|
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: 563.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 2 VETLLEVRQLSKTFRYRTGWFHRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFG 81
Cdd:PRK15112 1 VETLLEVRNLSKTFRYRTGWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 82 DYSYRSQKIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLDAEARQKQIIDTLRMVGLLPDHVSYYPHMLAPGQKQRLGL 161
Cdd:PRK15112 81 DYSYRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 162 ARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVLAS 241
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLAS 240
|
250 260
....*....|....*....|....*..
gi 490242029 242 PLHDLTRRLIAGHFGEALTADAWRKDG 268
Cdd:PRK15112 241 PLHELTKRLIAGHFGEALTADAWRKDR 267
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-266 |
0e+00 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 537.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 2 VETLLEVRQLSKTFRYRTGWFHRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFG 81
Cdd:COG4167 1 MSALLEVRNLSKTFKYRTGLFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 82 DYSYRSQKIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLDAEARQKQIIDTLRMVGLLPDHVSYYPHMLAPGQKQRLGL 161
Cdd:COG4167 81 DYKYRCKHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQKQRVAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 162 ARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVLAS 241
Cdd:COG4167 161 ARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFAN 240
|
250 260
....*....|....*....|....*
gi 490242029 242 PLHDLTRRLIAGHFGEALTADAWRK 266
Cdd:COG4167 241 PQHEVTKRLIESHFGEALTADAWRR 265
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-252 |
1.01e-103 |
|
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: 311.07 E-value: 1.01e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 3 ETLLEVRQLSKTFRYRTgwfhRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLT--- 79
Cdd:COG1123 258 EPLLEVRNLSKRYPVRG----KGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTkls 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 80 FGDYSYRSQKIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLDAEARQKQIIDTLRMVGLLPDHVSYYPHMLAPGQKQRL 159
Cdd:COG1123 334 RRSLRELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRV 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 160 GLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVL 239
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVF 493
|
250
....*....|...
gi 490242029 240 ASPLHDLTRRLIA 252
Cdd:COG1123 494 ANPQHPYTRALLA 506
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-252 |
8.49e-102 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 299.72 E-value: 8.49e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 1 MVETLLEVRQLSKTFRYRTGWFHRQ--TVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPL 78
Cdd:COG4608 3 MAEPLLEVRDLKKHFPVRGGLFGRTvgVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 79 TFGDYS----YRsQKIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLDAEARQKQIIDTLRMVGLLPDHVSYYPHMLAPG 154
Cdd:COG4608 83 TGLSGRelrpLR-RRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEFSGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 155 QKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGS 234
Cdd:COG4608 162 QRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAP 241
|
250
....*....|....*...
gi 490242029 235 TADVLASPLHDLTRRLIA 252
Cdd:COG4608 242 RDELYARPLHPYTQALLS 259
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-252 |
9.00e-91 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 271.45 E-value: 9.00e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 1 MVETLLEVRQLSKTFRYRTGWFH-RQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLT 79
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPVKRGLFKpERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 80 FGDYSYRS---QKIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLDAEARQKQIIDTLRMVGLLPDHVSYYPHMLAPGQK 156
Cdd:PRK11308 81 KADPEAQKllrQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 157 QRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTA 236
Cdd:PRK11308 161 QRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKE 240
|
250
....*....|....*.
gi 490242029 237 DVLASPLHDLTRRLIA 252
Cdd:PRK11308 241 QIFNNPRHPYTQALLS 256
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-252 |
2.16e-90 |
|
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: 270.39 E-value: 2.16e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 5 LLEVRQLSKTFRYRTGWFHrqtveAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEP---TSGELLIDDHPLTfg 81
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVK-----AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLL-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 82 DYS------YRSQKIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLDAEARQKQIIDTLRMVGLLP--DHVSYYPHMLAP 153
Cdd:COG0444 74 KLSekelrkIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDpeRRLDRYPHELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 154 GQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERG 233
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEG 233
|
250
....*....|....*....
gi 490242029 234 STADVLASPLHDLTRRLIA 252
Cdd:COG0444 234 PVEELFENPRHPYTRALLS 252
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-252 |
9.23e-88 |
|
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: 270.40 E-value: 9.23e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 3 ETLLEVRQLSKTFRYRTGWFHRQT--VEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVePTSGELLIDDHPLTF 80
Cdd:COG4172 273 PPLLEARDLKVWFPIKRGLFRRTVghVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 81 GDYS----YRSQkIRMIFQDPSTSLNPRQRISQILDFPLRL-NTDLDAEARQKQIIDTLRMVGLLPDHVSYYPHMLAPGQ 155
Cdd:COG4172 352 LSRRalrpLRRR-MQVVFQDPFGSLSPRMTVGQIIAEGLRVhGPGLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQ 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 156 KQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGST 235
Cdd:COG4172 431 RQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPT 510
|
250
....*....|....*..
gi 490242029 236 ADVLASPLHDLTRRLIA 252
Cdd:COG4172 511 EQVFDAPQHPYTRALLA 527
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-252 |
1.01e-85 |
|
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: 255.88 E-value: 1.01e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 5 LLEVRQLSKTFRYRtgwfhRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYS 84
Cdd:COG1124 1 MLEVRNLSVSYGQG-----GRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 85 YRSQKIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLDAEARqkqIIDTLRMVGLLPDHVSYYPHMLAPGQKQRLGLARA 164
Cdd:COG1124 76 AFRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHGLPDREER---IAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 165 LILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVLASPLH 244
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
....*...
gi 490242029 245 DLTRRLIA 252
Cdd:COG1124 233 PYTRELLA 240
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-233 |
4.74e-85 |
|
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: 253.58 E-value: 4.74e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 5 LLEVRQLSKTFRYRTGWfhrqtVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGD-- 82
Cdd:cd03257 1 LLEVKNLSVSFPTGGGS-----VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 83 -YSYRSQKIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLD-AEARQKQIIDTLRMVGLLPDHVSYYPHMLAPGQKQRLG 160
Cdd:cd03257 76 lRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSkKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490242029 161 LARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERG 233
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
5-252 |
2.34e-72 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 224.97 E-value: 2.34e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 5 LLEVRQLSKTFRYRTG----WFHRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLT- 79
Cdd:PRK15079 8 LLEVADLKVHFDIKDGkqwfWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 80 FGDYSYRS--QKIRMIFQDPSTSLNPRQRISQILDFPLRL-NTDLDAEARQKQIIDTLRMVGLLPDHVSYYPHMLAPGQK 156
Cdd:PRK15079 88 MKDDEWRAvrSDIQMIFQDPLASLNPRMTIGEIIAEPLRTyHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQC 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 157 QRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTA 236
Cdd:PRK15079 168 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYD 247
|
250
....*....|....*.
gi 490242029 237 DVLASPLHDLTRRLIA 252
Cdd:PRK15079 248 EVYHNPLHPYTKALMS 263
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-242 |
1.98e-60 |
|
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: 198.97 E-value: 1.98e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 3 ETLLEVRQLSktFRYRTGWfhrqtVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPT---SGELLIDDHPLT 79
Cdd:COG1123 2 TPLLEVRDLS--VRYPGGD-----VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 80 FGDYSYRSQKIRMIFQDPSTSLNPRQRISQIlDFPLRlNTDLDAEARQKQIIDTLRMVGLlPDHVSYYPHMLAPGQKQRL 159
Cdd:COG1123 75 ELSEALRGRRIGMVFQDPMTQLNPVTVGDQI-AEALE-NLGLSRAEARARVLELLEAVGL-ERRLDRYPHQLSGGQRQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 160 GLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVL 239
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEIL 231
|
...
gi 490242029 240 ASP 242
Cdd:COG1123 232 AAP 234
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-252 |
1.72e-59 |
|
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: 197.21 E-value: 1.72e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 1 MVETLLEVRQLSKTFRYRTGwfhrqTVEAVKPLSFTLRERQTLAIIGENGSGKS--TLAKM--LAGMVEPTSGELLIDDH 76
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGG-----TVEAVKGVSFDIAAGETLALVGESGSGKSvtALSILrlLPDPAAHPSGSILFDGQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 77 PL-TFGDY---SYRSQKIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLDAEARQKQIIDTLRMVGLlPD---HVSYYPH 149
Cdd:COG4172 77 DLlGLSERelrRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGI-PDperRLDAYPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 150 MLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEV 229
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEI 235
|
250 260
....*....|....*....|...
gi 490242029 230 VERGSTADVLASPLHDLTRRLIA 252
Cdd:COG4172 236 VEQGPTAELFAAPQHPYTRKLLA 258
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-252 |
6.41e-59 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 197.39 E-value: 6.41e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 3 ETLLEVRQLSKTFRYRTGWFHRQT--VEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPL-T 79
Cdd:PRK10261 311 EPILQVRNLVTRFPLRSGLLNRVTreVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdT 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 80 FGDYSYRS--QKIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLDAEARQKQIIDTLRMVGLLPDHVSYYPHMLAPGQKQ 157
Cdd:PRK10261 391 LSPGKLQAlrRDIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQ 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 158 RLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTAD 237
Cdd:PRK10261 471 RICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRA 550
|
250
....*....|....*
gi 490242029 238 VLASPLHDLTRRLIA 252
Cdd:PRK10261 551 VFENPQHPYTRKLMA 565
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
4-252 |
5.15e-58 |
|
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: 185.78 E-value: 5.15e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 4 TLLEVRQLSKtfRYRTGWF--HRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFG 81
Cdd:TIGR02769 1 SLLEVRDVTH--TYRTGGLfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 82 DYSYRS---QKIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLDAEARQKQIIDTLRMVGLLPDHVSYYPHMLAPGQKQR 158
Cdd:TIGR02769 79 DRKQRRafrRDVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 159 LGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADV 238
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQL 238
|
250
....*....|....
gi 490242029 239 LASPlHDLTRRLIA 252
Cdd:TIGR02769 239 LSFK-HPAGRNLQS 251
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-240 |
3.88e-55 |
|
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: 177.14 E-value: 3.88e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSktFRYRTGwfhrqtVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSY 85
Cdd:COG1122 1 IELENLS--FSYPGG------TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 RSQKIRMIFQDPStslnprqriSQILD--------FPLRlNTDLDAEARQKQIIDTLRMVGLLpDHVSYYPHMLAPGQKQ 157
Cdd:COG1122 73 LRRKVGLVFQNPD---------DQLFAptveedvaFGPE-NLGLPREEIRERVEEALELVGLE-HLADRPPHELSGGQKQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 158 RLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTAD 237
Cdd:COG1122 142 RVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLN-KEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPRE 220
|
...
gi 490242029 238 VLA 240
Cdd:COG1122 221 VFS 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-252 |
8.82e-55 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 184.52 E-value: 8.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 3 ETLLEVRQLSKTFRYRTGWFHRQTVE--AVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVePTSGELLIDDHPL-T 79
Cdd:PRK15134 273 SPLLDVEQLQVAFPIRKGILKRTVDHnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLhN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 80 FGDYS---YRSQkIRMIFQDPSTSLNPRQRISQILDFPLRLN-TDLDAEARQKQIIDTLRMVGLLPDHVSYYPHMLAPGQ 155
Cdd:PRK15134 352 LNRRQllpVRHR-IQVVFQDPNSSLNPRLNVLQIIEEGLRVHqPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQ 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 156 KQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGST 235
Cdd:PRK15134 431 RQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDC 510
|
250
....*....|....*..
gi 490242029 236 ADVLASPLHDLTRRLIA 252
Cdd:PRK15134 511 ERVFAAPQQEYTRQLLA 527
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-240 |
3.31e-54 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 176.42 E-value: 3.31e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 4 TLLEVRQLSKtfRYRTGWF-----HRQTVEAVkplSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPL 78
Cdd:PRK10419 2 TLLNVSGLSH--HYAHGGLsgkhqHQTVLNNV---SLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 79 TFGDysyRSQK------IRMIFQDPSTSLNPRQRISQILDFPLRLNTDLDAEARQKQIIDTLRMVGLLPDHVSYYPHMLA 152
Cdd:PRK10419 77 AKLN---RAQRkafrrdIQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 153 PGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVER 232
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
|
....*...
gi 490242029 233 GSTADVLA 240
Cdd:PRK10419 234 QPVGDKLT 241
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-252 |
3.70e-51 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 170.26 E-value: 3.70e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTFRYRTGwfhrqTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTfgDYSY 85
Cdd:COG1135 2 IELENLSKTFPTKGG-----PVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLT--ALSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 RS-----QKIRMIFQDPS--TSLNPRQRISqildFPLRLnTDLDAEARQKQIIDTLRMVGLlPDHVSYYPHMLAPGQKQR 158
Cdd:COG1135 75 RElraarRKIGMIFQHFNllSSRTVAENVA----LPLEI-AGVPKAEIRKRVAELLELVGL-SDKADAYPSQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 159 LGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADV 238
Cdd:COG1135 149 VGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDV 228
|
250
....*....|....
gi 490242029 239 LASPLHDLTRRLIA 252
Cdd:COG1135 229 FANPQSELTRRFLP 242
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-262 |
7.05e-49 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 162.18 E-value: 7.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 1 MVETLLEVRQLSKTFRYRTGwfhrqTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTf 80
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGG-----GVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 81 gdysYRSQKIRMIFQDPStsLNPRQRISQILDFPLRLnTDLDAEARQKQIIDTLRMVGLLpDHVSYYPHMLAPGQKQRLG 160
Cdd:COG1116 77 ----GPGPDRGVVFQEPA--LLPWLTVLDNVALGLEL-RGVPKAERRERARELLELVGLA-GFEDAYPHQLSGGMRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 161 LARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTqhlgmmkH-------ISDQVLVMHN--GEVVE 231
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVT-------HdvdeavfLADRVVVLSArpGRIVE 221
|
250 260 270
....*....|....*....|....*....|....*....
gi 490242029 232 -------RGSTADVLASP-LHDLTRRLIAGHFGEALTAD 262
Cdd:COG1116 222 eidvdlpRPRDRELRTSPeFAALRAEILDLLREEAERAA 260
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-233 |
8.83e-49 |
|
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: 160.38 E-value: 8.83e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTFRyrtgwfhrqTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTfgDYSY 85
Cdd:cd03259 1 LELKGLSKTYG---------SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT--GVPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 RSQKIRMIFQDPStsLNPRQRISQILDFPLRLNTdLDAEARQKQIIDTLRMVGLlPDHVSYYPHMLAPGQKQRLGLARAL 165
Cdd:cd03259 70 ERRNIGMVFQDYA--LFPHLTVAENIAFGLKLRG-VPKAEIRARVRELLELVGL-EGLLNRYPHELSGGQQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490242029 166 ILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERG 233
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-242 |
1.51e-48 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 164.12 E-value: 1.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 1 MVETLLEVRQLSKTFryrtgwfhrQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLT- 79
Cdd:COG3842 1 MAMPALELENVSKRY---------GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTg 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 80 -------FGdysyrsqkirMIFQD----PStsLNPRQRISqildFPLRLNtDLDAEARQKQIIDTLRMVGLlPDHVSYYP 148
Cdd:COG3842 72 lppekrnVG----------MVFQDyalfPH--LTVAENVA----FGLRMR-GVPKAEIRARVAELLELVGL-EGLADRYP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 149 HMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTqhlgmmkH-------ISDQV 221
Cdd:COG3842 134 HQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVT-------HdqeealaLADRI 206
|
250 260
....*....|....*....|.
gi 490242029 222 LVMHNGEVVERGSTADVLASP 242
Cdd:COG3842 207 AVMNDGRIEQVGTPEEIYERP 227
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-242 |
2.34e-48 |
|
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: 160.14 E-value: 2.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 1 MVETLLEVRQLSKTFryrtgwfHRQTVeaVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTF 80
Cdd:COG1127 1 MSEPMIEVRNLTKSF-------GDRVV--LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 81 GD----YSYRsQKIRMIFQDPS--TSLNPRQRISqildFPLRLNTDLDAEARQKQIIDTLRMVGlLPDHVSYYPHMLAPG 154
Cdd:COG1127 72 LSekelYELR-RRIGMLFQGGAlfDSLTVFENVA----FPLREHTDLSEAEIRELVLEKLELVG-LPGAADKMPSELSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 155 QKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGS 234
Cdd:COG1127 146 MRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGT 225
|
....*...
gi 490242029 235 TADVLASP 242
Cdd:COG1127 226 PEELLASD 233
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-254 |
4.94e-48 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 159.07 E-value: 4.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTFRyrtgwfhrqTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSY 85
Cdd:COG1131 1 IEVRGLTKRYG---------DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 RsQKIRMIFQDPstSLNPRQRISQILDFPLRLNtDLDAEARQKQIIDTLRMVGLLP---DHVSYYPHmlapGQKQRLGLA 162
Cdd:COG1131 72 R-RRIGYVPQEP--ALYPDLTVRENLRFFARLY-GLPRKEARERIDELLELFGLTDaadRKVGTLSG----GMKQRLGLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 163 RALILRPKVIVCDEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVLASP 242
Cdd:COG1131 144 LALLHDPELLILDEPTSGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
250
....*....|..
gi 490242029 243 LHDLTRRLIAGH 254
Cdd:COG1131 223 LEDVFLELTGEE 234
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-242 |
1.37e-47 |
|
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: 158.13 E-value: 1.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 5 LLEVRQLSKTFRYRTGWFHrqtveAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLT-FGDY 83
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVT-----ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTlLSGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 84 SYR--SQKIRMIFQDPS--TSLNPRQRISqildFPLRLnTDLDAEARQKQIIDTLRMVGLlPDHVSYYPHMLAPGQKQRL 159
Cdd:cd03258 76 ELRkaRRRIGMIFQHFNllSSRTVFENVA----LPLEI-AGVPKAEIEERVLELLELVGL-EDKADAYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 160 GLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVL 239
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVF 229
|
...
gi 490242029 240 ASP 242
Cdd:cd03258 230 ANP 232
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
30-179 |
8.28e-47 |
|
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: 153.19 E-value: 8.28e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 30 VKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSYRSQKIRMIFQDPstSLNPRQRISQ 109
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDP--QLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490242029 110 ILDFPLRL--NTDLDAEARQKQIIDTLRMVGLLPDHVSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALA 179
Cdd:pfam00005 79 NLRLGLLLkgLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-242 |
2.54e-46 |
|
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: 154.97 E-value: 2.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTFRYRTGWfhrqtveavKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLT----FG 81
Cdd:cd03261 1 IELRGLTKSFGGRTVL---------KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglseAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 82 DYSYRsQKIRMIFQDPS--TSLNPRQRISqildFPLRLNTDLDAEARQKQIIDTLRMVGLLPDHvSYYPHMLAPGQKQRL 159
Cdd:cd03261 72 LYRLR-RRMGMLFQSGAlfDSLTVFENVA----FPLREHTRLSEEEIREIVLEKLEAVGLRGAE-DLYPAELSGGMKKRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 160 GLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVL 239
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
...
gi 490242029 240 ASP 242
Cdd:cd03261 226 ASD 228
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-228 |
3.00e-45 |
|
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: 151.47 E-value: 3.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 7 EVRQLSktFRYrtgwfHRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSYR 86
Cdd:cd03225 1 ELKNLS--FSY-----PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 87 SQKIRMIFQDPSTSL-NPRqrisqILD---FPLRlNTDLDAEARQKQIIDTLRMVGL--LPDHVsyyPHMLAPGQKQRLG 160
Cdd:cd03225 74 RRKVGLVFQNPDDQFfGPT-----VEEevaFGLE-NLGLPEEEIEERVEEALELVGLegLRDRS---PFTLSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490242029 161 LARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMHNGE 228
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-240 |
2.61e-44 |
|
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: 150.01 E-value: 2.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 5 LLEVRQLSKTFryrtgwfhrQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYS 84
Cdd:COG4555 1 MIEVENLSKKY---------GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 85 YRsQKIRMIFQDPstSLNPRQRISQILDF--PLRLNTDLDAEARQKQIIDTLRMVGLLPDHVSYYPHmlapGQKQRLGLA 162
Cdd:COG4555 72 AR-RQIGVLPDER--GLYDRLTVRENIRYfaELYGLFDEELKKRIEELIELLGLEEFLDRRVGELST----GMKKKVALA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490242029 163 RALILRPKVIVCDEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVLA 240
Cdd:COG4555 145 RALVHDPKVLLLDEPTNGLDVMARRLLREILRALK-KEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-231 |
3.77e-44 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 149.04 E-value: 3.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 3 ETLLEVRQLSKTfrYRTGwfhRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTfgD 82
Cdd:COG1136 2 SPLLELRNLTKS--YGTG---EGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIS--S 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 83 YS------YRSQKIRMIFQD----PSTSlnprqrisqILD---FPLRLNtDLDAEARQKQIIDTLRMVGLlPDHVSYYPH 149
Cdd:COG1136 75 LSerelarLRRRHIGFVFQFfnllPELT---------ALEnvaLPLLLA-GVSRKERRERARELLERVGL-GDRLDHRPS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 150 MLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHNGEV 229
Cdd:COG1136 144 QLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRI 222
|
..
gi 490242029 230 VE 231
Cdd:COG1136 223 VS 224
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
3-244 |
4.34e-44 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 151.80 E-value: 4.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 3 ETLLEVRQLSKTFRYRTGwfhrqTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEP---TSG-------ELL 72
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDG-----DVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGsatfngrEIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 73 -IDDHPLTfgdySYRSQKIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLD-AEARQKQI--IDTLRMvgllPD---HVS 145
Cdd:PRK09473 85 nLPEKELN----KLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSkAEAFEESVrmLDAVKM----PEarkRMK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 146 YYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMH 225
Cdd:PRK09473 157 MYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMY 236
|
250
....*....|....*....
gi 490242029 226 NGEVVERGSTADVLASPLH 244
Cdd:PRK09473 237 AGRTMEYGNARDVFYQPSH 255
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-232 |
6.80e-44 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 148.00 E-value: 6.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTFRYRTGwfhrqTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTfgdysY 85
Cdd:cd03293 1 LEVRNVSKTYGGGGG-----AVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT-----G 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 RSQKIRMIFQDPStsLNPRQRISQILDFPLRLNTDLDAEARQkQIIDTLRMVGLLpDHVSYYPHMLAPGQKQRLGLARAL 165
Cdd:cd03293 71 PGPDRGYVFQQDA--LLPWLTVLDNVALGLELQGVPKAEARE-RAEELLELVGLS-GFENAYPHQLSGGMRQRVALARAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490242029 166 ILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHN--GEVVER 232
Cdd:cd03293 147 AVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-262 |
1.26e-43 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 151.11 E-value: 1.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 7 EVRQLSKTFRYRTGWFHrqtveAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLT-FGDYSY 85
Cdd:PRK11153 3 ELKNISKVFPQGGRTIH-----ALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTaLSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 RS--QKIRMIFQDPSTsLNPRQRISQILdFPLRLnTDLDAEARQKQIIDTLRMVGLlPDHVSYYPHMLAPGQKQRLGLAR 163
Cdd:PRK11153 78 RKarRQIGMIFQHFNL-LSSRTVFDNVA-LPLEL-AGTPKAEIKARVTELLELVGL-SDKADRYPAQLSGGQKQRVAIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 164 ALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVLASPL 243
Cdd:PRK11153 154 ALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPK 233
|
250
....*....|....*....
gi 490242029 244 HDLTRRLIAGHFGEALTAD 262
Cdd:PRK11153 234 HPLTREFIQSTLHLDLPED 252
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-242 |
9.31e-43 |
|
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: 145.46 E-value: 9.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTFryrtGWFHrqtveAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSY 85
Cdd:cd03300 1 IELENVSKFY----GGFV-----ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 RsqKIRMIFQdpSTSLNPRQRISQILDFPLRLNTdLDAEARQKQIIDTLRMVGLLpDHVSYYPHMLAPGQKQRLGLARAL 165
Cdd:cd03300 72 R--PVNTVFQ--NYALFPHLTVFENIAFGLRLKK-LPKAEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490242029 166 ILRPKVIVCDEALASLDMSMRSQL-INLMlELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVLASP 242
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMqLELK-RLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEP 222
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-229 |
1.44e-41 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 141.86 E-value: 1.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTfrYRTGwfhRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTfgDYS- 84
Cdd:cd03255 1 IELKNLSKT--YGGG---GEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIS--KLSe 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 85 -----YRSQKIRMIFQDPStsLNPRQRISQILDFPLRLNTDLDAEARQKqIIDTLRMVGLlPDHVSYYPHMLAPGQKQRL 159
Cdd:cd03255 74 kelaaFRRRHIGFVFQSFN--LLPDLTALENVELPLLLAGVPKKERRER-AEELLERVGL-GDRLNHYPSELSGGQQQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 160 GLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTqHLGMMKHISDQVLVMHNGEV 229
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVT-HDPELAEYADRIIELRDGKI 218
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-240 |
4.54e-41 |
|
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: 142.18 E-value: 4.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSktFRYrtgwfHRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDH-PLTFGDYS 84
Cdd:TIGR04520 1 IEVENVS--FSY-----PESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLdTLDEENLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 85 YRSQKIRMIFQDPSTslnprQRISQILD----FPLRlNTDLDAEARQKQIIDTLRMVGLLpDHVSYYPHMLAPGQKQRLG 160
Cdd:TIGR04520 74 EIRKKVGMVFQNPDN-----QFVGATVEddvaFGLE-NLGVPREEMRKRVDEALKLVGME-DFRDREPHLLSGGQKQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 161 LARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTqHlgMMKHI--SDQVLVMHNGEVVERGSTADV 238
Cdd:TIGR04520 147 IAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISIT-H--DMEEAvlADRVIVMNKGKIVAEGTPREI 223
|
..
gi 490242029 239 LA 240
Cdd:TIGR04520 224 FS 225
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-252 |
7.52e-41 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 148.46 E-value: 7.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 2 VETLLEVRQLSKTFRYrtgwfHRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPL--- 78
Cdd:PRK10261 9 ARDVLAVENLNIAFMQ-----EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 79 -----TFGDYS------YRSQKIRMIFQDPSTSLNPRQRISQILDFPLRLNTDL---DAEARQKQIIDTLRmvglLPDH- 143
Cdd:PRK10261 84 srqviELSEQSaaqmrhVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGAsreEAMVEAKRMLDQVR----IPEAq 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 144 --VSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQV 221
Cdd:PRK10261 160 tiLSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRV 239
|
250 260 270
....*....|....*....|....*....|.
gi 490242029 222 LVMHNGEVVERGSTADVLASPLHDLTRRLIA 252
Cdd:PRK10261 240 LVMYQGEAVETGSVEQIFHAPQHPYTRALLA 270
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-229 |
2.54e-40 |
|
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: 137.53 E-value: 2.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTFRyrtgwfhrqTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTfgdysy 85
Cdd:cd03230 1 IEVRNLSKRYG---------KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 rsqkirmifqdpstslnprqrisqildfplrlntdldaearqKQIIDTLRMVGLLPDHVSYYPHM-------LAPGQKQR 158
Cdd:cd03230 66 ------------------------------------------KEPEEVKRRIGYLPEEPSLYENLtvrenlkLSGGMKQR 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490242029 159 LGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHNGEV 229
Cdd:cd03230 104 LALAQALLHDPELLILDEPTSGLDPESRREFWELLRELK-KEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-252 |
3.16e-40 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 145.62 E-value: 3.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 1 MVETLLEVRQLSKTFRYRTgwfhrQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGM-----VEPTSGELLIDD 75
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQ-----TVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 76 HPLTFGDYS----YRSQKIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLDAEARQKQIIDTLRMVGL--LPDHVSYYPH 149
Cdd:PRK15134 76 ESLLHASEQtlrgVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIrqAAKRLTDYPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 150 MLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEV 229
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRC 235
|
250 260
....*....|....*....|...
gi 490242029 230 VERGSTADVLASPLHDLTRRLIA 252
Cdd:PRK15134 236 VEQNRAATLFSAPTHPYTQKLLN 258
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-251 |
4.67e-40 |
|
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: 138.97 E-value: 4.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTFRYRTgwfhrqtvEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSY 85
Cdd:cd03295 1 IEFENVTKRYGGGK--------KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 RSQKIRMIFQdpSTSLNPRQRISQILDFPLRLNtDLDAEARQKQIIDTLRMVGLLPDH-VSYYPHMLAPGQKQRLGLARA 164
Cdd:cd03295 73 LRRKIGYVIQ--QIGLFPHMTVEENIALVPKLL-KWPKEKIRERADELLALVGLDPAEfADRYPHELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 165 LILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVLASPLH 244
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPAN 229
|
....*..
gi 490242029 245 DLTRRLI 251
Cdd:cd03295 230 DFVAEFV 236
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-240 |
5.30e-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: 146.90 E-value: 5.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSktFRYrtgwfHRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLT-FGDYS 84
Cdd:COG2274 474 IELENVS--FRY-----PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRqIDPAS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 85 YRSQkIRMIFQDP---STSL--NprqrisqildfpLRLNtdlDAEARQKQIIDTLRMVGLLPDhVSYYPH---------- 149
Cdd:COG2274 547 LRRQ-IGVVLQDVflfSGTIreN------------ITLG---DPDATDEEIIEAARLAGLHDF-IEALPMgydtvvgegg 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 150 -MLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELqeKQGISYIYVTQHLGMMKHiSDQVLVMHNGE 228
Cdd:COG2274 610 sNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRLSTIRL-ADRIIVLDKGR 686
|
250
....*....|..
gi 490242029 229 VVERGSTADVLA 240
Cdd:COG2274 687 IVEDGTHEELLA 698
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
6-253 |
2.52e-39 |
|
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: 137.77 E-value: 2.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTFRYRTGWFHR----------------QTVeAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSG 69
Cdd:cd03294 1 IKIKGLYKIFGKNPQKAFKllakgkskeeilkktgQTV-GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 70 ELLIDDHPLTFGDYS----YRSQKIRMIFQdpSTSLNPRQRISQILDFPLRLNtDLDAEARQKQIIDTLRMVGLLPDHVS 145
Cdd:cd03294 80 KVLIDGQDIAAMSRKelreLRRKKISMVFQ--SFALLPHRTVLENVAFGLEVQ-GVPRAEREERAAEALELVGLEGWEHK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 146 YyPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMH 225
Cdd:cd03294 157 Y-PDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMK 235
|
250 260
....*....|....*....|....*...
gi 490242029 226 NGEVVERGSTADVLASPLHDLTRRLIAG 253
Cdd:cd03294 236 DGRLVQVGTPEEILTNPANDYVREFFRG 263
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
5-251 |
3.19e-39 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 139.11 E-value: 3.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 5 LLEVRQLSKTFRYRTGWFhrqtvEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVE-P---TSGELLIDDHPLTF 80
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPF-----RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPgrvMAEKLEFNGQDLQR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 81 GDYSYRSQ----KIRMIFQDPSTSLNPRQRIS-QILDfPLRLNTDLDAEARQKQIIDTLRMVGLlPDHVS---YYPHMLA 152
Cdd:PRK11022 78 ISEKERRNlvgaEVAMIFQDPMTSLNPCYTVGfQIME-AIKVHQGGNKKTRRQRAIDLLNQVGI-PDPASrldVYPHQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 153 PGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVER 232
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVET 235
|
250
....*....|....*....
gi 490242029 233 GSTADVLASPLHDLTRRLI 251
Cdd:PRK11022 236 GKAHDIFRAPRHPYTQALL 254
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-228 |
8.31e-39 |
|
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: 133.85 E-value: 8.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTFRYRTgwfhrqtveAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSY 85
Cdd:cd03229 1 LELKNVSKRYGQKT---------VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 RS--QKIRMIFQDPStsLNPRQRISQILDFPLrlntdldaearqkqiidtlrmvgllpdhvsyyphmlAPGQKQRLGLAR 163
Cdd:cd03229 72 PPlrRRIGMVFQDFA--LFPHLTVLENIALGL------------------------------------SGGQQQRVALAR 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490242029 164 ALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGE 228
Cdd:cd03229 114 ALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
6-242 |
3.25e-38 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 137.13 E-value: 3.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTFryrtgwfhrQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTfgDYSY 85
Cdd:COG3839 4 LELENVSKSY---------GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT--DLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 RSQKIRMIFQD----PSTSLnpRQRISqildFPLRLNtDLDAEARQKQIIDTLRMVGLLP--DHvsyYPHMLAPGQKQRL 159
Cdd:COG3839 73 KDRNIAMVFQSyalyPHMTV--YENIA----FPLKLR-KVPKAEIDRRVREAAELLGLEDllDR---KPKQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 160 GLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVT--QHLGMMkhISDQVLVMHNGEVVERGSTAD 237
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVThdQVEAMT--LADRIAVMNDGRIQQVGTPEE 220
|
....*
gi 490242029 238 VLASP 242
Cdd:COG3839 221 LYDRP 225
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-228 |
9.06e-38 |
|
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: 130.58 E-value: 9.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSktFRYRTGwfhrqTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSY 85
Cdd:cd03228 1 IEFKNVS--FSYPGR-----PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 RSQKIRMIFQDPstslnprqrisQILDFPLRLNtdldaearqkqiidtlrmvgllpdhvsyyphMLAPGQKQRLGLARAL 165
Cdd:cd03228 74 LRKNIAYVPQDP-----------FLFSGTIREN-------------------------------ILSGGQRQRIAIARAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490242029 166 ILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHiSDQVLVMHNGE 228
Cdd:cd03228 112 LRDPPILILDEATSALDPETEALILEALRALAKGKTV--IVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-242 |
2.33e-37 |
|
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: 131.79 E-value: 2.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTFryrtGWFHrqtveAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSY 85
Cdd:cd03219 1 LEVRGLTKRF----GGLV-----ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 RSQK-IRMIFQDPS------------TSLNPRQRISQILDFPLRLNTDLDAEARqkqiiDTLRMVGLlpDHVSYYP-HML 151
Cdd:cd03219 72 IARLgIGRTFQIPRlfpeltvlenvmVAAQARTGSGLLLARARREEREARERAE-----ELLERVGL--ADLADRPaGEL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 152 APGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMHNGEVVE 231
Cdd:cd03219 145 SYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSLADRVTVLDQGRVIA 223
|
250
....*....|.
gi 490242029 232 RGSTADVLASP 242
Cdd:cd03219 224 EGTPDEVRNNP 234
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
20-228 |
3.35e-36 |
|
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: 126.21 E-value: 3.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 20 GWFHRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSYRSQKIRMIFQdpst 99
Cdd:cd00267 5 LSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 100 slnprqrisqildfplrlntdldaearqkqiidtlrmvgllpdhvsyyphmLAPGQKQRLGLARALILRPKVIVCDEALA 179
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490242029 180 SLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMHNGE 228
Cdd:cd00267 110 GLDPASRERLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-230 |
1.15e-35 |
|
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: 124.85 E-value: 1.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTFRyrtgwfhrqTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFgdysy 85
Cdd:cd03216 1 LELRGITKRFG---------GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSF----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 rsqkirmifqdpstsLNPRqrisqildfplrlntdldaEARQKQIidtlRMVgllpdhvsyypHMLAPGQKQRLGLARAL 165
Cdd:cd03216 67 ---------------ASPR-------------------DARRAGI----AMV-----------YQLSVGERQMVEIARAL 97
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490242029 166 ILRPKVIVCDEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHNGEVV 230
Cdd:cd03216 98 ARNARLLILDEPTAALTPAEVERLFKVIRRLR-AQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-229 |
1.38e-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: 1.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTFryrtGWFHrqtveAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSY 85
Cdd:cd03262 1 IEIKNLHKSF----GDFH-----VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 RS--QKIRMIFQdpSTSLNPRQRISQILDFPLRLNTDLDAEARQKQIIDTLRMVGLLpDHVSYYPHMLAPGQKQRLGLAR 163
Cdd:cd03262 72 NElrQKVGMVFQ--QFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLA-DKADAYPAQLSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490242029 164 ALILRPKVIVCDEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMHNGEV 229
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAE-EGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-246 |
1.91e-35 |
|
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: 126.91 E-value: 1.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTFRyrtgwfhrQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTF-GDYS 84
Cdd:cd03256 1 IEVENLSKTYP--------NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlKGKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 85 YRSQ--KIRMIFQDPStsLNPRQRISQILDFPlRLNT---------DLDAEARQKQIiDTLRMVGLLPDH---VSYyphm 150
Cdd:cd03256 73 LRQLrrQIGMIFQQFN--LIERLSVLENVLSG-RLGRrstwrslfgLFPKEEKQRAL-AALERVGLLDKAyqrADQ---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 151 LAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVV 230
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
250
....*....|....*.
gi 490242029 231 ERGSTADVLASPLHDL 246
Cdd:cd03256 225 FDGPPAELTDEVLDEI 240
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
14-241 |
2.30e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 127.41 E-value: 2.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 14 TFRYRTgwfhrQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSYRSQKIRMI 93
Cdd:PRK13632 14 SFSYPN-----SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 94 FQDPSTslnprQRI-SQILD---FPLRlNTDLDAEARQKQIIDTLRMVGLLpDHVSYYPHMLAPGQKQRLGLARALILRP 169
Cdd:PRK13632 89 FQNPDN-----QFIgATVEDdiaFGLE-NKKVPPKKMKDIIDDLAKKVGME-DYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490242029 170 KVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHlgmMKHI--SDQVLVMHNGEVVERGSTADVLAS 241
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHD---MDEAilADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-256 |
2.56e-35 |
|
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: 126.70 E-value: 2.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 5 LLEVRQLSktFRYRTgwfhrqtVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTfgDYS 84
Cdd:COG1120 1 MLEAENLS--VGYGG-------RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLA--SLS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 85 YR--SQKIRMIFQDPSTSLN------------PRQRisqildfPLRLNTDLDAEArqkqIIDTLRMVGLlpDHVSYYP-H 149
Cdd:COG1120 70 RRelARRIAYVPQEPPAPFGltvrelvalgryPHLG-------LFGRPSAEDREA----VEEALERTGL--EHLADRPvD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 150 MLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEV 229
Cdd:COG1120 137 ELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
250 260
....*....|....*....|....*..
gi 490242029 230 VERGSTADVlasplhdLTRRLIAGHFG 256
Cdd:COG1120 217 VAQGPPEEV-------LTPELLEEVYG 236
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-241 |
6.36e-35 |
|
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: 131.42 E-value: 6.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSktFRYRTGwfhrqtVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSY 85
Cdd:COG4988 337 IELEDVS--FSYPGG------RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 RSQKIRMIFQDPstslnprqrisQILDFPLRLNTDL-DAEARQKQIIDTLRMVGLLpDHVSYYPHMLA-----------P 153
Cdd:COG4988 409 WRRQIAWVPQNP-----------YLFAGTIRENLRLgRPDASDEELEAALEAAGLD-EFVAALPDGLDtplgeggrglsG 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 154 GQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHiSDQVLVMHNGEVVERG 233
Cdd:COG4988 477 GQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTV--ILITHRLALLAQ-ADRILVLDDGRIVEQG 553
|
....*...
gi 490242029 234 STADVLAS 241
Cdd:COG4988 554 THEELLAK 561
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
29-253 |
6.97e-35 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 129.38 E-value: 6.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 29 AVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLT-FGDYSYRS---QKIRMIFQdpSTSLNPR 104
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkISDAELREvrrKKIAMVFQ--SFALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 105 QRISQILDFPLRLnTDLDAEARQKQIIDTLRMVGLlPDHVSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMS 184
Cdd:PRK10070 121 MTVLDNTAFGMEL-AGINAEERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490242029 185 MRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVLASPLHDLTRRLIAG 253
Cdd:PRK10070 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRG 267
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-238 |
9.22e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 130.52 E-value: 9.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 3 ETLLEVRQLSKTFRyrtgwfhrqTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGD 82
Cdd:COG1129 2 EPLLEMRGISKSFG---------GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 83 YSyRSQK--IRMIFQDPstSLNP-------------------------RQRISQILDfplRLNTDLDAEARqkqiidtlr 135
Cdd:COG1129 73 PR-DAQAagIAIIHQEL--NLVPnlsvaeniflgreprrgglidwramRRRARELLA---RLGLDIDPDTP--------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 136 mVGLLPdhvsyyphmlaPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMK 215
Cdd:COG1129 138 -VGDLS-----------VAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKA-QGVAIIYISHRLDEVF 204
|
250 260
....*....|....*....|...
gi 490242029 216 HISDQVLVMHNGEVVERGSTADV 238
Cdd:COG1129 205 EIADRVTVLRDGRLVGTGPVAEL 227
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
3-242 |
1.39e-34 |
|
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: 125.15 E-value: 1.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 3 ETLLEVRQLSKTFryrtGwfhrqTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTfgd 82
Cdd:COG0411 2 DPLLEVRGLTKRF----G-----GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDIT--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 83 ySYRSQKI-RM----IFQDPS------------TSLNPRQR---ISQILDFPLRLNTDLDAEARqkqIIDTLRMVGLLpD 142
Cdd:COG0411 70 -GLPPHRIaRLgiarTFQNPRlfpeltvlenvlVAAHARLGrglLAALLRLPRARREEREARER---AEELLERVGLA-D 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 143 HVSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVL 222
Cdd:COG0411 145 RADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIV 224
|
250 260
....*....|....*....|
gi 490242029 223 VMHNGEVVERGSTADVLASP 242
Cdd:COG0411 225 VLDFGRVIAEGTPAEVRADP 244
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
34-251 |
1.46e-34 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 124.48 E-value: 1.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 34 SFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTfgDYSYRSQKIRMIFQDpsTSLNPRQRISQILDF 113
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLT--ALPPAERPVSMLFQE--NNLFPHLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 114 PLRLNTDLDAEARQkQIIDTLRMVGLLpDHVSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLM 193
Cdd:COG3840 95 GLRPGLKLTAEQRA-QVEQALERVGLA-GLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490242029 194 LELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVLASPLHDLTRRLI 251
Cdd:COG3840 173 DELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-238 |
2.80e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 124.48 E-value: 2.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 3 ETLLEVRQLSktFRYRT-GWFhrqtveAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFG 81
Cdd:PRK13648 5 NSIIVFKNVS--FQYQSdASF------TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 82 DYSYRSQKIRMIFQDPSTslnprQRISQILDFPLRL---NTDLDAEARQKQIIDTLRMVGLLpDHVSYYPHMLAPGQKQR 158
Cdd:PRK13648 77 NFEKLRKHIGIVFQNPDN-----QFVGSIVKYDVAFgleNHAVPYDEMHRRVSEALKQVDML-ERADYEPNALSGGQKQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 159 LGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHNGEVVERGSTADV 238
Cdd:PRK13648 151 VAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-233 |
3.75e-34 |
|
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: 122.75 E-value: 3.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTFryrtgwfhrQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTfgDYSY 85
Cdd:cd03301 1 VELENVTKRF---------GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 RSQKIRMIFQdpSTSLNPRQRISQILDFPLRLNTDLDAE--ARQKQIIDTLRMVGLLpdhvSYYPHMLAPGQKQRLGLAR 163
Cdd:cd03301 70 KDRDIAMVFQ--NYALYPHMTVYDNIAFGLKLRKVPKDEidERVREVAELLQIEHLL----DRKPKQLSGGQRQRVALGR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 164 ALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERG 233
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
28-235 |
5.98e-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: 5.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 28 EAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVE-----PTSGELLIDDHPLTFGDY---SYRsQKIRMIFQDPst 99
Cdd:cd03260 14 HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVdvlELR-RRVGMVFQKP-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 100 slNP-RQRISQILDFPLRLNTDLDAEARQKQIIDTLRMVGLlPDHVS--YYPHMLAPGQKQRLGLARALILRPKVIVCDE 176
Cdd:cd03260 91 --NPfPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAAL-WDEVKdrLHALGLSGGQQQRLCLARALANEPEVLLLDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490242029 177 ALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHISDQVLVMHNGEVVERGST 235
Cdd:cd03260 168 PTSALDPISTAKIEELIAELKKEYTI--VIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-242 |
7.27e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 122.89 E-value: 7.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 1 MVETLLEVRQLskTFRYRTgwfhrqtVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTF 80
Cdd:COG1121 2 MMMPAIELENL--TVSYGG-------RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 81 GDY--SYRSQKIRMifqDPSTSLNPRQRISQILDFPLRLNTDLDAEARQKqIIDTLRMVGLLPdhvsyyphmLAP----- 153
Cdd:COG1121 73 ARRriGYVPQRAEV---DWDFPITVRDVVLMGRYGRRGLFRRPSRADREA-VDEALERVGLED---------LADrpige 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 154 ---GQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMhNGEVV 230
Cdd:COG1121 140 lsgGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELR-REGKTILVVTHDLGAVREYFDRVLLL-NRGLV 217
|
250
....*....|..
gi 490242029 231 ERGSTADVLASP 242
Cdd:COG1121 218 AHGPPEEVLTPE 229
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
14-231 |
9.63e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 121.70 E-value: 9.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 14 TFRYRTGwfhrqtVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLT---FGDYSYRSQKI 90
Cdd:COG2884 8 SKRYPGG------REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSrlkRREIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 91 RMIFQDpsTSLNPRQRISQILDFPLRLnTDLDAEARQKQIIDTLRMVGLLpDHVSYYPHMLAPGQKQRLGLARALILRPK 170
Cdd:COG2884 82 GVVFQD--FRLLPDRTVYENVALPLRV-TGKSRKEIRRRVREVLDLVGLS-DKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490242029 171 VIVCDEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVE 231
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-249 |
1.04e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 123.37 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 5 LLEVRQLSKTFRyrtgwfhrQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYS 84
Cdd:PRK13652 3 LIETRDLCYSYS--------GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 85 YRSQKIRMIFQDPSTSLNPRQRISQILDFPLrlNTDLDAEARQKQIIDTLRMVGLlPDHVSYYPHMLAPGQKQRLGLARA 164
Cdd:PRK13652 75 EVRKFVGLVFQNPDDQIFSPTVEQDIAFGPI--NLGLDEETVAHRVSSALHMLGL-EELRDRVPHHLSGGEKKRVAIAGV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 165 LILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVLASPlh 244
Cdd:PRK13652 152 IAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP-- 229
|
....*
gi 490242029 245 DLTRR 249
Cdd:PRK13652 230 DLLAR 234
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-258 |
1.09e-33 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 128.36 E-value: 1.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 14 TFRYRTGwfhrqtVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTfgDY---SYRSQkI 90
Cdd:COG1132 346 SFSYPGD------RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIR--DLtleSLRRQ-I 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 91 RMIFQDPstslnprqrisQILDFPLRLNTDL-DAEARQKQIIDTLRMVGL------LPD----HVSYYPHMLAPGQKQRL 159
Cdd:COG1132 417 GVVPQDT-----------FLFSGTIRENIRYgRPDATDEEVEEAAKAAQAhefieaLPDgydtVVGERGVNLSGGQRQRI 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 160 GLARALILRPKVIVCDEALASLD----MSMRSQLINLMlelqekQGISYIYVTQHLGMMKHiSDQVLVMHNGEVVERGST 235
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDteteALIQEALERLM------KGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTH 558
|
250 260
....*....|....*....|...
gi 490242029 236 ADVLASplHDLTRRLIAGHFGEA 258
Cdd:COG1132 559 EELLAR--GGLYARLYRLQFGEE 579
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-242 |
1.23e-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: 1.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTFryrtGWFHRQTVeavkplSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTfgDYSY 85
Cdd:cd03299 1 LKVENLSKDW----KEFKLKNV------SLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 RSQKIRMIFQDpsTSLNPRQRISQILDFPLRLNTDLDAEaRQKQIIDTLRMVGLlpDHV-SYYPHMLAPGQKQRLGLARA 164
Cdd:cd03299 69 EKRDISYVPQN--YALFPHMTVYKNIAYGLKKRKVDKKE-IERKVLEIAEMLGI--DHLlNRKPETLSGGEQQRVAIARA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490242029 165 LILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVLASP 242
Cdd:cd03299 144 LVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-229 |
2.77e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 120.31 E-value: 2.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTFRYRTGWfhrqtveavKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTfgDYS- 84
Cdd:COG4619 1 LELEGLSFRVGGKPIL---------SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLS--AMPp 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 85 --YRSQkIRMIFQDPSTslnPRQRISQILDFPLRLNTDLDAEARqkqIIDTLRMVGLLPDHVSYYPHMLAPGQKQRLGLA 162
Cdd:COG4619 70 peWRRQ-VAYVPQEPAL---WGGTVRDNLPFPFQLRERKFDRER---ALELLERLGLPPDILDKPVERLSGGERQRLALI 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490242029 163 RALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEV 229
Cdd:COG4619 143 RALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
3-246 |
2.77e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 122.15 E-value: 2.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 3 ETLLEVRQLskTFRYRTgwfhRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGD 82
Cdd:PRK13650 2 SNIIEVKNL--TFKYKE----DQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 83 YSYRSQKIRMIFQDPSTslnprQRISQILD----FPLRlNTDLDAEARQKQIIDTLRMVGLLpDHVSYYPHMLAPGQKQR 158
Cdd:PRK13650 76 VWDIRHKIGMVFQNPDN-----QFVGATVEddvaFGLE-NKGIPHEEMKERVNEALELVGMQ-DFKEREPARLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 159 LGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKhISDQVLVMHNGEvVERGSTADV 238
Cdd:PRK13650 149 VAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQ-VESTSTPRE 226
|
....*...
gi 490242029 239 LASPLHDL 246
Cdd:PRK13650 227 LFSRGNDL 234
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-241 |
3.10e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 122.05 E-value: 3.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 1 MVETLLEVRQLSktFRYRtgwfhRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTF 80
Cdd:PRK13635 1 MKEEIIRVEHIS--FRYP-----DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 81 GDYSYRSQKIRMIFQDPSTslnprQRI-SQILD---FPLRlNTDLDAEARQKQIIDTLRMVGLLpDHVSYYPHMLAPGQK 156
Cdd:PRK13635 74 ETVWDVRRQVGMVFQNPDN-----QFVgATVQDdvaFGLE-NIGVPREEMVERVDQALRQVGME-DFLNREPHRLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 157 QRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHNGEVVERGSTA 236
Cdd:PRK13635 147 QRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPE 225
|
....*
gi 490242029 237 DVLAS 241
Cdd:PRK13635 226 EIFKS 230
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-242 |
3.51e-33 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 123.72 E-value: 3.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTFryrtGWFHrqtveAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLtFGDYSY 85
Cdd:COG1118 3 IEVRNISKRF----GSFT-----LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL-FTNLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 RSQKIRMIFQDPStsLNP----RQRISqildFPLRLNTDLDAEARQKqIIDTLRMVGL--LPDHvsyYPHMLAPGQKQRL 159
Cdd:COG1118 73 RERRVGFVFQHYA--LFPhmtvAENIA----FGLRVRPPSKAEIRAR-VEELLELVQLegLADR---YPSQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 160 GLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTqhlgmmkH-------ISDQVLVMHNGEVVER 232
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVT-------HdqeealeLADRVVVMNQGRIEQV 215
|
250
....*....|
gi 490242029 233 GSTADVLASP 242
Cdd:COG1118 216 GTPDEVYDRP 225
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-242 |
5.50e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 121.34 E-value: 5.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 5 LLEVRQLSktFRYRTGwfhrqtVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLtfgDYS 84
Cdd:PRK13639 1 ILETRDLK--YSYPDG------TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI---KYD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 85 YRS-----QKIRMIFQDPSTSL-NPrqRISQILDF-PlrLNTDLDAEARQKQIIDTLRMVGLLpDHVSYYPHMLAPGQKQ 157
Cdd:PRK13639 70 KKSllevrKTVGIVFQNPDDQLfAP--TVEEDVAFgP--LNLGLSKEEVEKRVKEALKAVGME-GFENKPPHHLSGGQKK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 158 RLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTAD 237
Cdd:PRK13639 145 RVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLN-KEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKE 223
|
....*
gi 490242029 238 VLASP 242
Cdd:PRK13639 224 VFSDI 228
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
33-258 |
3.44e-32 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 120.98 E-value: 3.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 33 LSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTfgDYSYRSQKIRMIFQdpSTSLNPRQRISQILD 112
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT--HRSIQQRDICMVFQ--SYALFPHMSLGENVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 113 FPLRLnTDLDAEARQKQIIDTLRMVGL--LPDHvsyYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLI 190
Cdd:PRK11432 101 YGLKM-LGVPKEERKQRVKEALELVDLagFEDR---YVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMR 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490242029 191 NLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVLASPlhdlTRRLIAGHFGEA 258
Cdd:PRK11432 177 EKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP----ASRFMASFMGDA 240
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-242 |
7.16e-32 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 120.82 E-value: 7.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 1 MVETLLEVRQLSKTFryrtgwfhrQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTf 80
Cdd:PRK09452 10 SLSPLVELRGISKSF---------DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 81 gDYSYRSQKIRMIFQdpSTSLNPRQRISQILDFPLRLNTDLDAEARqKQIIDTLRMVGLlPDHVSYYPHMLAPGQKQRLG 160
Cdd:PRK09452 80 -HVPAENRHVNTVFQ--SYALFPHMTVFENVAFGLRMQKTPAAEIT-PRVMEALRMVQL-EEFAQRKPHQLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 161 LARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTqH-----LGMmkhiSDQVLVMHNGEVVERGST 235
Cdd:PRK09452 155 IARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVT-HdqeeaLTM----SDRIVVMRDGRIEQDGTP 229
|
....*..
gi 490242029 236 ADVLASP 242
Cdd:PRK09452 230 REIYEEP 236
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
5-259 |
1.13e-31 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 119.24 E-value: 1.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 5 LLEVRQLSKTFRYRTGWfhrqtVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEP----TSGELLIDDHPLTf 80
Cdd:COG4170 3 LLDIRNLTIEIDTPQGR-----VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 81 gDYSYRSQK------IRMIFQDPSTSLNPRQRISQILDFPLrLNTDLD------AEARQKQIIDTLRMVGLlPDHVSY-- 146
Cdd:COG4170 77 -KLSPRERRkiigreIAMIFQEPSSCLDPSAKIGDQLIEAI-PSWTFKgkwwqrFKWRKKRAIELLHRVGI-KDHKDImn 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 147 -YPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMH 225
Cdd:COG4170 154 sYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLY 233
|
250 260 270
....*....|....*....|....*....|....*.
gi 490242029 226 NGEVVERGSTADVLASPLHDLTRRLI--AGHFGEAL 259
Cdd:COG4170 234 CGQTVESGPTEQILKSPHHPYTKALLrsMPDFRQPL 269
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-231 |
1.27e-31 |
|
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: 116.76 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 1 MVETLLEVRQLSKTFRYRTGwfhrqTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTF 80
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAG-----ELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 81 GD----YSYRSQKIRMIFQDpstslnprqriSQILD---------FPLRLNTDLDAEARQKQIidtLRMVGL--LPDHvs 145
Cdd:COG4181 79 LDedarARLRARHVGFVFQS-----------FQLLPtltalenvmLPLELAGRRDARARARAL---LERVGLghRLDH-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 146 yYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHiSDQVLVMH 225
Cdd:COG4181 143 -YPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLR 220
|
....*.
gi 490242029 226 NGEVVE 231
Cdd:COG4181 221 AGRLVE 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
29-238 |
2.53e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 117.11 E-value: 2.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 29 AVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLID--DHPLTFGDYSYRsQKIRMIFQDPSTslnprQR 106
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDglDTSDEENLWDIR-NKAGMVFQNPDN-----QI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 107 ISQILDFPLRL---NTDLDAEARQKQIIDTLRMVGLLpDHVSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDM 183
Cdd:PRK13633 99 VATIVEEDVAFgpeNLGIPPEEIRERVDESLKKVGMY-EYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490242029 184 SMRSQLINLMLELQEKQGISYIYVTQHlgMMKHI-SDQVLVMHNGEVVERGSTADV 238
Cdd:PRK13633 178 SGRREVVNTIKELNKKYGITIILITHY--MEEAVeADRIIVMDSGKVVMEGTPKEI 231
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-240 |
3.21e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 116.87 E-value: 3.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 1 MVETLLEVRQLSktFRYRTGwfhrqtVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLtf 80
Cdd:PRK13636 1 MEDYILKVEELN--YNYSDG------THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 81 gDYSYRS-----QKIRMIFQDPSTSLNpRQRISQILDFPLrLNTDLDAEARQKQIIDTLRMVGLlpDHVSYYP-HMLAPG 154
Cdd:PRK13636 71 -DYSRKGlmklrESVGMVFQDPDNQLF-SASVYQDVSFGA-VNLKLPEDEVRKRVDNALKRTGI--EHLKDKPtHCLSFG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 155 QKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGS 234
Cdd:PRK13636 146 QKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGN 225
|
....*.
gi 490242029 235 TADVLA 240
Cdd:PRK13636 226 PKEVFA 231
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
6-240 |
3.56e-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: 121.03 E-value: 3.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSktFRYRTgwfhrQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSY 85
Cdd:COG4987 334 LELEDVS--FRYPG-----AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 RSQKIRMIFQDP---STSL--NprqrisqildfpLRL-NTDLDAEarqkQIIDTLRMVGL------LPD----HVSYYPH 149
Cdd:COG4987 407 LRRRIAVVPQRPhlfDTTLreN------------LRLaRPDATDE----ELWAALERVGLgdwlaaLPDgldtWLGEGGR 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 150 MLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHIsDQVLVMHNGEV 229
Cdd:COG4987 471 RLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTV--LLITHRLAGLERM-DRILVLEDGRI 547
|
250
....*....|.
gi 490242029 230 VERGSTADVLA 240
Cdd:COG4987 548 VEQGTHEELLA 558
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-256 |
3.79e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 115.90 E-value: 3.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 3 ETLLEVRQLSktFRYrtGWFHrqtveAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVE--P---TSGELLIDDHP 77
Cdd:COG1117 9 EPKIEVRNLN--VYY--GDKQ-----ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 78 LtfgdysYRSQ--------KIRMIFQDPstslNPrqrisqildFP----------LRLNtdldaEARQKQIID-----TL 134
Cdd:COG1117 80 I------YDPDvdvvelrrRVGMVFQKP----NP---------FPksiydnvaygLRLH-----GIKSKSELDeiveeSL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 135 RMVGLlPDHVSYYPHM----LAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGIsyIYVTqH 210
Cdd:COG1117 136 RKAAL-WDEVKDRLKKsalgLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTI--VIVT-H 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 490242029 211 lgMMKH---ISDQVLVMHNGEVVERGSTADVLASPLHDLTRRLIAGHFG 256
Cdd:COG1117 212 --NMQQaarVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTEDYITGRFG 258
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
34-242 |
6.24e-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: 6.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 34 SFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLtfgdysYRSQK----------IRMIFQDPStsLNP 103
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL------QDSARgiflpphrrrIGYVFQEAR--LFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 104 RQRISQILDFPLRLNTDLDAEARQKQIIDTLRMVGLLpDHvsyYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDM 183
Cdd:COG4148 91 HLSVRGNLLYGRKRAPRAERRISFDEVVELLGIGHLL-DR---RPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490242029 184 SMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVLASP 242
Cdd:COG4148 167 ARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-233 |
2.02e-30 |
|
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: 112.14 E-value: 2.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 7 EVRQLSktFRYRTGWfhrqtveAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLtfgdysyr 86
Cdd:cd03214 1 EVENLS--VGYGGRT-------VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDL-------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 87 sqkirmifqdpsTSLNPRQRISQILDFPlrlntdldaearqkQIIDTLRMVGLLPDHVSyyphMLAPGQKQRLGLARALI 166
Cdd:cd03214 64 ------------ASLSPKELARKIAYVP--------------QALELLGLAHLADRPFN----ELSGGERQRVLLARALA 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490242029 167 LRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERG 233
Cdd:cd03214 114 QEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
21-241 |
2.28e-30 |
|
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: 113.47 E-value: 2.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 21 WF-HRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPL-TFGDYSYRSqKIRMIFQDP- 97
Cdd:cd03254 9 NFsYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIrDISRKSLRS-MIGVVLQDTf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 98 --STSlnprqrisqILDfPLRLNTDldaEARQKQIIDTLRMVGL------LPDHVSYYP----HMLAPGQKQRLGLARAL 165
Cdd:cd03254 88 lfSGT---------IME-NIRLGRP---NATDEEVIEAAKEAGAhdfimkLPNGYDTVLgengGNLSQGERQLLAIARAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490242029 166 ILRPKVIVCDEALASLDMSMRSQLINLMLELQEkqGISYIYVTQHLGMMKHiSDQVLVMHNGEVVERGSTADVLAS 241
Cdd:cd03254 155 LRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLAK 227
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-236 |
2.34e-30 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 112.98 E-value: 2.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTfrYRTGWFHrqtveAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSY 85
Cdd:cd03263 1 LQIRNLTKT--YKKGTKP-----AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 RsQKIRMIFQDPS--TSLNPRqrisQILDFPLRL----NTDLDAEarqkqIIDTLRMVGLLpDHVSYYPHMLAPGQKQRL 159
Cdd:cd03263 74 R-QSLGYCPQFDAlfDELTVR----EHLRFYARLkglpKSEIKEE-----VELLLRVLGLT-DKANKRARTLSGGMKRKL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490242029 160 GLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHISDQVLVMHNGEVVERGSTA 236
Cdd:cd03263 143 SLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSI--ILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQ 217
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-202 |
4.44e-30 |
|
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: 111.80 E-value: 4.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 5 LLEVRQLSKTFRYRTgwfhrqtveAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYS 84
Cdd:COG4133 2 MLEAENLSCRRGERL---------LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 85 YRSQkirMIFQDPSTSLNPRQRISQILDFPLRLNTDLDAEARQKQIIDTLRMVGLLpdHVsyYPHMLAPGQKQRLGLARA 164
Cdd:COG4133 73 YRRR---LAYLGHADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGLA--DL--PVRQLSAGQKRRVALARL 145
|
170 180 190
....*....|....*....|....*....|....*...
gi 490242029 165 LILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGI 202
Cdd:COG4133 146 LLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGA 183
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
27-253 |
6.20e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 112.70 E-value: 6.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 27 VEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVE-----PTSGELLIDDHPLTFGDYSYRSQKIRMIFQDPSTSl 101
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPI- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 102 nPRQRISQILDFPLRLN----TDLDAEARQKQIIDTLRMVGLLPDHVSYYPHMLAPGQKQRLGLARALILRPKVIVCDEA 177
Cdd:PRK14247 95 -PNLSIFENVALGLKLNrlvkSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490242029 178 LASLDMSMRSQLINLMLELqeKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVLASPLHDLTRRLIAG 253
Cdd:PRK14247 174 TANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEKYVTG 247
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-242 |
1.29e-29 |
|
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: 111.66 E-value: 1.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTFryrtGWFhrqtvEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTfgDYSY 85
Cdd:cd03296 3 IEVRNVSKRF----GDF-----VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT--DVPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 RSQKIRMIFQDpsTSLNPRQRISQILDFPLRL---NTDLDAEARQKQIIDTLRMVGL--LPDHvsyYPHMLAPGQKQRLG 160
Cdd:cd03296 72 QERNVGFVFQH--YALFRHMTVFDNVAFGLRVkprSERPPEAEIRAKVHELLKLVQLdwLADR---YPAQLSGGQRQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 161 LARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVLA 240
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
..
gi 490242029 241 SP 242
Cdd:cd03296 227 HP 228
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
33-242 |
1.59e-29 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 111.26 E-value: 1.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 33 LSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTF----GDYSYRS--QKIRMIFQdpSTSLNPRQR 106
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFsktpSDKAIRElrRNVGMVFQ--QYNLWPHLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 107 ISQIL-DFPLRLN--TDLDAEARQKQIIDTLRmvglLPDHVSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDM 183
Cdd:PRK11124 99 VQQNLiEAPCRVLglSKDQALARAEKLLERLR----LKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490242029 184 SMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGsTADVLASP 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 ... |
14-233 |
2.68e-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: 109.89 E-value: 2.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 14 TFRYRTGWFHrqtveavkpLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSYRSqkIRMI 93
Cdd:cd03298 7 RFSYGEQPMH---------FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP--VSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 94 FQDpsTSLNPRQRISQILDFPLRLNTDLDAEARQKqIIDTLRMVGLlPDHVSYYPHMLAPGQKQRLGLARALILRPKVIV 173
Cdd:cd03298 76 FQE--NNLFAHLTVEQNVGLGLSPGLKLTAEDRQA-IEVALARVGL-AGLEKRLPGELSGGERQRVALARVLVRDKPVLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 174 CDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERG 233
Cdd:cd03298 152 LDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
9-242 |
4.72e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 111.27 E-value: 4.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 9 RQLSKTFRYRTGwFHRQtveAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFG----DYS 84
Cdd:PRK13634 6 QKVEHRYQYKTP-FERR---ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGkknkKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 85 YRSQKIRMIFQDPSTSLNPRQRISQILDFPLRLN-TDLDAEARQKQIIDtlrMVGLLPDHVSYYPHMLAPGQKQRLGLAR 163
Cdd:PRK13634 82 PLRKKVGIVFQFPEHQLFEETVEKDICFGPMNFGvSEEDAKQKAREMIE---LVGLPEELLARSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490242029 164 ALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVLASP 242
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
15-233 |
4.74e-29 |
|
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: 109.31 E-value: 4.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 15 FRYRTGWFHRQtveavkpLSFTLRErQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFG----DYSYRSQKI 90
Cdd:cd03297 6 IEKRLPDFTLK-------IDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSrkkiNLPPQQRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 91 RMIFQDpsTSLNPRQRISQILDFPLRLNTDLDAEARQKQIIDTLRMvgllpDHVSY-YPHMLAPGQKQRLGLARALILRP 169
Cdd:cd03297 78 GLVFQQ--YALFPHLNVRENLAFGLKRKRNREDRISVDELLDLLGL-----DHLLNrYPAQLSGGEKQRVALARALAAQP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490242029 170 KVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERG 233
Cdd:cd03297 151 ELLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
28-238 |
1.33e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 110.14 E-value: 1.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 28 EAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTfgDYSYRSQKIR----MIFQDPSTSLNp 103
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDIT--DKKVKLSDIRkkvgLVFQYPEYQLF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 104 RQRISQILDFPLRlNTDLDAEARQKQIIDTLRMVGLlpDHVSY---YPHMLAPGQKQRLGLARALILRPKVIVCDEALAS 180
Cdd:PRK13637 98 EETIEKDIAFGPI-NLGLSEEEIENRVKRAMNIVGL--DYEDYkdkSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490242029 181 LDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADV 238
Cdd:PRK13637 175 LDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
26-261 |
1.84e-28 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 109.02 E-value: 1.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 26 TVEAVKPL----SFTLRERQTLAIIGENGSGKSTLAKMLAGMVEP----TSGELLIDDHPLTFGdySYRSQKIRMIFQDP 97
Cdd:PRK10418 11 ALQAAQPLvhgvSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPC--ALRGRKIATIMQNP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 98 STSLNPRQRISQILDFPLRLntdLDAEARQKQIIDTLRMVGLLPDH--VSYYPHMLAPGQKQRLGLARALILRPKVIVCD 175
Cdd:PRK10418 89 RSAFNPLHTMHTHARETCLA---LGKPADDATLTAALEAVGLENAArvLKLYPFEMSGGMLQRMMIALALLCEAPFIIAD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 176 EALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVLASPLHDLTRRLIAGH- 254
Cdd:PRK10418 166 EPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSAHl 245
|
....*....
gi 490242029 255 --FGEALTA 261
Cdd:PRK10418 246 alYGMELAS 254
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-240 |
4.42e-28 |
|
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: 112.20 E-value: 4.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 3 ETLLEVRQLSKtfRYRTgwFHRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGEL-------LIDD 75
Cdd:TIGR03269 277 EPIIKVRNVSK--RYIS--VDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDM 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 76 HPLTFGDYSYRSQKIRMIFQD----PSTSL--NPRQRISqiLDFPLRLntdldaeARQKQIIdTLRMVGLLPDH----VS 145
Cdd:TIGR03269 353 TKPGPDGRGRAKRYIGILHQEydlyPHRTVldNLTEAIG--LELPDEL-------ARMKAVI-TLKMVGFDEEKaeeiLD 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 146 YYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMH 225
Cdd:TIGR03269 423 KYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMR 502
|
250
....*....|....*
gi 490242029 226 NGEVVERGSTADVLA 240
Cdd:TIGR03269 503 DGKIVKIGDPEEIVE 517
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-242 |
6.48e-28 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 109.92 E-value: 6.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 5 LLEVRQLSKTFryrtgwfhrQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTfgDYS 84
Cdd:PRK11607 19 LLEIRNLTKSF---------DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 85 YRSQKIRMIFQdpSTSLNPRQRISQILDFPLRLNTDLDAEARQKqIIDTLRMVGLLpDHVSYYPHMLAPGQKQRLGLARA 164
Cdd:PRK11607 88 PYQRPINMMFQ--SYALFPHMTVEQNIAFGLKQDKLPKAEIASR-VNEMLGLVHMQ-EFAKRKPHQLSGGQRQRVALARS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490242029 165 LILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVLASP 242
Cdd:PRK11607 164 LAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
14-234 |
8.82e-28 |
|
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: 106.42 E-value: 8.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 14 TFRYRTGwfhrqTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPL-TFGDYSYRSQkIRM 92
Cdd:cd03244 9 SLRYRPN-----LPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDIsKIGLHDLRSR-ISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 93 IFQDPstslnprqrisQILDFPLRLNTDLDAEARQKQIIDTLRMVGLLpDHVSYYPHML-----------APGQKQRLGL 161
Cdd:cd03244 83 IPQDP-----------VLFSGTIRSNLDPFGEYSDEELWQALERVGLK-EFVESLPGGLdtvveeggenlSVGQRQLLCL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490242029 162 ARALILRPKVIVCDEALASLDMSMRSQLINLmleLQEK-QGISYIYVTQHLGMMKHiSDQVLVMHNGEVVERGS 234
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDPETDALIQKT---IREAfKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDS 220
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-253 |
1.51e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 106.67 E-value: 1.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 30 VKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSYRSQKIR------MIFQDPSTSlnP 103
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAIKlrkevgMVFQQPNPF--P 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 104 RQRISQILDFPLRLNTDLDAEARQKQIIDTLRMVGL---LPDHVSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALAS 180
Cdd:PRK14246 104 HLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwkeVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490242029 181 LDMSMRSQLINLMLELqeKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVLASPLHDLTRRLIAG 253
Cdd:PRK14246 184 IDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYVIG 254
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
6-240 |
1.77e-27 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 105.93 E-value: 1.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTFR-YRTGWF------------HRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELL 72
Cdd:COG1134 5 IEVENVSKSYRlYHEPSRslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 73 IDDH---PLTFG-----DYSYRsQKIRMIFqdpstSLN------PRQRISQILDFplrlnTDL-DAearqkqiIDTlrmv 137
Cdd:COG1134 85 VNGRvsaLLELGagfhpELTGR-ENIYLNG-----RLLglsrkeIDEKFDEIVEF-----AELgDF-------IDQ---- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 138 gllPdhVSYYPhmlaPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHI 217
Cdd:COG1134 143 ---P--VKTYS----SGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRE-SGRTVIFVSHSMGAVRRL 212
|
250 260
....*....|....*....|...
gi 490242029 218 SDQVLVMHNGEVVERGSTADVLA 240
Cdd:COG1134 213 CDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
30-241 |
2.15e-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: 110.22 E-value: 2.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 30 VKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLT------FGDY-SYRSQKIrmifqdpstSLN 102
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSqwdreeLGRHiGYLPQDV---------ELF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 103 P---RQRISqildfplRLnTDLDAEArqkqIIDTLRMVGL------LPD----HVSYYPHMLAPGQKQRLGLARALILRP 169
Cdd:COG4618 419 DgtiAENIA-------RF-GDADPEK----VVAAAKLAGVhemilrLPDgydtRIGEGGARLSGGQRQRIGLARALYGDP 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490242029 170 KVIVCDEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHiSDQVLVMHNGEVVERGSTADVLAS 241
Cdd:COG4618 487 RLVVLDEPNSNLDDEGEAALAAAIRALKA-RGATVVVITHRPSLLAA-VDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
28-230 |
2.56e-27 |
|
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: 104.92 E-value: 2.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 28 EAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFG--DYSYRSQKirmifqdpsTSLNPRQ 105
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKErkRIGYVPQR---------RSIDRDF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 106 RISqILDF-------PLRLNTDLDAEARQKqIIDTLRMVGLLpdHVSYYP-HMLAPGQKQRLGLARALILRPKVIVCDEA 177
Cdd:cd03235 84 PIS-VRDVvlmglygHKGLFRRLSKADKAK-VDEALERVGLS--ELADRQiGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490242029 178 LASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMhNGEVV 230
Cdd:cd03235 160 FAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL-NRTVV 210
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-252 |
2.84e-27 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 105.78 E-value: 2.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 1 MVETLLEVRQLSKTFRYRTGwFHRqtveavkpLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTF 80
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKG-CRD--------VSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 81 GD-YSYRSQKIRMIF--------QDPSTSLnpRQRISQILDFPLRLNT-------DLDAEArqkqiIDTLRMVGLLPDHV 144
Cdd:PRK11701 73 RDlYALSEAERRRLLrtewgfvhQHPRDGL--RMQVSAGGNIGERLMAvgarhygDIRATA-----GDWLERVEIDAARI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 145 SYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVM 224
Cdd:PRK11701 146 DDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVM 225
|
250 260
....*....|....*....|....*...
gi 490242029 225 HNGEVVERGSTADVLASPLHDLTRRLIA 252
Cdd:PRK11701 226 KQGRVVESGLTDQVLDDPQHPYTQLLVS 253
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
5-241 |
4.33e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 105.95 E-value: 4.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 5 LLEVRQLskTFRYRTgwfhRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYS 84
Cdd:PRK13642 4 ILEVENL--VFKYEK----ESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 85 YRSQKIRMIFQDPSTSLnPRQRISQILDFPLRlNTDLDAEARQKQIIDTLRMVGLLpDHVSYYPHMLAPGQKQRLGLARA 164
Cdd:PRK13642 78 NLRRKIGMVFQNPDNQF-VGATVEDDVAFGME-NQGIPREEMIKRVDEALLAVNML-DFKTREPARLSGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490242029 165 LILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHNGEVVERGSTADVLAS 241
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFAT 230
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
41-229 |
7.67e-27 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 104.76 E-value: 7.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 41 QTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLtfgdySYRSQKIRMIFQDpsTSLNPRQRIsqILDFPLRLNTD 120
Cdd:PRK11247 39 QFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPL-----AEAREDTRLMFQD--ARLLPWKKV--IDNVGLGLKGQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 121 LDAEARQkqiidTLRMVGLlPDHVSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQ 200
Cdd:PRK11247 110 WRDAALQ-----ALAAVGL-ADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQH 183
|
170 180
....*....|....*....|....*....
gi 490242029 201 GISYIYVTQHLGMMKHISDQVLVMHNGEV 229
Cdd:PRK11247 184 GFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
14-240 |
1.18e-26 |
|
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: 103.77 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 14 TFRYRTgwfhRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPL-TFGDYSYRSQkIRM 92
Cdd:cd03249 7 SFRYPS----RPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIrDLNLRWLRSQ-IGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 93 IFQDPstslnprqrisQILDFPLRLNTDL-DAEARQKQIIDTLRMVGL------LPD----HVSYYPHMLAPGQKQRLGL 161
Cdd:cd03249 82 VSQEP-----------VLFDGTIAENIRYgKPDATDEEVEEAAKKANIhdfimsLPDgydtLVGERGSQLSGGQKQRIAI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490242029 162 ARALILRPKVIVCDEALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHNGEVVERGSTADVLA 240
Cdd:cd03249 151 ARALLRNPKILLLDEATSALD-AESEKLVQEALD-RAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMA 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
22-230 |
1.33e-26 |
|
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: 102.72 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 22 FHRQTvEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDysyRSQKIRMIFQDPStsl 101
Cdd:cd03226 9 YKKGT-EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIGYVMQDVD--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 102 npRQRISQILDFPLRLNTDL--DAEARQKQIIDTLRMVGLLPDHvsyyPHMLAPGQKQRLGLARALILRPKVIVCDEALA 179
Cdd:cd03226 82 --YQLFTDSVREELLLGLKEldAGNEQAETVLKDLDLYALKERH----PLSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490242029 180 SLDM-SMRSqLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHNGEVV 230
Cdd:cd03226 156 GLDYkNMER-VGELIRELA-AQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-240 |
2.11e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 103.93 E-value: 2.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 21 WFHRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLtfgDYSYRS-----QKIRMIFQ 95
Cdd:PRK13638 8 WFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL---DYSKRGllalrQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 96 DPSTSLNpRQRISQILDFPLRlNTDLDAEARQKQIIDTLRMVGllPDHVSYYP-HMLAPGQKQRLGLARALILRPKVIVC 174
Cdd:PRK13638 85 DPEQQIF-YTDIDSDIAFSLR-NLGVPEAEITRRVDEALTLVD--AQHFRHQPiQCLSHGQKKRVAIAGALVLQARYLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490242029 175 DEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVLA 240
Cdd:PRK13638 161 DEPTAGLDPAGRTQMIAIIRRIVA-QGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
14-229 |
2.18e-26 |
|
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: 102.93 E-value: 2.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 14 TFRYRTgwfhRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSYRSQKIRMI 93
Cdd:cd03248 18 TFAYPT----RPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 94 FQDP---STSLnpRQRISQILDfplRLNTDLDAEARQKQIIDTLrmVGLLPD----HVSYYPHMLAPGQKQRLGLARALI 166
Cdd:cd03248 94 GQEPvlfARSL--QDNIAYGLQ---SCSFECVKEAAQKAHAHSF--ISELASgydtEVGEKGSQLSGGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490242029 167 LRPKVIVCDEALASLDMSMRSQLINLMLELQEKQgiSYIYVTQHLGMMKHiSDQVLVMHNGEV 229
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
47-230 |
2.33e-26 |
|
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: 102.40 E-value: 2.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 47 GENGSGKSTLAKMLAGMVEPTSGELLIDDHPLtFGDYSYRSQKIR----MIFQDPS--TSLNPRQRISQILDfplrLNTD 120
Cdd:TIGR02982 38 GPSGSGKTTLLTLIGGLRSVQEGSLKVLGQEL-HGASKKQLVQLRrrigYIFQAHNllGFLTARQNVQMALE----LQPN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 121 LDAEARQKQIIDTLRMVGLlPDHVSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQ 200
Cdd:TIGR02982 113 LSYQEARERARAMLEAVGL-GDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQ 191
|
170 180 190
....*....|....*....|....*....|
gi 490242029 201 GISYIYVTqHLGMMKHISDQVLVMHNGEVV 230
Cdd:TIGR02982 192 GCTILMVT-HDNRILDVADRILQMEDGKLL 220
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
28-241 |
2.34e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 104.32 E-value: 2.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 28 EAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSYRSQK-----IRMIFQDPSTSLN 102
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVKrlrkeIGLVFQFPEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 103 pRQRISQILDF-PLRLNTDldAEARQKQIIDTLRMVGLLPDHVSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASL 181
Cdd:PRK13645 105 -QETIEKDIAFgPVNLGEN--KQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 182 DMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVLAS 241
Cdd:PRK13645 182 DPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-259 |
2.99e-26 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 104.88 E-value: 2.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 5 LLEVRQLSKTFRYRTGWfhrqtVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEP----TSGELLIDDHPLTf 80
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGW-----VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 81 gDYSYRSQK------IRMIFQDPSTSLNPRQRISQ--ILDFP---------LRLNTdldaeaRQKQIIDTLRMVGLlPDH 143
Cdd:PRK15093 77 -RLSPRERRklvghnVSMIFQEPQSCLDPSERVGRqlMQNIPgwtykgrwwQRFGW------RKRRAIELLHRVGI-KDH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 144 ---VSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQ 220
Cdd:PRK15093 149 kdaMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADK 228
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 490242029 221 VLVMHNGEVVERGSTADVLASPLHDLTRRLIAG--HFGEAL 259
Cdd:PRK15093 229 INVLYCGQTVETAPSKELVTTPHHPYTQALIRAipDFGSAM 269
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
28-241 |
3.07e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 103.71 E-value: 3.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 28 EAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFG--DYSYRS--QKIRMIFQDPSTSLNP 103
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkDKYIRPvrKRIGMVFQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 104 RQRISQILDFPLRLNTDLDaEARQKQIiDTLRMVGLLPDHVSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDM 183
Cdd:PRK13646 101 DTVEREIIFGPKNFKMNLD-EVKNYAH-RLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490242029 184 SMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVLAS 241
Cdd:PRK13646 179 QSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
14-233 |
3.97e-26 |
|
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: 101.50 E-value: 3.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 14 TFRYRTGWfhrqtveAVKPLSFTLrERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSYRsQKIRMI 93
Cdd:cd03264 7 TKRYGKKR-------ALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLR-RRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 94 FQDPSTSlnPRQRISQILDFPLRLNTDLDAEARqKQIIDTLRMVGLLpDHVSYYPHMLAPGQKQRLGLARALILRPKVIV 173
Cdd:cd03264 78 PQEFGVY--PNFTVREFLDYIAWLKGIPSKEVK-ARVDEVLELVNLG-DRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 174 CDEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHISDQVLVMHNGEVVERG 233
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELGEDRIV--ILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-240 |
4.60e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 104.01 E-value: 4.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 7 EVRQLSKTFRYR----------TGWFHRQ--TVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLID 74
Cdd:COG4586 3 EVENLSKTYRVYekepglkgalKGLFRREyrEVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 75 DH-PltfgdysYRSQK-----IRMIFQdpstslnprQRiSQIL-DFP----LRLNTDL----DAEARQ--KQIIDTLRMV 137
Cdd:COG4586 83 GYvP-------FKRRKefarrIGVVFG---------QR-SQLWwDLPaidsFRLLKAIyripDAEYKKrlDELVELLDLG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 138 GLLPDHVsyypHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHI 217
Cdd:COG4586 146 ELLDTPV----RQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEAL 221
|
250 260
....*....|....*....|...
gi 490242029 218 SDQVLVMHNGEVVERGSTADVLA 240
Cdd:COG4586 222 CDRVIVIDHGRIIYDGSLEELKE 244
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-233 |
5.96e-26 |
|
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: 101.14 E-value: 5.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTFryrtgwfhrQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDhpltfgdysy 85
Cdd:cd03268 1 LKTNDLTKTY---------GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG---------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 rsqkirmifQDPSTSLNPRQRISQILDFP-----LRLNTDLDAEARQ----KQIID-TLRMVGLlpdhvSYYPHMLAP-- 153
Cdd:cd03268 62 ---------KSYQKNIEALRRIGALIEAPgfypnLTARENLRLLARLlgirKKRIDeVLDVVGL-----KDSAKKKVKgf 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 154 --GQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQeKQGISyIYVTQH-LGMMKHISDQVLVMHNGEVV 230
Cdd:cd03268 128 slGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLR-DQGIT-VLISSHlLSEIQKVADRIGIINKGKLI 205
|
...
gi 490242029 231 ERG 233
Cdd:cd03268 206 EEG 208
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-233 |
6.87e-26 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 106.34 E-value: 6.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 2 VETLLEVRQLSktFRYRTgwfhRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFG 81
Cdd:TIGR00958 475 LEGLIEFQDVS--FSYPN----RPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQY 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 82 DYSYRSQKIRMIFQDPST-SLNPRQRISQILDFplRLNTDLDAEARQKQIIDtlrMVGLLPD----HVSYYPHMLAPGQK 156
Cdd:TIGR00958 549 DHHYLHRQVALVGQEPVLfSGSVRENIAYGLTD--TPDEEIMAAAKAANAHD---FIMEFPNgydtEVGEKGSQLSGGQK 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490242029 157 QRLGLARALILRPKVIVCDEALASLDmsmrSQLINLMLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHNGEVVERG 233
Cdd:TIGR00958 624 QRIAIARALVRKPRVLILDEATSALD----AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMG 695
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
26-235 |
7.32e-26 |
|
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: 101.29 E-value: 7.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 26 TVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHpltfgDYSYRSQKIR----MIFQDPstSL 101
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGH-----DVVREPREVRrrigIVFQDL--SV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 102 NPRQRISQILDFPLRLNTDLDAEARQKqIIDTLRMVGLLP---DHVSYYphmlAPGQKQRLGLARALILRPKVIVCDEAL 178
Cdd:cd03265 85 DDELTGWENLYIHARLYGVPGAERRER-IDELLDFVGLLEaadRLVKTY----SGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490242029 179 ASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGST 235
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
27-240 |
9.08e-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: 100.97 E-value: 9.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 27 VEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTfgdySYRSQKI-----------RMIFQ 95
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT----GLPPHERaragigyvpegRRIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 96 D------------PSTSLNPRQRISQILD-FPlRLntdldaEARQKQiidtlrMVGLlpdhvsyyphmLAPGQKQRLGLA 162
Cdd:cd03224 89 EltveenlllgayARRRAKRKARLERVYElFP-RL------KERRKQ------LAGT-----------LSGGEQQMLAIA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490242029 163 RALILRPKVIVCDEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVLA 240
Cdd:cd03224 145 RALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRD-EGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-242 |
1.73e-25 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 100.55 E-value: 1.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 5 LLEVRQLSKTFryrtgwfhrQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDhpLTFGDYS 84
Cdd:PRK09493 1 MIEFKNVSKHF---------GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 85 YRSQKIR----MIFQdpSTSLNPRQRISQILDF-PLRLNTDLDAEARqKQIIDTLRMVGLlPDHVSYYPHMLAPGQKQRL 159
Cdd:PRK09493 70 VDERLIRqeagMVFQ--QFYLFPHLTALENVMFgPLRVRGASKEEAE-KQARELLAKVGL-AERAHHYPSELSGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 160 GLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVL 239
Cdd:PRK09493 146 AIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAE-EGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLI 224
|
...
gi 490242029 240 ASP 242
Cdd:PRK09493 225 KNP 227
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
30-238 |
2.47e-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: 100.23 E-value: 2.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 30 VKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTfgdysyRSQKIRMI-FQDpsTSLNP----R 104
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT------EPGPDRMVvFQN--YSLLPwltvR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 105 QRISQILDfplRLNTDLDAEARQKQIIDTLRMVGLlPDHVSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMS 184
Cdd:TIGR01184 73 ENIALAVD---RVLPDLSKSERRAIVEEHIALVGL-TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490242029 185 MRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADV 238
Cdd:TIGR01184 149 TRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-233 |
2.79e-25 |
|
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: 99.75 E-value: 2.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 5 LLEVRQLSKTFRYRtgwfhRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTfgdYS 84
Cdd:cd03266 1 MITADALTKRFRDV-----KKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV---KE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 85 YRSQKIRMIFQDPSTSLNPRQRISQILDFPLRL---NTDlDAEARQKQIIDTLRMVGLLPDHVSyyphMLAPGQKQRLGL 161
Cdd:cd03266 73 PAEARRRLGFVSDSTGLYDRLTARENLEYFAGLyglKGD-ELTARLEELADRLGMEELLDRRVG----GFSTGMRQKVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490242029 162 ARALILRPKVIVCDEALASLDMsMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERG 233
Cdd:cd03266 148 ARALVHDPPVLLLDEPTTGLDV-MATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
14-241 |
3.21e-25 |
|
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: 99.87 E-value: 3.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 14 TFRYRTgwfhrQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSYRSQKIRMI 93
Cdd:cd03252 7 RFRYKP-----DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 94 FQDpstslnprqriSQILDFPLRLNTDL-DAEARQKQIIDTLRMVGL------LPDHvsyYPHM-------LAPGQKQRL 159
Cdd:cd03252 82 LQE-----------NVLFNRSIRDNIALaDPGMSMERVIEAAKLAGAhdfiseLPEG---YDTIvgeqgagLSGGQRQRI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 160 GLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEkqGISYIYVTQHLGMMKHiSDQVLVMHNGEVVERGSTADVL 239
Cdd:cd03252 148 AIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELL 224
|
..
gi 490242029 240 AS 241
Cdd:cd03252 225 AE 226
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
4-251 |
3.52e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 100.21 E-value: 3.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 4 TLLEVRQLSKTFryrtgwfHRQTVeaVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSG-----ELLID-DHP 77
Cdd:PRK11264 2 SAIEVKNLVKKF-------HGQTV--LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDtARS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 78 LTFGDYSYRS--QKIRMIFQdpSTSLNP-RQRISQILDFPLRLNTDL--DAEARQKQIidtLRMVGLLPDHVSYyPHMLA 152
Cdd:PRK11264 73 LSQQKGLIRQlrQHVGFVFQ--NFNLFPhRTVLENIIEGPVIVKGEPkeEATARAREL---LAKVGLAGKETSY-PRRLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 153 PGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLEL-QEKQgiSYIYVTQHLGMMKHISDQVLVMHNGEVVE 231
Cdd:PRK11264 147 GGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLaQEKR--TMVIVTHEMSFARDVADRAIFMDQGRIVE 224
|
250 260
....*....|....*....|
gi 490242029 232 RGSTADVLASPLHDLTRRLI 251
Cdd:PRK11264 225 QGPAKALFADPQQPRTRQFL 244
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-242 |
4.93e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 100.64 E-value: 4.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 1 MVETLLEVRQLSKTFRyrtgwfhRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGE---LLIDDHP 77
Cdd:PRK13640 1 MKDNIVEFKHVSFTYP-------DSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGIT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 78 LTFGDYSYRSQKIRMIFQDPSTSLnPRQRISQILDFPLRlNTDLDAEARQKQIIDTLRMVGLLpDHVSYYPHMLAPGQKQ 157
Cdd:PRK13640 74 LTAKTVWDIREKVGIVFQNPDNQF-VGATVGDDVAFGLE-NRAVPRPEMIKIVRDVLADVGML-DYIDSEPANLSGGQKQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 158 RLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHNGEVVERGSTAD 237
Cdd:PRK13640 151 RVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVE 229
|
....*
gi 490242029 238 VLASP 242
Cdd:PRK13640 230 IFSKV 234
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
5-227 |
6.54e-25 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 99.12 E-value: 6.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 5 LLEVRQLSKtfRYRTGWFHrqtVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPL----TF 80
Cdd:PRK11629 5 LLQCDNLCK--RYQEGSVQ---TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklsSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 81 GDYSYRSQKIRMIFQdpSTSLNPRQRISQILDFPLRLNTDLDAEARQKQiIDTLRMVGLlpDHVSYY-PHMLAPGQKQRL 159
Cdd:PRK11629 80 AKAELRNQKLGFIYQ--FHHLLPDFTALENVAMPLLIGKKKPAEINSRA-LEMLAAVGL--EHRANHrPSELSGGERQRV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490242029 160 GLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQvLVMHNG 227
Cdd:PRK11629 155 AIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQ-LEMRDG 221
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-240 |
7.70e-25 |
|
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: 98.84 E-value: 7.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 14 TFRYRTGwfhrqtVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSYRSQKIRMI 93
Cdd:cd03253 7 TFAYDPG------RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 94 FQDpsTSLnprqrisqiLDFPLRLNT---DLDA------EARQKQIIDTLRMVglLPDH----VSYYPHMLAPGQKQRLG 160
Cdd:cd03253 81 PQD--TVL---------FNDTIGYNIrygRPDAtdeeviEAAKAAQIHDKIMR--FPDGydtiVGERGLKLSGGEKQRVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 161 LARALILRPKVIVCDEALASLDMSMRSQLINLMLELqeKQGISYIYVTQHLGMMKHiSDQVLVMHNGEVVERGSTADVLA 240
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAALRDV--SKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLA 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
32-240 |
8.18e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 98.89 E-value: 8.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 32 PLSFTLR----ERqtLAIIGENGSGKSTLAKMLAGMVEPTSGELLID--DHPLTfgdySYRSQKIRMIFQDPS--TSLNP 103
Cdd:PRK10771 15 PMRFDLTvergER--VAILGPSGAGKSTLLNLIAGFLTPASGSLTLNgqDHTTT----PPSRRPVSMLFQENNlfSHLTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 104 RQRISQILDFPLRLNtdldaEARQKQIIDTLRMVGLLpDHVSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDM 183
Cdd:PRK10771 89 AQNIGLGLNPGLKLN-----AAQREKLHAIARQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490242029 184 SMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVLA 240
Cdd:PRK10771 163 ALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-238 |
8.82e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 102.80 E-value: 8.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 1 MVETLLEVRQLSKTFryrtGwfhrqTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTF 80
Cdd:COG3845 1 MMPPALELRGITKRF----G-----GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 81 GDYSY-RSQKIRMIFQ------------------DPSTSLNP-----RQRISQILD-FPLRLntDLDAEARQkqiidtlr 135
Cdd:COG3845 72 RSPRDaIALGIGMVHQhfmlvpnltvaenivlglEPTKGGRLdrkaaRARIRELSErYGLDV--DPDAKVED-------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 136 mvgllpdhvsyyphmLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMK 215
Cdd:COG3845 142 ---------------LSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAA-EGKSIIFITHKLREVM 205
|
250 260
....*....|....*....|...
gi 490242029 216 HISDQVLVMHNGEVVERGSTADV 238
Cdd:COG3845 206 AIADRVTVLRRGKVVGTVDTAET 228
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-233 |
1.04e-24 |
|
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: 97.74 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTFRyrtgwfhrqTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSy 85
Cdd:cd03269 1 LEVENVTKRFG---------RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARN- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 rsqkiRMIFQDPSTSLNPRQRISQILDFPLRLNtDLDAEARQKQIIDTLRMVGlLPDHVSYYPHMLAPGQKQRLGLARAL 165
Cdd:cd03269 71 -----RIGYLPEERGLYPKMKVIDQLVYLAQLK-GLKKEEARRRIDEWLERLE-LSEYANKRVEELSKGNQQKVQFIAAV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490242029 166 ILRPKVIVCDEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHNGEVVERG 233
Cdd:cd03269 144 IHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
33-242 |
3.24e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 98.36 E-value: 3.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 33 LSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSYRSQKIR----MIFQDPSTSLNPRQRIS 108
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLRkkvsLVFQFPEAQLFENTVLK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 109 QILDFPLRLNTDlDAEARQKQiIDTLRMVGLLPDHVSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQ 188
Cdd:PRK13641 106 DVEFGPKNFGFS-EDEAKEKA-LKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKE 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490242029 189 LINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVLASP 242
Cdd:PRK13641 184 MMQLFKDYQ-KAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
6-233 |
4.82e-24 |
|
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: 96.63 E-value: 4.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTFRYRT----------GWFHR--QTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLI 73
Cdd:cd03267 1 IEVSNLSKSYRVYSkepgligslkSLFKRkyREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 74 DDhpltFGDYSYRSQKIRMIfqdpstSLNPRQRISQILDFP----LRLNTDL----DAEARQ--KQIIDTLRMVGLLPDH 143
Cdd:cd03267 81 AG----LVPWKRRKKFLRRI------GVVFGQKTQLWWDLPvidsFYLLAAIydlpPARFKKrlDELSELLDLEELLDTP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 144 VsyypHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLV 223
Cdd:cd03267 151 V----RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLV 226
|
250
....*....|
gi 490242029 224 MHNGEVVERG 233
Cdd:cd03267 227 IDKGRLLYDG 236
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-224 |
5.44e-24 |
|
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: 96.35 E-value: 5.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 3 ETLLEVRQLSKTFRyrtgwFHRQ---TVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDhplt 79
Cdd:COG4778 2 TTLLEVENLSKTFT-----LHLQggkRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRH---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 80 fgdysyRSQKIRMIFQDPSTSLNPRQR----ISQILDF------------PLR-LNTDLD-AEARQKQIIDTLRmvglLP 141
Cdd:COG4778 73 ------DGGWVDLAQASPREILALRRRtigyVSQFLRViprvsaldvvaePLLeRGVDREeARARARELLARLN----LP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 142 DHV-SYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQ 220
Cdd:COG4778 143 ERLwDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAK-ARGTAIIGIFHDEEVREAVADR 221
|
....
gi 490242029 221 VLVM 224
Cdd:COG4778 222 VVDV 225
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
6-241 |
1.90e-23 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 99.02 E-value: 1.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSktFRYRTGwfhrQTVeaVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSY 85
Cdd:PRK10790 341 IDIDNVS--FAYRDD----NLV--LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSV 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 RSQKIRMIFQDPStslnprqrisqILDFPLRLNTDLDAEARQKQIIDTLRMVGL------LPD----HVSYYPHMLAPGQ 155
Cdd:PRK10790 413 LRQGVAMVQQDPV-----------VLADTFLANVTLGRDISEEQVWQALETVQLaelarsLPDglytPLGEQGNNLSVGQ 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 156 KQRLGLARALILRPKVIVCDEALASLDmSMRSQLINLMLELQEKQgISYIYVTQHLGMMKHiSDQVLVMHNGEVVERGST 235
Cdd:PRK10790 482 KQLLALARVLVQTPQILILDEATANID-SGTEQAIQQALAAVREH-TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTH 558
|
....*.
gi 490242029 236 ADVLAS 241
Cdd:PRK10790 559 QQLLAA 564
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-229 |
2.43e-23 |
|
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: 93.05 E-value: 2.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSktFRYRTGwfhRQTVeaVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSY 85
Cdd:cd03246 1 LEVENVS--FRYPGA---EPPV--LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 RSQKIRMIFQDpstslnprqrisqildfplrlntdldaearqkqiidtlrmVGLLPDHVSyyPHMLAPGQKQRLGLARAL 165
Cdd:cd03246 74 LGDHVGYLPQD----------------------------------------DELFSGSIA--ENILSGGQRQRLGLARAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490242029 166 ILRPKVIVCDEALASLDmSMRSQLINLMLELQEKQGISYIYVTQHLGMMKhISDQVLVMHNGEV 229
Cdd:cd03246 112 YGNPRILVLDEPNSHLD-VEGERALNQAIAALKAAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
28-240 |
5.24e-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: 97.89 E-value: 5.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 28 EAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSYRSQKIRMIFQDP---------S 98
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPyifsgsileN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 99 TSLNPRQRISQ---------------ILDFPLRLNTDLDAEARQkqiidtlrmvgllpdhvsyyphmLAPGQKQRLGLAR 163
Cdd:TIGR01193 568 LLLGAKENVSQdeiwaaceiaeikddIENMPLGYQTELSEEGSS-----------------------ISGGQKQRIALAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490242029 164 ALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKqgiSYIYVTQHLGMMKHiSDQVLVMHNGEVVERGSTADVLA 240
Cdd:TIGR01193 625 ALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELLD 697
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-240 |
5.35e-23 |
|
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: 97.86 E-value: 5.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 2 VETLLEVRQLskTFRYRTgwfhrQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTfg 81
Cdd:TIGR02203 327 ARGDVEFRNV--TFRYPG-----RDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLA-- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 82 DYSYR---------SQKIrMIFQDpSTSLN---------PRQRISQILdfplrlntdldAEARQKQIIDtlRMVGLLPDH 143
Cdd:TIGR02203 398 DYTLAslrrqvalvSQDV-VLFND-TIANNiaygrteqaDRAEIERAL-----------AAAYAQDFVD--KLPLGLDTP 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 144 VSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQekQGISYIYVTQHLGMMKHiSDQVLV 223
Cdd:TIGR02203 463 IGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLM--QGRTTLVIAHRLSTIEK-ADRIVV 539
|
250
....*....|....*..
gi 490242029 224 MHNGEVVERGSTADVLA 240
Cdd:TIGR02203 540 MDDGRIVERGTHNELLA 556
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-233 |
7.48e-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: 91.99 E-value: 7.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSktFRYRtgwfhRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSy 85
Cdd:cd03247 1 LSINNVS--FSYP-----EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 RSQKIRMIFQDPstslnprqrisQILDFPLRLNtdldaearqkqiidtlrmVGLlpdhvsyyphMLAPGQKQRLGLARAL 165
Cdd:cd03247 73 LSSLISVLNQRP-----------YLFDTTLRNN------------------LGR----------RFSGGERQRLALARIL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490242029 166 ILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHIsDQVLVMHNGEVVERG 233
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTL--IWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-256 |
1.48e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 93.30 E-value: 1.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 1 MVETLLEVRQLSKTFRYRtgwfhrqtvEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGM--VEP---TSGELLIDD 75
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKK---------KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 76 HPLtfgdYSYRS------QKIRMIFQDPstslNP-RQRISQILDFPLRLNTDLDAEARQKQIIDTLRMVGL---LPDHVS 145
Cdd:PRK14239 72 HNI----YSPRTdtvdlrKEIGMVFQQP----NPfPMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIwdeVKDRLH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 146 YYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHISDQVLVMH 225
Cdd:PRK14239 144 DSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTM--LLVTRSMQQASRISDRTGFFL 221
|
250 260 270
....*....|....*....|....*....|.
gi 490242029 226 NGEVVERGSTADVLASPLHDLTRRLIAGHFG 256
Cdd:PRK14239 222 DGDLIEYNDTKQMFMNPKHKETEDYISGKFG 252
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
28-234 |
1.67e-22 |
|
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: 92.09 E-value: 1.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 28 EAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSYRSQKIRMIFQDPStslnprqri 107
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPT--------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 108 sqILDFPLRLNTDLDAEARQKQIIDTLRmvgllpdhVSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRS 187
Cdd:cd03369 93 --LFSGTIRSNLDPFDEYSDEEIYGALR--------VSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490242029 188 QLINLMLElqEKQGISYIYVTQHLGMMKHIsDQVLVMHNGEVVERGS 234
Cdd:cd03369 163 LIQKTIRE--EFTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDH 206
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-238 |
1.99e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 96.01 E-value: 1.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 1 MVETLLEVRQLSKTFryrtgwfhrQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHpltf 80
Cdd:PRK09700 1 MATPYISMAGIGKSF---------GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNI---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 81 gDYSYRSQK------IRMIFQDPS-----TSLNP----RQRISQILDFPLrlntdLD-AEARQKQIIDTLRmVGLLPDhV 144
Cdd:PRK09700 68 -NYNKLDHKlaaqlgIGIIYQELSvidelTVLENlyigRHLTKKVCGVNI-----IDwREMRVRAAMMLLR-VGLKVD-L 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 145 SYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVM 224
Cdd:PRK09700 140 DEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLR-KEGTAIVYISHKLAEIRRICDRYTVM 218
|
250
....*....|....
gi 490242029 225 HNGEVVERGSTADV 238
Cdd:PRK09700 219 KDGSSVCSGMVSDV 232
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
25-233 |
2.16e-22 |
|
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: 91.88 E-value: 2.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 25 QTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSYRSQKIRMIFQDPStslnpr 104
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVT------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 105 qrisqiLDF-PLRLNTDL-DAEARQKQIIDTLRMVGL---LPDHVSYYPHM-------LAPGQKQRLGLARALILRPKVI 172
Cdd:cd03245 89 ------LFYgTLRDNITLgAPLADDERILRAAELAGVtdfVNKHPNGLDLQigergrgLSGGQRQAVALARALLNDPPIL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490242029 173 VCDEALASLDMSMRSQLI-NLMLELQEKqgiSYIYVTQHLGMMKhISDQVLVMHNGEVVERG 233
Cdd:cd03245 163 LLDEPTSAMDMNSEERLKeRLRQLLGDK---TLIIITHRPSLLD-LVDRIIVMDSGRIVADG 220
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-242 |
3.37e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 92.34 E-value: 3.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 1 MVETLLEVRQLSKtfRYRTGwfhrqtvEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLT- 79
Cdd:PRK10619 1 MSENKLNVIDLHK--RYGEH-------EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINl 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 80 ----------FGDYSYRSQKIR--MIFQDPSTsLNPRQRISQILDFPLRLNTDLDAEARQKQIIdTLRMVGLLPDHVSYY 147
Cdd:PRK10619 72 vrdkdgqlkvADKNQLRLLRTRltMVFQHFNL-WSHMTVLENVMEAPIQVLGLSKQEARERAVK-YLAKVGIDERAQGKY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 148 PHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMHNG 227
Cdd:PRK10619 150 PVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFARHVSSHVIFLHQG 228
|
250
....*....|....*
gi 490242029 228 EVVERGSTADVLASP 242
Cdd:PRK10619 229 KIEEEGAPEQLFGNP 243
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-242 |
4.60e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 92.99 E-value: 4.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 5 LLEVRQLSKTFRYRTgwfhRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDD-----HPLT 79
Cdd:PRK13631 21 ILRVKNLYCVFDEKQ----ENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdKKNN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 80 FGDYSYRSQK-----------IRMIFQDPSTSLNPRQRISQILDFPLRLNTDlDAEARQKQIIdTLRMVGLLPDHVSYYP 148
Cdd:PRK13631 97 HELITNPYSKkiknfkelrrrVSMVFQFPEYQLFKDTIEKDIMFGPVALGVK-KSEAKKLAKF-YLNKMGLDDSYLERSP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 149 HMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHISDQVLVMHNGE 228
Cdd:PRK13631 175 FGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGK 253
|
250
....*....|....
gi 490242029 229 VVERGSTADVLASP 242
Cdd:PRK13631 254 ILKTGTPYEIFTDQ 267
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
29-246 |
6.91e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 91.97 E-value: 6.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 29 AVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDhpLTFGDYSyRSQKIR----MIFQDPSTSLNPR 104
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFS-KLQGIRklvgIVFQNPETQFVGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 105 QrISQILDFPLRlNTDLDAEARQKQIIDTLRMVGlLPDHVSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMS 184
Cdd:PRK13644 94 T-VEEDLAFGPE-NLCLPPIEIRKRVDRALAEIG-LEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490242029 185 MRSQLINLMLELQEKqGISYIYVTQHLGMMkHISDQVLVMHNGEVVERGSTADVLASP-LHDL 246
Cdd:PRK13644 171 SGIAVLERIKKLHEK-GKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDVsLQTL 231
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-224 |
9.20e-22 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 94.28 E-value: 9.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSktFRYRTGWfhrqtvEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSY 85
Cdd:TIGR02857 322 LEFSGVS--VAYPGRR------PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 RSQKIRMIFQDPstslnprqrisQILDFPLRLNTDL-DAEARQKQIIDTLRMVGL------LPDH----VSYYPHMLAPG 154
Cdd:TIGR02857 394 WRDQIAWVPQHP-----------FLFAGTIAENIRLaRPDASDAEIREALERAGLdefvaaLPQGldtpIGEGGAGLSGG 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 155 QKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELqeKQGISYIYVTQHLGMMkHISDQVLVM 224
Cdd:TIGR02857 463 QAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL--AQGRTVLLVTHRLALA-ALADRIVVL 529
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
28-256 |
1.68e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 90.29 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 28 EAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVE-----PTSGELLIddhpltFGDYSYRS--------QKIRMIF 94
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRL------FGRNIYSPdvdpievrREVGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 95 QDPSTSlnPRQRISQILDFPLRLNTDLDAEARQKQIID-TLRMVGL---LPDHVSYYPHMLAPGQKQRLGLARALILRPK 170
Cdd:PRK14267 92 QYPNPF--PHLTIYDNVAIGVKLNGLVKSKKELDERVEwALKKAALwdeVKDRLNDYPSNLSGGQRQRLVIARALAMKPK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 171 VIVCDEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVLASPLHDLTRRL 250
Cdd:PRK14267 170 ILLMDEPTANIDPVGTAKIEELLFELKKEYTI--VLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKY 247
|
....*.
gi 490242029 251 IAGHFG 256
Cdd:PRK14267 248 VTGALG 253
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-239 |
2.35e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 89.83 E-value: 2.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 4 TLLEVRQLSktfrYRTGwfHRQTVEAVkplSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTfgdy 83
Cdd:PRK13548 1 AMLEARNLS----VRLG--GRTLLDDV---SLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLA---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 84 SYRSQ---KIRMIFqdpstslnpRQRISqiLDFPLR--------LNTDLDAEARQKQIIDT-LRMVGLLPDHVSYYPHmL 151
Cdd:PRK13548 68 DWSPAelaRRRAVL---------PQHSS--LSFPFTveevvamgRAPHGLSRAEDDALVAAaLAQVDLAHLAGRDYPQ-L 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 152 APGQKQRLGLARALI------LRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMH 225
Cdd:PRK13548 136 SGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLH 215
|
250
....*....|....
gi 490242029 226 NGEVVERGSTADVL 239
Cdd:PRK13548 216 QGRLVADGTPAEVL 229
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
46-256 |
3.34e-21 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 91.63 E-value: 3.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 46 IGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSYRSqkIRMIFQdpSTSLNPRQRISQILDFPLRLNTDLDAEA 125
Cdd:PRK11000 35 VGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG--VGMVFQ--SYALYPHLSVAENMSFGLKLAGAKKEEI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 126 RQK--QIIDTLRMVGLLPDHvsyyPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGIS 203
Cdd:PRK11000 111 NQRvnQVAEVLQLAHLLDRK----PKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRT 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490242029 204 YIYVTQhlgmmkhisDQVLVMHNGE---VVERGSTADVlASPL---HDLTRRLIAGHFG 256
Cdd:PRK11000 187 MIYVTH---------DQVEAMTLADkivVLDAGRVAQV-GKPLelyHYPANRFVAGFIG 235
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-229 |
3.45e-21 |
|
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: 87.87 E-value: 3.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 3 ETLLEVRQLSktfryrtgwfhrqTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGD 82
Cdd:cd03215 2 EPVLEVRGLS-------------VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 83 YSYR-SQKIRMIFQDpstslnpRQRISQILDFPLRLNTDLdaearqkqiidtlrmvgllpdhvsyyPHMLAPGQKQRLGL 161
Cdd:cd03215 69 PRDAiRAGIAYVPED-------RKREGLVLDLSVAENIAL--------------------------SSLLSGGNQQKVVL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490242029 162 ARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMHNGEV 229
Cdd:cd03215 116 ARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAD-AGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
24-241 |
4.00e-21 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 89.37 E-value: 4.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 24 RQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSG-ELLIDDHplTFGDYSYRSQKIRMIFQDPSTSLN 102
Cdd:COG1119 13 RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGE--RRGGEDVWELRKRIGLVSPALQLR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 103 PRQRISqILD------FP-LRLNTDLDAEARQK--QIIDTLRMVGLLpDHvsyYPHMLAPGQKQRLGLARALILRPKVIV 173
Cdd:COG1119 91 FPRDET-VLDvvlsgfFDsIGLYREPTDEQRERarELLELLGLAHLA-DR---PFGTLSQGEQRRVLIARALVKDPELLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490242029 174 CDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLG-MMKHISdQVLVMHNGEVVERGSTADVLAS 241
Cdd:COG1119 166 LDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeIPPGIT-HVLLLKDGRVVAAGPKEEVLTS 233
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-230 |
4.26e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 89.37 E-value: 4.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTFryrtgwfHRQTVE---AVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTF-G 81
Cdd:COG1101 2 LELKNLSKTF-------NPGTVNekrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKlP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 82 DYSyRSQKIRMIFQDPSTSLNPRQRISQIL--------DFPLRLNTDldaEARQKQIIDTLRMVGL-LPDHVSYYPHMLA 152
Cdd:COG1101 75 EYK-RAKYIGRVFQDPMMGTAPSMTIEENLalayrrgkRRGLRRGLT---KKRRELFRELLATLGLgLENRLDTKVGLLS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 153 PGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHlgmMKH---ISDQVLVMHNGEV 229
Cdd:COG1101 151 GGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHN---MEQaldYGNRLIMMHEGRI 227
|
.
gi 490242029 230 V 230
Cdd:COG1101 228 I 228
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
26-229 |
5.73e-21 |
|
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: 88.23 E-value: 5.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 26 TVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTfgDY-----SYRSQKIRMIFQDpsTS 100
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS--DLrgraiPYLRRKIGVVFQD--FR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 101 LNPRQRISQILDFPLRLnTDLDAEARQKQIIDTLRMVGLLPDHVSyYPHMLAPGQKQRLGLARALILRPKVIVCDEALAS 180
Cdd:cd03292 89 LLPDRNVYENVAFALEV-TGVPPREIRKRVPAALELVGLSHKHRA-LPAELSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490242029 181 LDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHNGEV 229
Cdd:cd03292 167 LDPDTTWEIMNLLKKIN-KAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-233 |
9.43e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 88.64 E-value: 9.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 2 VETLLEVRQLskTFRYRTGwfhrqtVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFG 81
Cdd:PRK13647 1 MDNIIEVEDL--HFRYKDG------TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 82 DYSYRSQKIRMIFQDPSTSLNPRQRISQILDFPLrlNTDLDAEARQKQIIDTLRMVGLLpDHVSYYPHMLAPGQKQRLGL 161
Cdd:PRK13647 73 NEKWVRSKVGLVFQDPDDQVFSSTVWDDVAFGPV--NMGLDKDEVERRVEEALKAVRMW-DFRDKPPYHLSYGQKKRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490242029 162 ARALILRPKVIVCDEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERG 233
Cdd:PRK13647 150 AGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLH-NQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-241 |
9.53e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 89.01 E-value: 9.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTFryrtgwfhrQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYsy 85
Cdd:COG4152 2 LELKGLTKRF---------GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDR-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 rsQKI------RmifqdpstSLNPRQRISQILDFPLRLN--TDLDAEARQKQIIDTLRMVGLLPDHVsyypHMLAPGQKQ 157
Cdd:COG4152 71 --RRIgylpeeR--------GLYPKMKVGEQLVYLARLKglSKAEAKRRADEWLERLGLGDRANKKV----EELSKGNQQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 158 RLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTAD 237
Cdd:COG4152 137 KVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDE 215
|
....
gi 490242029 238 VLAS 241
Cdd:COG4152 216 IRRQ 219
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
44-238 |
1.18e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 88.65 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 44 AIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSYRSQKIR----MIFQDPSTSLNPRQRISQILDFPLRLN- 118
Cdd:PRK13649 37 AFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRkkvgLVFQFPESQLFEETVLKDVAFGPQNFGv 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 119 TDLDAE--ARQKqiidtLRMVGLLPDHVSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLEL 196
Cdd:PRK13649 117 SQEEAEalAREK-----LALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKL 191
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490242029 197 QEKqGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADV 238
Cdd:PRK13649 192 HQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
14-240 |
1.21e-20 |
|
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: 87.67 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 14 TFRYRtgwfhRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTfgDYSYRS--QKIR 91
Cdd:cd03251 7 TFRYP-----GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVR--DYTLASlrRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 92 MIFQDP---STSLNPRQRISqildfplrlntdlDAEARQKQIIDTLRMVGL------LPDHvsyYPHM-------LAPGQ 155
Cdd:cd03251 80 LVSQDVflfNDTVAENIAYG-------------RPGATREEVEEAARAANAhefimeLPEG---YDTVigergvkLSGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 156 KQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEkqGISYIYVTQHLGMMKHiSDQVLVMHNGEVVERGST 235
Cdd:cd03251 144 RQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTH 220
|
....*
gi 490242029 236 ADVLA 240
Cdd:cd03251 221 EELLA 225
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-208 |
1.27e-20 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 87.53 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 2 VETLLEVRQLSKtfryRTGWFHRQtVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFG 81
Cdd:PRK10584 3 AENIVEVHHLKK----SVGQGEHE-LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 82 D----YSYRSQKIRMIFQdpSTSLNPRQRISQILDFPLRLNTDLDAEARQkQIIDTLRMVGlLPDHVSYYPHMLAPGQKQ 157
Cdd:PRK10584 78 DeearAKLRAKHVGFVFQ--SFMLIPTLNALENVELPALLRGESSRQSRN-GAKALLEQLG-LGKRLDHLPAQLSGGEQQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490242029 158 RLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVT 208
Cdd:PRK10584 154 RVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVT 204
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
13-238 |
1.49e-20 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 91.24 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 13 KTFRYRTGWFH---RQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDD-HPLTFGDYSYRSQ 88
Cdd:PTZ00265 381 KKIQFKNVRFHydtRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDsHNLKDINLKWWRS 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 89 KIRMIFQDP-----------------------------------STSLNPRQ--RISQILDFPLRLNT----DLDAEARQ 127
Cdd:PTZ00265 461 KIGVVSQDPllfsnsiknnikyslyslkdlealsnyynedgndsQENKNKRNscRAKCAGDLNDMSNTtdsnELIEMRKN 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 128 KQIIDTLRMVG-----LLPDHVSYYP-----------HMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLIN 191
Cdd:PTZ00265 541 YQTIKDSEVVDvskkvLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 490242029 192 LMLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHNGevvERGSTADV 238
Cdd:PTZ00265 621 TINNLKGNENRITIIIAHRLSTIRY-ANTIFVLSNR---ERGSTVDV 663
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
6-233 |
1.61e-20 |
|
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: 87.20 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTFR---YRTGWFHRQ----------TVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELL 72
Cdd:cd03220 1 IELENVSKSYPtykGGSSSLKKLgilgrkgevgEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 73 ID---DHPLTFG-----DYSYRsQKIRMI--FQDPSTSLnPRQRISQILDFplrlnTDLdaearqKQIIDTlrmvgllpd 142
Cdd:cd03220 81 VRgrvSSLLGLGggfnpELTGR-ENIYLNgrLLGLSRKE-IDEKIDEIIEF-----SEL------GDFIDL--------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 143 HVSYYphmlAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISyIYVTQHLGMMKHISDQVL 222
Cdd:cd03220 139 PVKTY----SSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTV-ILVSHDPSSIKRLCDRAL 213
|
250
....*....|.
gi 490242029 223 VMHNGEVVERG 233
Cdd:cd03220 214 VLEKGKIRFDG 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-243 |
2.49e-20 |
|
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: 86.83 E-value: 2.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTFRYRTgwfhrqtveAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSY 85
Cdd:cd03218 1 LRAENLSKRYGKRK---------VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 RSQK-IRMIFQDPST--SLNPRQRISQILDFplrlnTDLDAEARQKQIIDTLRMVGL--LPDHVSYYphmLAPGQKQRLG 160
Cdd:cd03218 72 RARLgIGYLPQEASIfrKLTVEENILAVLEI-----RGLSKKEREEKLEELLEEFHIthLRKSKASS---LSGGERRRVE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 161 LARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKqGISyIYVTQH-----LGmmkhISDQVLVMHNGEVVERGST 235
Cdd:cd03218 144 IARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDR-GIG-VLITDHnvretLS----ITDRAYIIYEGKVLAEGTP 217
|
....*...
gi 490242029 236 ADVLASPL 243
Cdd:cd03218 218 EEIAANEL 225
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
44-243 |
6.25e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 87.62 E-value: 6.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 44 AIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLtfgdySYRSQKI------RMI---FQDpsTSLNPRQRISQILDFP 114
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVL-----FDAEKGIclppekRRIgyvFQD--ARLFPHYKVRGNLRYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 115 LrlntdldAEARQKQIIDTLRMVGLLPdHVSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLML 194
Cdd:PRK11144 101 M-------AKSMVAQFDKIVALLGIEP-LLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490242029 195 ELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVLASPL 243
Cdd:PRK11144 173 RLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-258 |
7.54e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 85.81 E-value: 7.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 1 MVETLLEVRQLSKTFryrtgwfhrQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTf 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRF---------GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 81 gdySYRSQKI-RM----------IFQDPSTSLN-----PRQR----ISQILDFPLRLNTDLDAEARQKQIIDTlrmVGLL 140
Cdd:PRK11300 71 ---GLPGHQIaRMgvvrtfqhvrLFREMTVIENllvaqHQQLktglFSGLLKTPAFRRAESEALDRAATWLER---VGLL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 141 pDHVSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQ 220
Cdd:PRK11300 145 -EHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDR 223
|
250 260 270
....*....|....*....|....*....|....*...
gi 490242029 221 VLVMHNGEVVERGSTADVLASPlhdltrRLIAGHFGEA 258
Cdd:PRK11300 224 IYVVNQGTPLANGTPEEIRNNP------DVIKAYLGEA 255
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
44-239 |
1.14e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 85.94 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 44 AIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSYRSQKIR----MIFQDPSTSLNPRQRISQILDFPLrlNT 119
Cdd:PRK13643 36 ALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRkkvgVVFQFPESQLFEETVLKDVAFGPQ--NF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 120 DLDAEARQKQIIDTLRMVGLLPDHVSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLmLELQEK 199
Cdd:PRK13643 114 GIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQL-FESIHQ 192
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490242029 200 QGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVL 239
Cdd:PRK13643 193 SGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
33-261 |
2.11e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 85.15 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 33 LSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSG-----ELLIDDHPLtfgdYSYRS-----QKIRMIFQDPstslN 102
Cdd:PRK14271 40 VSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSI----FNYRDvlefrRRVGMLFQRP----N 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 103 PrqrisqildFPLRLNTDLDAEARQKQIIDT----------LRMVGL---LPDHVSYYPHMLAPGQKQRLGLARALILRP 169
Cdd:PRK14271 112 P---------FPMSIMDNVLAGVRAHKLVPRkefrgvaqarLTEVGLwdaVKDRLSDSPFRLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 170 KVIVCDEALASLDMSMRSQLINLMLELQEKqgISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVLASPLHDLTRR 249
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETAR 260
|
250
....*....|..
gi 490242029 250 LIAGHFGEALTA 261
Cdd:PRK14271 261 YVAGLSGDVKDA 272
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-237 |
3.37e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 86.64 E-value: 3.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 5 LLEVRQLSKTFryrtgwfhrQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYS 84
Cdd:PRK15439 11 LLCARSISKQY---------SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 85 YRSQ-KIRMIFQDPstSLNPRQRISQ-ILdfpLRLNTDLDAEARQKQIIDTLrmvgllpdHVSYYPHMLAP----GQKQR 158
Cdd:PRK15439 82 KAHQlGIYLVPQEP--LLFPNLSVKEnIL---FGLPKRQASMQKMKQLLAAL--------GCQLDLDSSAGslevADRQI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490242029 159 LGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTAD 237
Cdd:PRK15439 149 VEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLA-QGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTAD 226
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
30-242 |
1.02e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 85.28 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 30 VKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVePTSGELLIDDHPLTFGDYSYRSQKIRMIFQDPstslnprqrisQ 109
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNP-----------Q 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 110 ILDFPLRLNTDL-DAEARQKQIIDTLRMVGLLpDHVSYYPHMLAP-----------GQKQRLGLARALILRPKVIVCDEA 177
Cdd:PRK11174 434 LPHGTLRDNVLLgNPDASDEQLQQALENAWVS-EFLPLLPQGLDTpigdqaaglsvGQAQRLALARALLQPCQLLLLDEP 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490242029 178 LASLDmsMRS-QLINLMLElQEKQGISYIYVTQHLGMMKHIsDQVLVMHNGEVVERGSTADVLASP 242
Cdd:PRK11174 513 TASLD--AHSeQLVMQALN-AASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
33-243 |
1.14e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 82.75 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 33 LSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLT-FGDYSYrSQKIRMIFQDPST--SLNPRQRI-- 107
Cdd:PRK11231 21 LSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISmLSSRQL-ARRLALLPQHHLTpeGITVRELVay 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 108 --SQILDFPLRLNTD---LDAEARQKQIIDTLrMVGLLPDhvsyyphmLAPGQKQRLGLARALILRPKVIVCDEALASLD 182
Cdd:PRK11231 100 grSPWLSLWGRLSAEdnaRVNQAMEQTRINHL-ADRRLTD--------LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490242029 183 MSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVLASPL 243
Cdd:PRK11231 171 INHQVELMRLMRELNT-QGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGL 230
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-211 |
1.23e-18 |
|
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: 85.10 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSktFRYRTGwfhrqtVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSY 85
Cdd:TIGR02868 335 LELRDLS--AGYPGA------PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 RSQKIRMIFQDPstslnprqrisQILDFPLRLNTDLDA-EARQKQIIDTLRMVGLLpDHVSYYPH-----------MLAP 153
Cdd:TIGR02868 407 VRRRVSVCAQDA-----------HLFDTTVRENLRLARpDATDEELWAALERVGLA-DWLRALPDgldtvlgeggaRLSG 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490242029 154 GQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMleLQEKQGISYIYVTQHL 211
Cdd:TIGR02868 475 GERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
41-242 |
2.29e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 83.21 E-value: 2.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 41 QTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIddHPLTFGDYSYRSQKIRMIFQDpsTSLNPRQRISQILDFPLRL--- 117
Cdd:PRK10851 29 QMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRF--HGTDVSRLHARDRKVGFVFQH--YALFRHMTVFDNIAFGLTVlpr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 118 NTDLDAEARQKQIIDTLRMVGLlpDHVS-YYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLEL 196
Cdd:PRK10851 105 RERPNAAAIKAKVTQLLEMVQL--AHLAdRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490242029 197 QEKQGISYIYVT--QHLGMmkHISDQVLVMHNGEVVERGSTADVLASP 242
Cdd:PRK10851 183 HEELKFTSVFVThdQEEAM--EVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
6-240 |
2.52e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 82.44 E-value: 2.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTFRYRTGWfhrqTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGE---LLIDDHPLTFGD 82
Cdd:PRK13651 3 IKVKNIVKIFNKKLPT----ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTiewIFKDEKNKKKTK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 83 YSY-----------RSQKIRMIFQdpstslnPRQRISQILDF-----------------PLRLNTD-LDAEARQKQIIdt 133
Cdd:PRK13651 79 EKEkvleklviqktRFKKIKKIKE-------IRRRVGVVFQFaeyqlfeqtiekdiifgPVSMGVSkEEAKKRAAKYI-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 134 lRMVGLLPDHVSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGM 213
Cdd:PRK13651 150 -ELVGLDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDN 227
|
250 260
....*....|....*....|....*..
gi 490242029 214 MKHISDQVLVMHNGEVVERGSTADVLA 240
Cdd:PRK13651 228 VLEWTKRTIFFKDGKIIKDGDTYDILS 254
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-212 |
2.62e-18 |
|
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: 80.48 E-value: 2.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSktfrYRTGWfhrqtVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSY 85
Cdd:TIGR01189 1 LAARNLA----CSRGE-----RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 RSQkirMIFQDPSTSLNPRQRISQILDFplrLNTDLDAEarQKQIIDTLRMVGLlpDHVSYYP-HMLAPGQKQRLGLARA 164
Cdd:TIGR01189 72 HEN---ILYLGHLPGLKPELSALENLHF---WAAIHGGA--QRTIEDALAAVGL--TGFEDLPaAQLSAGQQRRLALARL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490242029 165 LILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLG 212
Cdd:TIGR01189 142 WLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLG 189
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
31-241 |
3.03e-18 |
|
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: 84.10 E-value: 3.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 31 KPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTfgDYSYRS--QKIRMIFQDpsTSL------- 101
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIR--DVTQASlrAAIGIVPQD--TVLfndtiay 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 102 -----NP-------RQ--RISQILDFPLRLntdldaearqKQIIDTlrMV---GLlpdhvsyyphMLAPGQKQRLGLARA 164
Cdd:COG5265 451 niaygRPdaseeevEAaaRAAQIHDFIESL----------PDGYDT--RVgerGL----------KLSGGEKQRVAIART 508
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490242029 165 LILRPKVIVCDEALASLDmSMRSQLInlMLELQE-KQGISYIYVTQHLGMMKHiSDQVLVMHNGEVVERGSTADVLAS 241
Cdd:COG5265 509 LLKNPPILIFDEATSALD-SRTERAI--QAALREvARGRTTLVIAHRLSTIVD-ADEILVLEAGRIVERGTHAELLAQ 582
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
5-265 |
5.86e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 83.23 E-value: 5.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 5 LLEVRQLSKTfrYRTGwfhRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLI--------DDH 76
Cdd:PRK10535 4 LLELKDIRRS--YPSG---EEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVagqdvatlDAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 77 PLTfgdySYRSQKIRMIFQdpSTSLNPRQRISQILDFPlRLNTDLDAEARQKQIIDTLRMVGLlPDHVSYYPHMLAPGQK 156
Cdd:PRK10535 79 ALA----QLRREHFGFIFQ--RYHLLSHLTAAQNVEVP-AVYAGLERKQRLLRAQELLQRLGL-EDRVEYQPSQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 157 QRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEkQGISYIYVTqHLGMMKHISDQVLVMHNGEVV------ 230
Cdd:PRK10535 151 QRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRD-RGHTVIIVT-HDPQVAAQAERVIEIRDGEIVrnppaq 228
|
250 260 270
....*....|....*....|....*....|....*..
gi 490242029 231 --ERGSTADVLASPLHDLTRRLIAGhFGEALTAdAWR 265
Cdd:PRK10535 229 ekVNVAGGTEPVVNTASGWRQFVSG-FREALTM-AWR 263
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
6-249 |
6.24e-18 |
|
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: 83.08 E-value: 6.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLskTFRYRTGwfHRQTVEAVkplSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSY 85
Cdd:TIGR03797 452 IEVDRV--TFRYRPD--GPLILDDV---SLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQA 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 RSQKIRMIFQDpstslnprqriSQILDFPLRLNTDLDAEARQKQIIDTLRMVGLLPD--------H--VSYYPHMLAPGQ 155
Cdd:TIGR03797 525 VRRQLGVVLQN-----------GRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDirampmgmHtvISEGGGTLSGGQ 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 156 KQRLGLARALILRPKVIVCDEALASLDmsMRSQLInlMLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHNGEVVERGST 235
Cdd:TIGR03797 594 RQRLLIARALVRKPRILLFDEATSALD--NRTQAI--VSESLERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTY 668
|
250
....*....|....*.
gi 490242029 236 ADVLASP--LHDLTRR 249
Cdd:TIGR03797 669 DELMAREglFAQLARR 684
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
28-230 |
9.22e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 79.53 E-value: 9.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 28 EAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTF---GDYSYRSQKIRMIFQDPSTSLNpr 104
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlknREVPFLRRQIGMIFQDHHLLMD-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 105 QRISQILDFPLRLnTDLDAEARQKQIIDTLRMVGLLpDHVSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMS 184
Cdd:PRK10908 94 RTVYDNVAIPLII-AGASGDDIRRRVSAALDKVGLL-DKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490242029 185 MRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHNGEVV 230
Cdd:PRK10908 172 LSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
33-213 |
1.09e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.15 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 33 LSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSYRSQKIrmifqDPSTSLNPRQRISQILD 112
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYL-----GHRNAMKPALTVAENLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 113 F--PLRLNTDLDAEArqkqiidTLRMVGLlpDHVSYYP-HMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQL 189
Cdd:PRK13539 96 FwaAFLGGEELDIAA-------ALEAVGL--APLAHLPfGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALF 166
|
170 180
....*....|....*....|....
gi 490242029 190 INLMLELQEKQGISYIYVTQHLGM 213
Cdd:PRK13539 167 AELIRAHLAQGGIVIAATHIPLGL 190
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-228 |
1.85e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.51 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 1 MVETLLEVRQLSKTFryrtgwfhrQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGmVEPT---SGELLIDDHP 77
Cdd:PRK13549 1 MMEYLLEMKNITKTF---------GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 78 LTFGDYSYRSQK-IRMIFQDpsTSLNPRQRISQildfplrlNTDLDAEARQKQIID----TLRMVGLLPD-HVSYYPHM- 150
Cdd:PRK13549 71 LQASNIRDTERAgIAIIHQE--LALVKELSVLE--------NIFLGNEITPGGIMDydamYLRAQKLLAQlKLDINPATp 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 151 ---LAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHNG 227
Cdd:PRK13549 141 vgnLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDG 219
|
.
gi 490242029 228 E 228
Cdd:PRK13549 220 R 220
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
6-250 |
2.43e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 81.17 E-value: 2.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLskTFRYRTGWFhrqtveAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGD-YS 84
Cdd:PRK10522 323 LELRNV--TFAYQDNGF------SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQpED 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 85 YRSQkIRMIFQD---------PSTSLNPRQRISQILDFpLRLNTDLDAEARQkqiIDTLRmvgllpdhvsyyphmLAPGQ 155
Cdd:PRK10522 395 YRKL-FSAVFTDfhlfdqllgPEGKPANPALVEKWLER-LKMAHKLELEDGR---ISNLK---------------LSKGQ 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 156 KQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTqHLGMMKHISDQVLVMHNGEVVERGST 235
Cdd:PRK10522 455 KKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAIS-HDDHYFIHADRLLEMRNGQLSELTGE 533
|
250
....*....|....*
gi 490242029 236 ADVLASplHDLTRRL 250
Cdd:PRK10522 534 ERDAAS--RDAVART 546
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-240 |
2.44e-17 |
|
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: 81.39 E-value: 2.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTFryrtgwfhrQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGM--VEPTSGELLI---------- 73
Cdd:TIGR03269 1 IEVKNLTKKF---------DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYhvalcekcgy 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 74 ------DDHPLTFGDYSYRSQKIRMIFQDPSTSLNPRQRIS-------------QILDFPLRLNTDLDAEARQ--KQIID 132
Cdd:TIGR03269 72 verpskVGEPCPVCGGTLEPEEVDFWNLSDKLRRRIRKRIAimlqrtfalygddTVLDNVLEALEEIGYEGKEavGRAVD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 133 TLRMVGLlpDH-VSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDmSMRSQLI-NLMLELQEKQGISYIyVTQH 210
Cdd:TIGR03269 152 LIEMVQL--SHrITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLD-PQTAKLVhNALEEAVKASGISMV-LTSH 227
|
250 260 270
....*....|....*....|....*....|.
gi 490242029 211 LG-MMKHISDQVLVMHNGEVVERGSTADVLA 240
Cdd:TIGR03269 228 WPeVIEDLSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
29-262 |
3.23e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 78.59 E-value: 3.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 29 AVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTfGDYSYRSqkirMIFQDpsTSLNPRQRIS 108
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE-GPGAERG----VVFQN--EGLLPWRNVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 109 QILDFPLRLnTDLDAEARQKQIIDTLRMVGLLPDHvSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQ 188
Cdd:PRK11248 89 DNVAFGLQL-AGVEKMQRLEIAHQMLKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490242029 189 LINLMLELQEKQGISYIYVTQHLGMMKHI-SDQVLVMHN-GEVVERGSTadvlasplhDLTRRLIAGHFGEALTAD 262
Cdd:PRK11248 167 MQTLLLKLWQETGKQVLLITHDIEEAVFMaTELVLLSPGpGRVVERLPL---------NFARRFVAGESSRSIKSD 233
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
33-231 |
3.99e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 77.83 E-value: 3.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 33 LSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPL-TFGDYSYRsQKIRMIFQDPSTSlnpRQRISQIL 111
Cdd:PRK10247 26 ISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIsTLKPEIYR-QQVSYCAQTPTLF---GDTVYDNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 112 DFPLRLNTDldaEARQKQIIDTLRMVGlLPDHVSYYP-HMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLI 190
Cdd:PRK10247 102 IFPWQIRNQ---QPDPAIFLDDLERFA-LPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVN 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490242029 191 NLMLELQEKQGISYIYVTQHLGMMKHiSDQVLVM--HNGEVVE 231
Cdd:PRK10247 178 EIIHRYVREQNIAVLWVTHDKDEINH-ADKVITLqpHAGEMQE 219
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
33-233 |
4.57e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 78.19 E-value: 4.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 33 LSFTLRERQTLAIIGENGSGKSTLAKMLAG--MVEPTSGELLIDDHPLTFGDYSYRSQK-IRMIFQDP------------ 97
Cdd:COG0396 19 VNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLDGEDILELSPDERARAgIFLAFQYPveipgvsvsnfl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 98 STSLNPRQRisqildfplrlnTDLDAEARQKQIIDTLRMVGLLPDHVSYYPHM-LAPGQKQRLGLARALILRPKVIVCDE 176
Cdd:COG0396 99 RTALNARRG------------EELSAREFLKLLKEKMKELGLDEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490242029 177 ALASLDM-SMR--SQLINLMLElqekQGISYIYVTQHLGMMKHIS-DQVLVMHNGEVVERG 233
Cdd:COG0396 167 TDSGLDIdALRivAEGVNKLRS----PDRGILIITHYQRILDYIKpDFVHVLVDGRIVKSG 223
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
28-234 |
1.11e-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: 76.03 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 28 EAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGM--VEPTSGELLIDDHPLTFGDYSYRSQK-IRMIFQDPStslnpr 104
Cdd:cd03217 14 EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLgIFLAFQYPP------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 105 qRISQIldfplrlntdldaearqkQIIDTLRMVGLlpdhvsyyphMLAPGQKQRLGLARALILRPKVIVCDEALASLD-- 182
Cdd:cd03217 88 -EIPGV------------------KNADFLRYVNE----------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDid 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490242029 183 -MSMRSQLINLMLElqekQGISYIYVTQHLGMMKHI-SDQVLVMHNGEVVERGS 234
Cdd:cd03217 139 aLRLVAEVINKLRE----EGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGD 188
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-256 |
1.19e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 77.38 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 22 FHRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEpTSGELLIDDHPLTFGDYSYR--------SQKIRMI 93
Cdd:PRK14258 15 FYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRVEFFNQNIYErrvnlnrlRRQVSMV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 94 FQDPS----------------TSLNPRQRISQILDFPLRlNTDLDAEARQKQIIDTLRMVGllpdhvsyyphmlapGQKQ 157
Cdd:PRK14258 94 HPKPNlfpmsvydnvaygvkiVGWRPKLEIDDIVESALK-DADLWDEIKHKIHKSALDLSG---------------GQQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 158 RLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHN-----GEVVER 232
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEF 237
|
250 260
....*....|....*....|....
gi 490242029 233 GSTADVLASPLHDLTRRLIAGHFG 256
Cdd:PRK14258 238 GLTKKIFNSPHDSRTREYVLSRLG 261
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
2-242 |
1.25e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 77.50 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 2 VETLLEVRQLSktfryrtgwFHRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDdhpltfG 81
Cdd:PRK11831 4 VANLVDMRGVS---------FTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFD------G 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 82 D----------YSYRsQKIRMIFQDPS--TSLNPRQRISqildFPLRLNTDLDAEARQKQIIDTLRMVGlLPDHVSYYPH 149
Cdd:PRK11831 69 EnipamsrsrlYTVR-KRMSMLFQSGAlfTDMNVFDNVA----YPLREHTQLPAPLLHSTVMMKLEAVG-LRGAAKLMPS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 150 MLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEV 229
Cdd:PRK11831 143 ELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKI 222
|
250
....*....|...
gi 490242029 230 VERGSTADVLASP 242
Cdd:PRK11831 223 VAHGSAQALQANP 235
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
30-210 |
1.75e-16 |
|
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: 74.88 E-value: 1.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 30 VKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFgdysYRSQKIRMifqdPSTSLnprqrisq 109
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLL----FLPQRPYL----PLGTL-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 110 ildfplrlntdldaeaRQkQIIdtlrmvgllpdhvsyYP--HMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRS 187
Cdd:cd03223 81 ----------------RE-QLI---------------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170 180
....*....|....*....|...
gi 490242029 188 QlinlMLELQEKQGISYIYVTQH 210
Cdd:cd03223 129 R----LYQLLKELGITVISVGHR 147
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
33-242 |
1.97e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 78.34 E-value: 1.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 33 LSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSYRSQKIRMIFQDPSTSLNPRQRisQILD 112
Cdd:PRK09536 22 VDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLSFEFDVR--QVVE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 113 ---------FPLRLNTDLDAEARQKQIIDTLRMVGLLPDHVSyyphmlaPGQKQRLGLARALILRPKVIVCDEALASLDM 183
Cdd:PRK09536 100 mgrtphrsrFDTWTETDRAAVERAMERTGVAQFADRPVTSLS-------GGERQRVLLARALAQATPVLLLDEPTASLDI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490242029 184 SMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVLASP 242
Cdd:PRK09536 173 NHQVRTLELVRRLVD-DGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
29-261 |
2.52e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 78.46 E-value: 2.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 29 AVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDhpLTFGDYSYRS--QKIRMIFQDP-----STSL 101
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDG--TDIRTVTRASlrRNIAVVFQDAglfnrSIED 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 102 NPR--------------QRISQILDFPLRLNTDLDAearqkqiidtlrmvgllpdHVSYYPHMLAPGQKQRLGLARALIL 167
Cdd:PRK13657 428 NIRvgrpdatdeemraaAERAQAHDFIERKPDGYDT-------------------VVGERGRQLSGGERQRLAIARALLK 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 168 RPKVIVCDEALASLDMSMRSQLiNLMLELQEKQGISYIyVTQHLGMMKHiSDQVLVMHNGEVVERGSTADVLASplhdlt 247
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKV-KAALDELMKGRTTFI-IAHRLSTVRN-ADRILVFDNGRVVESGSFDELVAR------ 559
|
250
....*....|....
gi 490242029 248 rrliAGHFGEALTA 261
Cdd:PRK13657 560 ----GGRFAALLRA 569
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
29-256 |
2.96e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 76.36 E-value: 2.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 29 AVKPLSFTLRERQTLAIIGENGSGKSTLAK---MLAGMVEP--TSGELLIDDHPLTFG--DYSYRSQKIRMIFQDPstsl 101
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnRLNDLIPGfrVEGKVTFHGKNLYAPdvDPVEVRRRIGMVFQKP---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 102 NP-RQRISQILDFPLRLN---TDLD--AEARQKQ------IIDTLRMVGLlpdhvsyyphMLAPGQKQRLGLARALILRP 169
Cdd:PRK14243 101 NPfPKSIYDNIAYGARINgykGDMDelVERSLRQaalwdeVKDKLKQSGL----------SLSGGQQQRLCIARAIAVQP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 170 KVIVCDEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHISDQVLVMH---------NGEVVERGSTADVLA 240
Cdd:PRK14243 171 EVILMDEPCSALDPISTLRIEELMHELKEQYTI--IIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEFDRTEKIFN 248
|
250
....*....|....*.
gi 490242029 241 SPLHDLTRRLIAGHFG 256
Cdd:PRK14243 249 SPQQQATRDYVSGRFG 264
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-240 |
3.03e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 77.94 E-value: 3.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 5 LLEVRQLSktFRYrtgwfHRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTfgdyS 84
Cdd:PRK11160 338 SLTLNNVS--FTY-----PDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIA----D 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 85 YRSQKIRmifqdPSTSLNPrQRIsQILDFPLRLNTDL-DAEARQKQIIDTLRMVGLlPDHVSYYPHM----------LAP 153
Cdd:PRK11160 407 YSEAALR-----QAISVVS-QRV-HLFSATLRDNLLLaAPNASDEALIEVLQQVGL-EKLLEDDKGLnawlgeggrqLSG 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 154 GQKQRLGLARALiLRPKVIV-CDEALASLDMSMRSQLINLMLELQekQGISYIYVTQHLGMMKHIsDQVLVMHNGEVVER 232
Cdd:PRK11160 479 GEQRRLGIARAL-LHDAPLLlLDEPTEGLDAETERQILELLAEHA--QNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQ 554
|
....*...
gi 490242029 233 GSTADVLA 240
Cdd:PRK11160 555 GTHQELLA 562
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
33-193 |
4.00e-16 |
|
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: 74.84 E-value: 4.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 33 LSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSYRSQKIRMIFQDP-STSLNPRQRisqiL 111
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGiKTTLSVLEN----L 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 112 DFPLRLNTDldaearqKQIIDTLRMVGLLP-DHVSYypHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLI 190
Cdd:cd03231 95 RFWHADHSD-------EQVEEALARVGLNGfEDRPV--AQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFA 165
|
...
gi 490242029 191 NLM 193
Cdd:cd03231 166 EAM 168
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
30-227 |
5.08e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 77.54 E-value: 5.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 30 VKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHpltfGDYSYRSQKIRMifqdPSTSLnprqRisQ 109
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAG----ARVLFLPQRPYL----PLGTL----R--E 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 110 ILDFPLRLNTDLDAEARQkqiidTLRMVGLlPDHVSYY------PHMLAPGQKQRLGLARALILRPKVIVCDEALASLDM 183
Cdd:COG4178 445 ALLYPATAEAFSDAELRE-----ALEAVGL-GHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490242029 184 SMRSQLINLMLElqEKQGISYIYVTQHLGMMKHiSDQVLVMHNG 227
Cdd:COG4178 519 ENEAALYQLLRE--ELPGTTVISVGHRSTLAAF-HDRVLELTGD 559
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
6-242 |
7.40e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 76.04 E-value: 7.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTfrYRTGwfhrqtVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTfgDYSY 85
Cdd:PRK11650 4 LKLQAVRKS--YDGK------TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVN--ELEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 RSQKIRMIFQDpsTSLNPRQRISQILDFPLRlNTDLDAEARQKQIIDTLRMVGLLPdhvsyY----PHMLAPGQKQRLGL 161
Cdd:PRK11650 74 ADRDIAMVFQN--YALYPHMSVRENMAYGLK-IRGMPKAEIEERVAEAARILELEP-----LldrkPRELSGGQRQRVAM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 162 ARALILRPKVIVCDEALASLDMSMRSQlinlM-LELQEKQ---GISYIYVT--QHLGMMkhISDQVLVMhNGEVVER-GS 234
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLDAKLRVQ----MrLEIQRLHrrlKTTSLYVThdQVEAMT--LADRVVVM-NGGVAEQiGT 218
|
....*...
gi 490242029 235 TADVLASP 242
Cdd:PRK11650 219 PVEVYEKP 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
6-233 |
8.96e-16 |
|
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: 73.35 E-value: 8.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTFRYRTGWFHRQTVeavKPLSFTLRERQTLAIIGENGSGKSTLAKMLAG--MVEPTSGELLIDDHPLTFGDY 83
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGKQLL---KNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 84 SYRsqkIRMIFQDpsTSLNPRQRISQILDFPLRLntdldaeaRQkqiidtlrmvgllpdhvsyyphmLAPGQKQRLGLAR 163
Cdd:cd03213 81 RKI---IGYVPQD--DILHPTLTVRETLMFAAKL--------RG-----------------------LSGGERKRVSIAL 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490242029 164 ALILRPKVIVCDEALASLDMSMRSQLINLMLELQeKQGISYIYVT-QHLGMMKHISDQVLVMHNGEVVERG 233
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLA-DTGRTIICSIhQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-230 |
2.36e-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: 75.25 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 5 LLEVRQLSKTFryrtgwfhrQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGmVEPT---SGELLIDDHPLTFG 81
Cdd:TIGR02633 1 LLEMKGIVKTF---------GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSPLKAS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 82 DYSYRSQK-IRMIFQDpsTSLNPRQRISQ--ILDFPLRLN---TDLDAEARQKQiiDTLRMVGLLPDHVSYYPHMLAPGQ 155
Cdd:TIGR02633 71 NIRDTERAgIVIIHQE--LTLVPELSVAEniFLGNEITLPggrMAYNAMYLRAK--NLLRELQLDADNVTRPVGDYGGGQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490242029 156 KQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHNGEVV 230
Cdd:TIGR02633 147 QQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
32-239 |
3.22e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 72.95 E-value: 3.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 32 PLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVePTSGELLIDDHPLtfGDYS---------YRSQkirmifQDPSTSLN 102
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPL--SDWSaaelarhraYLSQ------QQSPPFAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 103 PrqrISQILDFPLRLNTDLDA-EARQKQIIDTLRMVGLLPDHVsyypHMLAPGQKQRLGLARALI-------LRPKVIVC 174
Cdd:COG4138 85 P---VFQYLALHQPAGASSEAvEQLLAQLAEALGLEDKLSRPL----TQLSGGEWQRVRLAAVLLqvwptinPEGQLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490242029 175 DEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVL 239
Cdd:COG4138 158 DEPMNSLDVAQQAALDRLLRELCQ-QGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
14-242 |
3.65e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 73.28 E-value: 3.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 14 TFRYRTGWFHRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSYRSQKIRMI 93
Cdd:PRK10575 11 TFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 94 FQD--PSTSLNPRQRISqILDFPLRLNTDLDAEARQKQIIDTLRMVGLLPdHVSYYPHMLAPGQKQRLGLARALILRPKV 171
Cdd:PRK10575 91 PQQlpAAEGMTVRELVA-IGRYPWHGALGRFGAADREKVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490242029 172 IVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVLASP 242
Cdd:PRK10575 169 LLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
29-240 |
4.15e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 74.67 E-value: 4.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 29 AVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTfgDYSYR---------SQKIRMiFQDpsT 99
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLR--DYTLAslrnqvalvSQNVHL-FND--T 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 100 SLNprqrisqildfplrlNTDLDAEAR--QKQIIDTLRMVGLLpDHVSYYPH-----------MLAPGQKQRLGLARALI 166
Cdd:PRK11176 433 IAN---------------NIAYARTEQysREQIEEAARMAYAM-DFINKMDNgldtvigengvLLSGGQRQRIAIARALL 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490242029 167 LRPKVIVCDEALASLDM-SMRSqlINLMLELQEKQGISYIyVTQHLGMMKHiSDQVLVMHNGEVVERGSTADVLA 240
Cdd:PRK11176 497 RDSPILILDEATSALDTeSERA--IQAALDELQKNRTSLV-IAHRLSTIEK-ADEILVVEDGEIVERGTHAELLA 567
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-230 |
7.71e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 73.90 E-value: 7.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 3 ETLLEVRQLSKTfryrtgwfhrqtvEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGd 82
Cdd:COG1129 254 EVVLEVEGLSVG-------------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIR- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 83 ysyrsqkirmifqdpstslNPRQRISQ--------------ILDFPLRLNT--------------DLDAEARQ-KQIIDT 133
Cdd:COG1129 320 -------------------SPRDAIRAgiayvpedrkgeglVLDLSIRENItlasldrlsrggllDRRRERALaEEYIKR 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 134 LRMVgllpdhvsyYPHMLAP------GQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEkQGISYIYV 207
Cdd:COG1129 381 LRIK---------TPSPEQPvgnlsgGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAA-EGKAVIVI 450
|
250 260
....*....|....*....|...
gi 490242029 208 TQHLGMMKHISDQVLVMHNGEVV 230
Cdd:COG1129 451 SSELPELLGLSDRILVMREGRIV 473
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-260 |
9.64e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 73.29 E-value: 9.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 5 LLEVRQLSKTFryrTGwfhrqtVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGmVEPT---SGELLIDDHPLTFG 81
Cdd:NF040905 1 ILEMRGITKTF---PG------VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDGEVCRFK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 82 DYSYRSQK-IRMIFQD----PSTSL-------NPRQRISQIldfplrlntdlDAEARQKQIIDTLRMVGLLPDhvsyyPH 149
Cdd:NF040905 71 DIRDSEALgIVIIHQElaliPYLSIaeniflgNERAKRGVI-----------DWNETNRRARELLAKVGLDES-----PD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 150 MLAP----GQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMH 225
Cdd:NF040905 135 TLVTdigvGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKA-QGITSIIISHKLNEIRRVADSITVLR 213
|
250 260 270
....*....|....*....|....*....|....*
gi 490242029 226 NGEVVErgsTADVLASPLHDltRRLIAGHFGEALT 260
Cdd:NF040905 214 DGRTIE---TLDCRADEVTE--DRIIRGMVGRDLE 243
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
6-96 |
1.03e-14 |
|
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: 73.29 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLskTFRYRTGwfHRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDY-S 84
Cdd:COG4615 328 LELRGV--TYRYPGE--DGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNReA 403
|
90
....*....|..
gi 490242029 85 YRsQKIRMIFQD 96
Cdd:COG4615 404 YR-QLFSAVFSD 414
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
23-229 |
1.15e-14 |
|
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: 73.32 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 23 HRQTVEAVkplSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPT-SGELLIDDHPLTFGDYSYR-SQKIRMIFQD---- 96
Cdd:TIGR02633 272 HRKRVDDV---SFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAiRAGIAMVPEDrkrh 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 97 ---PSTSLNPRQRISQILDFPLRlnTDLDAEARQKQIIDTLRMVGLLPDHVSYYPHMLAPGQKQRLGLARALILRPKVIV 173
Cdd:TIGR02633 349 givPILGVGKNITLSVLKSFCFK--MRIDAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490242029 174 CDEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHNGEV 229
Cdd:TIGR02633 427 LDEPTRGVDVGAKYEIYKLINQLA-QEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
7-231 |
1.32e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 70.76 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 7 EVRQLSKTF--RYRTGWFHrqtveAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGdys 84
Cdd:COG2401 26 RVAIVLEAFgvELRVVERY-----VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFG--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 85 yrsqkirmifqdpstslnprQRISQILDFPLRLNTDLDAEArqkqiidtLRMVGLlPDHVSYY--PHMLAPGQKQRLGLA 162
Cdd:COG2401 98 --------------------REASLIDAIGRKGDFKDAVEL--------LNAVGL-SDAVLWLrrFKELSTGQKFRFRLA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 163 RALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVM-HNGEVVE 231
Cdd:COG2401 149 LLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIFvGYGGVPE 218
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
10-230 |
1.92e-14 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 70.38 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 10 QLSKTFRYRTGWfhRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEP---TSGELLIDDHPLTFGDYSYR 86
Cdd:cd03234 5 PWWDVGLKAKNW--NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPDQFQKC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 87 SQKIRmifQDPST--SLNPRQRISQILdfPLRLNTDLDAEARQKQIIDT-LRMVGLLPDHVSYYPHmLAPGQKQRLGLAR 163
Cdd:cd03234 83 VAYVR---QDDILlpGLTVRETLTYTA--ILRLPRKSSDAIRKKRVEDVlLRDLALTRIGGNLVKG-ISGGERRRVSIAV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490242029 164 ALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVV 230
Cdd:cd03234 157 QLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIV 223
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-252 |
3.54e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.87 E-value: 3.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTFryrtgwfhrQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGdySY 85
Cdd:PRK11288 5 LSFDGIGKTF---------PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFA--ST 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 RS---QKIRMIFQD------------------PSTS--LNPRQRISQILDFPLRLNTDLDAEARQKQiidtlrmvgllpd 142
Cdd:PRK11288 74 TAalaAGVAIIYQElhlvpemtvaenlylgqlPHKGgiVNRRLLNYEAREQLEHLGVDIDPDTPLKY------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 143 hvsyyphmLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVL 222
Cdd:PRK11288 141 --------LSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELR-AEGRVILYVSHRMEEIFALCDAIT 211
|
250 260 270
....*....|....*....|....*....|
gi 490242029 223 VMHNGEVVErgsTADVLASPLHDltrRLIA 252
Cdd:PRK11288 212 VFKDGRYVA---TFDDMAQVDRD---QLVQ 235
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
36-223 |
3.60e-14 |
|
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: 70.13 E-value: 3.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 36 TLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDdhpltFGDYSYRSQKIRmifqdPSTSLNPRQRISQILDfpl 115
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE-----LDTVSYKPQYIK-----ADYEGTVRDLLSSITK--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 116 RLNTDldaEARQKQIIDTLRMVGLLPDHVSyyphMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMR---SQLINL 192
Cdd:cd03237 88 DFYTH---PYFKTEIAKPLQIEQILDREVP----ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRlmaSKVIRR 160
|
170 180 190
....*....|....*....|....*....|..
gi 490242029 193 MLELQEKQgisyIYVTQH-LGMMKHISDQVLV 223
Cdd:cd03237 161 FAENNEKT----AFVVEHdIIMIDYLADRLIV 188
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
31-228 |
3.70e-14 |
|
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: 67.86 E-value: 3.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 31 KPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLiddhpltfgdysyRSQKIRmifqdpstslnprqrisqi 110
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT-------------WGSTVK------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 111 ldfplrlntdldaearqkqiidtlrmvgllpdhVSYYPHmLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLI 190
Cdd:cd03221 65 ---------------------------------IGYFEQ-LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALE 110
|
170 180 190
....*....|....*....|....*....|....*...
gi 490242029 191 NlmlELQEKQGIsYIYVTQHLGMMKHISDQVLVMHNGE 228
Cdd:cd03221 111 E---ALKEYPGT-VILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
32-239 |
6.23e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.58 E-value: 6.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 32 PLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVePTSGELLIDDHPLTfgDYSYRSQKIRMIF---QDPSTSLNPrqrIS 108
Cdd:PRK03695 14 PLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLE--AWSAAELARHRAYlsqQQTPPFAMP---VF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 109 QILDFPLRLNTDLDAEARQ-KQIIDTLRMVGLLPDHVsyypHMLAPGQKQRLGLARALI-----LRP--KVIVCDEALAS 180
Cdd:PRK03695 88 QYLTLHQPDKTRTEAVASAlNEVAEALGLDDKLGRSV----NQLSGGEWQRVRLAAVVLqvwpdINPagQLLLLDEPMNS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490242029 181 LDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVL 239
Cdd:PRK03695 164 LDVAQQAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
33-240 |
1.52e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 70.39 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 33 LSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLT-FGDYSYRsQKIRMIFQDPStslnprqrisqIL 111
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAkFGLTDLR-RVLSIIPQSPV-----------LF 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 112 DFPLRLNTDLDAEARQKQIIDTLRMVGLlPDHVSYYPHML-----------APGQKQRLGLARALILRPKVIVCDEALAS 180
Cdd:PLN03232 1323 SGTVRFNIDPFSEHNDADLWEALERAHI-KDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 181 LDMSMRSqLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHNGEVVERGSTADVLA 240
Cdd:PLN03232 1402 VDVRTDS-LIQRTIR-EEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLS 1458
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
15-240 |
2.01e-13 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 69.53 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 15 FRYRTGWFHRqtveAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDhpltfgdysyrSQKIRMIf 94
Cdd:PRK13545 29 FRSKDGEYHY----ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-----------SAALIAI- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 95 qdpSTSLNprQRISQILDFPLR-LNTDLDAEARQK---QIIDTLRMVGLLPDHVSYYphmlAPGQKQRLGLARALILRPK 170
Cdd:PRK13545 93 ---SSGLN--GQLTGIENIELKgLMMGLTKEKIKEiipEIIEFADIGKFIYQPVKTY----SSGMKSRLGFAISVHINPD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 171 VIVCDEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVLA 240
Cdd:PRK13545 164 ILVIDEALSVGDQTFTKKCLDKMNEFKE-QGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVD 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-231 |
2.21e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 69.32 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 4 TLLEVRQLSKTFRYRTgwfhrqtveAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHpLTFGdy 83
Cdd:COG0488 314 KVLELEGLSKSYGDKT---------LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET-VKIG-- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 84 sYRSQKirmifQDpstSLNPRQRISQILdfplrlnTDLDAEARQKQIIDTLRMVGLLPDHVSYYPHMLAPGQKQRLGLAR 163
Cdd:COG0488 382 -YFDQH-----QE---ELDPDKTVLDEL-------RDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490242029 164 ALILRPKVIVCDEALASLDMSMRSQLINLmleLQEKQGiSYIYVTQHLGMMKHISDQVLVMHNGEVVE 231
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLDIETLEALEEA---LDDFPG-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-234 |
2.32e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 67.74 E-value: 2.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 4 TLLEVRQLSKTFryrtgwfhrQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGmvEP----TSGELLIDDHPLT 79
Cdd:CHL00131 6 PILEIKNLHASV---------NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPaykiLEGDILFKGESIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 80 FGDYSYRSQK-IRMIFQDP------------STSLNPRQRISQIldfplrlnTDLDAEARQKQIIDTLRMVGLLPDHVSY 146
Cdd:CHL00131 75 DLEPEERAHLgIFLAFQYPieipgvsnadflRLAYNSKRKFQGL--------PELDPLEFLEIINEKLKLVGMDPSFLSR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 147 YPHM-LAPGQKQRLGLARALILRPKVIVCDEALASLDM-SMR--SQLINlMLELQEKqgiSYIYVTQHLGMMKHIS-DQV 221
Cdd:CHL00131 147 NVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLDIdALKiiAEGIN-KLMTSEN---SIILITHYQRLLDYIKpDYV 222
|
250
....*....|...
gi 490242029 222 LVMHNGEVVERGS 234
Cdd:CHL00131 223 HVMQNGKIIKTGD 235
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
33-210 |
2.36e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.14 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 33 LSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSYRSQkirMIFQDPSTSLNPRQRISQILD 112
Cdd:PRK13538 20 LSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQD---LLYLGHQPGIKTELTALENLR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 113 FPLRLNTDLDAEArqkqIIDTLRMVGL-----LPDHVsyyphmLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRS 187
Cdd:PRK13538 97 FYQRLHGPGDDEA----LWEALAQVGLagfedVPVRQ------LSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVA 166
|
170 180
....*....|....*....|...
gi 490242029 188 QLINLMLELQEKQGIsyIYVTQH 210
Cdd:PRK13538 167 RLEALLAQHAEQGGM--VILTTH 187
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-241 |
4.57e-13 |
|
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: 68.82 E-value: 4.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 19 TGWFHRQTVE--------------AVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLT-FGDY 83
Cdd:TIGR00957 1277 SGWPPRGRVEfrnyclryredldlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAkIGLH 1356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 84 SYRSqKIRMIFQDPStslnprqrisqILDFPLRLNTDLDAEARQKQIIDTLRM------VGLLPDHVSYY----PHMLAP 153
Cdd:TIGR00957 1357 DLRF-KITIIPQDPV-----------LFSGSLRMNLDPFSQYSDEEVWWALELahlktfVSALPDKLDHEcaegGENLSV 1424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 154 GQKQRLGLARALILRPKVIVCDEALASLDMSMrSQLINLMLELQeKQGISYIYVTQHLGMMKHISdQVLVMHNGEVVERG 233
Cdd:TIGR00957 1425 GQRQLVCLARALLRKTKILVLDEATAAVDLET-DNLIQSTIRTQ-FEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFG 1501
|
....*...
gi 490242029 234 STADVLAS 241
Cdd:TIGR00957 1502 APSNLLQQ 1509
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
34-176 |
4.70e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.55 E-value: 4.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 34 SFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLID----------DHPLtFGDYSYRSQkIRMIFQDPSTSLNP 103
Cdd:COG0488 18 SLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkglrigylpqEPPL-DDDLTVLDT-VLDGDAELRALEAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 104 RQRISQILDFPL-------RLNTDLD------AEARQKQIIDTLRMVGLLPDH-VSyyphMLAPGQKQRLGLARALILRP 169
Cdd:COG0488 96 LEELEAKLAEPDedlerlaELQEEFEalggweAEARAEEILSGLGFPEEDLDRpVS----ELSGGWRRRVALARALLSEP 171
|
....*..
gi 490242029 170 KVIVCDE 176
Cdd:COG0488 172 DLLLLDE 178
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
15-241 |
6.40e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 68.52 E-value: 6.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 15 FRYRTgwfhRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKML---------------------------------- 60
Cdd:PTZ00265 1173 FRYIS----RPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtndmtneqdyqgdeeq 1248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 61 -AGM-------------------VEPTSGELLIDDhpLTFGDYSYRSqkIRMIF----QDPstsLNPRQRISQILDFPlR 116
Cdd:PTZ00265 1249 nVGMknvnefsltkeggsgedstVFKNSGKILLDG--VDICDYNLKD--LRNLFsivsQEP---MLFNMSIYENIKFG-K 1320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 117 LNTDLDAEARQKQIIDTLRMVGLLPD----HVSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINL 192
Cdd:PTZ00265 1321 EDATREDVKRACKFAAIDEFIESLPNkydtNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1400
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 490242029 193 MLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHN----GEVVERGSTADVLAS 241
Cdd:PTZ00265 1401 IVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVQAHGTHEELLS 1452
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-235 |
8.94e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 66.57 E-value: 8.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 2 VETLLEVRQLSKTFRyrtgwfHRQTVEAVkplSFTLRERQTLAIIGENGSGKSTLAKMLAGMVeptSGELLIDDHPLTFG 81
Cdd:PRK09984 1 MQTIIRVEKLAKTFN------QHQALHAV---DLNIHHGEMVALLGPSGSGKSTLLRHLSGLI---TGDKSAGSHIELLG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 82 DYSYRSQK----IR-------MIFQdpstSLNPRQRISQILDF--------PL-RLNTDLDAEARQKQIIDTLRMVGLlp 141
Cdd:PRK09984 69 RTVQREGRlardIRksrantgYIFQ----QFNLVNRLSVLENVligalgstPFwRTCFSWFTREQKQRALQALTRVGM-- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 142 dhvSYYPHM----LAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHI 217
Cdd:PRK09984 143 ---VHFAHQrvstLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRY 219
|
250
....*....|....*...
gi 490242029 218 SDQVLVMHNGEVVERGST 235
Cdd:PRK09984 220 CERIVALRQGHVFYDGSS 237
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
13-242 |
1.11e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 67.43 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 13 KTFRYRTgwfhrQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTfgdysyrsqKIRM 92
Cdd:PRK10789 319 RQFTYPQ-----TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLT---------KLQL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 93 IfqdpstslNPRQRISQILDFPLrLNTDLDA--------EARQKQIIDTLRMVGL------LPD----HVSYYPHMLAPG 154
Cdd:PRK10789 385 D--------SWRSRLAVVSQTPF-LFSDTVAnnialgrpDATQQEIEHVARLASVhddilrLPQgydtEVGERGVMLSGG 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 155 QKQRLGLARALILRPKVIVCDEALASLDMSMRSQLI-NLMlelQEKQGISYIYVTQHLGMMKHiSDQVLVMHNGEVVERG 233
Cdd:PRK10789 456 QKQRISIARALLLNAEILILDDALSAVDGRTEHQILhNLR---QWGEGRTVIISAHRLSALTE-ASEILVMQHGHIAQRG 531
|
....*....
gi 490242029 234 STADVLASP 242
Cdd:PRK10789 532 NHDQLAQQS 540
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
29-211 |
1.99e-12 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 64.18 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 29 AVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHpltfGDYSYRSQKIRMIFQDPSTSlnpRQRIS 108
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG----ARVAYVPQRSEVPDSLPLTV---RDLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 109 QILDFPLRLNTDLDAEARqKQIIDTLRMVGLLpDHVSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQ 188
Cdd:NF040873 80 MGRWARRGLWRRLTRDDR-AAVDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRER 157
|
170 180
....*....|....*....|...
gi 490242029 189 LINLMLELQEkQGISYIYVTQHL 211
Cdd:NF040873 158 IIALLAEEHA-RGATVVVVTHDL 179
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-242 |
2.12e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 67.11 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 16 RYRTGWfhrqtveavkPL-----SFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLtfGDYSYRS--Q 88
Cdd:PTZ00243 1317 RYREGL----------PLvlrgvSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREI--GAYGLRElrR 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 89 KIRMIFQDPStslnprqrisqILDFPLRLNTDLDAEARQKQIIDTLRMVGlLPDHV---------------SYYphmlAP 153
Cdd:PTZ00243 1385 QFSMIPQDPV-----------LFDGTVRQNVDPFLEASSAEVWAALELVG-LRERVasesegidsrvleggSNY----SV 1448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 154 GQKQRLGLARALILR-PKVIVCDEALASLDMSMRSQLIN-LMLELQEKQGISYIY----VTQHlgmmkhisDQVLVMHNG 227
Cdd:PTZ00243 1449 GQRQLMCMARALLKKgSGFILMDEATANIDPALDRQIQAtVMSAFSAYTVITIAHrlhtVAQY--------DKIIVMDHG 1520
|
250
....*....|....*
gi 490242029 228 EVVERGSTADVLASP 242
Cdd:PTZ00243 1521 AVAEMGSPRELVMNR 1535
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-229 |
7.74e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.02 E-value: 7.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 3 ETLLEVRQLSKtfryrtgwfhrqtvEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTfgd 82
Cdd:PRK10762 255 EVRLKVDNLSG--------------PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVV--- 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 83 ysYRSQK------IRMIFQDpstslnpRQRISQILDFPLRLN---TDLDAEARQKQIIDTLRMVGLLPDHVSYY----PH 149
Cdd:PRK10762 318 --TRSPQdglangIVYISED-------RKRDGLVLGMSVKENmslTALRYFSRAGGSLKHADEQQAVSDFIRLFniktPS 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 150 M------LAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRS---QLINlmlelQEKQ-GISYIYVTQH----LGMmk 215
Cdd:PRK10762 389 MeqaiglLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKeiyQLIN-----QFKAeGLSIILVSSEmpevLGM-- 461
|
250
....*....|....
gi 490242029 216 hiSDQVLVMHNGEV 229
Cdd:PRK10762 462 --SDRILVMHEGRI 473
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
33-222 |
8.54e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.59 E-value: 8.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 33 LSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGeLLIDDHPLTFGdysYRSQKIRMifqDPSTSLNprqrISQILD 112
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG-VIKRNGKLRIG---YVPQKLYL---DTTLPLT----VNRFLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 113 fpLRLNTdldaeaRQKQIIDTLRMVGllPDHVSYYP-HMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLIN 191
Cdd:PRK09544 92 --LRPGT------KKEDILPALKRVQ--AGHLIDAPmQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYD 161
|
170 180 190
....*....|....*....|....*....|...
gi 490242029 192 LMLELQEKQGISYIYVTQ--HLGMMKhiSDQVL 222
Cdd:PRK09544 162 LIDQLRRELDCAVLMVSHdlHLVMAK--TDEVL 192
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
33-240 |
1.12e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 64.76 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 33 LSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPL-TFGDYSYRsQKIRMIFQDP-----STSLNprqr 106
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIsKFGLMDLR-KVLGIIPQAPvlfsgTVRFN---- 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 107 isqiLDfPLRLNTDLDA-EARQK-QIIDTLRMVGL-LPDHVSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDM 183
Cdd:PLN03130 1333 ----LD-PFNEHNDADLwESLERaHLKDVIRRNSLgLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDV 1407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490242029 184 SMRSqLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHNGEVVERGSTADVLA 240
Cdd:PLN03130 1408 RTDA-LIQKTIR-EEFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLS 1461
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
33-228 |
1.61e-11 |
|
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: 61.72 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 33 LSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIddhpltFGDYSYRSQK--IRmifqdpSTSLnpRQRISqi 110
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV------PGSIAYVSQEpwIQ------NGTI--RENIL-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 111 ldFPLRLNtdldaEARQKQiidTLRMVGLLPDhVSYYPH-----------MLAPGQKQRLGLARALILRPKVIVCDEALA 179
Cdd:cd03250 88 --FGKPFD-----EERYEK---VIKACALEPD-LEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490242029 180 SLDMSMRSQLIN--LMLELQEKQGIsyIYVTQHLGMMKHiSDQVLVMHNGE 228
Cdd:cd03250 157 AVDAHVGRHIFEncILGLLLNNKTR--ILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-229 |
2.09e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.53 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 23 HRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHpltfgDYSYRSQKIRM------IFQD 96
Cdd:PRK15439 272 EDLTGEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGK-----EINALSTAQRLarglvyLPED 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 97 pstslnpRQRISQILDFPLRLNTD----------LDaEARQKQIIDTL-RMVGLLPDHVSYYPHMLAPGQKQRLGLARAL 165
Cdd:PRK15439 347 -------RQSSGLYLDAPLAWNVCalthnrrgfwIK-PARENAVLERYrRALNIKFNHAEQAARTLSGGNQQKVLIAKCL 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490242029 166 ILRPKVIVCDEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHNGEV 229
Cdd:PRK15439 419 EASPQLLIVDEPTRGVDVSARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-241 |
2.32e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 62.90 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 1 MVETLLEVRQLSKTFRYRTgwfhrqtveAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTf 80
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKL---------VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 81 GDYSYRSQKIRMIFQ----DPS----------------TSLNPRQRISQILDFPlRLNTDLDAEARQkqiidtlrmvgll 140
Cdd:PRK13537 73 SRARHARQRVGVVPQfdnlDPDftvrenllvfgryfglSAAAARALVPPLLEFA-KLENKADAKVGE------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 141 pdhvsyyphmLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRsQLINLMLELQEKQGISYIYVTQHLGMMKHISDQ 220
Cdd:PRK13537 139 ----------LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQAR-HLMWERLRSLLARGKTILLTTHFMEEAERLCDR 207
|
250 260
....*....|....*....|.
gi 490242029 221 VLVMHNGEVVERGSTADVLAS 241
Cdd:PRK13537 208 LCVIEEGRKIAEGAPHALIES 228
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-243 |
2.79e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 62.31 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 1 MVETLLEVRQLSKTFRYrtgwfHRQTVeaVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTF 80
Cdd:PRK10253 1 MTESVARLRGEQLTLGY-----GKYTV--AENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 81 GDYSYRSQKIRMIFQDPST-------SLNPRQRISQILDFPLRLNTDLDAEARQKQIIDTLRMVGLLPDhvsyyphMLAP 153
Cdd:PRK10253 74 YASKEVARRIGLLAQNATTpgditvqELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVD-------TLSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 154 GQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERG 233
Cdd:PRK10253 147 GQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
|
250
....*....|
gi 490242029 234 STADVLASPL 243
Cdd:PRK10253 227 APKEIVTAEL 236
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-235 |
3.03e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 62.21 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 1 MVETLLEVRQLSKTfrYRTGwfHrqtvEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTf 80
Cdd:PRK15056 2 MQQAGIVVNDVTVT--WRNG--H----TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 81 gdysyRSQKIRMIFQDPStslnprqriSQILD--FPLrLNTDL-------------DAEARQKQIID-TLRMVGLLpDHV 144
Cdd:PRK15056 73 -----QALQKNLVAYVPQ---------SEEVDwsFPV-LVEDVvmmgryghmgwlrRAKKRDRQIVTaALARVDMV-EFR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 145 SYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVlVM 224
Cdd:PRK15056 137 HRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRD-EGKTMLVSTHNLGSVTEFCDYT-VM 214
|
250
....*....|.
gi 490242029 225 HNGEVVERGST 235
Cdd:PRK15056 215 VKGTVLASGPT 225
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
30-233 |
4.05e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 62.16 E-value: 4.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 30 VKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLtfgdysyrsqkirmifqdPSTSLNPRQRISQ 109
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV------------------PARARLARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 110 ILDFPlrlNTDLDAEARQ----------------KQIIDTLRMVGLLPDHVSYYPHMLAPGQKQRLGLARALILRPKVIV 173
Cdd:PRK13536 119 VPQFD---NLDLEFTVREnllvfgryfgmstreiEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 174 CDEALASLDMSMRsQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERG 233
Cdd:PRK13536 196 LDEPTTGLDPHAR-HLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
33-210 |
4.47e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.73 E-value: 4.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 33 LSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSYRSQkirMIFQDPSTSLNPrqrisqilD 112
Cdd:PRK13540 20 ISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQ---LCFVGHRSGINP--------Y 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 113 FPLRLNT--DLDAEARQKQIIDTLRMVGLlpDHVSYYP-HMLAPGQKQRLGLARALILRPKVIVCDEALASLDmsmRSQL 189
Cdd:PRK13540 89 LTLRENClyDIHFSPGAVGITELCRLFSL--EHLIDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD---ELSL 163
|
170 180
....*....|....*....|...
gi 490242029 190 INLMLELQE--KQGiSYIYVTQH 210
Cdd:PRK13540 164 LTIITKIQEhrAKG-GAVLLTSH 185
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-229 |
4.80e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.64 E-value: 4.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 3 ETLLEVRQLsktfryrTGWF----HRQTVEAVkplSFTLRERQTLAIIGENGSGKSTLAKMLAGmVEP--TSGELLIDDH 76
Cdd:PRK13549 257 EVILEVRNL-------TAWDpvnpHIKRVDDV---SFSLRRGEILGIAGLVGAGRTELVQCLFG-AYPgrWEGEIFIDGK 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 77 PLTFgdysyRS------QKIRMIFQDpstslnpRQRISQILDFPLRLNTDL------------DAEARQKQIIDTLRMVG 138
Cdd:PRK13549 326 PVKI-----RNpqqaiaQGIAMVPED-------RKRDGIVPVMGVGKNITLaaldrftggsriDDAAELKTILESIQRLK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 139 LLPDHVSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHIS 218
Cdd:PRK13549 394 VKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLV-QQGVAIIVISSELPEVLGLS 472
|
250
....*....|.
gi 490242029 219 DQVLVMHNGEV 229
Cdd:PRK13549 473 DRVLVMHEGKL 483
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-223 |
8.02e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.75 E-value: 8.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 3 ETLLEVRQLSKTFryrtGWFhRQTVEAVkplsfTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDdhpLTFgd 82
Cdd:PRK13409 338 ETLVEYPDLTKKL----GDF-SLEVEGG-----EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE---LKI-- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 83 ySYRSQKIRmifqdPSTSLNPRQRISQIldfplrlNTDLDAEARQKQIIDTLRMVGLLPDHVSyyphMLAPGQKQRLGLA 162
Cdd:PRK13409 403 -SYKPQYIK-----PDYDGTVEDLLRSI-------TDDLGSSYYKSEIIKPLQLERLLDKNVK----DLSGGELQRVAIA 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490242029 163 RALILRPKVIVCDEALASLDMSMR---SQLINLMLELQEKQgisyIYVTQH-LGMMKHISDQVLV 223
Cdd:PRK13409 466 ACLSRDADLYLLDEPSAHLDVEQRlavAKAIRRIAEEREAT----ALVVDHdIYMIDYISDRLMV 526
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
22-194 |
8.69e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 60.25 E-value: 8.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 22 FHRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDysyRSQKIRMIFQDPSTsl 101
Cdd:PRK13543 19 FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD---RSRFMAYLGHLPGL-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 102 npRQRISQILDfpLRLNTDLDAEARQKQIIDTLRMVGlLPDHVSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASL 181
Cdd:PRK13543 94 --KADLSTLEN--LHFLCGLHGRRAKQMPGSALAIVG-LAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANL 168
|
170
....*....|...
gi 490242029 182 DMSMRSqLINLML 194
Cdd:PRK13543 169 DLEGIT-LVNRMI 180
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
24-240 |
1.41e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 59.91 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 24 RQTVEAVkplSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSYRSQK-IRMIFQDPstSLN 102
Cdd:PRK10895 16 RRVVEDV---SLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGYLPQEA--SIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 103 PRQRISQILDFPLRLNTDLDAEARQKqiidtlRMVGLLPD-HVSYYP----HMLAPGQKQRLGLARALILRPKVIVCDEA 177
Cdd:PRK10895 91 RRLSVYDNLMAVLQIRDDLSAEQRED------RANELMEEfHIEHLRdsmgQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490242029 178 LASLDmSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVLA 240
Cdd:PRK10895 165 FAGVD-PISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
34-243 |
2.43e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.41 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 34 SFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGElliddhpltfgdysYRSQkirmiFQDPS-TSLNPRQRIsqILD 112
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE--------------RQSQ-----FSHITrLSFEQLQKL--VSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 113 FPLRLNTDL--------------------DAEARQKQIIDTLRMVGLLPDHVSYyphmLAPGQKQRLGLARALILRPKVI 172
Cdd:PRK10938 82 EWQRNNTDMlspgeddtgrttaeiiqdevKDPARCEQLAQQFGITALLDRRFKY----LSTGETRKTLLCQALMSEPDLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490242029 173 VCDEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVLASPL 243
Cdd:PRK10938 158 ILDEPFDGLDVASRQQLAELLASLH-QSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQAL 227
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
25-239 |
3.27e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 59.06 E-value: 3.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 25 QTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGEllIDDHpltfGDYSYRSqkirmifqdPSTSLNPR 104
Cdd:PRK13546 35 KTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK--VDRN----GEVSVIA---------ISAGLSGQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 105 QRISQILDFPLRLNTDLDAEARQ--KQIIDTLRMVGLLPDHVSYYphmlAPGQKQRLGLARALILRPKVIVCDEALASLD 182
Cdd:PRK13546 100 LTGIENIEFKMLCMGFKRKEIKAmtPKIIEFSELGEFIYQPVKKY----SSGMRAKLGFSINITVNPDILVIDEALSVGD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490242029 183 MSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGSTADVL 239
Cdd:PRK13546 176 QTFAQKCLDKIYEFKE-QNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL 231
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
30-216 |
3.73e-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: 60.15 E-value: 3.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 30 VKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMvEPTSGELLIDDhpltfgdysyRSQKIRMIFQDPSTSLNP-RQRI- 107
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL-WPVYGGRLTKP----------AKGKLFYVPQRPYMTLGTlRDQIi 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 108 --SQILDFPLRLNTDLDAEarqkQIIDTLRMVGLLPDHVSY-----YPHMLAPGQKQRLGLARALILRPKVIVCDEALA- 179
Cdd:TIGR00954 537 ypDSSEDMKRRGLSDKDLE----QILDNVQLTHILEREGGWsavqdWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSa 612
|
170 180 190
....*....|....*....|....*....|....*...
gi 490242029 180 -SLDMSMRsqlinlMLELQEKQGISYIYVTQHLGMMKH 216
Cdd:TIGR00954 613 vSVDVEGY------MYRLCREFGITLFSVSHRKSLWKY 644
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
43-235 |
3.98e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 59.68 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 43 LAIIGENGSGKSTLAKMLAGMVEP---TSGELLIDDHPLTfgdysyrSQKIRMI----FQD----PstSLNPRQRisqiL 111
Cdd:TIGR00955 54 LAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPID-------AKEMRAIsayvQQDdlfiP--TLTVREH----L 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 112 DFP--LRLNTDLDAEARQKQIIDTLRMVGLLP--DHVSYYPHM---LAPGQKQRLGLARALILRPKVIVCDEALASLDMS 184
Cdd:TIGR00955 121 MFQahLRMPRRVTKKEKRERVDEVLQALGLRKcaNTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSF 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490242029 185 MRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGST 235
Cdd:TIGR00955 201 MAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSP 251
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
27-249 |
7.37e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.97 E-value: 7.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 27 VEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFgdysyRSQK------IRMIFQDpsts 100
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDF-----KSSKealengISMVHQE---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 101 LNP-RQRisQILD------FPLR-LNTDLDAEARQ-KQIIDTLRMVGLLPDHVSyyphMLAPGQKQRLGLARALILRPKV 171
Cdd:PRK10982 82 LNLvLQR--SVMDnmwlgrYPTKgMFVDQDKMYRDtKAIFDELDIDIDPRAKVA----TLSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 172 IVCDEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHNGEVVE----RGSTADVLASPL--HD 245
Cdd:PRK10982 156 VIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWIAtqplAGLTMDKIIAMMvgRS 234
|
....
gi 490242029 246 LTRR 249
Cdd:PRK10982 235 LTQR 238
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
29-229 |
1.06e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.60 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 29 AVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDysyrsqkirmifqdpstsLNPRQRI- 107
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGD------------------IATRRRVg 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 108 --SQilDFPL------RLNTDLDA------EARQKQIIDTL-RMVGLLpDHVSYYPHMLAPGQKQRLGLARALILRPKVI 172
Cdd:NF033858 343 ymSQ--AFSLygeltvRQNLELHArlfhlpAAEIAARVAEMlERFDLA-DVADALPDSLPLGIRQRLSLAVAVIHKPELL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490242029 173 VCDEALASLDMSMRSQLINLMLELQEKQGISyIYVTQHLgmMKH------ISdqvlVMHNGEV 229
Cdd:NF033858 420 ILDEPTSGVDPVARDMFWRLLIELSREDGVT-IFISTHF--MNEaercdrIS----LMHAGRV 475
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1-223 |
1.13e-09 |
|
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: 58.26 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 1 MVETLLEVRQLSKTFryrtGWFhRQTVEAVkplsfTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDhpltf 80
Cdd:COG1245 337 EEETLVEYPDLTKSY----GGF-SLEVEGG-----EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDL----- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 81 gDYSYRSQKIRmIFQDPSTSLNPRQRISQILD---------FPLRLNTDLDAEARQkqiidtlrmvgllpdhvsyyphmL 151
Cdd:COG1245 402 -KISYKPQYIS-PDYDGTVEEFLRSANTDDFGssyykteiiKPLGLEKLLDKNVKD-----------------------L 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490242029 152 APGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLV 223
Cdd:COG1245 457 SGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
29-234 |
1.29e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 58.49 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 29 AVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGDYSYRsQKIRMIFQdpSTSLNPRQRIS 108
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVR-QSLGMCPQ--HNILFHHLTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 109 QILDFPLRLNTDLDAEARqkqiidtLRMVGLLPDHVSYYPHM-----LAPGQKQRLGLARALILRPKVIVCDEALASLDM 183
Cdd:TIGR01257 1022 EHILFYAQLKGRSWEEAQ-------LEMEAMLEDTGLHHKRNeeaqdLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP 1094
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490242029 184 SMRSQLINLMLELqeKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGS 234
Cdd:TIGR01257 1095 YSRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
41-240 |
1.83e-09 |
|
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: 56.84 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 41 QTLAIIGENGSGKSTLAKMLAGMVEPTSGELLID-----DHPLtfgdYSYRSqKIRMIFQDPStslnprqrisqILDFPL 115
Cdd:cd03288 48 QKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDgidisKLPL----HTLRS-RLSIILQDPI-----------LFSGSI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 116 RLNTDLDAEARQKQIIDTLR------MVGLLPDH----VSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSM 185
Cdd:cd03288 112 RFNLDPECKCTDDRLWEALEiaqlknMVKSLPGGldavVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490242029 186 RSQLIN-LMLELQEKQGISYIYVTQHLgmmkHISDQVLVMHNGEVVERGSTADVLA 240
Cdd:cd03288 192 ENILQKvVMTAFADRTVVTIAHRVSTI----LDADLVLVLSRGILVECDTPENLLA 243
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-257 |
6.62e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.19 E-value: 6.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 3 ETLLEVRQLSktFRYRTGwfhrqtVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGD 82
Cdd:COG3845 255 EVVLEVENLS--VRDDRG------VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 83 YSYRSQK-IRMIFQDpstslnpRQRISQILDFPLRLNTDLD-----------------AEARQKQIIDTLRMVGLLPD-H 143
Cdd:COG3845 327 PRERRRLgVAYIPED-------RLGRGLVPDMSVAENLILGryrrppfsrggfldrkaIRAFAEELIEEFDVRTPGPDtP 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 144 VSyyphMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLG--MMkhISDQV 221
Cdd:COG3845 400 AR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDeiLA--LSDRI 472
|
250 260 270
....*....|....*....|....*....|....*...
gi 490242029 222 LVMHNGEVVERGSTADVlasplhDLTR--RLIAGHFGE 257
Cdd:COG3845 473 AVMYEGRIVGEVPAAEA------TREEigLLMAGVKEE 504
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-241 |
1.31e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 54.11 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 1 MVETLLEVRQLSKtfryrtgwfHRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTf 80
Cdd:PRK11614 1 MEKVMLSFDKVSA---------HYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 81 gdysyRSQKIRMIFQDPSTSLNPRQRISQIldfPLRLNTDL-----DAEARQKQIIDTLRMVGLLPDHVSYYPHMLAPGQ 155
Cdd:PRK11614 71 -----DWQTAKIMREAVAIVPEGRRVFSRM---TVEENLAMggffaERDQFQERIKWVYELFPRLHERRIQRAGTMSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 156 KQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGST 235
Cdd:PRK11614 143 QQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLRE-QGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTG 221
|
....*.
gi 490242029 236 ADVLAS 241
Cdd:PRK11614 222 DALLAN 227
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
43-229 |
2.45e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.41 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 43 LAIIGENGSGKSTLAKMLAGMVEPTSGELliddhPLTFG-DYSYRSQ-KIRMIFQDPStslnprqrisqildfPLRLNTD 120
Cdd:PRK10636 341 IGLLGRNGAGKSTLIKLLAGELAPVSGEI-----GLAKGiKLGYFAQhQLEFLRADES---------------PLQHLAR 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 121 LDAEARQKQIIDTLRMVGLLPDHVSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEkq 200
Cdd:PRK10636 401 LAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEG-- 478
|
170 180
....*....|....*....|....*....
gi 490242029 201 giSYIYVTQHLGMMKHISDQVLVMHNGEV 229
Cdd:PRK10636 479 --ALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-228 |
2.72e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 54.24 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 3 ETLLEVRQLSKTFryrtgwfhrQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTF-G 81
Cdd:PRK10762 2 QALLQLKGIDKAF---------PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFnG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 82 DYSYRSQKIRMIFQDpstsLN--PRQRISQildfplrlNTDLDAEARQK-QIIDTLRMV----GLLPD-HVSYYPHM--- 150
Cdd:PRK10762 73 PKSSQEAGIGIIHQE----LNliPQLTIAE--------NIFLGREFVNRfGRIDWKKMYaeadKLLARlNLRFSSDKlvg 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490242029 151 -LAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMHNGE 228
Cdd:PRK10762 141 eLSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKS-QGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
9-230 |
5.20e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 51.88 E-value: 5.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 9 RQLSKTFRYRtgwfhRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPT---SGELLIDDHPLTFGDYSY 85
Cdd:cd03233 7 RNISFTTGKG-----RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 RSQkirMIFQDPSTSLNPRQRISQILDFPLRLNTDldaearqkqiiDTLRMVgllpdhvsyyphmlAPGQKQRLGLARAL 165
Cdd:cd03233 82 PGE---IIYVSEEDVHFPTLTVRETLDFALRCKGN-----------EFVRGI--------------SGGERKRVSIAEAL 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490242029 166 ILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQGIS-YIYVTQHLGMMKHISDQVLVMHNGEVV 230
Cdd:cd03233 134 VSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTtFVSLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
32-230 |
1.12e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.22 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 32 PLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFgdysyRSQK--IRM-------------IFQD 96
Cdd:PRK11288 271 PISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDI-----RSPRdaIRAgimlcpedrkaegIIPV 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 97 PSTSLNprQRIS---QILDFPLRLNTDLDAEARQKQI---------IDTLRMvgllpdhvsyyphMLAPGQKQRLGLARA 164
Cdd:PRK11288 346 HSVADN--INISarrHHLRAGCLINNRWEAENADRFIrslniktpsREQLIM-------------NLSGGNQQKAILGRW 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490242029 165 LILRPKVIVCDEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMHNGEVV 230
Cdd:PRK11288 411 LSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAA-QGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
30-227 |
3.98e-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: 51.06 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 30 VKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELlidDHPltfGDYSYRSQKIRMIfqdPSTslnprqrISQ 109
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI---KHS---GRISFSPQTSWIM---PGT-------IKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 110 ILDFPLRLNtdldaEARQKQIIDTLRmvglLPDHVSYYPH-----------MLAPGQKQRLGLARALILRPKVIVCDEAL 178
Cdd:TIGR01271 506 NIIFGLSYD-----EYRYTSVIKACQ----LEEDIALFPEkdktvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPF 576
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490242029 179 ASLDMSMRSQLINLML-ELQEKQgiSYIYVTQHLGMMKHiSDQVLVMHNG 227
Cdd:TIGR01271 577 THLDVVTEKEIFESCLcKLMSNK--TRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-225 |
4.14e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 49.67 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 25 QTVEAVKPLSFTL------RERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELliDDHP-----LTF------GDY--SY 85
Cdd:cd03236 5 EPVHRYGPNSFKLhrlpvpREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKF--DDPPdwdeiLDEfrgselQNYftKL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 RSQKIRMIFQDPSTSLNPRQ---RISQILDfplrlntDLDAEARQKQIIDTLRMVGLLPDHVSYyphmLAPGQKQRLGLA 162
Cdd:cd03236 83 LEGDVKVIVKPQYVDLIPKAvkgKVGELLK-------KKDERGKLDELVDQLELRHVLDRNIDQ----LSGGELQRVAIA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490242029 163 RALILRPKVIVCDEALASLDMSMRSQLINLMLELQEKQgiSYIYVTQH-LGMMKHISDQVLVMH 225
Cdd:cd03236 152 AALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDD--NYVLVVEHdLAVLDYLSDYIHCLY 213
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-75 |
5.08e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 50.32 E-value: 5.08e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTFRYRTgwfhrqtveAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDD 75
Cdd:TIGR03719 323 IEAENLTKAFGDKL---------LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE 383
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-70 |
7.90e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.89 E-value: 7.90e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490242029 6 LEVRQLSKTFRYRTgwfhrqtveAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGE 70
Cdd:PRK15064 320 LEVENLTKGFDNGP---------LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT 375
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
31-211 |
7.96e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.86 E-value: 7.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 31 KPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELliddhpltfgdysYRSQKIRM-IFQDPST-----SLNPR 104
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-------------FRSAKVRMaVFSQHHVdgldlSSNPL 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 105 QRISQIldFPLRLNTDLDAEarqkqiIDTLRMVGLLPDHVSYyphMLAPGQKQRLGLARALILRPKVIVCDEALASLDMS 184
Cdd:PLN03073 593 LYMMRC--FPGVPEQKLRAH------LGSFGVTGNLALQPMY---TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLD 661
|
170 180
....*....|....*....|....*..
gi 490242029 185 MRSQLINLMLELQekQGISYIYVTQHL 211
Cdd:PLN03073 662 AVEALIQGLVLFQ--GGVLMVSHDEHL 686
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
40-228 |
9.97e-07 |
|
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: 47.37 E-value: 9.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 40 RQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIddhpltfgdysyrsqkirmifqdpstslnprqrisqildfplrlnt 119
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY---------------------------------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 120 dLDAEARQKQIIDTLRMVGLLPDhvsyyPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLI-----NLML 194
Cdd:smart00382 36 -IDGEDILEEVLDQLLLIIVGGK-----KASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRLLL 109
|
170 180 190
....*....|....*....|....*....|....*....
gi 490242029 195 ELQEKQGISYIYVTQHL-----GMMKHISDQVLVMHNGE 228
Cdd:smart00382 110 LLKSEKNLTVILTTNDEkdlgpALLRRRFDRRIVLLLIL 148
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-75 |
1.05e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.35 E-value: 1.05e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKTFRYRTgwfhrqtveAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDD 75
Cdd:PRK11819 325 IEAENLSKSFGDRL---------LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE 385
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
28-233 |
1.49e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 48.25 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 28 EAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGM--VEPTSGELLIDDHPLTFGDYSYRS-QKIRMIFQDP------- 97
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAgEGIFMAFQYPveipgvs 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 98 -----STSLNPRQRisqildfpLRLNTDLDAEARQKQIIDTLRMVGLLPDHVSYYPHM-LAPGQKQRLGLARALILRPKV 171
Cdd:PRK09580 95 nqfflQTALNAVRS--------YRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVgFSGGEKKRNDILQMAVLEPEL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490242029 172 IVCDEALASLDMSMRSQLINLMLELQEKQGiSYIYVTQHLGMMKHIS-DQVLVMHNGEVVERG 233
Cdd:PRK09580 167 CILDESDSGLDIDALKIVADGVNSLRDGKR-SFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
44-241 |
1.71e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.97 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 44 AIIGENGSGKSTLAKMLAGMVEPTSgelliDDHPLTFGDYSYRSQkIRMIFqdpstSLNPRQRISQILDF-PLRLNTDLD 122
Cdd:PLN03130 647 AIVGSTGEGKTSLISAMLGELPPRS-----DASVVIRGTVAYVPQ-VSWIF-----NATVRDNILFGSPFdPERYERAID 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 123 AEARQkqiidtlRMVGLLPDH----VSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLElQE 198
Cdd:PLN03130 716 VTALQ-------HDLDLLPGGdlteIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIK-DE 787
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490242029 199 KQGISYIYVTQHLGMMKHIsDQVLVMHNGEVVERGSTADVLAS 241
Cdd:PLN03130 788 LRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNN 829
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
33-182 |
2.02e-06 |
|
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: 48.75 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 33 LSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEpTSGELLIDdhpltfgDYSYRS---QKIRMIFqdpstSLNPrQRISq 109
Cdd:TIGR01271 1238 LSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQID-------GVSWNSvtlQTWRKAF-----GVIP-QKVF- 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 110 ILDFPLRLNTDLDAEARQKQIIDTLRMVGL------LPDHVSYY----PHMLAPGQKQRLGLARALILRPKVIVCDEALA 179
Cdd:TIGR01271 1303 IFSGTFRKNLDPYEQWSDEEIWKVAEEVGLksvieqFPDKLDFVlvdgGYVLSNGHKQLMCLARSILSKAKILLLDEPSA 1382
|
...
gi 490242029 180 SLD 182
Cdd:TIGR01271 1383 HLD 1385
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
30-182 |
2.49e-06 |
|
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: 47.54 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 30 VKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEpTSGELLIDdhpltfgDYSYRS---QKIRMIFqdpstSLNPRQR 106
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQID-------GVSWNSvplQKWRKAF-----GVIPQKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 107 IsqILDFPLRLNTDLDAEARQKQIIDTLRMVGL------LPDHVSYY----PHMLAPGQKQRLGLARALILRPKVIVCDE 176
Cdd:cd03289 87 F--IFSGTFRKNLDPYGKWSDEEIWKVAEEVGLksvieqFPGQLDFVlvdgGCVLSHGHKQLMCLARSVLSKAKILLLDE 164
|
....*.
gi 490242029 177 ALASLD 182
Cdd:cd03289 165 PSAHLD 170
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
30-228 |
2.51e-06 |
|
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: 47.54 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 30 VKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELlidDHPltfGDYSYRSQKIRMIfqdPSTslnprqrISQ 109
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI---KHS---GRISFSSQFSWIM---PGT-------IKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 110 ILDFPLRLNtdldaEARQKQIIDTLRmvglLPDHVSYYPH-----------MLAPGQKQRLGLARALILRPKVIVCDEAL 178
Cdd:cd03291 117 NIIFGVSYD-----EYRYKSVVKACQ----LEEDITKFPEkdntvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPF 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490242029 179 ASLDMSMRSQLI-NLMLELQEKQgiSYIYVTQHLGMMKhISDQVLVMHNGE 228
Cdd:cd03291 188 GYLDVFTEKEIFeSCVCKLMANK--TRILVTSKMEHLK-KADKILILHEGS 235
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
41-227 |
4.76e-06 |
|
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: 46.56 E-value: 4.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 41 QTLAIIGENGSGKSTLAKMLAGMVEPTSGELliddhpltfgdysYRSQKIRMIFQDPSTSLNPRQRISQILDFPLRLNTD 120
Cdd:cd03290 28 QLTMIVGQVGCGKSSLLLAILGEMQTLEGKV-------------HWSNKNESEPSFEATRSRNRYSVAYAAQKPWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 121 LDA---------EARQKQIIDTlrmVGLLPDhVSYYPH-----------MLAPGQKQRLGLARALILRPKVIVCDEALAS 180
Cdd:cd03290 95 VEEnitfgspfnKQRYKAVTDA---CSLQPD-IDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490242029 181 LDMSMRSQLINL-MLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHNG 227
Cdd:cd03290 171 LDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
35-182 |
5.44e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.25 E-value: 5.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 35 FTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLID----------DHP--LTFGDYSYRSQKI------------ 90
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEqdlivarlqqDPPrnVEGTVYDFVAEGIeeqaeylkryhd 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 91 --RMIFQDPSTS-LNPRQRISQILDfplrlntDLDAEARQKQIIDTLRMVGLLPD-HVSyyphMLAPGQKQRLGLARALI 166
Cdd:PRK11147 104 isHLVETDPSEKnLNELAKLQEQLD-------HHNLWQLENRINEVLAQLGLDPDaALS----SLSGGWLRKAALGRALV 172
|
170
....*....|....*.
gi 490242029 167 LRPKVIVCDEALASLD 182
Cdd:PRK11147 173 SNPDVLLLDEPTNHLD 188
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
6-257 |
8.22e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 46.27 E-value: 8.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 6 LEVRQLSKtfryrtgwfHRQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAkMLAGMVEPTSGElliddHPLTFGDYSY 85
Cdd:NF000106 14 VEVRGLVK---------HFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGR-----RPWRF*TWCA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 86 RSQKIRM-------IFQDPSTSLNPRQR---ISQILDFPLRlntdlDAEARQKQIIDTLRMVGLLPDHVSYYphmlAPGQ 155
Cdd:NF000106 79 NRRALRRtig*hrpVR*GRRESFSGRENlymIGR*LDLSRK-----DARARADELLERFSLTEAAGRAAAKY----SGGM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 156 KQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHNGEVVERGST 235
Cdd:NF000106 150 RRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV-RDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKV 228
|
250 260
....*....|....*....|..
gi 490242029 236 aDVLASPLHDLTRRLIAGHFGE 257
Cdd:NF000106 229 -DELKTKVGGRTLQIRPAHAAE 249
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
33-240 |
9.35e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 46.86 E-value: 9.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 33 LSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDdhpltfGDYSYRSQKirmifqdpstslnprqriSQILD 112
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMK------GSVAYVPQQ------------------AWIQN 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 113 FPLRLNTDLDAEARQKQIIDTLRMVGLLPDhVSYYPH-----------MLAPGQKQRLGLARALILRPKVIVCDEALASL 181
Cdd:TIGR00957 713 DSLRENILFGKALNEKYYQQVLEACALLPD-LEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 182 DMSMRSQLI-NLMLELQEKQGISYIYVTQHLGMMKHIsDQVLVMHNGEVVERGSTADVLA 240
Cdd:TIGR00957 792 DAHVGKHIFeHVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
30-182 |
1.34e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.10 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 30 VKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELliddHPLTFGDYSYrsqkirmiFQDPSTSLNPRQrisq 109
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI----HCGTKLEVAY--------FDQHRAELDPEK---- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 110 ildfplrlnTDLDAEARQKQIIdtlrMVGLLPDHV-SY-----YPHM--------LAPGQKQRLGLARaLILRP-KVIVC 174
Cdd:PRK11147 399 ---------TVMDNLAEGKQEV----MVNGRPRHVlGYlqdflFHPKramtpvkaLSGGERNRLLLAR-LFLKPsNLLIL 464
|
....*...
gi 490242029 175 DEALASLD 182
Cdd:PRK11147 465 DEPTNDLD 472
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
43-241 |
1.71e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.12 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 43 LAIIGENGSGKSTLAKMLAGMVEPTSgelliDDHPLTFGDYSYRSQkIRMIFqdpstSLNPRQRISQILDF-PLRLNTDL 121
Cdd:PLN03232 646 VAIVGGTGEGKTSLISAMLGELSHAE-----TSSVVIRGSVAYVPQ-VSWIF-----NATVRENILFGSDFeSERYWRAI 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 122 DAEARQKQIidtlrmvGLLPDH----VSYYPHMLAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLElQ 197
Cdd:PLN03232 715 DVTALQHDL-------DLLPGRdlteIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMK-D 786
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490242029 198 EKQGISYIYVTQHLGMMKHIsDQVLVMHNGEVVERGSTADVLAS 241
Cdd:PLN03232 787 ELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSKS 829
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
3-229 |
2.69e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.11 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 3 ETLLEVRQLSKTfryrtgwfhRQTveAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLI--------D 74
Cdd:PRK10982 248 EVILEVRNLTSL---------RQP--SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLhgkkinnhN 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 75 DHPLTFGDYSYRSQKIRM--IFQDPSTSLNprQRISQILDF--PLRLNTDLDAEARQKQIIDTLRMVglLPDHVSYYPHm 150
Cdd:PRK10982 317 ANEAINHGFALVTEERRStgIYAYLDIGFN--SLISNIRNYknKVGLLDNSRMKSDTQWVIDSMRVK--TPGHRTQIGS- 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 151 LAPGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEK-QGIsyIYVTQHLGMMKHISDQVLVMHNGEV 229
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKdKGI--IIISSEMPELLGITDRILVMSNGLV 469
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
37-107 |
3.57e-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: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 37 LRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLtfgdySYRSQKIRM---------------------IFQ 95
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP-----VYKPQYIDLsggelqrvaiaaallrnatfyLFD 96
|
90
....*....|..
gi 490242029 96 DPSTSLNPRQRI 107
Cdd:cd03222 97 EPSAYLDIEQRL 108
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
46-76 |
5.86e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.11 E-value: 5.86e-05
10 20 30
....*....|....*....|....*....|.
gi 490242029 46 IGENGSGKSTLAKMLAGMVEPTSGELLIDDH 76
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGNVSLDPN 63
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
45-243 |
8.16e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.00 E-value: 8.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 45 IIGENGSGKSTLAKMLAGMVEPTSGElliddhpltfgdysyrsqkirmIFQDPSTSLNPRQriSQILDFPLRLNTDLDAE 124
Cdd:PTZ00243 691 VLGATGSGKSTLLQSLLSQFEISEGR----------------------VWAERSIAYVPQQ--AWIMNATVRGNILFFDE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 125 ARQKQIIDTLRMVGLLPDHVSYYPHM----------LAPGQKQRLGLARALILRPKVIVCDEALASLDMSMrSQLINLML 194
Cdd:PTZ00243 747 EDAARLADAVRVSQLEADLAQLGGGLeteigekgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHV-GERVVEEC 825
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490242029 195 ELQEKQGISYIYVTQHLGMMKHiSDQVLVMHNGEVVERGSTADVLASPL 243
Cdd:PTZ00243 826 FLGALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFMRTSL 873
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
33-73 |
1.07e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.17 E-value: 1.07e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 490242029 33 LSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLI 73
Cdd:PRK13541 19 LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYY 59
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
36-228 |
1.85e-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: 42.46 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 36 TLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELlidDHPLT------------FGDY-----------SYRSQKIRM 92
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDY---DEEPSwdevlkrfrgteLQDYfkklangeikvAHKPQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 93 IfqdpstslnPRQ---RISQILDfplrlntDLDAEARQKQIIDTLRMVGLLPDHVSYyphmLAPGQKQRLGLARALILRP 169
Cdd:COG1245 172 I---------PKVfkgTVRELLE-------KVDERGKLDELAEKLGLENILDRDISE----LSGGELQRVAIAAALLRDA 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 170 KVIVCDEALASLDMSMRSQLINLMLELQEKQgiSYIYVTQH-LGMMKHISDQVLVMHnGE 228
Cdd:COG1245 232 DFYFFDEPSSYLDIYQRLNVARLIRELAEEG--KYVLVVEHdLAILDYLADYVHILY-GE 288
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
26-233 |
8.12e-04 |
|
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: 39.23 E-value: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 26 TVEAVKPLSFTLRERQTLAIIGENGSGKSTLAkmLAGMVEptSGELLIDDHPLTFGDysyrsQKIRMIFQdpstslnpRQ 105
Cdd:cd03238 7 NVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLYA--SGKARLISFLPKFSR-----NKLIFIDQ--------LQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 106 RISQI-LDFpLRLNtdldaearqkQIIDTLrmvgllpdhvsyyphmlAPGQKQRLGLARALILRPK--VIVCDEALASLD 182
Cdd:cd03238 70 FLIDVgLGY-LTLG----------QKLSTL-----------------SGGELQRVKLASELFSEPPgtLFILDEPSTGLH 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490242029 183 MSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHiSDQVLVM------HNGEVVERG 233
Cdd:cd03238 122 QQDINQLLEVIKGLID-LGNTVILIEHNLDVLSS-ADWIIDFgpgsgkSGGKVVFSG 176
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-231 |
1.35e-03 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 39.77 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 3 ETLLEVRQLSKTFRYRtgwfhrqtveaVKPLSFTLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELLIDDHPLTFGD 82
Cdd:PRK09700 263 ETVFEVRNVTSRDRKK-----------VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRS 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 83 ySYRSQKIRMIFQDPSTSLNP-------RQRIS---QILDFPLRLNTDLDAEARQKQIIDTLRMVGLLPDH-VSYYPHML 151
Cdd:PRK09700 332 -PLDAVKKGMAYITESRRDNGffpnfsiAQNMAisrSLKDGGYKGAMGLFHEVDEQRTAENQRELLALKCHsVNQNITEL 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 152 APGQKQRLGLARALILRPKVIVCDEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVLVMHNGEVVE 231
Cdd:PRK09700 411 SGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
33-135 |
1.41e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 39.21 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 33 LSFTLRERQTLaIIGENGSGKSTLAKMLAGMVEPTSGEL-LIDDHPLTFGDYSYRSQKIRMIFQDPS-----TSLNPRQR 106
Cdd:COG3950 19 IDFDNPPRLTV-LVGENGSGKTTLLEAIALALSGLLSRLdDVKFRKLLIRNGEFGDSAKLILYYGTSrllldGPLKKLER 97
|
90 100 110
....*....|....*....|....*....|
gi 490242029 107 ISQILDFPL-RLNTDLDAEARQKQIIDTLR 135
Cdd:COG3950 98 LKEEYFSRLdGYDSLLDEDSNLREFLEWLR 127
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
44-197 |
1.72e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 38.45 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 44 AIIGENGSGKSTL---------------AKMLAGMVEPTSGELLIDdhpLTF--GDYSYRSQKirmiFQ---DPSTSLNP 103
Cdd:COG0419 27 LIVGPNGAGKSTIleairyalygkarsrSKLRSDLINVGSEEASVE---LEFehGGKRYRIER----RQgefAEFLEAKP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 104 RQR---ISQILDFPL---------RLNTDLDAEARQKQIIDTL------RMVGLLPdhvsyyPHMLAPGQKQRLGLARAL 165
Cdd:COG0419 100 SERkeaLKRLLGLEIyeelkerlkELEEALESALEELAELQKLkqeilaQLSGLDP------IETLSGGERLRLALADLL 173
|
170 180 190
....*....|....*....|....*....|..
gi 490242029 166 ILrpkviVCDeaLASLDMSMRSQLINLMLELQ 197
Cdd:COG0419 174 SL-----ILD--FGSLDEERLERLLDALEELA 198
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
45-70 |
2.82e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 38.95 E-value: 2.82e-03
10 20
....*....|....*....|....*.
gi 490242029 45 IIGENGSGKSTLAKMLAGMVEPTSGE 70
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGE 63
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
23-94 |
4.04e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 38.10 E-value: 4.04e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490242029 23 HRQTVEAVKPLSFTLRerqTLAIIGENGSGKSTLAK----MLAGMVEPTSGELLIDDHPLTFGDYSYRSQKIRMIF 94
Cdd:COG1106 15 DELTLSMVASGLRLLR---VNLIYGANASGKSNLLEalyfLRNLVLNSSQPGDKLVEPFLLDSESKNEPSEFEILF 87
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
45-182 |
7.78e-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: 7.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 45 IIGENGSGKSTLAKMLAGMVEPTSGELLIDDhpltfgdysyrSQKIRMIFQDPstSLNPR-----------QRISQILDf 113
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEARPQP-----------GIKVGYLPQEP--QLDPTktvrenveegvAEIKDALD- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 114 plRLN------TDLDAE--------ARQKQIIDT----------------LRmvglLPDHVSYYPHmLAPGQKQRLGLAR 163
Cdd:TIGR03719 102 --RFNeisakyAEPDADfdklaaeqAELQEIIDAadawdldsqleiamdaLR----CPPWDADVTK-LSGGERRRVALCR 174
|
170
....*....|....*....
gi 490242029 164 ALILRPKVIVCDEALASLD 182
Cdd:TIGR03719 175 LLLSKPDMLLLDEPTNHLD 193
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
24-61 |
8.24e-03 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 37.48 E-value: 8.24e-03
10 20 30
....*....|....*....|....*....|....*...
gi 490242029 24 RQTVEAVKPLSFTLRERQTLAIIGENGSGKSTLAKMLA 61
Cdd:COG5635 164 LERIESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLA 201
|
|
| DUF87 |
pfam01935 |
Helicase HerA, central domain; This entry represents the central domain found in archaeal ... |
43-131 |
8.34e-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: 36.57 E-value: 8.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 43 LAIIGENGSGKSTLAK-MLAGMVE-PTSGELLIDDHpltfGDYSYR-----SQKIRMIFQDPSTSLNPRQ-RISQILDFP 114
Cdd:pfam01935 26 FAILGSTGSGKSNTVAvLLEELLEkKGATVLIFDPH----GEYGTLfrdlgAENVNVITPDPELKINPWLlSPEDLADLL 101
|
90
....*....|....*..
gi 490242029 115 LRLNtdLDAEARQKQII 131
Cdd:pfam01935 102 EELN--LPNAEVQRSIL 116
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
36-228 |
9.27e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 37.10 E-value: 9.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 36 TLRERQTLAIIGENGSGKSTLAKMLAGMVEPTSGELlidDHPLT------------FGDYSYR--------SQKIRMIfq 95
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDY---EEEPSwdevlkrfrgteLQNYFKKlyngeikvVHKPQYV-- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490242029 96 dpstSLNPRQ---RISQILdfplrlnTDLDAEARQKQIIDTLRMVGLLPDHVSYyphmLAPGQKQRLGLARALILRPKVI 172
Cdd:PRK13409 170 ----DLIPKVfkgKVRELL-------KKVDERGKLDEVVERLGLENILDRDISE----LSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490242029 173 VCDEALASLDMSMRSQLINLMLELQEKqgiSYIYVTQH-LGMMKHISDQVLVMHnGE 228
Cdd:PRK13409 235 FFDEPTSYLDIRQRLNVARLIRELAEG---KYVLVVEHdLAVLDYLADNVHIAY-GE 287
|
|
| MhpD |
COG3971 |
2-keto-4-pentenoate hydratase [Secondary metabolites biosynthesis, transport and catabolism]; |
220-261 |
9.33e-03 |
|
2-keto-4-pentenoate hydratase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443171 Cd Length: 259 Bit Score: 36.65 E-value: 9.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 490242029 220 QVLVMHNGEVVERGSTADVLASPLH---DLTRRLIAghFGEALTA 261
Cdd:COG3971 181 GVVLEKNGEVVATGAGAAVLGHPLNavaWLANKLAA--RGIPLKA 223
|
|
| PRK07261 |
PRK07261 |
DNA topology modulation protein; |
43-60 |
9.38e-03 |
|
DNA topology modulation protein;
Pssm-ID: 180911 [Multi-domain] Cd Length: 171 Bit Score: 36.23 E-value: 9.38e-03
|
| |
