsTSLNPRQRISQIL-DFPLRLntnlepeqrrKQIIETMRMVGLLPD--------H--VSYYPHMLAPG 154
Cdd:TIGR03797 525 VRRQLGVVLQN--GRLMSGSIFENIAgGAPLTL----------DEAWEAARMAGLAEDirampmgmHtvISEGGGTLSGG 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 155 QKQRLGLARALILRPKVIIADEALASLDmsMRSQLInlMLELQEKQGISYIYVTQHIGMMKHiSDQVLVMHQGEVVERGS 234
Cdd:TIGR03797 593 QRQRLLIARALVRKPRILLFDEATSALD--NRTQAI--VSESLERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGT 667
|
250
....*....|....*..
gi 446495558 235 TADVLASP--LHELTKR 249
Cdd:TIGR03797 668 YDELMAREglFAQLARR 684
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-230 |
1.80e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 81.60 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 3 ETLLEVRNLSKTfryrtgwfrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGd 82
Cdd:COG1129 254 EVVLEVEGLSVG-------------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIR- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 83 ysfrsqrirmifqdpstslNPRQRISQ--------------ILDFPLRLNTNL-------------EPEQRR--KQIIET 133
Cdd:COG1129 320 -------------------SPRDAIRAgiayvpedrkgeglVLDLSIRENITLasldrlsrgglldRRRERAlaEEYIKR 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 134 MRMVgllpdhvsyYPHMLAP------GQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEkQGISYIYV 207
Cdd:COG1129 381 LRIK---------TPSPEQPvgnlsgGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAA-EGKAVIVI 450
|
250 260
....*....|....*....|...
gi 446495558 208 TQHIGMMKHISDQVLVMHQGEVV 230
Cdd:COG1129 451 SSELPELLGLSDRILVMREGRIV 473
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
33-231 |
2.27e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 78.60 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 33 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdysfrsqrirmifqdpsTSLNP---RQRISQ 109
Cdd:PRK10247 26 ISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDI--------------------STLKPeiyRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 110 ILDFPL----RLNTNLE-PEQRRKQIIETMRMV-GL----LPDHVSYYP-HMLAPGQKQRLGLARALILRPKVIIADEAL 178
Cdd:PRK10247 86 CAQTPTlfgdTVYDNLIfPWQIRNQQPDPAIFLdDLerfaLPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEIT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446495558 179 ASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHiSDQVLVM--HQGEVVE 231
Cdd:PRK10247 166 SALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITLqpHAGEMQE 219
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
32-239 |
8.37e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.57 E-value: 8.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 32 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIePTSGELLIDDHPLhfGDYSFRSQ-RIRMIF--QDPSTSLNPrqrIS 108
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPL--SDWSAAELaRHRAYLsqQQSPPFAMP---VF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 109 QILDFPLRLNTNLEP-EQRRKQIIETMRMVGLLPDHVsyypHMLAPGQKQRLGLARALI-------LRPKVIIADEALAS 180
Cdd:COG4138 88 QYLALHQPAGASSEAvEQLLAQLAEALGLEDKLSRPL----TQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPMNS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446495558 181 LDMSMRSQLINLMLELQEkQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVL 239
Cdd:COG4138 164 LDVAQQAALDRLLRELCQ-QGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-228 |
1.02e-16 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 74.79 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLiddhplhfgdysf 85
Cdd:cd03221 1 IELENLSKTYGGKL---------LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RSQRIRmifqdpstslnprqrisqildfplrlntnlepeqrrkqiietmrmvgllpdhVSYYPHmLAPGQKQRLGLARAL 165
Cdd:cd03221 59 WGSTVK----------------------------------------------------IGYFEQ-LSGGEKMRLALAKLL 85
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446495558 166 ILRPKVIIADEALASLDMSMRSQLINlmlELQEKQGIsYIYVTQHIGMMKHISDQVLVMHQGE 228
Cdd:cd03221 86 LENPNLLLLDEPTNHLDLESIEALEE---ALKEYPGT-VILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
15-230 |
1.96e-16 |
|
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: 76.16 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 15 FRYRTGWfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEP---TSGELLIDDHPLHFGDYSFRSQRIR 91
Cdd:cd03234 10 GLKAKNW--NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPDQFQKCVAYVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 92 mifQDPST--SLNPRQRISQILDFPLRlntNLEPEQRRKQIIETMRMVGLLPDHV-SYYPHMLAPGQKQRLGLARALILR 168
Cdd:cd03234 88 ---QDDILlpGLTVRETLTYTAILRLP---RKSSDAIRKKRVEDVLLRDLALTRIgGNLVKGISGGERRRVSIAVQLLWD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446495558 169 PKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVV 230
Cdd:cd03234 162 PKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIV 223
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-240 |
3.76e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 77.56 E-value: 3.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 5 LLEVRNLSktFRYRtgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYS 84
Cdd:PRK11160 338 SLTLNNVS--FTYP-----DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIA--DYS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 85 FRSQRIRMIFQDpstslnprQRIsQILDFPLRLNTNL-EPEQRRKQIIETMRMVGlLPDHVSYYPHM----------LAP 153
Cdd:PRK11160 409 EAALRQAISVVS--------QRV-HLFSATLRDNLLLaAPNASDEALIEVLQQVG-LEKLLEDDKGLnawlgeggrqLSG 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 154 GQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQekQGISYIYVTQHIGMMKHIsDQVLVMHQGEVVERG 233
Cdd:PRK11160 479 GEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA--QNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQG 555
|
....*..
gi 446495558 234 STADVLA 240
Cdd:PRK11160 556 THQELLA 562
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-234 |
3.91e-16 |
|
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: 74.49 E-value: 3.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLsktfryrtgWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGM--IEPTSGELLIDDHPLHFGDY 83
Cdd:cd03217 1 LEIKDL---------HVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 84 SFRSQR-IRMIFQDPStslnprqRIS--QILDFpLR-LNtnlepeqrrkqiietmrmVGllpdhvsyyphmLAPGQKQRL 159
Cdd:cd03217 72 EERARLgIFLAFQYPP-------EIPgvKNADF-LRyVN------------------EG------------FSGGEKKRN 113
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446495558 160 GLARALILRPKVIIADEALASLD---MSMRSQLINLMLElqekQGISYIYVTQHIGMMKHI-SDQVLVMHQGEVVERGS 234
Cdd:cd03217 114 EILQLLLLEPDLAILDEPDSGLDidaLRLVAEVINKLRE----EGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGD 188
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
32-239 |
4.24e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 75.35 E-value: 4.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 32 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIePTSGELLIDDHPLhfGDYSFRSQ-RIRMIF--QDPSTSLNPrqrIS 108
Cdd:PRK03695 14 PLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPL--EAWSAAELaRHRAYLsqQQTPPFAMP---VF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 109 QILDfpLRLNTNLEPEQRRKQIIETMRMVGL---LPDHVsyypHMLAPGQKQRLGLARALI-----LRP--KVIIADEAL 178
Cdd:PRK03695 88 QYLT--LHQPDKTRTEAVASALNEVAEALGLddkLGRSV----NQLSGGEWQRVRLAAVVLqvwpdINPagQLLLLDEPM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446495558 179 ASLDMSMRSQLINLMLELQEkQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVL 239
Cdd:PRK03695 162 NSLDVAQQAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-230 |
5.17e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 77.17 E-value: 5.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 5 LLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGmIEPT---SGELLIDDHPLHFG 81
Cdd:TIGR02633 1 LLEMKGIVKTF---------GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSPLKAS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 82 DYSFRSQR-IRMIFQDpsTSLNPRQRISQ--ILDFPLRLN---TNLEPEQRRKQiiETMRMVGLLPDHVSYYPHMLAPGQ 155
Cdd:TIGR02633 71 NIRDTERAgIVIIHQE--LTLVPELSVAEniFLGNEITLPggrMAYNAMYLRAK--NLLRELQLDADNVTRPVGDYGGGQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446495558 156 KQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHIGMMKHISDQVLVMHQGEVV 230
Cdd:TIGR02633 147 QQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
23-231 |
7.26e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 74.22 E-value: 7.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 23 RRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGdysfrsqrirmifQDPStsln 102
Cdd:COG2401 39 RVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFG-------------REAS---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 103 prqrisqILDfplrlntNLEPEQRRKQIIETMRMVGLlPDHVSYY--PHMLAPGQKQRLGLARALILRPKVIIADEALAS 180
Cdd:COG2401 102 -------LID-------AIGRKGDFKDAVELLNAVGL-SDAVLWLrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446495558 181 LDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVM-HQGEVVE 231
Cdd:COG2401 167 LDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIFvGYGGVPE 218
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
6-96 |
9.03e-16 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 76.38 E-value: 9.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLskTFRYRTGwfRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDY-S 84
Cdd:COG4615 328 LELRGV--TYRYPGE--DGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNReA 403
|
90
....*....|..
gi 446495558 85 FRsQRIRMIFQD 96
Cdd:COG4615 404 YR-QLFSAVFSD 414
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-235 |
1.14e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 74.66 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 2 IETLLEVRNLSKTFRYRtgwfrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIeptSGELLIDDHPLHFG 81
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQH---------QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLI---TGDKSAGSHIELLG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 82 DYSFRSQRIRmifQDPSTSLNPRQRISQILDFPLRLnTNLE--------------------PEQRRKQIIETMRMVGLlp 141
Cdd:PRK09984 69 RTVQREGRLA---RDIRKSRANTGYIFQQFNLVNRL-SVLEnvligalgstpfwrtcfswfTREQKQRALQALTRVGM-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 142 dhvSYYPHM----LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHI 217
Cdd:PRK09984 143 ---VHFAHQrvstLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRY 219
|
250
....*....|....*...
gi 446495558 218 SDQVLVMHQGEVVERGST 235
Cdd:PRK09984 220 CERIVALRQGHVFYDGSS 237
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
36-223 |
1.49e-15 |
|
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: 73.98 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 36 TLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDdhplhFGDYSFRSQRIRmifqdPSTSLNPRQRISQILDfpl 115
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE-----LDTVSYKPQYIK-----ADYEGTVRDLLSSITK--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 116 rlnTNLEPEQRRKQIIETMRMVGLLPDHVSyyphMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR---SQLINL 192
Cdd:cd03237 88 ---DFYTHPYFKTEIAKPLQIEQILDREVP----ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRlmaSKVIRR 160
|
170 180 190
....*....|....*....|....*....|..
gi 446495558 193 MLELQEKQgisyIYVTQH-IGMMKHISDQVLV 223
Cdd:cd03237 161 FAENNEKT----AFVVEHdIIMIDYLADRLIV 188
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-256 |
2.81e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 73.66 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 3 ETLLEVRNLSKTFryrtGWFRrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAK---MLAGMIEP--TSGELLIDDHP 77
Cdd:PRK14243 8 ETVLRTENLNVYY----GSFL-----AVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnRLNDLIPGfrVEGKVTFHGKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 78 LHFGDY---SFRSqRIRMIFQDPstslNP-RQRISQILDFPLRLN---TNLEP--EQRRKQ------IIETMRMVGLlpd 142
Cdd:PRK14243 79 LYAPDVdpvEVRR-RIGMVFQKP----NPfPKSIYDNIAYGARINgykGDMDElvERSLRQaalwdeVKDKLKQSGL--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 143 hvsyyphMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHIGMMKHISDQVL 222
Cdd:PRK14243 151 -------SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTI--IIVTHNMQQAARVSDMTA 221
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 446495558 223 VMH---------QGEVVERGSTADVLASPLHELTKRLIAGHFG 256
Cdd:PRK14243 222 FFNveltegggrYGYLVEFDRTEKIFNSPQQQATRDYVSGRFG 264
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-229 |
5.40e-15 |
|
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: 74.09 E-value: 5.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 3 ETLLEVRNLSKtfrYRTGWFRRQTVEAVkplSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPT-SGELLIDDHPLhfg 81
Cdd:TIGR02633 255 DVILEARNLTC---WDVINPHRKRVDDV---SFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPV--- 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 82 DYSFRSQRIR----MIFQD-------PSTSLNPRQRISQILDFPLRLNTNLEPEQrrKQIIETMRMVGLLPDHVSYYPHM 150
Cdd:TIGR02633 326 DIRNPAQAIRagiaMVPEDrkrhgivPILGVGKNITLSVLKSFCFKMRIDAAAEL--QIIGSAIQRLKVKTASPFLPIGR 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446495558 151 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHIGMMKHISDQVLVMHQGEV 229
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLA-QEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-249 |
1.66e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 71.21 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 4 TLLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGmiEP----TSGELLIDDHPLH 79
Cdd:CHL00131 6 PILEIKNLHASV---------NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPaykiLEGDILFKGESIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 80 FGDYSFRSQR-IRMIFQDP------------STSLNPRQRISQIldfplrlnTNLEPEQRRKQIIETMRMVGLLPDHVSY 146
Cdd:CHL00131 75 DLEPEERAHLgIFLAFQYPieipgvsnadflRLAYNSKRKFQGL--------PELDPLEFLEIINEKLKLVGMDPSFLSR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 147 YPHM-LAPGQKQRLGLARALILRPKVIIADEALASLDM-SMR--SQLINlMLELQEKqgiSYIYVTQHIGMMKHIS-DQV 221
Cdd:CHL00131 147 NVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLDIdALKiiAEGIN-KLMTSEN---SIILITHYQRLLDYIKpDYV 222
|
250 260
....*....|....*....|....*...
gi 446495558 222 LVMHQGEVVERGStadvlASPLHELTKR 249
Cdd:CHL00131 223 HVMQNGKIIKTGD-----AELAKELEKK 245
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-231 |
2.13e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.40 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 4 TLLEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHpLHFGDY 83
Cdd:COG0488 314 KVLELEGLSKSYGDKT---------LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET-VKIGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 84 SfrsqrirmifQDPSTsLNPRQRISQildfplrlntNLEPEQRRKQIIETMRMVGLL---PDHVSYYPHMLAPGQKQRLG 160
Cdd:COG0488 384 D----------QHQEE-LDPDKTVLD----------ELRDGAPGGTEQEVRGYLGRFlfsGDDAFKPVGVLSGGEKARLA 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446495558 161 LARALILRPKVIIADEALASLDMSMRSQLINLmleLQEKQGiSYIYVTQHIGMMKHISDQVLVMHQGEVVE 231
Cdd:COG0488 443 LAKLLLSPPNVLLLDEPTNHLDIETLEALEEA---LDDFPG-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
13-242 |
2.15e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 72.44 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 13 KTFRYRTgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH-FGDYSFRSqRIR 91
Cdd:PRK10789 319 RQFTYPQ-----TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTkLQLDSWRS-RLA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 92 MIFQDPstslnprqrisqiLDFPLRLNTNL---EPEQRRKQIIETMRMVGL------LPD----HVSYYPHMLAPGQKQR 158
Cdd:PRK10789 393 VVSQTP-------------FLFSDTVANNIalgRPDATQQEIEHVARLASVhddilrLPQgydtEVGERGVMLSGGQKQR 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 159 LGLARALILRPKVIIADEALASLDMSMRSQLI-NLMlelQEKQGISYIYVTQHIGMMKHiSDQVLVMHQGEVVERGSTAD 237
Cdd:PRK10789 460 ISIARALLLNAEILILDDALSAVDGRTEHQILhNLR---QWGEGRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQ 535
|
....*
gi 446495558 238 VLASP 242
Cdd:PRK10789 536 LAQQS 540
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-231 |
2.31e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 72.25 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDY-- 83
Cdd:PRK11288 5 LSFDGIGKTF---------PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTta 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 84 SFRSQrIRMIFQD------------------PSTS--LNPRQRISQILDFPLRLNTNLEPEQRRKQiietmrmvgllpdh 143
Cdd:PRK11288 76 ALAAG-VAIIYQElhlvpemtvaenlylgqlPHKGgiVNRRLLNYEAREQLEHLGVDIDPDTPLKY-------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 144 vsyyphmLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHIGMMKHISDQVLV 223
Cdd:PRK11288 141 -------LSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELR-AEGRVILYVSHRMEEIFALCDAITV 212
|
....*...
gi 446495558 224 MHQGEVVE 231
Cdd:PRK11288 213 FKDGRYVA 220
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
26-229 |
2.60e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.39 E-value: 2.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 26 TVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHplhfgDYSFRSQRIRM------IFQDpst 99
Cdd:PRK15439 275 TGEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGK-----EINALSTAQRLarglvyLPED--- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 100 slnpRQRISQILDFPLRLNTN----------LEPEQRRKQIIETMRMVGLLPDHVSYYPHMLAPGQKQRLGLARALILRP 169
Cdd:PRK15439 347 ----RQSSGLYLDAPLAWNVCalthnrrgfwIKPARENAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASP 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 170 KVIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHIGMMKHISDQVLVMHQGEV 229
Cdd:PRK15439 423 QLLIVDEPTRGVDVSARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
6-241 |
4.24e-14 |
|
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: 71.90 E-value: 4.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSktFRYRTGwfrrqtVEAV-KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD-HPLHFGDY 83
Cdd:TIGR00957 1285 VEFRNYC--LRYRED------LDLVlRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlNIAKIGLH 1356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 84 SFRSQrIRMIFQDPstslnprqrisqILdFPLRLNTNLEP-EQRRKQIIETMRMVGLLPDHVSYYP-----------HML 151
Cdd:TIGR00957 1357 DLRFK-ITIIPQDP------------VL-FSGSLRMNLDPfSQYSDEEVWWALELAHLKTFVSALPdkldhecaeggENL 1422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 152 APGQKQRLGLARALILRPKVIIADEALASLDMSMrSQLINLMLELQEKQgiSYIYVTQHigMMKHISD--QVLVMHQGEV 229
Cdd:TIGR00957 1423 SVGQRQLVCLARALLRKTKILVLDEATAAVDLET-DNLIQSTIRTQFED--CTVLTIAH--RLNTIMDytRVIVLDKGEV 1497
|
250
....*....|..
gi 446495558 230 VERGSTADVLAS 241
Cdd:TIGR00957 1498 AEFGAPSNLLQQ 1509
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
29-240 |
4.57e-14 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 71.46 E-value: 4.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 29 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgdysfrSQRIRMIfqdpSTSLNprQRIS 108
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-----------SAALIAI----SSGLN--GQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 109 QILDFPLR-LNTNLEPEQRRK---QIIETMRMVGLLPDHVSYYphmlAPGQKQRLGLARALILRPKVIIADEALASLDMS 184
Cdd:PRK13545 102 GIENIELKgLMMGLTKEKIKEiipEIIEFADIGKFIYQPVKTY----SSGMKSRLGFAISVHINPDILVIDEALSVGDQT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446495558 185 MRSQLINLMLELQEkQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVLA 240
Cdd:PRK13545 178 FTKKCLDKMNEFKE-QGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVD 232
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-253 |
4.63e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.92 E-value: 4.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 5 LLEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 84
Cdd:PRK10895 3 TLTAKNLAKAYKGRR---------VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 85 FRSQR-IRMIFQDPstSLNPRQRISQILDFPLRLNTNLEPEQRRKQIIETMRMVgllpdHVSY----YPHMLAPGQKQRL 159
Cdd:PRK10895 74 ARARRgIGYLPQEA--SIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEF-----HIEHlrdsMGQSLSGGERRRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 160 GLARALILRPKVIIADEALASLDmSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVL 239
Cdd:PRK10895 147 EIARALAANPKFILLDEPFAGVD-PISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
250
....*....|....
gi 446495558 240 ASplhELTKRLIAG 253
Cdd:PRK10895 226 QD---EHVKRVYLG 236
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
15-241 |
7.70e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 71.21 E-value: 7.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 15 FRYrtgwFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKML---------------------------------- 60
Cdd:PTZ00265 1173 FRY----ISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtndmtneqdyqgdeeq 1248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 61 -AGM-------------------IEPTSGELLIDDhpLHFGDYSFRSQR--IRMIFQDPstsLNPRQRISQILDFPlRLN 118
Cdd:PTZ00265 1249 nVGMknvnefsltkeggsgedstVFKNSGKILLDG--VDICDYNLKDLRnlFSIVSQEP---MLFNMSIYENIKFG-KED 1322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 119 TNLEPEQRRKQIIETMRMVGLLPD----HVSYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLML 194
Cdd:PTZ00265 1323 ATREDVKRACKFAAIDEFIESLPNkydtNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1402
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446495558 195 ELQEKQGISYIYVTQHIGMMKHiSDQVLVMHQ----GEVVERGSTADVLAS 241
Cdd:PTZ00265 1403 DIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVQAHGTHEELLS 1452
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
8-239 |
8.64e-14 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 69.46 E-value: 8.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 8 VRNLSKTFR-YRTGWFR----------RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEllIDDH 76
Cdd:PRK13546 7 IKNVTKEYRiYRTNKERmkdalipkhkNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK--VDRN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 77 plhfGDYSFRSqrirmifqdPSTSLNPRQRISQILDFPLrLNTNLEPEQRRK---QIIETMRMVGLLPDHVSYYphmlAP 153
Cdd:PRK13546 85 ----GEVSVIA---------ISAGLSGQLTGIENIEFKM-LCMGFKRKEIKAmtpKIIEFSELGEFIYQPVKKY----SS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 154 GQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERG 233
Cdd:PRK13546 147 GMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKE-QNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
|
....*.
gi 446495558 234 STADVL 239
Cdd:PRK13546 226 ELDDVL 231
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
37-240 |
9.27e-14 |
|
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: 69.17 E-value: 9.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 37 LREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLID-----DHPLHfgdySFRSqRIRMIFQDPstslnprqrisqIL 111
Cdd:cd03288 44 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDgidisKLPLH----TLRS-RLSIILQDP------------IL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 112 dFPLRLNTNLEPEQR--------RKQIIETMRMVGLLPDH----VSYYPHMLAPGQKQRLGLARALILRPKVIIADEALA 179
Cdd:cd03288 107 -FSGSIRFNLDPECKctddrlweALEIAQLKNMVKSLPGGldavVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATA 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446495558 180 SLDMSMRSQLIN-LMLELQEKQGISYIYVTQHIgmmkHISDQVLVMHQGEVVERGSTADVLA 240
Cdd:cd03288 186 SIDMATENILQKvVMTAFADRTVVTIAHRVSTI----LDADLVLVLSRGILVECDTPENLLA 243
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-176 |
1.29e-13 |
|
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: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 8 VRNLSKTFryrtgwfrrqtveAVKPL----SFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLID--------- 74
Cdd:COG0488 1 LENLSKSF-------------GGRPLlddvSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkglrigylp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 75 -DHPLhFGDYSFRsQRIRMIFQDPSTSLNPRQRISQILDFPL-------RLNTNLE------PEQRRKQIIETMRMVGLL 140
Cdd:COG0488 68 qEPPL-DDDLTVL-DTVLDGDAELRALEAELEELEAKLAEPDedlerlaELQEEFEalggweAEARAEEILSGLGFPEED 145
|
170 180 190
....*....|....*....|....*....|....*..
gi 446495558 141 PDH-VSyyphMLAPGQKQRLGLARALILRPKVIIADE 176
Cdd:COG0488 146 LDRpVS----ELSGGWRRRVALARALLSEPDLLLLDE 178
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
29-229 |
1.29e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 70.54 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 29 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSFRsQRIRMIFQDPS--TSLNPRQR 106
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATR-RRVGYMSQAFSlyGELTVRQN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 107 isqiLDFPLRLnTNLEPEQRRKQIIETMRMVGLLpDHVSYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR 186
Cdd:NF033858 360 ----LELHARL-FHLPAAEIAARVAEMLERFDLA-DVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVAR 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446495558 187 SQLINLMLELQEKQGISyIYVTQHigMMKHIS--DQVLVMHQGEV 229
Cdd:NF033858 434 DMFWRLLIELSREDGVT-IFISTH--FMNEAErcDRISLMHAGRV 475
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
33-210 |
1.34e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.52 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 33 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSFRSQrirMIFQDPSTSLNPRQRISQILD 112
Cdd:PRK13538 20 LSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQD---LLYLGHQPGIKTELTALENLR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 113 FPLRLNTnlepEQRRKQIIETMRMVGL-----LPDHVsyyphmLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRS 187
Cdd:PRK13538 97 FYQRLHG----PGDDEALWEALAQVGLagfedVPVRQ------LSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVA 166
|
170 180
....*....|....*....|...
gi 446495558 188 QLINLMLELQEKQGIsyIYVTQH 210
Cdd:PRK13538 167 RLEALLAQHAEQGGM--VILTTH 187
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-245 |
3.27e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 67.70 E-value: 3.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 1 MIETLLEVRNLSKTFRYRtgwfrRQTVeaVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLID-DHPLH 79
Cdd:PRK10253 1 MTESVARLRGEQLTLGYG-----KYTV--AENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDgEHIQH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 80 FGDYSFrSQRIRMIFQDPST-------SLNPRQRISQIldfPLRLNTNLEPEQrrkQIIETMRMVGLlPDHVSYYPHMLA 152
Cdd:PRK10253 74 YASKEV-ARRIGLLAQNATTpgditvqELVARGRYPHQ---PLFTRWRKEDEE---AVTKAMQATGI-THLADQSVDTLS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 153 PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVER 232
Cdd:PRK10253 146 GGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQ 225
|
250
....*....|...
gi 446495558 233 GSTADVLASPLHE 245
Cdd:PRK10253 226 GAPKEIVTAELIE 238
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-229 |
3.76e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.88 E-value: 3.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 3 ETLLEVRNLSKtfryrtgwfrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFgd 82
Cdd:PRK10762 255 EVRLKVDNLSG--------------PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVT-- 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 83 ysfRSQR------IRMIFQDpstslnpRQRISQILDFPLRLN---TNLEPEQRRKQIIETMRMVGLLPDHVSYY----PH 149
Cdd:PRK10762 319 ---RSPQdglangIVYISED-------RKRDGLVLGMSVKENmslTALRYFSRAGGSLKHADEQQAVSDFIRLFniktPS 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 150 M------LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRS---QLINlmlelQEKQ-GISYIYVTQH----IGMmk 215
Cdd:PRK10762 389 MeqaiglLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKeiyQLIN-----QFKAeGLSIILVSSEmpevLGM-- 461
|
250
....*....|....
gi 446495558 216 hiSDQVLVMHQGEV 229
Cdd:PRK10762 462 --SDRILVMHEGRI 473
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
21-235 |
7.29e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.15 E-value: 7.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 21 WFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEP---TSGELLIDDHPLhfgDYSFRSQRIRMIFQD- 96
Cdd:TIGR00955 32 CRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI---DAKEMRAISAYVQQDd 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 97 ---PstSLNPRQRisqiLDFP--LRLNTNLEPEQRRKQIIETMRMVGLLP--DHVSYYPHM---LAPGQKQRLGLARALI 166
Cdd:TIGR00955 109 lfiP--TLTVREH----LMFQahLRMPRRVTKKEKRERVDEVLQALGLRKcaNTRIGVPGRvkgLSGGERKRLAFASELL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446495558 167 LRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGST 235
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSP 251
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
4-226 |
8.89e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.29 E-value: 8.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 4 TLLEVRNLSKTFRYRtgwfrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGeLLIDDHPLHFGdy 83
Cdd:PRK09544 3 SLVSLENVSVSFGQR---------RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG-VIKRNGKLRIG-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 84 sFRSQRIRMifqDPSTSLNprqrISQILdfplrlntNLEPEQRRKQIIETMRMVGllPDHVSYYP-HMLAPGQKQRLGLA 162
Cdd:PRK09544 71 -YVPQKLYL---DTTLPLT----VNRFL--------RLRPGTKKEDILPALKRVQ--AGHLIDAPmQKLSGGETQRVLLA 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446495558 163 RALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQ--HIGMMKhiSDQVLVMHQ 226
Cdd:PRK09544 133 RALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHdlHLVMAK--TDEVLCLNH 196
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
33-228 |
1.20e-12 |
|
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: 65.18 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 33 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLiddhplHFGDYSFRSQR--IRmifqdpSTSLnpRQRISqi 110
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVS------VPGSIAYVSQEpwIQ------NGTI--RENIL-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 111 ldFPLRLNtnlepEQRRKQIIETmrmVGLLPDhVSYYPH-----------MLAPGQKQRLGLARALILRPKVIIADEALA 179
Cdd:cd03250 88 --FGKPFD-----EERYEKVIKA---CALEPD-LEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446495558 180 SLDMSMRSQLIN--LMLELQEKQGIsyIYVTQHIGMMKHiSDQVLVMHQGE 228
Cdd:cd03250 157 AVDAHVGRHIFEncILGLLLNNKTR--ILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
29-210 |
2.21e-12 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 64.18 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 29 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHplhfGDYSFRSQRIRMIFQDPSTSlnpRQRIS 108
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG----ARVAYVPQRSEVPDSLPLTV---RDLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 109 QILDFPLRLNTNLEPEQRRKqIIETMRMVGLLpDHVSYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQ 188
Cdd:NF040873 80 MGRWARRGLWRRLTRDDRAA-VDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRER 157
|
170 180
....*....|....*....|..
gi 446495558 189 LINLMLELQEkQGISYIYVTQH 210
Cdd:NF040873 158 IIALLAEEHA-RGATVVVVTHD 178
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-229 |
3.19e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.11 E-value: 3.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 3 ETLLEVRNLsktfryrTGWFRRQT-VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIE-PTSGELLIDDHPLhf 80
Cdd:PRK13549 257 EVILEVRNL-------TAWDPVNPhIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPV-- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 81 gdysfrsqRIRmifqdpstslNPRQRIsqildfplRLNTNLEPEQRRKQIIETMRMVG---LLPDHVSYYPHM------- 150
Cdd:PRK13549 328 --------KIR----------NPQQAI--------AQGIAMVPEDRKRDGIVPVMGVGkniTLAALDRFTGGSriddaae 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 151 ------------------------LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISYIY 206
Cdd:PRK13549 382 lktilesiqrlkvktaspelaiarLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLV-QQGVAIIV 460
|
250 260
....*....|....*....|...
gi 446495558 207 VTQHIGMMKHISDQVLVMHQGEV 229
Cdd:PRK13549 461 ISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
33-210 |
4.27e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.43 E-value: 4.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 33 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSFRSQrirMIFQDPSTSLNPRQRISQILD 112
Cdd:PRK13540 20 ISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQ---LCFVGHRSGINPYLTLRENCL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 113 FPLRL-NTNLEpeqrrkqIIETMRMVGLlpDHVSYYP-HMLAPGQKQRLGLARALILRPKVIIADEALASLDmsmRSQLI 190
Cdd:PRK13540 97 YDIHFsPGAVG-------ITELCRLFSL--EHLIDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD---ELSLL 164
|
170 180
....*....|....*....|..
gi 446495558 191 NLMLELQE--KQGiSYIYVTQH 210
Cdd:PRK13540 165 TIITKIQEhrAKG-GAVLLTSH 185
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
30-233 |
5.50e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 64.85 E-value: 5.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 30 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdysfrsqrirmifqdPSTSLNPRQRISQ 109
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV------------------PARARLARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 110 ILDFplrlnTNLEPE-QRRKQIIETMRMVGL-----------------LPDHVSYYPHMLAPGQKQRLGLARALILRPKV 171
Cdd:PRK13536 119 VPQF-----DNLDLEfTVRENLLVFGRYFGMstreieavipsllefarLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446495558 172 IIADEALASLDMSMRsQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERG 233
Cdd:PRK13536 194 LILDEPTTGLDPHAR-HLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-223 |
9.16e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.83 E-value: 9.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 3 ETLLEVRNLSKTFryrtGWFRrQTVEAVkplsfTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgD 82
Cdd:PRK13409 338 ETLVEYPDLTKKL----GDFS-LEVEGG-----EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPEL------K 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 83 YSFRSQRIRmifqdPSTSLNPRQRISQILDfplRLNTN-LEPEqrrkqIIETMRMVGLLPDHVSyyphMLAPGQKQRLGL 161
Cdd:PRK13409 402 ISYKPQYIK-----PDYDGTVEDLLRSITD---DLGSSyYKSE-----IIKPLQLERLLDKNVK----DLSGGELQRVAI 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446495558 162 ARALILRPKVIIADEALASLDMSMR---SQLINLMLELQEKQgisyIYVTQH-IGMMKHISDQVLV 223
Cdd:PRK13409 465 AACLSRDADLYLLDEPSAHLDVEQRlavAKAIRRIAEEREAT----ALVVDHdIYMIDYISDRLMV 526
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
33-240 |
2.22e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.84 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 33 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYSFRsQRIRMIFQDPStslnprqrisqIL 111
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVaKFGLTDLR-RVLSIIPQSPV-----------LF 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 112 DFPLRLNTNLEPEQRRKQIIETMRMVGLlPDHVSYYPHML-----------APGQKQRLGLARALILRPKVIIADEALAS 180
Cdd:PLN03232 1323 SGTVRFNIDPFSEHNDADLWEALERAHI-KDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 181 LDMSMRSqLINLMLElQEKQGISYIYVTQHIGMMKHiSDQVLVMHQGEVVERGSTADVLA 240
Cdd:PLN03232 1402 VDVRTDS-LIQRTIR-EEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLS 1458
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-241 |
2.62e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 62.52 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 1 MIETLLEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhf 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKL---------VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 81 gdysfrsqrirmifqdPSTSLNPRQRISQILDFplrlnTNLEPE-QRRKQIIETMRMVGL-----------------LPD 142
Cdd:PRK13537 72 ----------------PSRARHARQRVGVVPQF-----DNLDPDfTVRENLLVFGRYFGLsaaaaralvppllefakLEN 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 143 HVSYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRsQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVL 222
Cdd:PRK13537 131 KADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQAR-HLMWERLRSLLARGKTILLTTHFMEEAERLCDRLC 209
|
250
....*....|....*....
gi 446495558 223 VMHQGEVVERGSTADVLAS 241
Cdd:PRK13537 210 VIEEGRKIAEGAPHALIES 228
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
9-230 |
2.95e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 61.12 E-value: 2.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 9 RNLSKTFRYRtgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPT---SGELLIDDHPLHFGDYSF 85
Cdd:cd03233 7 RNISFTTGKG-----RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RSQrirMIFQDPSTSLNPRQRISQILDFPLRLNTNlepeqrrkqiiETMRMVgllpdhvsyyphmlAPGQKQRLGLARAL 165
Cdd:cd03233 82 PGE---IIYVSEEDVHFPTLTVRETLDFALRCKGN-----------EFVRGI--------------SGGERKRVSIAEAL 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446495558 166 ILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGIS-YIYVTQHIGMMKHISDQVLVMHQGEVV 230
Cdd:cd03233 134 VSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTtFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
29-235 |
2.99e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 62.21 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 29 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdysfRSQRIRMIFQDPStslnprqriS 108
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR------QALQKNLVAYVPQ---------S 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 109 QILD--FPLRLNTNL------------EPEQRRKQII-ETMRMVGLLpDHVSYYPHMLAPGQKQRLGLARALILRPKVII 173
Cdd:PRK15056 87 EEVDwsFPVLVEDVVmmgryghmgwlrRAKKRDRQIVtAALARVDMV-EFRHRQIGELSGGQKKRVFLARAIAQQGQVIL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446495558 174 ADEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHIGMMKHISDQVlVMHQGEVVERGST 235
Cdd:PRK15056 166 LDEPFTGVDVKTEARIISLLRELRD-EGKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASGPT 225
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
22-194 |
3.64e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 61.02 E-value: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 22 FRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDysfRSQRIRMIFQDPSTsl 101
Cdd:PRK13543 19 FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD---RSRFMAYLGHLPGL-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 102 npRQRISQILDfpLRLNTNLEPEQRRKQIIETMRMVGlLPDHVSYYPHMLAPGQKQRLGLARALILRPKVIIADEALASL 181
Cdd:PRK13543 94 --KADLSTLEN--LHFLCGLHGRRAKQMPGSALAIVG-LAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANL 168
|
170
....*....|...
gi 446495558 182 DMSMRSqLINLML 194
Cdd:PRK13543 169 DLEGIT-LVNRMI 180
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
34-243 |
7.99e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.95 E-value: 7.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 34 SFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLID-DHPLHFgdySFR--SQRIRMIFQDPSTS-LNP------ 103
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQfSHITRL---SFEqlQKLVSDEWQRNNTDmLSPgeddtg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 104 RQRISQILDfplrlntNLEPEQRRKQIIETMRMVGLLPDHVSYyphmLAPGQKQRLGLARALILRPKVIIADEALASLDM 183
Cdd:PRK10938 100 RTTAEIIQD-------EVKDPARCEQLAQQFGITALLDRRFKY----LSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 184 SMRSQLINLMLELQeKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVLASPL 243
Cdd:PRK10938 169 ASRQQLAELLASLH-QSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQAL 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-238 |
8.41e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 61.58 E-value: 8.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 3 ETLLEVRNLSktfryrtgWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFG 81
Cdd:COG3845 255 EVVLEVENLS--------VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDItGLS 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 82 DYSFRSQRIRMIFQDpstslnpRQRISQILDFPLRLNTNL-----EPEQRR------------KQIIETMRMVGLLPD-H 143
Cdd:COG3845 327 PRERRRLGVAYIPED-------RLGRGLVPDMSVAENLILgryrrPPFSRGgfldrkairafaEELIEEFDVRTPGPDtP 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 144 VSyyphMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQ---HIgmMKhISDQ 220
Cdd:COG3845 400 AR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEdldEI--LA-LSDR 471
|
250
....*....|....*...
gi 446495558 221 VLVMHQGEVVERGSTADV 238
Cdd:COG3845 472 IAVMYEGRIVGEVPAAEA 489
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1-223 |
9.85e-11 |
|
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: 61.72 E-value: 9.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 1 MIETLLEVRNLSKTFryrtGWFRrQTVEAVkplsfTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhf 80
Cdd:COG1245 337 EEETLVEYPDLTKSY----GGFS-LEVEGG-----EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDL----- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 81 gDYSFRSQRIRmIFQDPSTSLNPRQRISQILDfplrlNTNLEPEqrrkqIIETMRMVGLLPDHVSyyphMLAPGQKQRLG 160
Cdd:COG1245 402 -KISYKPQYIS-PDYDGTVEEFLRSANTDDFG-----SSYYKTE-----IIKPLGLEKLLDKNVK----DLSGGELQRVA 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446495558 161 LARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLV 223
Cdd:COG1245 466 IAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
30-216 |
1.70e-10 |
|
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: 60.92 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 30 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGmIEPTSGELLIDDHPL---------HFGDYSFRSQrirMIFQDPSTS 100
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGE-LWPVYGGRLTKPAKGklfyvpqrpYMTLGTLRDQ---IIYPDSSED 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 101 LNPR----QRISQILDfplrlNTNLEpeqrrkQIIEtmRMVGLlpDHVSYYPHMLAPGQKQRLGLARALILRPKVIIADE 176
Cdd:TIGR00954 544 MKRRglsdKDLEQILD-----NVQLT------HILE--REGGW--SAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDE 608
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446495558 177 ALA--SLDMSMRsqlinlMLELQEKQGISYIYVTQHIGMMKH 216
Cdd:TIGR00954 609 CTSavSVDVEGY------MYRLCREFGITLFSVSHRKSLWKY 644
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
29-234 |
8.90e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 59.26 E-value: 8.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 29 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSFRsQRIRMIFQdpSTSLNPRQRIS 108
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVR-QSLGMCPQ--HNILFHHLTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 109 QILDFPLRLNTNLEPEQRrkqiietMRMVGLLPDHVSYYPHM-----LAPGQKQRLGLARALILRPKVIIADEALASLDM 183
Cdd:TIGR01257 1022 EHILFYAQLKGRSWEEAQ-------LEMEAMLEDTGLHHKRNeeaqdLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP 1094
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446495558 184 SMRSQLINLMLELqeKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGS 234
Cdd:TIGR01257 1095 YSRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
33-240 |
1.40e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.60 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 33 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYSFRsQRIRMIFQDPstslnprqrisqIL 111
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIsKFGLMDLR-KVLGIIPQAP------------VL 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 112 dFPLRLNTNLEP--EQRRKQIIETMRMVGL----------LPDHVSYYPHMLAPGQKQRLGLARALILRPKVIIADEALA 179
Cdd:PLN03130 1325 -FSGTVRFNLDPfnEHNDADLWESLERAHLkdvirrnslgLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446495558 180 SLDMSMRSqLINLMLElQEKQGISYIYVTQHIGMMKHiSDQVLVMHQGEVVERGSTADVLA 240
Cdd:PLN03130 1404 AVDVRTDA-LIQKTIR-EEFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLS 1461
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
32-230 |
2.12e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 57.61 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 32 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdySFRSQR--IRM-------------IFQD 96
Cdd:PRK11288 271 PISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI-----DIRSPRdaIRAgimlcpedrkaegIIPV 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 97 PSTSLNprQRIS---QILDFPLRLNTNLEPEQRRKQI----IETmrmvgllPDHVSyyPHM-LAPGQKQRLGLARALILR 168
Cdd:PRK11288 346 HSVADN--INISarrHHLRAGCLINNRWEAENADRFIrslnIKT-------PSREQ--LIMnLSGGNQQKAILGRWLSED 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446495558 169 PKVIIADEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHIGMMKHISDQVLVMHQGEVV 230
Cdd:PRK11288 415 MKVILLDEPTRGIDVGAKHEIYNVIYELAA-QGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-261 |
2.89e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.48 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 16 RYRTGWfrrqtveavkPL-----SFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfGDYSFRSQR- 89
Cdd:PTZ00243 1317 RYREGL----------PLvlrgvSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREI--GAYGLRELRr 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 90 -IRMIFQDPStslnprqrisqILDFPLRLNTNLEPEQRRKQIIETMRMVGlLPDHV---------------SYYphmlAP 153
Cdd:PTZ00243 1385 qFSMIPQDPV-----------LFDGTVRQNVDPFLEASSAEVWAALELVG-LRERVasesegidsrvleggSNY----SV 1448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 154 GQKQRLGLARALILR-PKVIIADEALASLDMSMRSQLINLMLELQEkqgiSYIYVTqhIGMMKHI---SDQVLVMHQGEV 229
Cdd:PTZ00243 1449 GQRQLMCMARALLKKgSGFILMDEATANIDPALDRQIQATVMSAFS----AYTVIT--IAHRLHTvaqYDKIIVMDHGAV 1522
|
250 260 270
....*....|....*....|....*....|....*...
gi 446495558 230 VERGSTADVLASP---LHELTK---RLIAGHFGEALTA 261
Cdd:PTZ00243 1523 AEMGSPRELVMNRqsiFHSMVEalgRSEAKRFLQLVGR 1560
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-70 |
3.52e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.82 E-value: 3.52e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446495558 6 LEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGE 70
Cdd:PRK15064 320 LEVENLTKGFDNGP---------LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT 375
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-229 |
4.26e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.72 E-value: 4.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 20 GWFRRQTVEAVKplsFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEL-LIDDHPLHFgdysFRSQRIRMIFQDPS 98
Cdd:PRK10636 321 GYGDRIILDSIK---LNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGY----FAQHQLEFLRADES 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 99 tslnprqrisqildfPLRLNTNLEPEQRRKQIIETMRMVGLLPDHVSYYPHMLAPGQKQRLGLARALILRPKVIIADEAL 178
Cdd:PRK10636 394 ---------------PLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPT 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446495558 179 ASLDMSMRSQLINLMLELQEkqgiSYIYVTQHIGMMKHISDQVLVMHQGEV 229
Cdd:PRK10636 459 NHLDLDMRQALTEALIDFEG----ALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
30-228 |
4.64e-09 |
|
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: 56.02 E-value: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 30 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELliddhpLHFGDYSFRSQRIRMIfqdPSTslnprqrISQ 109
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI------KHSGRISFSSQFSWIM---PGT-------IKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 110 ILDFPLRLNtnlepEQRRKQIIETMRmvglLPDHVSYYPH-----------MLAPGQKQRLGLARALILRPKVIIADEAL 178
Cdd:cd03291 117 NIIFGVSYD-----EYRYKSVVKACQ----LEEDITKFPEkdntvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPF 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446495558 179 ASLDMSMRSQLI-NLMLELQEKQgiSYIYVTQHIGMMKhISDQVLVMHQGE 228
Cdd:cd03291 188 GYLDVFTEKEIFeSCVCKLMANK--TRILVTSKMEHLK-KADKILILHEGS 235
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-75 |
5.09e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.28 E-value: 5.09e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD 75
Cdd:PRK11819 325 IEAENLSKSFGDRL---------LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE 385
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-75 |
7.51e-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: 55.71 E-value: 7.51e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD 75
Cdd:TIGR03719 323 IEAENLTKAFGDKL---------LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE 383
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-228 |
1.01e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.39 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 3 ETLLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF-G 81
Cdd:PRK10762 2 QALLQLKGIDKAF---------PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFnG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 82 DYSFRSQRIRMIFQDpstsLN--PRQRISQildfplrlNTNL--EPEQR------RKQIIETMRMVGLLpdHVSYYPHM- 150
Cdd:PRK10762 73 PKSSQEAGIGIIHQE----LNliPQLTIAE--------NIFLgrEFVNRfgridwKKMYAEADKLLARL--NLRFSSDKl 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 151 ---LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHIGMMKHISDQVLVMHQG 227
Cdd:PRK10762 139 vgeLSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKS-QGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
.
gi 446495558 228 E 228
Cdd:PRK10762 218 Q 218
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
31-197 |
1.48e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.25 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 31 KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELliddhplhfgdysFRSQRIRM-IFQDPST-----SLNPR 104
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-------------FRSAKVRMaVFSQHHVdgldlSSNPL 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 105 QRISQIldFPlrlntnLEPEQRRKQIIETMRMVGLLPDHVSYyphMLAPGQKQRLGLARALILRPKVIIADEALASLDMS 184
Cdd:PLN03073 593 LYMMRC--FP------GVPEQKLRAHLGSFGVTGNLALQPMY---TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLD 661
|
170
....*....|...
gi 446495558 185 MRSQLINLMLELQ 197
Cdd:PLN03073 662 AVEALIQGLVLFQ 674
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
30-227 |
1.57e-08 |
|
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: 55.30 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 30 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELliddhpLHFGDYSFRSQRIRMIfqdPSTslnprqrISQ 109
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI------KHSGRISFSPQTSWIM---PGT-------IKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 110 ILDFPLRLNtnlepEQRRKQIIETMRmvglLPDHVSYYPH-----------MLAPGQKQRLGLARALILRPKVIIADEAL 178
Cdd:TIGR01271 506 NIIFGLSYD-----EYRYTSVIKACQ----LEEDIALFPEkdktvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPF 576
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446495558 179 ASLDMSMRSQLINLML-ELQEKQgiSYIYVTQHIGMMKHiSDQVLVMHQG 227
Cdd:TIGR01271 577 THLDVVTEKEIFESCLcKLMSNK--TRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-249 |
2.90e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.97 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 9 RNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdySFRSQ 88
Cdd:PRK10982 2 SNISKSF---------PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-----DFKSS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 89 R------IRMIFQDpstsLNP-RQRisQILD------FPLR-------------------LNTNLEPEQRrkqiietmrm 136
Cdd:PRK10982 68 KealengISMVHQE----LNLvLQR--SVMDnmwlgrYPTKgmfvdqdkmyrdtkaifdeLDIDIDPRAK---------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 137 VGLLPdhVSyyphmlapgQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHIGMMKH 216
Cdd:PRK10982 132 VATLS--VS---------QMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQ 199
|
250 260 270
....*....|....*....|....*....|....*....
gi 446495558 217 ISDQVLVMHQGEVVE----RGSTADVLASPL--HELTKR 249
Cdd:PRK10982 200 LCDEITILRDGQWIAtqplAGLTMDKIIAMMvgRSLTQR 238
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
27-241 |
4.76e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 52.57 E-value: 4.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 27 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdYSFRSQRI-----------RMIFQ 95
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI----TDWQTAKImreavaivpegRRVFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 96 DPSTSLNP------------RQRISQILDFPLRLntnlepEQRRKQIIETMrmvgllpdhvsyyphmlAPGQKQRLGLAR 163
Cdd:PRK11614 94 RMTVEENLamggffaerdqfQERIKWVYELFPRL------HERRIQRAGTM-----------------SGGEQQMLAIGR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446495558 164 ALILRPKVIIADEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADVLAS 241
Cdd:PRK11614 151 ALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLRE-QGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
28-233 |
4.96e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 52.49 E-value: 4.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 28 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGM--IEPTSGELLIDDHPLHFGDYSFRS-QRIRMIFQDP------- 97
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAgEGIFMAFQYPveipgvs 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 98 -----STSLNprqrisqildfPLRLNTNLEPEQR---RKQIIETMRMVGLLPDHVSYYPHM-LAPGQKQRLGLARALILR 168
Cdd:PRK09580 95 nqfflQTALN-----------AVRSYRGQEPLDRfdfQDLMEEKIALLKMPEDLLTRSVNVgFSGGEKKRNDILQMAVLE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446495558 169 PKVIIADEALASLDMSMRSQLINLMLELQEKQGiSYIYVTQHIGMMKHIS-DQVLVMHQGEVVERG 233
Cdd:PRK09580 164 PELCILDESDSGLDIDALKIVADGVNSLRDGKR-SFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
40-227 |
3.03e-07 |
|
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: 50.02 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 40 GQTLAIIGENGSGKSTLAKMLAGMIEPTSGELliddhplhfgdysFRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNT 119
Cdd:cd03290 27 GQLTMIVGQVGCGKSSLLLAILGEMQTLEGKV-------------HWSNKNESEPSFEATRSRNRYSVAYAAQKPWLLNA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 120 NLEP---------EQRRKQIIETmrmVGLLPDhVSYYPH-----------MLAPGQKQRLGLARALILRPKVIIADEALA 179
Cdd:cd03290 94 TVEEnitfgspfnKQRYKAVTDA---CSLQPD-IDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446495558 180 SLDMSMRSQLINL-MLELQEKQGISYIYVTQHIGMMKHiSDQVLVMHQG 227
Cdd:cd03290 170 ALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
33-182 |
6.18e-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: 50.29 E-value: 6.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 33 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEpTSGELLIDDHPLHfgdySFRSQRIRMIFqdpstSLNPRqrisQILD 112
Cdd:TIGR01271 1238 LSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWN----SVTLQTWRKAF-----GVIPQ----KVFI 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 113 FPLRLNTNLEPEQR--RKQIIETMRMVGL------LPDHVSYY----PHMLAPGQKQRLGLARALILRPKVIIADEALAS 180
Cdd:TIGR01271 1304 FSGTFRKNLDPYEQwsDEEIWKVAEEVGLksvieqFPDKLDFVlvdgGYVLSNGHKQLMCLARSILSKAKILLLDEPSAH 1383
|
..
gi 446495558 181 LD 182
Cdd:TIGR01271 1384 LD 1385
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
33-240 |
7.12e-07 |
|
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: 7.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 33 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDdhplhfGDYSFRSQRIRMifQDPSTSLNprqrisqILd 112
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMK------GSVAYVPQQAWI--QNDSLREN-------IL- 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 113 FPLRLNtnlepEQRRKQIIETmrmVGLLPDhVSYYPH-----------MLAPGQKQRLGLARALILRPKVIIADEALASL 181
Cdd:TIGR00957 721 FGKALN-----EKYYQQVLEA---CALLPD-LEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 182 DMSMRSQLI-NLMLELQEKQGISYIYVTQHIGMMKHIsDQVLVMHQGEVVERGSTADVLA 240
Cdd:TIGR00957 792 DAHVGKHIFeHVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
35-182 |
7.30e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.95 E-value: 7.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 35 FTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLID----------DHPLHFGD--YSFRSQRI------------ 90
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEqdlivarlqqDPPRNVEGtvYDFVAEGIeeqaeylkryhd 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 91 --RMIFQDPSTS-LNPRQRISQILDfplrlNTNLepEQRRKQIIETMRMVGLLPD-HVSyyphMLAPGQKQRLGLARALI 166
Cdd:PRK11147 104 isHLVETDPSEKnLNELAKLQEQLD-----HHNL--WQLENRINEVLAQLGLDPDaALS----SLSGGWLRKAALGRALV 172
|
170
....*....|....*.
gi 446495558 167 LRPKVIIADEALASLD 182
Cdd:PRK11147 173 SNPDVLLLDEPTNHLD 188
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-244 |
8.42e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.05 E-value: 8.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 22 FRRQTVeAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAG-MIEP-------TSGELLIDDHPLHFGDySFRSQRIRMI 93
Cdd:PRK13547 10 ARRHRA-ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGgaprgarVTGDVTLNGEPLAAID-APRLARLRAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 94 F---QDPSTSLNPRQrISQILDFPLRLNTNLEPEQRRKQIIETMRMVG---LLPDHVSyyphMLAPGQKQRLGLARAL-- 165
Cdd:PRK13547 88 LpqaAQPAFAFSARE-IVLLGRYPHARRAGALTHRDGEIAWQALALAGataLVGRDVT----TLSGGELARVQFARVLaq 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 166 -------ILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGSTADV 238
Cdd:PRK13547 163 lwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
....*.
gi 446495558 239 LaSPLH 244
Cdd:PRK13547 243 L-TPAH 247
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
3-229 |
1.12e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.34 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 3 ETLLEVRNLSKtfryrtgwfRRQTveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELL-----IDDHP 77
Cdd:PRK10982 248 EVILEVRNLTS---------LRQP--SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITlhgkkINNHN 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 78 LHFG-DYSF----RSQRIRMIFQDPSTSLNprQRISQILDF--PLRLNTNLEPEQRRKQIIETMRMVglLPDHVSYYPHm 150
Cdd:PRK10982 317 ANEAiNHGFalvtEERRSTGIYAYLDIGFN--SLISNIRNYknKVGLLDNSRMKSDTQWVIDSMRVK--TPGHRTQIGS- 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 151 LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEK-QGIsyIYVTQHIGMMKHISDQVLVMHQGEV 229
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKdKGI--IIISSEMPELLGITDRILVMSNGLV 469
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
40-228 |
1.24e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 46.98 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 40 GQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgdysfrsqrirmifqdpstslnprqrisqildfplrlnt 119
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYID-------------------------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 120 nlePEQRRKQIIETMRMVGLLPDhvsyyPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLI-----NLML 194
Cdd:smart00382 38 ---GEDILEEVLDQLLLIIVGGK-----KASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRLLL 109
|
170 180 190
....*....|....*....|....*....|....*....
gi 446495558 195 ELQEKQGISYIYVTQHI-----GMMKHISDQVLVMHQGE 228
Cdd:smart00382 110 LLKSEKNLTVILTTNDEkdlgpALLRRRFDRRIVLLLIL 148
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
30-71 |
1.71e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.79 E-value: 1.71e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 446495558 30 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEL 71
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-251 |
2.27e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.82 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 21 WFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIddhplhfgdysfrsqrIRmifqdPSTS 100
Cdd:PLN03232 624 WDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV----------------IR-----GSVA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 101 LNPRqrISQILDFPLRLN----TNLEPEQRRKQIIETMRM--VGLLPDH----VSYYPHMLAPGQKQRLGLARALILRPK 170
Cdd:PLN03232 683 YVPQ--VSWIFNATVRENilfgSDFESERYWRAIDVTALQhdLDLLPGRdlteIGERGVNISGGQKQRVSMARAVYSNSD 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 171 VIIADEALASLDMSMRSQLINLMLElQEKQGISYIYVTQHIGMMKHIsDQVLVMHQGEVVERGSTADVLASplHELTKRL 250
Cdd:PLN03232 761 IYIFDDPLSALDAHVAHQVFDSCMK-DELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSKS--GSLFKKL 836
|
.
gi 446495558 251 I 251
Cdd:PLN03232 837 M 837
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-225 |
3.00e-06 |
|
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: 47.36 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 25 QTVEAVKPLSFTL------REGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELliDDHP------LHF-----GDY--SF 85
Cdd:cd03236 5 EPVHRYGPNSFKLhrlpvpREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKF--DDPPdwdeilDEFrgselQNYftKL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RSQRIRMIFQDPSTSLNPRQ---RISQILDfplrlntnlEPEQRRKQ--IIETMRMVGLLPDHVSYyphmLAPGQKQRLG 160
Cdd:cd03236 83 LEGDVKVIVKPQYVDLIPKAvkgKVGELLK---------KKDERGKLdeLVDQLELRHVLDRNIDQ----LSGGELQRVA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446495558 161 LARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQgiSYIYVTQH-IGMMKHISDQVLVMH 225
Cdd:cd03236 150 IAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDD--NYVLVVEHdLAVLDYLSDYIHCLY 213
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
154-241 |
4.00e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.81 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 154 GQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLElQEKQGISYIYVTQHIGMMKHIsDQVLVMHQGEVVERG 233
Cdd:PLN03130 744 GQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIK-DELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEG 821
|
....*...
gi 446495558 234 STADVLAS 241
Cdd:PLN03130 822 TYEELSNN 829
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-231 |
1.25e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 45.93 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 3 ETLLEVRNLSKTFRYRtgwfrrqtveaVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLiddhpLHFGD 82
Cdd:PRK09700 263 ETVFEVRNVTSRDRKK-----------VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIR-----LNGKD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 83 YSFRS------QRIRMIFQD-------PSTSLNPRQRIS-QILDFPLRLNTNLEPEQRRKQIIETMRMVGLLPDH-VSYY 147
Cdd:PRK09700 327 ISPRSpldavkKGMAYITESrrdngffPNFSIAQNMAISrSLKDGGYKGAMGLFHEVDEQRTAENQRELLALKCHsVNQN 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 148 PHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHIGMMKHISDQVLVMHQG 227
Cdd:PRK09700 407 ITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELPEIITVCDRIAVFCEG 485
|
....
gi 446495558 228 EVVE 231
Cdd:PRK09700 486 RLTQ 489
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
6-182 |
1.47e-05 |
|
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: 45.23 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLskTFRYRTGwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEpTSGELLIDDHPLHfgdySF 85
Cdd:cd03289 3 MTVKDL--TAKYTEG-----GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWN----SV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RSQRIRMIFqdpstSLNPRQRIsqILDFPLRLNTNLEPEQRRKQIIETMRMVGL------LPDHVSYY----PHMLAPGQ 155
Cdd:cd03289 71 PLQKWRKAF-----GVIPQKVF--IFSGTFRKNLDPYGKWSDEEIWKVAEEVGLksvieqFPGQLDFVlvdgGCVLSHGH 143
|
170 180
....*....|....*....|....*..
gi 446495558 156 KQRLGLARALILRPKVIIADEALASLD 182
Cdd:cd03289 144 KQLMCLARSVLSKAKILLLDEPSAHLD 170
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
31-76 |
2.40e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.27 E-value: 2.40e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 446495558 31 KPL----SFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH 76
Cdd:PRK15064 14 KPLfeniSVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPN 63
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
33-245 |
2.48e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.54 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 33 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGElliddhplhfgdysfrsqrirmIFQDPSTSLNPRQriSQILD 112
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGR----------------------VWAERSIAYVPQQ--AWIMN 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 113 FPLRLNTNLEPEQRRKQIIETMRMVGLLPDHVSYYPHM----------LAPGQKQRLGLARALILRPKVIIADEALASLD 182
Cdd:PTZ00243 735 ATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLeteigekgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446495558 183 MSMrSQLINLMLELQEKQGISYIYVTQHIGMMKHiSDQVLVMHQGEVVERGSTADVLASPLHE 245
Cdd:PTZ00243 815 AHV-GERVVEECFLGALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFMRTSLYA 875
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
6-257 |
2.63e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 44.73 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 6 LEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAkMLAGMIEPTSGElliddHPLHFGDYSF 85
Cdd:NF000106 14 VEVRGLVKHF---------GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGR-----RPWRF*TWCA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 86 RSQRIRM-------IFQDPSTSLNPRQR---ISQILDFPLRlntnlEPEQRRKQIIETMRMVGLLPDHVSYYphmlAPGQ 155
Cdd:NF000106 79 NRRALRRtig*hrpVR*GRRESFSGRENlymIGR*LDLSRK-----DARARADELLERFSLTEAAGRAAAKY----SGGM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 156 KQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHIGMMKHISDQVLVMHQGEVVERGST 235
Cdd:NF000106 150 RRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV-RDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKV 228
|
250 260
....*....|....*....|..
gi 446495558 236 aDVLASPLHELTKRLIAGHFGE 257
Cdd:NF000106 229 -DELKTKVGGRTLQIRPAHAAE 249
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
37-107 |
3.79e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 43.33 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 37 LREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdySFRSQRIRM---------------------IFQ 95
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP-----VYKPQYIDLsggelqrvaiaaallrnatfyLFD 96
|
90
....*....|..
gi 446495558 96 DPSTSLNPRQRI 107
Cdd:cd03222 97 EPSAYLDIEQRL 108
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
36-70 |
1.27e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.87 E-value: 1.27e-04
10 20 30
....*....|....*....|....*....|....*
gi 446495558 36 TLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGE 70
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGD 129
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
36-70 |
1.28e-04 |
|
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: 42.85 E-value: 1.28e-04
10 20 30
....*....|....*....|....*....|....*
gi 446495558 36 TLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGE 70
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGD 129
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
33-182 |
1.37e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.69 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 33 LSFTLREGQTLAIIGENGSGKSTLAKMLAGmieptsgellidDHPlhfGDYS-----FRSQR--------IRMIFQDPST 99
Cdd:PRK10938 279 LSWQVNPGEHWQIVGPNGAGKSTLLSLITG------------DHP---QGYSndltlFGRRRgsgetiwdIKKHIGYVSS 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 100 SLNprqrisqiLDFplRLNTNLE-----------------PEQRRKQIIETMRMVGlLPDHVSYYP-HMLAPGQkQRLGL 161
Cdd:PRK10938 344 SLH--------LDY--RVSTSVRnvilsgffdsigiyqavSDRQQKLAQQWLDILG-IDKRTADAPfHSLSWGQ-QRLAL 411
|
170 180
....*....|....*....|..
gi 446495558 162 -ARALILRPKVIIADEALASLD 182
Cdd:PRK10938 412 iVRALVKHPTLLILDEPLQGLD 433
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
26-191 |
1.46e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.17 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 26 TVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIE----PTSGELLIDDHPLHfgdySFRSQ-RIRMIFQDPSTS 100
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDGITPE----EIKKHyRGDVVYNAETDV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 101 LNPRQRISQILDFPLRLNT------NLEPEQRRKQIIE-TMRMVGLlpDH-------------VSyyphmlaPGQKQRLG 160
Cdd:TIGR00956 149 HFPHLTVGETLDFAARCKTpqnrpdGVSREEYAKHIADvYMATYGL--SHtrntkvgndfvrgVS-------GGERKRVS 219
|
170 180 190
....*....|....*....|....*....|.
gi 446495558 161 LARALILRPKVIIADEALASLDMSMRSQLIN 191
Cdd:TIGR00956 220 IAEASLGGAKIQCWDNATRGLDSATALEFIR 250
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
33-73 |
3.78e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 40.63 E-value: 3.78e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 446495558 33 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLI 73
Cdd:PRK13541 19 LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYY 59
|
|
| DUF87 |
pfam01935 |
Helicase HerA, central domain; This entry represents the central domain found in archaeal ... |
43-135 |
1.87e-03 |
|
Helicase HerA, central domain; This entry represents the central domain found in archaeal proteins such as DNA double-strand break repair helicase HerA (EC:3.6.4.12). HerA is a helicase which is able to utilize either 3' or 5' single-stranded DNA extensions for loading and subsequent DNA duplex unwinding. It forms a complex with NurA nuclease, this complex has the 5'-3' DNA end resection activity and is essential for cell viability in the crenarchaeon Sulfolobus islandicus. This domain includes the the central RecA-like catalytic core and a flanking four-helix bundle. The function of this prokaryotic domain is unknown. It contains several conserved aspartates and histidines that could be metal ligands.
Pssm-ID: 376671 [Multi-domain] Cd Length: 220 Bit Score: 38.50 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 43 LAIIGENGSGKSTLAK-MLAGMIEPTSGELLIDDHplHfGDYSFR-----SQRIRMIFQDPSTSLNPRQ-RISQILDFPL 115
Cdd:pfam01935 26 FAILGSTGSGKSNTVAvLLEELLEKKGATVLIFDP--H-GEYGTLfrdlgAENVNVITPDPELKINPWLlSPEDLADLLE 102
|
90 100
....*....|....*....|..
gi 446495558 116 RLNTNLEPEQRR--KQIIETMR 135
Cdd:pfam01935 103 ELNLPNAEVQRSilEEALDQLK 124
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
37-78 |
2.66e-03 |
|
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: 37.99 E-value: 2.66e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 446495558 37 LREGQTLAIIGENGSGKSTLAKMLA-----GMIEptsGELLIDDHPL 78
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAgrktaGVIT---GEILINGRPL 73
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
35-61 |
3.49e-03 |
|
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 37.72 E-value: 3.49e-03
10 20
....*....|....*....|....*..
gi 446495558 35 FTLREGQTLAIIGENGSGKSTLAKMLA 61
Cdd:pfam00006 9 LPIGRGQRIGIFGGSGVGKTVLAGMIA 35
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
151-233 |
3.59e-03 |
|
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: 37.30 E-value: 3.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 151 LAPGQKQRLGLARALILRPK--VIIADEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHIGMMKHiSDQVLVM---- 224
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLID-LGNTVILIEHNLDVLSS-ADWIIDFgpgs 165
|
90
....*....|.
gi 446495558 225 --HQGEVVERG 233
Cdd:cd03238 166 gkSGGKVVFSG 176
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
45-70 |
4.37e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 38.18 E-value: 4.37e-03
10 20
....*....|....*....|....*.
gi 446495558 45 IIGENGSGKSTLAKMLAGMIEPTSGE 70
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGE 63
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
24-61 |
5.84e-03 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 37.86 E-value: 5.84e-03
10 20 30
....*....|....*....|....*....|....*...
gi 446495558 24 RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLA 61
Cdd:COG5635 164 LERIESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLA 201
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
33-135 |
6.46e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 37.28 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446495558 33 LSFTLREGQTLaIIGENGSGKSTLAKMLAGMIEPTSGEL-LIDDHPLHFGDYSFRSQRIRMIFQDPS-----TSLNPRQR 106
Cdd:COG3950 19 IDFDNPPRLTV-LVGENGSGKTTLLEAIALALSGLLSRLdDVKFRKLLIRNGEFGDSAKLILYYGTSrllldGPLKKLER 97
|
90 100 110
....*....|....*....|....*....|
gi 446495558 107 ISQILDFPL-RLNTNLEPEQRRKQIIETMR 135
Cdd:COG3950 98 LKEEYFSRLdGYDSLLDEDSNLREFLEWLR 127
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
33-70 |
6.69e-03 |
|
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: 37.61 E-value: 6.69e-03
10 20 30
....*....|....*....|....*....|....*...
gi 446495558 33 LSFTlrEGQTLAIIGENGSGKSTLAKMLAGMIEPTSGE 70
Cdd:TIGR03719 26 LSFF--PGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE 61
|
|
| PRK07261 |
PRK07261 |
DNA topology modulation protein; |
43-60 |
9.33e-03 |
|
DNA topology modulation protein;
Pssm-ID: 180911 [Multi-domain] Cd Length: 171 Bit Score: 36.23 E-value: 9.33e-03
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