|
Name |
Accession |
Description |
Interval |
E-value |
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
5-261 |
1.27e-170 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 471.24 E-value: 1.27e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 5 PLLRVSGINKTFFNRVGLFRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDT 84
Cdd:COG4167 3 ALLEVRNLSKTFKYRTGLFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 85 QKRCKLIRMIFQDPNSSLNPQLRVGRILEAPLRLNTDLSEEERANTVIETLRMVGMLPEHALFYPQMISLGQKQRVAFAR 164
Cdd:COG4167 83 KYRCKHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQKQRVALAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 165 ALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNPQ 244
Cdd:COG4167 163 ALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANPQ 242
|
250
....*....|....*..
gi 502191832 245 HDVTKRLIQNHGHEYRR 261
Cdd:COG4167 243 HEVTKRLIESHFGEALT 259
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
6-255 |
2.18e-122 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 349.47 E-value: 2.18e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 6 LLRVSGINKTFFNRVGLFRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQ 85
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 86 KRCKLIRMIFQDPNSSLNPQLRVGRILEAPLRLNTDLSEEERANTVIETLRMVGMLPEHALFYPQMISLGQKQRVAFARA 165
Cdd:PRK15112 84 YRSQRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 166 LILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNPQH 245
Cdd:PRK15112 164 LILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLH 243
|
250
....*....|
gi 502191832 246 DVTKRLIQNH 255
Cdd:PRK15112 244 ELTKRLIAGH 253
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-252 |
4.69e-110 |
|
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: 326.86 E-value: 4.69e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 2 NSAPLLRVSGINKTFFNRvglfRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAF 81
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVR----GKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTK 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 82 EDTQKRCKL---IRMIFQDPNSSLNPQLRVGRILEAPLRLNTDLSEEERANTVIETLRMVGMLPEHALFYPQMISLGQKQ 158
Cdd:COG1123 332 LSRRSLRELrrrVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 159 RVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSE 238
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEE 491
|
250
....*....|....
gi 502191832 239 VFSNPQHDVTKRLI 252
Cdd:COG1123 492 VFANPQHPYTRALL 505
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-252 |
1.51e-109 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 318.98 E-value: 1.51e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 1 MNSAPLLRVSGINKTFFNRVGLFRRK--QVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEV 78
Cdd:COG4608 2 AMAEPLLEVRDLKKHFPVRGGLFGRTvgVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 79 IAFEDTQKRCKL---IRMIFQDPNSSLNPQLRVGRILEAPLRLNTDLSEEERANTVIETLRMVGMLPEHALFYPQMISLG 155
Cdd:COG4608 82 ITGLSGRELRPLrrrMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEFSGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 156 QKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGL 235
Cdd:COG4608 162 QRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAP 241
|
250
....*....|....*..
gi 502191832 236 TSEVFSNPQHDVTKRLI 252
Cdd:COG4608 242 RDELYARPLHPYTQALL 258
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
3-252 |
4.58e-96 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 284.93 E-value: 4.58e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 3 SAPLLRVSGINKTFFNRVGLFR-RKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAF 81
Cdd:PRK11308 2 QQPLLQAIDLKKHYPVKRGLFKpERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 82 EDTQKRCKL---IRMIFQDPNSSLNPQLRVGRILEAPLRLNTDLSEEERANTVIETLRMVGMLPEHALFYPQMISLGQKQ 158
Cdd:PRK11308 82 ADPEAQKLLrqkIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 159 RVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSE 238
Cdd:PRK11308 162 RIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQ 241
|
250
....*....|....
gi 502191832 239 VFSNPQHDVTKRLI 252
Cdd:PRK11308 242 IFNNPRHPYTQALL 255
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-253 |
3.51e-94 |
|
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: 279.63 E-value: 3.51e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 6 LLRVSGINKTFFNRVGlfrrkQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPP---TSGEIEVNGEVIAF- 81
Cdd:COG0444 1 LLEVRNLKVYFPTRRG-----VVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 82 ---EDTQKRCKLIRMIFQDPNSSLNPQLRVGRILEAPLRLNTDLSEEERANTVIETLRMVGMLPEHALF--YPQMISLGQ 156
Cdd:COG0444 76 sekELRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLdrYPHELSGGM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 157 KQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLT 236
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPV 235
|
250
....*....|....*..
gi 502191832 237 SEVFSNPQHDVTKRLIQ 253
Cdd:COG0444 236 EELFENPRHPYTRALLS 252
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-253 |
7.86e-94 |
|
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: 276.30 E-value: 7.86e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 6 LLRVSGINKTFFNRvglfrRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQ 85
Cdd:COG1124 1 MLEVRNLSVSYGQG-----GRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 86 KRCKLIRMIFQDPNSSLNPQLRVGRILEAPLRLNTDLSEEERantVIETLRMVGmLPEHALF-YPQMISLGQKQRVAFAR 164
Cdd:COG1124 76 AFRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHGLPDREER---IAELLEQVG-LPPSFLDrYPHQLSGGQRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 165 ALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNPQ 244
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPK 231
|
....*....
gi 502191832 245 HDVTKRLIQ 253
Cdd:COG1124 232 HPYTRELLA 240
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-253 |
1.41e-90 |
|
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: 277.34 E-value: 1.41e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 2 NSAPLLRVSGINKTFFNRVGLFRRK--QVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPpTSGEIEVNGEVI 79
Cdd:COG4172 271 DAPPLLEARDLKVWFPIKRGLFRRTvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 80 A---FEDTQKRCKLIRMIFQDPNSSLNPQLRVGRILEAPLRL-NTDLSEEERANTVIETLRMVGMLPEHALFYPQMISLG 155
Cdd:COG4172 350 DglsRRALRPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVhGPGLSAAERRARVAEALEEVGLDPAARHRYPHEFSGG 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 156 QKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGL 235
Cdd:COG4172 430 QRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGP 509
|
250
....*....|....*...
gi 502191832 236 TSEVFSNPQHDVTKRLIQ 253
Cdd:COG4172 510 TEQVFDAPQHPYTRALLA 527
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-234 |
2.60e-90 |
|
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: 266.68 E-value: 2.60e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 6 LLRVSGINKTFFNRVGlfrrkQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQ 85
Cdd:cd03257 1 LLEVKNLSVSFPTGGG-----SVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 86 ---KRCKLIRMIFQDPNSSLNPQLRVGRILEAPLRLNTDLSEEERAN-TVIETLRMVGMLPEHALFYPQMISLGQKQRVA 161
Cdd:cd03257 76 lrkIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKeAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502191832 162 FARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESG 234
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
26-252 |
1.64e-73 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 227.28 E-value: 1.64e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 26 KQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNG-EVIAFEDTQKRC--KLIRMIFQDPNSSL 102
Cdd:PRK15079 32 KTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGkDLLGMKDDEWRAvrSDIQMIFQDPLASL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 103 NPQLRVGRILEAPLRL-NTDLSEEERANTVIETLRMVGMLPEHALFYPQMISLGQKQRVAFARALILDPKIIVADEAFSM 181
Cdd:PRK15079 112 NPRMTIGEIIAEPLRTyHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502191832 182 LDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNPQHDVTKRLI 252
Cdd:PRK15079 192 LDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALM 262
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-252 |
1.54e-68 |
|
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: 220.33 E-value: 1.54e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 1 MNSAPLLRVSGINKTFfnRVGlfrRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPP----TSGEIEVNG 76
Cdd:COG4172 1 MMSMPLLSVEDLSVAF--GQG---GGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDpaahPSGSILFDG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 77 -EVIAFEDTQKRcKL----IRMIFQDPNSSLNPQLRVGRILEAPLRLNTDLSEEERANTVIETLRMVGmLPE---HALFY 148
Cdd:COG4172 76 qDLLGLSERELR-RIrgnrIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVG-IPDperRLDAY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 149 PQMISLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQG 228
Cdd:COG4172 154 PHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQG 233
|
250 260
....*....|....*....|....
gi 502191832 229 EIVESGLTSEVFSNPQHDVTKRLI 252
Cdd:COG4172 234 EIVEQGPTAELFAAPQHPYTRKLL 257
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-252 |
5.47e-67 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 218.57 E-value: 5.47e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 5 PLLRVSGINKTFFNRVGLFRR--KQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIafe 82
Cdd:PRK10261 312 PILQVRNLVTRFPLRSGLLNRvtREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRI--- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 83 DTQKRCKL------IRMIFQDPNSSLNPQLRVGRILEAPLRLNTDLSEEERANTVIETLRMVGMLPEHALFYPQMISLGQ 156
Cdd:PRK10261 389 DTLSPGKLqalrrdIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQ 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 157 KQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLT 236
Cdd:PRK10261 469 RQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPR 548
|
250
....*....|....*.
gi 502191832 237 SEVFSNPQHDVTKRLI 252
Cdd:PRK10261 549 RAVFENPQHPYTRKLM 564
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-244 |
1.56e-65 |
|
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: 212.07 E-value: 1.56e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 4 APLLRVSGINKTFfnrvglfRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPT---SGEIEVNGEVIA 80
Cdd:COG1123 2 TPLLEVRDLSVRY-------PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 81 FEDTQKRCKLIRMIFQDPNSSLNPqLRVGRILEAPLRlNTDLSEEERANTVIETLRMVGmLPEHALFYPQMISLGQKQRV 160
Cdd:COG1123 75 ELSEALRGRRIGMVFQDPMTQLNP-VTVGDQIAEALE-NLGLSRAEARARVLELLEAVG-LERRLDRYPHQLSGGQRQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 161 AFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVF 240
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEIL 231
|
....
gi 502191832 241 SNPQ 244
Cdd:COG1123 232 AAPQ 235
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-243 |
3.73e-65 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 204.15 E-value: 3.73e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 5 PLLRVSGINKTFfNRVGLFRRKQVQ-VLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIA-FE 82
Cdd:PRK10419 2 TLLNVSGLSHHY-AHGGLSGKHQHQtVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAkLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 83 DTQKRC--KLIRMIFQDPNSSLNPQLRVGRILEAPLRLNTDLSEEERANTVIETLRMVGMLPEHALFYPQMISLGQKQRV 160
Cdd:PRK10419 81 RAQRKAfrRDIQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 161 AFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEV- 239
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKl 240
|
....*
gi 502191832 240 -FSNP 243
Cdd:PRK10419 241 tFSSP 245
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
6-251 |
8.68e-64 |
|
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: 200.42 E-value: 8.68e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 6 LLRVSGINKTFFNRvGLFRRKQ-VQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDT 84
Cdd:TIGR02769 2 LLEVRDVTHTYRTG-GLFGAKQrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 85 QKRCKL---IRMIFQDPNSSLNPQLRVGRILEAPLRLNTDLSEEERANTVIETLRMVGMLPEHALFYPQMISLGQKQRVA 161
Cdd:TIGR02769 81 KQRRAFrrdVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 162 FARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFS 241
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLS 240
|
250
....*....|
gi 502191832 242 NpQHDVTKRL 251
Cdd:TIGR02769 241 F-KHPAGRNL 249
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-253 |
4.54e-63 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 206.09 E-value: 4.54e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 2 NSAPLLRVSGINKTFFNRVGLFRRKQVQ--VLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPpTSGEIEVNGEVI 79
Cdd:PRK15134 271 PASPLLDVEQLQVAFPIRKGILKRTVDHnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 80 AFEDTQKRCKL---IRMIFQDPNSSLNPQLRVGRILEAPLRLN-TDLSEEERANTVIETLRMVGMLPEHALFYPQMISLG 155
Cdd:PRK15134 350 HNLNRRQLLPVrhrIQVVFQDPNSSLNPRLNVLQIIEEGLRVHqPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGG 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 156 QKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGL 235
Cdd:PRK15134 430 QRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGD 509
|
250
....*....|....*...
gi 502191832 236 TSEVFSNPQHDVTKRLIQ 253
Cdd:PRK15134 510 CERVFAAPQQEYTRQLLA 527
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
17-244 |
4.34e-62 |
|
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: 194.86 E-value: 4.34e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 17 FNRVGLFRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIRMIFQ 96
Cdd:COG1122 3 LENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 97 DPNSslnpQLrVGRILE-----APLRLNtdLSEEERANTVIETLRMVGMLpEHALFYPQMISLGQKQRVAFARALILDPK 171
Cdd:COG1122 83 NPDD----QL-FAPTVEedvafGPENLG--LPREEIRERVEEALELVGLE-HLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502191832 172 IIVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNPQ 244
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-240 |
4.63e-61 |
|
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: 192.50 E-value: 4.63e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 3 SAPLLRVSGINKTFFNRVglfrrkqvqVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFE 82
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRV---------VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 83 DTQKRCKLIR---MIFQDPN--SSLNpqlrVGRILEAPLRLNTDLSEEERANTVIETLRMVGmLPEHALFYPQMISLGQK 157
Cdd:COG1127 73 SEKELYELRRrigMLFQGGAlfDSLT----VFENVAFPLREHTDLSEAEIRELVLEKLELVG-LPGAADKMPSELSGGMR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 158 QRVAFARALILDPKIIVADEAFSMLD-VSMRSqVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLT 236
Cdd:COG1127 148 KRVALARALALDPEILLYDEPTAGLDpITSAV-IDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTP 226
|
....
gi 502191832 237 SEVF 240
Cdd:COG1127 227 EELL 230
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-253 |
2.69e-58 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 188.75 E-value: 2.69e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 7 LRVSGINKTFFNRvglfrRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQK 86
Cdd:COG1135 2 IELENLSKTFPTK-----GGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 87 RCKL---IRMIFQDPN--SSLNpqlrVGRILEAPLRLnTDLSEEERANTVIETLRMVGmLPEHALFYPQMISLGQKQRVA 161
Cdd:COG1135 77 LRAArrkIGMIFQHFNllSSRT----VAENVALPLEI-AGVPKAEIRKRVAELLELVG-LSDKADAYPSQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 162 FARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFS 241
Cdd:COG1135 151 IARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFA 230
|
250
....*....|..
gi 502191832 242 NPQHDVTKRLIQ 253
Cdd:COG1135 231 NPQSELTRRFLP 242
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-250 |
3.46e-58 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 185.20 E-value: 3.46e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 6 LLRVSGINKTFfnrvglfrrKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQ 85
Cdd:COG1126 1 MIEIENLHKSF---------GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 86 KRcKLIR---MIFQDPNssLNPQLRVGR-ILEAPLR-LNTDLSE-EERAntvIETLRMVGmLPEHALFYPQMISLGQKQR 159
Cdd:COG1126 72 IN-KLRRkvgMVFQQFN--LFPHLTVLEnVTLAPIKvKKMSKAEaEERA---MELLERVG-LADKADAYPAQLSGGQQQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 160 VAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEV 239
Cdd:COG1126 145 VAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEF 223
|
250
....*....|.
gi 502191832 240 FSNPQHDVTKR 250
Cdd:COG1126 224 FENPQHERTRA 234
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-244 |
8.63e-55 |
|
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: 176.15 E-value: 8.63e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 7 LRVSGINKTFFNRVglfrrkqvqVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIA----FE 82
Cdd:cd03261 1 IELRGLTKSFGGRT---------VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglseAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 83 DTQKRCKlIRMIFQDPN--SSLNpqlrVGRILEAPLRLNTDLSEEERANTVIETLRMVGmLPEHALFYPQMISLGQKQRV 160
Cdd:cd03261 72 LYRLRRR-MGMLFQSGAlfDSLT----VFENVAFPLREHTRLSEEEIREIVLEKLEAVG-LRGAEDLYPAELSGGMKKRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 161 AFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVF 240
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
....*.
gi 502191832 241 S--NPQ 244
Cdd:cd03261 226 AsdDPL 231
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-244 |
4.16e-54 |
|
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: 174.69 E-value: 4.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 6 LLRVSGINKTFFNRvglfrRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQ 85
Cdd:cd03258 1 MIELKNVSKVFGDT-----GGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 86 KRCKL---IRMIFQDPNssLNPQLRVGRILEAPLRLnTDLSEEERANTVIETLRMVGmLPEHALFYPQMISLGQKQRVAF 162
Cdd:cd03258 76 ELRKArrrIGMIFQHFN--LLSSRTVFENVALPLEI-AGVPKAEIEERVLELLELVG-LEDKADAYPAQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 163 ARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSN 242
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
..
gi 502191832 243 PQ 244
Cdd:cd03258 232 PQ 233
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
3-244 |
3.84e-53 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 175.67 E-value: 3.84e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 3 SAPLLRVSGINKTFfnrvglfrrKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFE 82
Cdd:COG3842 2 AMPALELENVSKRY---------GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 83 DTQKRCklIRMIFQDPnsSLNPQLRVGRILEAPLRLNtDLSEEERANTVIETLRMVGmLPEHALFYPQMISLGQKQRVAF 162
Cdd:COG3842 73 PPEKRN--VGMVFQDY--ALFPHLTVAENVAFGLRMR-GVPKAEIRARVAELLELVG-LEGLADRYPHQLSGGQQQRVAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 163 ARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLG--LVrhISDKVLIMHQGEIVESGLTSEVF 240
Cdd:COG3842 147 ARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEeaLA--LADRIAVMNDGRIEQVGTPEEIY 224
|
....
gi 502191832 241 SNPQ 244
Cdd:COG3842 225 ERPA 228
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-232 |
8.84e-53 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 171.81 E-value: 8.84e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 1 MN-SAPLLRVSGINKTFFNRVGlfrrkQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVI 79
Cdd:COG1116 1 MSaAAPALELRGVSKRFPTGGG-----GVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 80 AFEDTQkrcklIRMIFQDPnsSLNPQLRVGRILEAPLRLnTDLSEEERANTVIETLRMVGmLPEHALFYPQMISLGQKQR 159
Cdd:COG1116 76 TGPGPD-----RGVVFQEP--ALLPWLTVLDNVALGLEL-RGVPKAERRERARELLELVG-LAGFEDAYPHQLSGGMRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502191832 160 VAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLG----LvrhiSDKVLIM--HQGEIVE 232
Cdd:COG1116 147 VAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDeavfL----ADRVVVLsaRPGRIVE 221
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-234 |
1.28e-51 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 167.31 E-value: 1.28e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 7 LRVSGINKTFfnrvglfrrKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQK 86
Cdd:cd03259 1 LELKGLSKTY---------GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 87 RCklIRMIFQDPnsSLNPQLRVGRILEAPLRLNTdLSEEERANTVIETLRMVGmLPEHALFYPQMISLGQKQRVAFARAL 166
Cdd:cd03259 72 RN--IGMVFQDY--ALFPHLTVAENIAFGLKLRG-VPKAEIRARVRELLELVG-LEGLLNRYPHELSGGQQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502191832 167 ILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESG 234
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
23-229 |
1.98e-51 |
|
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: 166.87 E-value: 1.98e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 23 FRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIRMIFQDPNSsl 102
Cdd:cd03225 9 YPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNPDD-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 103 npQL---RVGRILEAPLRlNTDLSEEERANTVIETLRMVGM--LPEHalfYPQMISLGQKQRVAFARALILDPKIIVADE 177
Cdd:cd03225 87 --QFfgpTVEEEVAFGLE-NLGLPEEEIEERVEEALELVGLegLRDR---SPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502191832 178 AFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGE 229
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-232 |
4.33e-51 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 166.37 E-value: 4.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 4 APLLRVSGINKTFfnRVGlfrRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFED 83
Cdd:COG1136 2 SPLLELRNLTKSY--GTG---EGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 84 TQKRCKL----IRMIFQDPNssLNPQLRVGRILEAPLRLNtDLSEEERANTVIETLRMVGmLPEHALFYPQMISLGQKQR 159
Cdd:COG1136 77 ERELARLrrrhIGFVFQFFN--LLPELTALENVALPLLLA-GVSRKERRERARELLERVG-LGDRLDHRPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502191832 160 VAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHiSDKVLIMHQGEIVE 232
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
7-230 |
4.08e-50 |
|
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: 163.81 E-value: 4.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 7 LRVSGINKTFFNRvglfrRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQK 86
Cdd:cd03255 1 IELKNLSKTYGGG-----GEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 87 RCKLIR----MIFQDPNssLNPQLRVGRILEAPLRLNTDLSEEERANtVIETLRMVGmLPEHALFYPQMISLGQKQRVAF 162
Cdd:cd03255 76 LAAFRRrhigFVFQSFN--LLPDLTALENVELPLLLAGVPKKERRER-AEELLERVG-LGDRLNHYPSELSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502191832 163 ARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHiSDKVLIMHQGEI 230
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-253 |
4.24e-49 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 164.97 E-value: 4.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 8 RVSGINKTFfnRVGlfrRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNG-EVIAFEDTQK 86
Cdd:PRK11153 3 ELKNISKVF--PQG---GRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGqDLTALSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 87 RC--KLIRMIFQDPN--SSL----NPQLrvgrileaPLRLnTDLSEEERANTVIETLRMVGmLPEHALFYPQMISLGQKQ 158
Cdd:PRK11153 78 RKarRQIGMIFQHFNllSSRtvfdNVAL--------PLEL-AGTPKAEIKARVTELLELVG-LSDKADRYPAQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 159 RVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSE 238
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSE 227
|
250
....*....|....*
gi 502191832 239 VFSNPQHDVTKRLIQ 253
Cdd:PRK11153 228 VFSHPKHPLTREFIQ 242
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-232 |
8.64e-49 |
|
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: 160.33 E-value: 8.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 7 LRVSGINKTFFNRVGlfrrkQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQk 86
Cdd:cd03293 1 LEVRNVSKTYGGGGG-----AVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 87 rcklIRMIFQDPnsSLNPQLRVGRILEAPLRLNtDLSEEERANTVIETLRMVGmLPEHALFYPQMISLGQKQRVAFARAL 166
Cdd:cd03293 75 ----RGYVFQQD--ALLPWLTVLDNVALGLELQ-GVPKAEARERAEELLELVG-LSGFENAYPHQLSGGMRQRVALARAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502191832 167 ILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQ--GEIVE 232
Cdd:cd03293 147 AVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVA 214
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
2-253 |
1.33e-48 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 163.36 E-value: 1.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 2 NSAPLLRVSGINKTFFNRVGLfrrkqVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPP---TSGEIEVNG-E 77
Cdd:PRK09473 8 QADALLDVKDLRVTFSTPDGD-----VTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGrE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 78 VIAFEDTQ---KRCKLIRMIFQDPNSSLNPQLRVGRILEAPLRLNTDLSEEERANTVIETLRMVGMlPE---HALFYPQM 151
Cdd:PRK09473 83 ILNLPEKElnkLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKM-PEarkRMKMYPHE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 152 ISLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIV 231
Cdd:PRK09473 162 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTM 241
|
250 260
....*....|....*....|..
gi 502191832 232 ESGLTSEVFSNPQHDVTKRLIQ 253
Cdd:PRK09473 242 EYGNARDVFYQPSHPYSIGLLN 263
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-231 |
6.51e-47 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 156.37 E-value: 6.51e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 5 PLLRVSGINKTFFNrvglfrrkQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDT 84
Cdd:COG3638 1 PMLELRNLSKRYPG--------GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 85 QKRCKL---IRMIFQDPNssLNPQLRV------GR-----ILEAPLRLntdLSEEERANtVIETLRMVGMLpEHALFYPQ 150
Cdd:COG3638 73 RALRRLrrrIGMIFQQFN--LVPRLSVltnvlaGRlgrtsTWRSLLGL---FPPEDRER-ALEALERVGLA-DKAYQRAD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 151 MISLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEI 230
Cdd:COG3638 146 QLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
.
gi 502191832 231 V 231
Cdd:COG3638 226 V 226
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
27-242 |
6.78e-46 |
|
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: 154.51 E-value: 6.78e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 27 QVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDT--QKRCKlIRMIFQDPNSslnp 104
Cdd:TIGR04520 14 EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENlwEIRKK-VGMVFQNPDN---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 105 QLrVGRILE-----APLRLNTDLSE-EERantVIETLRMVGMLpEHALFYPQMISLGQKQRVAFARALILDPKIIVADEA 178
Cdd:TIGR04520 89 QF-VGATVEddvafGLENLGVPREEmRKR---VDEALKLVGME-DFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502191832 179 FSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHiSDKVLIMHQGEIVESGLTSEVFSN 242
Cdd:TIGR04520 164 TSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-244 |
8.91e-46 |
|
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: 153.16 E-value: 8.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 7 LRVSGINKTFfnrvglfrrKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQK 86
Cdd:cd03300 1 IELENVSKFY---------GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 87 RckLIRMIFQdpNSSLNPQLRVGRILEAPLRLNTdLSEEERANTVIETLRMVGMLpEHALFYPQMISLGQKQRVAFARAL 166
Cdd:cd03300 72 R--PVNTVFQ--NYALFPHLTVFENIAFGLRLKK-LPKAEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502191832 167 ILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNPQ 244
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
7-239 |
2.22e-45 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 152.14 E-value: 2.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 7 LRVSGINKTFfnrvglfrrKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQK 86
Cdd:COG1131 1 IEVRGLTKRY---------GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 87 RcKLIRMIFQDPNssLNPQLRVGRILE--APLRlntDLSEEERANTVIETLRMVGmLPEHALFYPQMISLGQKQRVAFAR 164
Cdd:COG1131 72 R-RRIGYVPQEPA--LYPDLTVRENLRffARLY---GLPRKEARERIDELLELFG-LTDAADRKVGTLSGGMKQRLGLAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502191832 165 ALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEV 239
Cdd:COG1131 145 ALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
7-229 |
4.40e-45 |
|
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: 149.64 E-value: 4.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 7 LRVSGINKTFfnrvglfrrKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFED--T 84
Cdd:cd03229 1 LELKNVSKRY---------GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 85 QKRCKLIRMIFQDPNssLNPQLRVGRILEAPLrlntdlseeerantvietlrmvgmlpehalfypqmiSLGQKQRVAFAR 164
Cdd:cd03229 72 PPLRRRIGMVFQDFA--LFPHLTVLENIALGL------------------------------------SGGQQQRVALAR 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502191832 165 ALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGE 229
Cdd:cd03229 114 ALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
31-180 |
5.43e-45 |
|
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: 148.56 E-value: 5.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 31 LKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIRMIFQDPNssLNPQLRVGR 110
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQ--LFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502191832 111 ILEAPLRL--NTDLSEEERANTVIETLRMVGMLPEHALFYPQMISLGQKQRVAFARALILDPKIIVADEAFS 180
Cdd:pfam00005 79 NLRLGLLLkgLSKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-252 |
8.80e-45 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 159.25 E-value: 8.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 1 MNSAPLLRVSGINKTFFNRvglfrRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEV------ 74
Cdd:PRK10261 7 LDARDVLAVENLNIAFMQE-----QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCdkmllr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 75 --NGEVIAF-EDTQKRCKLIR-----MIFQDPNSSLNPQLRVGRILEAPLRLNTDLSEEERANTVIETLRMVGMLPEHAL 146
Cdd:PRK10261 82 rrSRQVIELsEQSAAQMRHVRgadmaMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 147 F--YPQMISLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLI 224
Cdd:PRK10261 162 LsrYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLV 241
|
250 260
....*....|....*....|....*...
gi 502191832 225 MHQGEIVESGLTSEVFSNPQHDVTKRLI 252
Cdd:PRK10261 242 MYQGEAVETGSVEQIFHAPQHPYTRALL 269
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
7-244 |
1.08e-43 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 151.07 E-value: 1.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 7 LRVSGINKTFfnrvglfrrKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFE-DTQ 85
Cdd:COG1118 3 IEVRNISKRF---------GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNlPPR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 86 KRckliRM--IFQDPnsSLNPQLRVGRILEAPLRlNTDLSEEERANTVIETLRMVGmLPEHALFYPQMISLGQKQRVAFA 163
Cdd:COG1118 74 ER----RVgfVFQHY--ALFPHMTVAENIAFGLR-VRPPSKAEIRARVEELLELVQ-LEGLADRYPSQLSGGQRQRVALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 164 RALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNP 243
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRP 225
|
.
gi 502191832 244 Q 244
Cdd:COG1118 226 A 226
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
7-244 |
1.18e-43 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 147.85 E-value: 1.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 7 LRVSGINKTFFNRvglfrrkqvQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDT-- 84
Cdd:PRK11124 3 IQLNGINCFYGAH---------QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTps 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 85 QKRCKLIR----MIFQDPNssLNPQLRV-GRILEAPLRLnTDLSEEE---RANTVIETLRmvgmLPEHALFYPQMISLGQ 156
Cdd:PRK11124 74 DKAIRELRrnvgMVFQQYN--LWPHLTVqQNLIEAPCRV-LGLSKDQalaRAEKLLERLR----LKPYADRFPLHLSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 157 KQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQErLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGlT 236
Cdd:PRK11124 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAE-TGITQVIVTHEVEVARKTASRVVYMENGHIVEQG-D 224
|
....*...
gi 502191832 237 SEVFSNPQ 244
Cdd:PRK11124 225 ASCFTQPQ 232
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
29-230 |
6.00e-43 |
|
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: 145.37 E-value: 6.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 29 QVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIafEDTQKRCKLIR----MIFQDPNssLNP 104
Cdd:cd03262 14 HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL--TDDKKNINELRqkvgMVFQQFN--LFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 105 QLRV-GRILEAPLRLNtDLSEEERANTVIETLRMVGmLPEHALFYPQMISLGQKQRVAFARALILDPKIIVADEAFSMLD 183
Cdd:cd03262 90 HLTVlENITLAPIKVK-GMSKAEAEERALELLEKVG-LADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALD 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502191832 184 VSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEI 230
Cdd:cd03262 168 PELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
34-253 |
9.41e-43 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 147.97 E-value: 9.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 34 ISFTLEPGETLALVGETGSGKSTLAKILAGVVP-P---TSGEIEVNG-EVIAFEDTQKRcKLI----RMIFQDPNSSLNP 104
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPgrvMAEKLEFNGqDLQRISEKERR-NLVgaevAMIFQDPMTSLNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 105 QLRVG-RILEApLRLNTDLSEEERANTVIETLRMVGML-PEHAL-FYPQMISLGQKQRVAFARALILDPKIIVADEAFSM 181
Cdd:PRK11022 105 CYTVGfQIMEA-IKVHQGGNKKTRRQRAIDLLNQVGIPdPASRLdVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTA 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502191832 182 LDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNPQHDVTKRLIQ 253
Cdd:PRK11022 184 LDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLR 255
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-239 |
1.40e-42 |
|
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: 145.02 E-value: 1.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 7 LRVSGINKTFFNrvglfrrkQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQK 86
Cdd:cd03256 1 IEVENLSKTYPN--------GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 87 RCKL---IRMIFQDPNssLNPQLRVgriLEAPL--RLNT---------DLSEEERANTvIETLRMVGMLpEHALFYPQMI 152
Cdd:cd03256 73 LRQLrrqIGMIFQQFN--LIERLSV---LENVLsgRLGRrstwrslfgLFPKEEKQRA-LAALERVGLL-DKAYQRADQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 153 SLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVE 232
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVF 225
|
....*..
gi 502191832 233 SGLTSEV 239
Cdd:cd03256 226 DGPPAEL 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-239 |
1.65e-42 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 150.94 E-value: 1.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 3 SAPLLRVSGINKTFFNrvglfrrkqVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFE 82
Cdd:COG1129 1 AEPLLEMRGISKSFGG---------VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 83 DTQKRCKL-IRMIFQDPNssLNPQLRV------GRILEAPLRLNTDlSEEERANTVIETL-------RMVGMLpehalfy 148
Cdd:COG1129 72 SPRDAQAAgIAIIHQELN--LVPNLSVaeniflGREPRRGGLIDWR-AMRRRARELLARLgldidpdTPVGDL------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 149 pqmiSLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQG 228
Cdd:COG1129 142 ----SVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDG 216
|
250
....*....|.
gi 502191832 229 EIVESGLTSEV 239
Cdd:COG1129 217 RLVGTGPVAEL 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
17-234 |
2.71e-42 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 143.65 E-value: 2.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 17 FNRVGLFRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAfedTQKRCKL------ 90
Cdd:COG2884 4 FENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLS---RLKRREIpylrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 91 IRMIFQDPNssLNPQLRVGRILEAPLRLnTDLSEEERANTVIETLRMVGMLpEHALFYPQMISLGQKQRVAFARALILDP 170
Cdd:COG2884 81 IGVVFQDFR--LLPDRTVYENVALPLRV-TGKSRKEIRRRVREVLDLVGLS-DKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502191832 171 KIIVADEAFSMLDVSMRSQVVNLLLKLQeRLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESG 234
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
24-254 |
2.80e-42 |
|
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: 145.09 E-value: 2.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 24 RRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAF----EDTQKRCKLIRMIFQdpN 99
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmsrkELRELRRKKISMVFQ--S 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 100 SSLNPQLRVGRILEAPLRLNtDLSEEERANTVIETLRMVGmLPEHALFYPQMISLGQKQRVAFARALILDPKIIVADEAF 179
Cdd:cd03294 111 FALLPHRTVLENVAFGLEVQ-GVPRAEREERAAEALELVG-LEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502191832 180 SMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNPQHDVTKRLIQN 254
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRG 263
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
7-245 |
4.38e-42 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 146.76 E-value: 4.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 7 LRVSGINKTFfnrvglfrrKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQK 86
Cdd:COG3839 4 LELENVSKSY---------GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 87 RCklIRMIFQDPnsSLNPQLRVGRILEAPLRLNtDLSEEERANTVIETLRMVGMlpEHAL-FYPQMISLGQKQRVAFARA 165
Cdd:COG3839 75 RN--IAMVFQSY--ALYPHMTVYENIAFPLKLR-KVPKAEIDRRVREAAELLGL--EDLLdRKPKQLSGGQRQRVALGRA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 166 LILDPKIIVADEAFSMLD----VSMRSQvvnlLLKLQERLGLSYVVVAND----LGLvrhiSDKVLIMHQGEIVESGLTS 237
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDaklrVEMRAE----IKRLHRRLGTTTIYVTHDqveaMTL----ADRIAVMNDGRIQQVGTPE 219
|
....*...
gi 502191832 238 EVFSNPQH 245
Cdd:COG3839 220 ELYDRPAN 227
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-239 |
4.68e-42 |
|
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: 143.84 E-value: 4.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 6 LLRVSGINKTFfnrvglfrrKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQ 85
Cdd:COG4555 1 MIEVENLSKKY---------GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 86 KRcKLIRMIFQDPNssLNPQLRVGRILE--APLRLNTDLSEEERANTVIETLRMVGMLPEHALFYpqmiSLGQKQRVAFA 163
Cdd:COG4555 72 AR-RQIGVLPDERG--LYDRLTVRENIRyfAELYGLFDEELKKRIEELIELLGLEEFLDRRVGEL----STGMKKKVALA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502191832 164 RALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEV 239
Cdd:COG4555 145 RALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-241 |
6.93e-42 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 144.39 E-value: 6.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 5 PLLRVSGINktffnrvglFRRKQV--QVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFE 82
Cdd:PRK13635 4 EIIRVEHIS---------FRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 83 DTQKRCKLIRMIFQDPNSSLnpqlrVGRILEAPLRL---NTDLSEEERANTVIETLRMVGMLpEHALFYPQMISLGQKQR 159
Cdd:PRK13635 75 TVWDVRRQVGMVFQNPDNQF-----VGATVQDDVAFgleNIGVPREEMVERVDQALRQVGME-DFLNREPHRLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 160 VAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHiSDKVLIMHQGEIVESGLTSEV 239
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
..
gi 502191832 240 FS 241
Cdd:PRK13635 228 FK 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
23-252 |
1.16e-41 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 149.47 E-value: 1.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 23 FRRKQV--QVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPP-----TSGEIEVNGEVIAFEDTQK----RCKLI 91
Cdd:PRK15134 15 FRQQQTvrTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSppvvyPSGDIRFHGESLLHASEQTlrgvRGNKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 92 RMIFQDPNSSLNPQLRVGRILEAPLRLNTDLSEEERANTVIETLRMVGM--LPEHALFYPQMISLGQKQRVAFARALILD 169
Cdd:PRK15134 95 AMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIrqAAKRLTDYPHQLSGGERQRVMIAMALLTR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 170 PKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNPQHDVTK 249
Cdd:PRK15134 175 PELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQ 254
|
...
gi 502191832 250 RLI 252
Cdd:PRK15134 255 KLL 257
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-230 |
3.05e-41 |
|
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: 139.46 E-value: 3.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 7 LRVSGINKTFfnrvglfrrKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIaFEDTQK 86
Cdd:cd03230 1 IEVRNLSKRY---------GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI-KKEPEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 87 RCKLIRMIFQDPnsSLNPQLrvgrileaplrlntdlseeeranTVIETLRMvgmlpehalfypqmiSLGQKQRVAFARAL 166
Cdd:cd03230 71 VKRRIGYLPEEP--SLYENL-----------------------TVRENLKL---------------SGGMKQRLALAQAL 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502191832 167 ILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEI 230
Cdd:cd03230 111 LHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-252 |
3.65e-41 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 141.99 E-value: 3.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 1 MNSAPLLRVSGINKTFFNRVGLfrrkqvqvlKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNG---- 76
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRKGC---------RDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgq 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 77 --EVIAFEDTQKRcKLIR----MIFQDPNSSLNPQLRVG-----RILEAPLRLNTDLSEeeranTVIETLRMVGMLPEHA 145
Cdd:PRK11701 72 lrDLYALSEAERR-RLLRtewgFVHQHPRDGLRMQVSAGgnigeRLMAVGARHYGDIRA-----TAGDWLERVEIDAARI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 146 LFYPQMISLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIM 225
Cdd:PRK11701 146 DDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVM 225
|
250 260
....*....|....*....|....*..
gi 502191832 226 HQGEIVESGLTSEVFSNPQHDVTKRLI 252
Cdd:PRK11701 226 KQGRVVESGLTDQVLDDPQHPYTQLLV 252
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
30-246 |
2.29e-40 |
|
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: 139.39 E-value: 2.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 30 VLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRckliRMIFQDPNSSLNPQLRVG 109
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR----DISYVPQNYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 110 RILEAPLRLNTdLSEEERANTVIETLRMVGMlpEHALF-YPQMISLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRS 188
Cdd:cd03299 90 KNIAYGLKKRK-VDKKEIERKVLEIAEMLGI--DHLLNrKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502191832 189 QVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNPQHD 246
Cdd:cd03299 167 KLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNE 224
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
17-253 |
3.25e-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: 3.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 17 FNRVGLFRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIRMIFQ 96
Cdd:cd03295 3 FENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 97 dpNSSLNPQLRVGRILEAPLRLNtDLSEEERANTVIETLRMVGMLPEH-ALFYPQMISLGQKQRVAFARALILDPKIIVA 175
Cdd:cd03295 83 --QIGLFPHMTVEENIALVPKLL-KWPKEKIRERADELLALVGLDPAEfADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502191832 176 DEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNPQHDVTKRLIQ 253
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVG 237
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
7-244 |
5.87e-40 |
|
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: 138.34 E-value: 5.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 7 LRVSGINKTFfnrvglfrrKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQK 86
Cdd:cd03219 1 LEVRGLTKRF---------GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 87 RCKL-IRMIFQDPN--SSL----NpqLRVGRILEAPLRLNTDL---SEEERANTVIETLRMVGmLPEHALFYPQMISLGQ 156
Cdd:cd03219 72 IARLgIGRTFQIPRlfPELtvleN--VMVAAQARTGSGLLLARarrEEREARERAEELLERVG-LADLADRPAGELSYGQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 157 KQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLT 236
Cdd:cd03219 149 QRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTP 227
|
....*...
gi 502191832 237 SEVFSNPQ 244
Cdd:cd03219 228 DEVRNNPR 235
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
23-241 |
6.39e-40 |
|
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: 138.64 E-value: 6.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 23 FRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIRMIFQDPNSSL 102
Cdd:COG1120 9 VGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEPPAPF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 103 NpqLRV------GRIleAPLRLNTDLSEEERAnTVIETLRMVGMLpEHALFYPQMISLGQKQRVAFARALILDPKIIVAD 176
Cdd:COG1120 89 G--LTVrelvalGRY--PHLGLFGRPSAEDRE-AVEEALERTGLE-HLADRPVDELSGGERQRVLIARALAQEPPLLLLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502191832 177 EAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFS 241
Cdd:COG1120 163 EPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
29-244 |
7.34e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 138.97 E-value: 7.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 29 QVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIRMIFQDPNSSLnpqlrV 108
Cdd:PRK13632 23 NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIFQNPDNQF-----I 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 109 GRILEAPLRL---NTDLSEEERANTVIETLRMVGMLpEHALFYPQMISLGQKQRVAFARALILDPKIIVADEAFSMLDVS 185
Cdd:PRK13632 98 GATVEDDIAFgleNKKVPPKKMKDIIDDLAKKVGME-DYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPK 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502191832 186 MRSQVVNLLLKLQERLGLSYVVVANDLGLVRhISDKVLIMHQGEIVESGLTSEVFSNPQ 244
Cdd:PRK13632 177 GKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
26-229 |
2.66e-39 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 134.43 E-value: 2.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 26 KQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIRMIFQDPNsslnpq 105
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQDPF------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 106 lrvgrILEAPLRLNtdlseeerantvietlrmvgmlpehalfypqMISLGQKQRVAFARALILDPKIIVADEAFSMLDVS 185
Cdd:cd03228 87 -----LFSGTIREN-------------------------------ILSGGQRQRIAIARALLRDPPILILDEATSALDPE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502191832 186 MRSQVVNLLLKLQERLGLsyVVVANDLGLVRHiSDKVLIMHQGE 229
Cdd:cd03228 131 TEALILEALRALAKGKTV--IVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-241 |
2.92e-39 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 136.76 E-value: 2.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 1 MNSAPLLRVSGINktffnrvglFRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGevia 80
Cdd:COG1121 1 MMMMPAIELENLT---------VSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 81 fEDTQKRCKLIRMIFQDPNSSLNPQLRV------GRILEAPLRLNtdLSEEERAnTVIETLRMVGMLPehalFYPQMISL 154
Cdd:COG1121 68 -KPPRRARRRIGYVPQRAEVDWDFPITVrdvvlmGRYGRRGLFRR--PSRADRE-AVDEALERVGLED----LADRPIGE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 155 ---GQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGeIV 231
Cdd:COG1121 140 lsgGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRG-LV 217
|
250
....*....|
gi 502191832 232 ESGLTSEVFS 241
Cdd:COG1121 218 AHGPPEEVLT 227
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
23-230 |
4.95e-39 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 134.94 E-value: 4.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 23 FRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVI-AFEDTQKRcKLIRMIFQDpnss 101
Cdd:COG4619 8 FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLsAMPPPEWR-RQVAYVPQE---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 102 lnPQL---RVGRILEAPLRLNTDLSEEERANTVIETLrmvgMLPEHALFYP-QMISLGQKQRVAFARALILDPKIIVADE 177
Cdd:COG4619 83 --PALwggTVRDNLPFPFQLRERKFDRERALELLERL----GLPPDILDKPvERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502191832 178 AFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEI 230
Cdd:COG4619 157 PTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
23-229 |
8.04e-39 |
|
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: 132.75 E-value: 8.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 23 FRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIRMIFQdpnssl 102
Cdd:cd00267 7 FRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 103 npqlrvgrileaplrlntdlseeerantvietlrmvgmlpehalfypqmISLGQKQRVAFARALILDPKIIVADEAFSML 182
Cdd:cd00267 81 -------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGL 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502191832 183 DVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGE 229
Cdd:cd00267 112 DPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
17-240 |
1.07e-38 |
|
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: 134.66 E-value: 1.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 17 FNRVGLFRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNG-EVIAFEDTQKRcKLIRMIF 95
Cdd:cd03254 5 FENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGiDIRDISRKSLR-SMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 96 QDpnsslnPQLRVGRILEApLRLNTDLSEEERantVIETLRMVGM------LPEHALFYP----QMISLGQKQRVAFARA 165
Cdd:cd03254 84 QD------TFLFSGTIMEN-IRLGRPNATDEE---VIEAAKEAGAhdfimkLPNGYDTVLgengGNLSQGERQLLAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502191832 166 LILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQErlGLSYVVVANDLGLVRHiSDKVLIMHQGEIVESGLTSEVF 240
Cdd:cd03254 154 MLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELL 225
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-231 |
1.20e-38 |
|
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: 132.55 E-value: 1.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 7 LRVSGINKTFfnrvglfrrKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQK 86
Cdd:cd03216 1 LELRGITKRF---------GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 87 RCKL-IRMIFQdpnsslnpqlrvgrileaplrlntdlseeerantvietlrmvgmlpehalfypqmISLGQKQRVAFARA 165
Cdd:cd03216 72 ARRAgIAMVYQ-------------------------------------------------------LSVGERQMVEIARA 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502191832 166 LILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEIV 231
Cdd:cd03216 97 LARNARLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
34-252 |
1.11e-37 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 132.19 E-value: 1.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 34 ISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRckLIRMIFQDPNssLNPQLRVGRILE 113
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAER--PVSMLFQENN--LFPHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 114 APLRLNTDLSEEERAnTVIETLRMVGmLPEHALFYPQMISLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNL 193
Cdd:COG3840 94 LGLRPGLKLTAEQRA-QVEQALERVG-LAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502191832 194 LLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNPQHDVTKRLI 252
Cdd:COG3840 172 VDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-234 |
2.17e-37 |
|
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: 130.84 E-value: 2.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 7 LRVSGINKTFFNRVglfrrkqvqVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQK 86
Cdd:cd03301 1 VELENVTKRFGNVT---------ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 87 RCklIRMIFQdpNSSLNPQLRVGRILEAPLRLNtDLSEEERANTVIETLRMVGMlpEHAL-FYPQMISLGQKQRVAFARA 165
Cdd:cd03301 72 RD--IAMVFQ--NYALYPHMTVYDNIAFGLKLR-KVPKDEIDERVREVAELLQI--EHLLdRKPKQLSGGQRQRVALGRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502191832 166 LILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESG 234
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
30-234 |
4.98e-37 |
|
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: 138.04 E-value: 4.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 30 VLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIRMIFQDpnsslnPQLRVG 109
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQD------VFLFSG 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 110 RILEApLRL-NTDLSEEErantVIETLRMVG--------------MLPEHAlfypQMISLGQKQRVAFARALILDPKIIV 174
Cdd:COG2274 564 TIREN-ITLgDPDATDEE----IIEAARLAGlhdfiealpmgydtVVGEGG----SNLSGGQRQRLAIARALLRNPRILI 634
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 175 ADEAFSMLDVSMRSQVVNLLLKLQERLGLsyVVVANDLGLVRHiSDKVLIMHQGEIVESG 234
Cdd:COG2274 635 LDEATSALDAETEAIILENLRRLLKGRTV--IIIAHRLSTIRL-ADRIIVLDKGRIVEDG 691
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
29-244 |
1.71e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 130.20 E-value: 1.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 29 QVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQ--KRCKLIRMIFQDPNSslnpQL 106
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllEVRKTVGIVFQNPDD----QL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 107 RVGRILE--APLRLNTDLSEEERANTVIETLRMVGML-----PEHALfypqmiSLGQKQRVAFARALILDPKIIVADEAF 179
Cdd:PRK13639 92 FAPTVEEdvAFGPLNLGLSKEEVEKRVKEALKAVGMEgfenkPPHHL------SGGQKKRVAIAGILAMKPEIIVLDEPT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502191832 180 SMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNPQ 244
Cdd:PRK13639 166 SGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
17-234 |
3.50e-36 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 134.91 E-value: 3.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 17 FNRVGlFR-RKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAfEDTQK--RcKLIRM 93
Cdd:COG1132 342 FENVS-FSyPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIR-DLTLEslR-RQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 94 IFQDP---NSSL--NpqLRVGRIleaplrlntDLSEEErantVIETLRMVGMLPE-HALfyPQ-----------MISLGQ 156
Cdd:COG1132 419 VPQDTflfSGTIreN--IRYGRP---------DATDEE----VEEAAKAAQAHEFiEAL--PDgydtvvgergvNLSGGQ 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502191832 157 KQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQErlGLSYVVVANDLGLVRHiSDKVLIMHQGEIVESG 234
Cdd:COG1132 482 RQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQG 556
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
31-242 |
4.20e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 129.78 E-value: 4.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 31 LKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIafedTQKRCKL--IR----MIFQDPNSSLNP 104
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDI----TDKKVKLsdIRkkvgLVFQYPEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 105 QLRVGRILEAPLRLNtdLSEEERANTVIETLRMVGMLPE-HALFYPQMISLGQKQRVAFARALILDPKIIVADEAFSMLD 183
Cdd:PRK13637 99 ETIEKDIAFGPINLG--LSEEEIENRVKRAMNIVGLDYEdYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502191832 184 VSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSN 242
Cdd:PRK13637 177 PKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
23-234 |
4.36e-36 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 126.40 E-value: 4.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 23 FRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIrmifqdpnsSL 102
Cdd:cd03214 7 VGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKI---------AY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 103 NPQlrvgrILEApLRLnTDLSEeerantvietlRMVGMLpehalfypqmiSLGQKQRVAFARALILDPKIIVADEAFSML 182
Cdd:cd03214 78 VPQ-----ALEL-LGL-AHLAD-----------RPFNEL-----------SGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502191832 183 DVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESG 234
Cdd:cd03214 129 DIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-238 |
6.85e-36 |
|
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: 127.55 E-value: 6.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 3 SAPLLRVSGINKTFFNRVGlfrrkQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAF- 81
Cdd:COG4181 5 SAPIIELRGLTKTVGTGAG-----ELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 82 -ED--TQKRCKLIRMIFQdpNSSLNPQLRVgriLE---APLRLNTDLSEEERAntvIETLRMVGmLPEHALFYPQMISLG 155
Cdd:COG4181 80 dEDarARLRARHVGFVFQ--SFQLLPTLTA---LEnvmLPLELAGRRDARARA---RALLERVG-LGHRLDHYPAQLSGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 156 QKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHiSDKVLIMHQGEIVESGL 235
Cdd:COG4181 151 EQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTA 229
|
...
gi 502191832 236 TSE 238
Cdd:COG4181 230 ATA 232
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
23-225 |
7.25e-36 |
|
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: 126.88 E-value: 7.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 23 FRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEviafeDTQKRCKLIRMIFQdpNSSL 102
Cdd:cd03235 7 VSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERKRIGYVPQ--RRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 103 NPQLRVgRILE-------APLRLNTDLSEEERAnTVIETLRMVGMLpEHALFYPQMISLGQKQRVAFARALILDPKIIVA 175
Cdd:cd03235 80 DRDFPI-SVRDvvlmglyGHKGLFRRLSKADKA-KVDEALERVGLS-ELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502191832 176 DEAFSMLDVSMRSQVVNLLLKLQeRLGLSYVVVANDLGLVRHISDKVLIM 225
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELR-REGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
29-234 |
7.47e-36 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 133.73 E-value: 7.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 29 QVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIRMIFQdpnsslNPQLRV 108
Cdd:COG4988 351 PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQ------NPYLFA 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 109 GRILEApLRL-NTDLSEEErantVIETLRMVGM------LP--------EHAlfypQMISLGQKQRVAFARALILDPKII 173
Cdd:COG4988 425 GTIREN-LRLgRPDASDEE----LEAALEAAGLdefvaaLPdgldtplgEGG----RGLSGGQAQRLALARALLRDAPLL 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502191832 174 VADEAFSMLDVSMRSQVVNLLLKLQErlGLSYVVVANDLGLVRHiSDKVLIMHQGEIVESG 234
Cdd:COG4988 496 LLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDDGRIVEQG 553
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
27-255 |
1.22e-35 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 127.51 E-value: 1.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 27 QVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPP----TSGEIEVNGEVIAFEDTqkRCKLIRMIFQDPNSSL 102
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCAL--RGRKIATIMQNPRSAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 103 NPQLRVGRILEAPLRLntdLSEEERANTVIETLRMVGMLPEHALF--YPQMISLGQKQRVAFARALILDPKIIVADEAFS 180
Cdd:PRK10418 93 NPLHTMHTHARETCLA---LGKPADDATLTAALEAVGLENAARVLklYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502191832 181 MLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNPQHDVTKRLIQNH 255
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSAH 244
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
33-243 |
1.32e-35 |
|
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: 129.84 E-value: 1.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 33 DISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEViaFEDTQKRCKL------IRMIFQDPnsSLNPQL 106
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEV--LQDSARGIFLpphrrrIGYVFQEA--RLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 107 RVGRILEAPLRLNTDLSEEERANTVIETLRMvgmlpEHAL-FYPQMISLGQKQRVAFARALILDPKIIVADEAFSMLDVS 185
Cdd:COG4148 93 SVRGNLLYGRKRAPRAERRISFDEVVELLGI-----GHLLdRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502191832 186 MRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNP 243
Cdd:COG4148 168 RKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
25-259 |
1.91e-35 |
|
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: 126.50 E-value: 1.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 25 RKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIRMIFQDpnsslnP 104
Cdd:cd03249 13 RPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQE------P 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 105 QLRVGRILEAPL--RLNTDLSEEERANTVIETLRMVGMLPE----HALFYPQMISLGQKQRVAFARALILDPKIIVADEA 178
Cdd:cd03249 87 VLFDGTIAENIRygKPDATDEEVEEAAKKANIHDFIMSLPDgydtLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 179 FSMLDVSMRSQVVNLLLKLqeRLGLSYVVVANDLGLVRHiSDKVLIMHQGEIVESGLTSEvfsnpqhdvtkrLIQNHGHE 258
Cdd:cd03249 167 TSALDAESEKLVQEALDRA--MKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDE------------LMAQKGVY 231
|
.
gi 502191832 259 Y 259
Cdd:cd03249 232 A 232
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
23-239 |
2.05e-35 |
|
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: 126.14 E-value: 2.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 23 FRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAG---VVP--PTSGEIEVNGEVIaFEDTQKRCKLIR---MI 94
Cdd:cd03260 8 VYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndLIPgaPDEGEVLLDGKDI-YDLDVDVLELRRrvgMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 95 FQDPNsslnP-QLRVGRILEAPLRLNTDLSEEERANTVIETLRMVGMLPE-----HALfypqMISLGQKQRVAFARALIL 168
Cdd:cd03260 87 FQKPN----PfPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEvkdrlHAL----GLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502191832 169 DPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLsyVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEV 239
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKEYTI--VIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-244 |
3.37e-35 |
|
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: 125.91 E-value: 3.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 7 LRVSGINKTFfnrvGLFRrkqvqVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQK 86
Cdd:cd03296 3 IEVRNVSKRF----GDFV-----ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 87 RCklIRMIFQdpNSSLNPQ----------LRVGRILEAPlrlntdlSEEERANTVIETLRMVGmLPEHALFYPQMISLGQ 156
Cdd:cd03296 74 RN--VGFVFQ--HYALFRHmtvfdnvafgLRVKPRSERP-------PEAEIRAKVHELLKLVQ-LDWLADRYPAQLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 157 KQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLT 236
Cdd:cd03296 142 RQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTP 221
|
....*...
gi 502191832 237 SEVFSNPQ 244
Cdd:cd03296 222 DEVYDHPA 229
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
28-254 |
3.90e-35 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 128.10 E-value: 3.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 28 VQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPP----TSGEIEVNG-EVIAFEDTQKR---CKLIRMIFQDPN 99
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGiDLLKLSPRERRkiiGREIAMIFQEPS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 100 SSLNPQLRVGRILEAPL-----------RLNTdlseeeRANTVIETLRMVGmLPEHALF---YPQMISLGQKQRVAFARA 165
Cdd:COG4170 100 SCLDPSAKIGDQLIEAIpswtfkgkwwqRFKW------RKKRAIELLHRVG-IKDHKDImnsYPHELTEGECQKVMIAMA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 166 LILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNPQH 245
Cdd:COG4170 173 IANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHH 252
|
....*....
gi 502191832 246 DVTKRLIQN 254
Cdd:COG4170 253 PYTKALLRS 261
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
23-241 |
8.33e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 126.00 E-value: 8.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 23 FRRKQVQ---VLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIRMIFQDPN 99
Cdd:PRK13650 12 FKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 100 SSLnpqlrVGRILEAPLRL---NTDLSEEERANTVIETLRMVGMLpEHALFYPQMISLGQKQRVAFARALILDPKIIVAD 176
Cdd:PRK13650 92 NQF-----VGATVEDDVAFgleNKGIPHEEMKERVNEALELVGMQ-DFKEREPARLSGGQKQRVAIAGAVAMRPKIIILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502191832 177 EAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRhISDKVLIMHQGEIVESGLTSEVFS 241
Cdd:PRK13650 166 EATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFS 229
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
27-243 |
2.00e-34 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 124.05 E-value: 2.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 27 QVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGevIAFEDTQKRCKLIR----MIFQDPNssL 102
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKVDERLIRqeagMVFQQFY--L 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 103 NPQLRVgriLE----APLRLNtDLSEEERANTVIETLRMVGmLPEHALFYPQMISLGQKQRVAFARALILDPKIIVADEA 178
Cdd:PRK09493 89 FPHLTA---LEnvmfGPLRVR-GASKEEAEKQARELLAKVG-LAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502191832 179 FSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNP 243
Cdd:PRK09493 164 TSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
12-243 |
3.90e-34 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 125.99 E-value: 3.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 12 INKTFFNRVglfrrkqvqVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCklI 91
Cdd:PRK11432 12 ITKRFGSNT---------VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRD--I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 92 RMIFQdpNSSLNPQLRVGRILEAPLRLnTDLSEEERANTVIETLRMVGMlpehALF---YPQMISLGQKQRVAFARALIL 168
Cdd:PRK11432 81 CMVFQ--SYALFPHMSLGENVGYGLKM-LGVPKEERKQRVKEALELVDL----AGFedrYVDQISGGQQQRVALARALIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502191832 169 DPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNP 243
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
31-244 |
4.72e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 123.71 E-value: 4.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 31 LKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIRMIFQDPNSSLnpqlrVGR 110
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPDNQF-----VGS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 111 ILEAPLRL---NTDLSEEERANTVIETLRMVGMLpEHALFYPQMISLGQKQRVAFARALILDPKIIVADEAFSMLDVSMR 187
Cdd:PRK13648 100 IVKYDVAFgleNHAVPYDEMHRRVSEALKQVDML-ERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDAR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502191832 188 SQVVNLLLKLQERLGLSYVVVANDLGLVRHiSDKVLIMHQGEIVESGLTSEVFSNPQ 244
Cdd:PRK13648 179 QNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
31-244 |
1.00e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 123.59 E-value: 1.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 31 LKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIR----MIFQDPNSSLNPQL 106
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLRkkvgIVFQFPEHQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 107 RVGRILEAPLrlNTDLSEEERANTVIETLRMVGmLPEHALFY-PQMISLGQKQRVAFARALILDPKIIVADEAFSMLDVS 185
Cdd:PRK13634 103 VEKDICFGPM--NFGVSEEDAKQKAREMIELVG-LPEELLARsPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502191832 186 MRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNPQ 244
Cdd:PRK13634 180 GRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
24-244 |
1.62e-33 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 122.00 E-value: 1.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 24 RRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAF---EDTQ------KRCKLIR-- 92
Cdd:PRK10619 14 RYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLvrdKDGQlkvadkNQLRLLRtr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 93 --MIFQDPNssLNPQLRV-GRILEAPLRLnTDLSEEERANTVIETLRMVGMLPEHALFYPQMISLGQKQRVAFARALILD 169
Cdd:PRK10619 94 ltMVFQHFN--LWSHMTVlENVMEAPIQV-LGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502191832 170 PKIIVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNPQ 244
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQ 244
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
29-234 |
1.66e-33 |
|
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: 121.57 E-value: 1.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 29 QVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIRMIFQDP---NSSLNPQ 105
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDTvlfNDTIGYN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 106 LRVGRIleaplrlntDLSEEE--------RANTVIETLR-----MVGmlpEHALfypqMISLGQKQRVAFARALILDPKI 172
Cdd:cd03253 95 IRYGRP---------DATDEEvieaakaaQIHDKIMRFPdgydtIVG---ERGL----KLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502191832 173 IVADEAFSMLDVSMRSQVVNLLLKLQErlGLSYVVVANDLGLVRHiSDKVLIMHQGEIVESG 234
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERG 217
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
5-241 |
1.94e-33 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 121.80 E-value: 1.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 5 PLLRVSGINktffnrvglFRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDT 84
Cdd:PRK13548 1 AMLEARNLS---------VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 85 QKRCKLIRMIFQdpNSSLNPQLRV------GRileAPLRlntdLSEEERANTVIETLRMVGMLPEHALFYPQMiSLGQKQ 158
Cdd:PRK13548 72 AELARRRAVLPQ--HSSLSFPFTVeevvamGR---APHG----LSRAEDDALVAAALAQVDLAHLAGRDYPQL-SGGEQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 159 RVAFARALI------LDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVE 232
Cdd:PRK13548 142 RVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVA 221
|
....*....
gi 502191832 233 SGLTSEVFS 241
Cdd:PRK13548 222 DGTPAEVLT 230
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
5-243 |
1.95e-33 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 124.67 E-value: 1.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 5 PLLRVSGINKTFFNRvglfrrkqvQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDT 84
Cdd:PRK09452 13 PLVELRGISKSFDGK---------EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 85 QKRckLIRMIFQdpNSSLNPQLRVGRILEAPLRLNTdLSEEERANTVIETLRMVgMLPEHALFYPQMISLGQKQRVAFAR 164
Cdd:PRK09452 84 ENR--HVNTVFQ--SYALFPHMTVFENVAFGLRMQK-TPAAEITPRVMEALRMV-QLEEFAQRKPHQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502191832 165 ALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNP 243
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 236
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
25-231 |
2.00e-33 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 120.44 E-value: 2.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 25 RKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKlirMIFQDPNSSLnp 104
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIG---YVMQDVDYQL-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 105 qlrVGRILEAPLRLNTDLSEE--ERANTVIETLRMVGMLPEHalfyPQMISLGQKQRVAFARALILDPKIIVADEAFSML 182
Cdd:cd03226 85 ---FTDSVREELLLGLKELDAgnEQAETVLKDLDLYALKERH----PLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502191832 183 DV-SMRSqVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEIV 231
Cdd:cd03226 158 DYkNMER-VGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
33-234 |
2.36e-33 |
|
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: 120.48 E-value: 2.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 33 DISFTLePGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEViaFEDTQKRCKL------IRMIFQdpNSSLNPQL 106
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTV--LFDSRKKINLppqqrkIGLVFQ--QYALFPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 107 RVGRILEAPLRLNTDLSEEERANTVIETLRMvgmlpEHALF-YPQMISLGQKQRVAFARALILDPKIIVADEAFSMLDVS 185
Cdd:cd03297 91 NVRENLAFGLKRKRNREDRISVDELLDLLGL-----DHLLNrYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502191832 186 MRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESG 234
Cdd:cd03297 166 LRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
31-249 |
2.43e-33 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 124.76 E-value: 2.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 31 LKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIA----FEDTQKRCKLIRMIFQdpNSSLNPQL 106
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisdAELREVRRKKIAMVFQ--SFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 107 RVGRILEAPLRLnTDLSEEERANTVIETLRMVGmLPEHALFYPQMISLGQKQRVAFARALILDPKIIVADEAFSMLDVSM 186
Cdd:PRK10070 122 TVLDNTAFGMEL-AGINAEERREKALDALRQVG-LENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502191832 187 RSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNPQHDVTK 249
Cdd:PRK10070 200 RTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-239 |
8.27e-33 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 119.80 E-value: 8.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 1 MNSAplLRVSGINKTF-------------FNRVGLFRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPP 67
Cdd:COG1134 1 MSSM--IEVENVSKSYrlyhepsrslkelLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 68 TSGEIEVNGEVIAfedtqkrckLIrmifqDPNSSLNPQL--R-----VGRILeaplrlntDLSEEE---RANTVIE--TL 135
Cdd:COG1134 79 TSGRVEVNGRVSA---------LL-----ELGAGFHPELtgReniylNGRLL--------GLSRKEideKFDEIVEfaEL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 136 rmvgmlpEHALFYP-QMISLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGL 214
Cdd:COG1134 137 -------GDFIDQPvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGA 208
|
250 260
....*....|....*....|....*
gi 502191832 215 VRHISDKVLIMHQGEIVESGLTSEV 239
Cdd:COG1134 209 VRRLCDRAIWLEKGRLVMDGDPEEV 233
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
23-209 |
9.28e-33 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 118.74 E-value: 9.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 23 FRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRcklIRMIFQDPNSSL 102
Cdd:COG4133 10 CRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYR---RRLAYLGHADGL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 103 NPQLRVGRILEAPLRLNTDLSEEERANTVIETLRmvgmLPEHALFYPQMISLGQKQRVAFARALILDPKIIVADEAFSML 182
Cdd:COG4133 87 KPELTVRENLRFWAALYGLRADREAIDEALEAVG----LAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTAL 162
|
170 180
....*....|....*....|....*..
gi 502191832 183 DVSMRSQVVNLLLKLQERLGLsyVVVA 209
Cdd:COG4133 163 DAAGVALLAELIAAHLARGGA--VLLT 187
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
30-242 |
9.48e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 120.58 E-value: 9.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 30 VLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEviafeDTQKRCKL--IR----MIFQDPNSSLn 103
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGL-----DTSDEENLwdIRnkagMVFQNPDNQI- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 104 pqlrVGRILEAPLRL---NTDLSEEERANTVIETLRMVGMLpEHALFYPQMISLGQKQRVAFARALILDPKIIVADEAFS 180
Cdd:PRK13633 99 ----VATIVEEDVAFgpeNLGIPPEEIRERVDESLKKVGMY-EYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502191832 181 MLDVSMRSQVVNLLLKLQERLGLSYVvvandlgLVRHI------SDKVLIMHQGEIVESGLTSEVFSN 242
Cdd:PRK13633 174 MLDPSGRREVVNTIKELNKKYGITII-------LITHYmeeaveADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
9-243 |
2.60e-32 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 121.34 E-value: 2.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 9 VSGINKtFFNRVglfrrkqvQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAfeDTQKRC 88
Cdd:PRK10851 5 IANIKK-SFGRT--------QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS--RLHARD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 89 KLIRMIFQdpNSSLNPQLRVGRILEAPLRLntdLSEEERANT------VIETLRMVgMLPEHALFYPQMISLGQKQRVAF 162
Cdd:PRK10851 74 RKVGFVFQ--HYALFRHMTVFDNIAFGLTV---LPRRERPNAaaikakVTQLLEMV-QLAHLADRYPAQLSGGQKQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 163 ARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSN 242
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWRE 227
|
.
gi 502191832 243 P 243
Cdd:PRK10851 228 P 228
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
27-239 |
4.65e-32 |
|
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: 117.15 E-value: 4.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 27 QVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKL-------IRMIFqdpn 99
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgigyvpeGRRIF---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 100 sslnPQLRVgrilEAPLRLNTDLSEEERANTVIEtlRMVGMLPEHALFYPQM---ISLGQKQRVAFARALILDPKIIVAD 176
Cdd:cd03224 88 ----PELTV----EENLLLGAYARRRAKRKARLE--RVYELFPRLKERRKQLagtLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502191832 177 EAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEV 239
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-241 |
2.56e-31 |
|
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: 121.06 E-value: 2.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 5 PLLRVSGINKTFFNrvglFRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVN-GEviAFED 83
Cdd:TIGR03269 278 PIIKVRNVSKRYIS----VDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGD--EWVD 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 84 TQKRCKLIR--------MIFQDpnSSLNPQLRV-GRILEAplrLNTDLSEEERANTVIETLRMVGMLPEHALF----YPQ 150
Cdd:TIGR03269 352 MTKPGPDGRgrakryigILHQE--YDLYPHRTVlDNLTEA---IGLELPDELARMKAVITLKMVGFDEEKAEEildkYPD 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 151 MISLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEI 230
Cdd:TIGR03269 427 ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
250
....*....|.
gi 502191832 231 VESGLTSEVFS 241
Cdd:TIGR03269 507 VKIGDPEEIVE 517
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
30-256 |
2.80e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 116.82 E-value: 2.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 30 VLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGE---IEVNGeviaFEDTQKRCKLIR----MIFQDPNSSL 102
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDG----ITLTAKTVWDIRekvgIVFQNPDNQF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 103 npqlrVGRILEAPLRL---NTDLSEEERANTVIETLRMVGMLpEHALFYPQMISLGQKQRVAFARALILDPKIIVADEAF 179
Cdd:PRK13640 98 -----VGATVGDDVAFgleNRAVPRPEMIKIVRDVLADVGML-DYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDEST 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502191832 180 SMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHiSDKVLIMHQGEIVESGLTSEVFSNPQhdvtkrLIQNHG 256
Cdd:PRK13640 172 SMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKVE------MLKEIG 241
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-243 |
1.35e-30 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 117.24 E-value: 1.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 5 PLLRVSGINKTFFNRvglfrrkqvQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDT 84
Cdd:PRK11607 18 PLLEIRNLTKSFDGQ---------HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 85 QKRCklIRMIFQdpNSSLNPQLRVGRILEAPLRLNTdLSEEERANTVIETLRMVGMLpEHALFYPQMISLGQKQRVAFAR 164
Cdd:PRK11607 89 YQRP--INMMFQ--SYALFPHMTVEQNIAFGLKQDK-LPKAEIASRVNEMLGLVHMQ-EFAKRKPHQLSGGQRQRVALAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502191832 165 ALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNP 243
Cdd:PRK11607 163 SLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
27-244 |
1.51e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 114.93 E-value: 1.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 27 QVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIR----MIFQDPNSSL 102
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLRkkvsLVFQFPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 103 NPQLRVGRILEAPlrLNTDLSEEERANTVIETLRMVGMLPEHALFYPQMISLGQKQRVAFARALILDPKIIVADEAFSML 182
Cdd:PRK13641 99 FENTVLKDVEFGP--KNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502191832 183 DVSMRSQVVNLLLKLQeRLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNPQ 244
Cdd:PRK13641 177 DPEGRKEMMQLFKDYQ-KAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
10-234 |
1.60e-30 |
|
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: 113.40 E-value: 1.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 10 SGINKTFFNRVGLFRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAfedtqkrck 89
Cdd:cd03220 17 SSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSS--------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 90 LIrmifqDPNSSLNPQL-------RVGRIL-----EAPLRLN--TDLSE-EERANTVIETLrmvgmlpehalfypqmiSL 154
Cdd:cd03220 88 LL-----GLGGGFNPELtgreniyLNGRLLglsrkEIDEKIDeiIEFSElGDFIDLPVKTY-----------------SS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 155 GQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEIVESG 234
Cdd:cd03220 146 GMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
30-261 |
2.11e-30 |
|
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: 118.72 E-value: 2.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 30 VLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIRMIFQDP---NSSLNPQL 106
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPhlfDTTLRENL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 107 RVGRileaPlrlntDLSEEErantVIETLRMVG--------------MLPEHAlfypQMISLGQKQRVAFARALILDPKI 172
Cdd:COG4987 430 RLAR----P-----DATDEE----LWAALERVGlgdwlaalpdgldtWLGEGG----RRLSGGERRRLALARALLRDAPI 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 173 IVADEAFSMLDVSMRSQVVNLLLK-LQERlglSYVVVANDLGLVRHIsDKVLIMHQGEIVESGLTSEvfsnpqhdvtkrL 251
Cdd:COG4987 493 LLLDEPTEGLDAATEQALLADLLEaLAGR---TVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEE------------L 556
|
250
....*....|
gi 502191832 252 IQNHGHeYRR 261
Cdd:COG4987 557 LAQNGR-YRQ 565
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
30-234 |
2.90e-30 |
|
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: 113.09 E-value: 2.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 30 VLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIRMIFQDP---NSSLNPQL 106
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQDVflfNDTVAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 107 RVGRileaplrlnTDLSEEErantVIETLRMVGM------LPEHalfYPQMI-------SLGQKQRVAFARALILDPKII 173
Cdd:cd03251 97 AYGR---------PGATREE----VEEAARAANAhefimeLPEG---YDTVIgergvklSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502191832 174 VADEAFSMLDVSMRSQVVNLLLKLQErlGLSYVVVANDLGLVRHiSDKVLIMHQGEIVESG 234
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERG 218
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
24-244 |
3.78e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 113.65 E-value: 3.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 24 RRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIRMIFQDPNSSLn 103
Cdd:PRK13642 16 KESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPDNQF- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 104 pqlrVGRILEAPLRL---NTDLSEEERANTVIETLRMVGMLpEHALFYPQMISLGQKQRVAFARALILDPKIIVADEAFS 180
Cdd:PRK13642 95 ----VGATVEDDVAFgmeNQGIPREEMIKRVDEALLAVNML-DFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502191832 181 MLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHiSDKVLIMHQGEIVESGLTSEVFSNPQ 244
Cdd:PRK13642 170 MLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
29-253 |
3.91e-30 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 112.92 E-value: 3.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 29 QVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEV-NGEVIAFEDTQKRCKLIR-------MIFQDPNs 100
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgDITIDTARSLSQQKGLIRqlrqhvgFVFQNFN- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 101 sLNPQLRV-GRILEAPLRLNTDLSEE--ERANtviETLRMVGML-PEHAlfYPQMISLGQKQRVAFARALILDPKIIVAD 176
Cdd:PRK11264 96 -LFPHRTVlENIIEGPVIVKGEPKEEatARAR---ELLAKVGLAgKETS--YPRRLSGGQQQRVAIARALAMRPEVILFD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502191832 177 EAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNPQHDVTKRLIQ 253
Cdd:PRK11264 170 EPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFLE 245
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
25-243 |
5.64e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 113.36 E-value: 5.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 25 RKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIRMIFQDPNSSLNP 104
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPDDQIFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 105 QLRVGRILEAPLRLNTDlsEEERANTVIETLRMVGmLPEHALFYPQMISLGQKQRVAFARALILDPKIIVADEAFSMLDV 184
Cdd:PRK13652 94 PTVEQDIAFGPINLGLD--EETVAHRVSSALHMLG-LEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502191832 185 SMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNP 243
Cdd:PRK13652 171 QGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
7-234 |
8.39e-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: 111.44 E-value: 8.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 7 LRVSGINKTFfnrvglfRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQK 86
Cdd:cd03263 1 LQIRNLTKTY-------KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 87 RcKLIRMIFQDpnSSLNPQLRVGRILE--APLRlntDLSEEERANTVIETLRMVGmLPEHALFYPQMISLGQKQRVAFAR 164
Cdd:cd03263 74 R-QSLGYCPQF--DALFDELTVREHLRfyARLK---GLPKSEIKEEVELLLRVLG-LTDKANKRARTLSGGMKRKLSLAI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 165 ALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQErlGLSYVVVANDLGLVRHISDKVLIMHQGEIVESG 234
Cdd:cd03263 147 ALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-234 |
8.58e-30 |
|
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: 111.22 E-value: 8.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 7 LRVSGINKTFfnrvglfrrKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQk 86
Cdd:cd03269 1 LEVENVTKRF---------GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARN- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 87 rckliRMIFQDPNSSLNPQLRVGRILE--APLRlntDLSEEERANTVIETLRMVGmLPEHALFYPQMISLGQKQRVAFAR 164
Cdd:cd03269 71 -----RIGYLPEERGLYPKMKVIDQLVylAQLK---GLKKEEARRRIDEWLERLE-LSEYANKRVEELSKGNQQKVQFIA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 165 ALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEIVESG 234
Cdd:cd03269 142 AVIHDPELLILDEPFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-255 |
9.16e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 112.95 E-value: 9.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 17 FNRVGLFRRK----QVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIR 92
Cdd:PRK13646 5 FDNVSYTYQKgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 93 ----MIFQDPNSSLNPQLRVGRILEAPLRLNTDLSE-EERANTVIETLRMVGMLPEHALFypQMiSLGQKQRVAFARALI 167
Cdd:PRK13646 85 krigMVFQFPESQLFEDTVEREIIFGPKNFKMNLDEvKNYAHRLLMDLGFSRDVMSQSPF--QM-SGGQMRKIAIVSILA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 168 LDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNpqhdv 247
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD----- 236
|
....*...
gi 502191832 248 TKRLIQNH 255
Cdd:PRK13646 237 KKKLADWH 244
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
24-190 |
1.16e-29 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 110.65 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 24 RRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPP---TSGEIEVNGEVIAFEDTQKRckLIRMIFQDPns 100
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQR--RIGILFQDD-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 101 SLNPQLRVGRILeaPLRLNTDLSEEERANTVIETLRMVGmLPEHALFYPQMISLGQKQRVAFARALILDPKIIVADEAFS 180
Cdd:COG4136 86 LLFPHLSVGENL--AFALPPTIGRAQRRARVEQALEEAG-LAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFS 162
|
170
....*....|
gi 502191832 181 MLDVSMRSQV 190
Cdd:COG4136 163 KLDAALRAQF 172
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
30-241 |
1.47e-29 |
|
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: 111.04 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 30 VLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIRMIFQDpNSSLNpqlrvG 109
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQE-NVLFN-----R 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 110 RILEAPLRLNTDLSEEErantVIETLRMVGM------LPEHalfYPQMI-------SLGQKQRVAFARALILDPKIIVAD 176
Cdd:cd03252 91 SIRDNIALADPGMSMER----VIEAAKLAGAhdfiseLPEG---YDTIVgeqgaglSGGQRQRIAIARALIHNPRILIFD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502191832 177 EAFSMLDVSMRSQVVNLLLKLQErlGLSYVVVANDLGLVRHiSDKVLIMHQGEIVESGLTSEVFS 241
Cdd:cd03252 164 EATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLA 225
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-234 |
1.68e-29 |
|
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: 110.38 E-value: 1.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 7 LRVSGINKTFfnrvglfrrKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEviafedtqk 86
Cdd:cd03268 1 LKTNDLTKTY---------GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK--------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 87 rcklirmIFQDPNSSLNpqlRVGRILEAPLrLNTDLSEEE-----------RANTVIETLRMVGmLPEHALFYPQMISLG 155
Cdd:cd03268 63 -------SYQKNIEALR---RIGALIEAPG-FYPNLTAREnlrllarllgiRKKRIDEVLDVVG-LKDSAKKKVKGFSLG 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502191832 156 QKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEIVESG 234
Cdd:cd03268 131 MKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
29-252 |
1.80e-29 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 111.28 E-value: 1.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 29 QVLKDISFTLEPGETLALVGETGSGKSTLAKIL-------AGVVppTSGEIEVNGEVIAFED---TQKRCKlIRMIFQDP 98
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndliPGAR--VEGEILLDGEDIYDPDvdvVELRRR-VGMVFQKP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 99 N---SSlnpqlrvgrILE---APLRLNTDLSEEERANTVIETLRMVGM-------LPEHALFypqmISLGQKQRVAFARA 165
Cdd:COG1117 102 NpfpKS---------IYDnvaYGLRLHGIKSKSELDEIVEESLRKAALwdevkdrLKKSALG----LSGGQQQRLCIARA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 166 LILDPKIIVADEAFSMLD-VSmRSQVVNLLLKLQERlglsYVVVandlgLVRH-------ISDKVLIMHQGEIVESGLTS 237
Cdd:COG1117 169 LAVEPEVLLMDEPTSALDpIS-TAKIEELILELKKD----YTIV-----IVTHnmqqaarVSDYTAFFYLGELVEFGPTE 238
|
250
....*....|....*
gi 502191832 238 EVFSNPQHDVTKRLI 252
Cdd:COG1117 239 QIFTNPKDKRTEDYI 253
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-239 |
1.95e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 115.51 E-value: 1.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 2 NSAPLLRVSGINKTFFNrvglfrrkqVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAF 81
Cdd:COG3845 1 MMPPALELRGITKRFGG---------VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 82 EDTQKRCKL-IRMIFQDPnsSLNPQLRV------GriLEAPLRLNTDLSEEERAntVIETLRMVGM-LPEHAlfYPQMIS 153
Cdd:COG3845 72 RSPRDAIALgIGMVHQHF--MLVPNLTVaenivlG--LEPTKGGRLDRKAARAR--IRELSERYGLdVDPDA--KVEDLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 154 LGQKQRVAFARALILDPKIIVADEAFSMLDvsmrSQVVNLLLKLQERL---GLSYVVVANDLGLVRHISDKVLIMHQGEI 230
Cdd:COG3845 144 VGEQQRVEILKALYRGARILILDEPTAVLT----PQEADELFEILRRLaaeGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
....*....
gi 502191832 231 VESGLTSEV 239
Cdd:COG3845 220 VGTVDTAET 228
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
33-234 |
2.46e-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: 2.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 33 DISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCklIRMIFQDPN--SSLNPQLRVGR 110
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP--VSMLFQENNlfAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 111 ILEAPLRLNtdlseEERANTVIETLRMVGmLPEHALFYPQMISLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQV 190
Cdd:cd03298 94 GLSPGLKLT-----AEDRQAIEVALARVG-LAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502191832 191 VNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESG 234
Cdd:cd03298 168 LDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
29-234 |
2.46e-29 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 115.83 E-value: 2.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 29 QVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIRMIFQDP---NSSLNPQ 105
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAglfNRSIEDN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 106 LRVGR--------------------ILEAPLRLNTDLSEEERantvietlrmvgmlpehalfypqMISLGQKQRVAFARA 165
Cdd:PRK13657 429 IRVGRpdatdeemraaaeraqahdfIERKPDGYDTVVGERGR-----------------------QLSGGERQRLAIARA 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502191832 166 LILDPKIIVADEAFSMLDVSMRSQVVNLLLKLqeRLGLSYVVVANDLGLVRHiSDKVLIMHQGEIVESG 234
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVKAALDEL--MKGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESG 551
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-252 |
4.02e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 110.52 E-value: 4.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 30 VLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFE------DTQKRCKLIRMIFQDPNSSln 103
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGkdifqiDAIKLRKEVGMVFQQPNPF-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 104 PQLRVGRILEAPLRLNTDLSEEERANTVIETLRMVGMLPE--HALFYP-QMISLGQKQRVAFARALILDPKIIVADEAFS 180
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEvyDRLNSPaSQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502191832 181 MLDVSMRSQVVNLLLKLQERLGLsyVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNPQHDVTKRLI 252
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNEIAI--VIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
29-241 |
1.27e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 109.94 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 29 QVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAF--EDTQKRCKLIRMIFQDPNSSLNPQL 106
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYsrKGLMKLRESVGMVFQDPDNQLFSAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 107 RVGRILEAPLrlNTDLSEEERANTVIETLRMVGML-----PEHALfypqmiSLGQKQRVAFARALILDPKIIVADEAFSM 181
Cdd:PRK13636 100 VYQDVSFGAV--NLKLPEDEVRKRVDNALKRTGIEhlkdkPTHCL------SFGQKKRVAIAGVLVMEPKVLVLDEPTAG 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 182 LDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFS 241
Cdd:PRK13636 172 LDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-253 |
1.51e-28 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 110.66 E-value: 1.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 5 PLLRVSGINKTFFNRVGlfrrkQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVvppTSGEIEVNGEVIAFEDT 84
Cdd:PRK15093 2 PLLDIRNLTIEFKTSDG-----WVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV---TKDNWRVTADRMRFDDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 85 -------QKRCKLIR----MIFQDPNSSLNPQLRVGRILEAPL-----------RLNTdlseeeRANTVIETLRMVGMLP 142
Cdd:PRK15093 74 dllrlspRERRKLVGhnvsMIFQEPQSCLDPSERVGRQLMQNIpgwtykgrwwqRFGW------RKRRAIELLHRVGIKD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 143 EHALF--YPQMISLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISD 220
Cdd:PRK15093 148 HKDAMrsFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWAD 227
|
250 260 270
....*....|....*....|....*....|...
gi 502191832 221 KVLIMHQGEIVESGLTSEVFSNPQHDVTKRLIQ 253
Cdd:PRK15093 228 KINVLYCGQTVETAPSKELVTTPHHPYTQALIR 260
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
30-230 |
2.52e-28 |
|
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: 106.15 E-value: 2.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 30 VLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIafedtqkrcklirmifqdpnSSLNP-QLRv 108
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADI--------------------SQWDPnELG- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 109 grileaplrlntdlseeerantvietlRMVGMLPEHALFYPQMI-----SLGQKQRVAFARALILDPKIIVADEAFSMLD 183
Cdd:cd03246 76 ---------------------------DHVGYLPQDDELFSGSIaenilSGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502191832 184 VSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRhISDKVLIMHQGEI 230
Cdd:cd03246 129 VEGERALNQAIAALKAA-GATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
27-241 |
2.66e-28 |
|
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: 112.92 E-value: 2.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 27 QVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIRMIFQDPnsslnpQL 106
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDV------EL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 107 RVGRILEAPLRLNTDLSEEerantVIETLRMVGM------LPE----------HALfypqmiSLGQKQRVAFARALILDP 170
Cdd:COG4618 418 FDGTIAENIARFGDADPEK-----VVAAAKLAGVhemilrLPDgydtrigeggARL------SGGQRQRIGLARALYGDP 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502191832 171 KIIVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHiSDKVLIMHQGEIVESGLTSEVFS 241
Cdd:COG4618 487 RLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLAA-VDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-247 |
3.45e-28 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 108.31 E-value: 3.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 1 MNSAPLLRVSGINktffnrvglFRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIA 80
Cdd:PRK11831 2 QSVANLVDMRGVS---------FTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 81 fedTQKRCKL------IRMIFQdpNSSLNPQLRVGRILEAPLRLNTDLSEEERANTVIETLRMVGmLPEHALFYPQMISL 154
Cdd:PRK11831 73 ---AMSRSRLytvrkrMSMLFQ--SGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVG-LRGAAKLMPSELSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 155 GQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESG 234
Cdd:PRK11831 147 GMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHG 226
|
250
....*....|...
gi 502191832 235 LTSEVFSNPQHDV 247
Cdd:PRK11831 227 SAQALQANPDPRV 239
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
24-197 |
5.25e-28 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 107.64 E-value: 5.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 24 RRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRcklirMIFQDpnSSLN 103
Cdd:COG4525 16 GGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRG-----VVFQK--DALL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 104 PQLRVGRILEAPLRLNtDLSEEERANTVIETLRMVGmLPEHALFYPQMISLGQKQRVAFARALILDPKIIVADEAFSMLD 183
Cdd:COG4525 89 PWLNVLDNVAFGLRLR-GVPKAERRARAEELLALVG-LADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
170
....*....|....
gi 502191832 184 VSMRSQVVNLLLKL 197
Cdd:COG4525 167 ALTREQMQELLLDV 180
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
24-230 |
7.76e-28 |
|
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: 106.40 E-value: 7.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 24 RRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIRMIFQDP---NS 100
Cdd:cd03248 23 TRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPvlfAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 101 SLNPQLRVGrILEAPLRLNTDLSEEERANTVIetlrmvgmlPEHALFYPQ-------MISLGQKQRVAFARALILDPKII 173
Cdd:cd03248 103 SLQDNIAYG-LQSCSFECVKEAAQKAHAHSFI---------SELASGYDTevgekgsQLSGGQKQRVAIARALIRNPQVL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502191832 174 VADEAFSMLDVSMRSQVVNLLLKLQERlgLSYVVVANDLGLVRHiSDKVLIMHQGEI 230
Cdd:cd03248 173 ILDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
24-243 |
7.91e-28 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 111.74 E-value: 7.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 24 RRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIRMIFQDpnssln 103
Cdd:TIGR00958 490 NRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQE------ 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 104 PQLRVGRILEAPLRLNTDLSEEERANTVIETL--RMVGMLP--------EHAlfypQMISLGQKQRVAFARALILDPKII 173
Cdd:TIGR00958 564 PVLFSGSVRENIAYGLTDTPDEEIMAAAKAANahDFIMEFPngydtevgEKG----SQLSGGQKQRIAIARALVRKPRVL 639
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 174 VADEAFSMLDVsmrsQVVNLLLKLQERLGLSYVVVANDLGLVRHiSDKVLIMHQGEIVESGLTSEVFSNP 243
Cdd:TIGR00958 640 ILDEATSALDA----ECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
27-252 |
1.06e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 106.54 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 27 QVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVV-----PPTSGEIEVNGEVIAFEDTQKRCKLIRMIFQDPNSS 101
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 102 lnPQLRVGRILEAPLRLNTDL-SEEERANTVIETLRMVGMLPE--HALFYPQ-MISLGQKQRVAFARALILDPKIIVADE 177
Cdd:PRK14247 95 --PNLSIFENVALGLKLNRLVkSKKELQERVRWALEKAQLWDEvkDRLDAPAgKLSGGQQQRLCIARALAFQPEVLLADE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502191832 178 AFSMLDVSMRSQVVNLLLKLQERLGLsyVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNPQHDVTKRLI 252
Cdd:PRK14247 173 PTANLDPENTAKIESLFLELKKDMTI--VLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEKYV 245
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
28-230 |
1.16e-27 |
|
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: 105.57 E-value: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 28 VQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIR---MIFQDpnSSLNP 104
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRkigVVFQD--FRLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 105 QLRVGRILEAPLRLnTDLSEEERANTVIETLRMVGmLPEHALFYPQMISLGQKQRVAFARALILDPKIIVADEAFSMLDV 184
Cdd:cd03292 92 DRNVYENVAFALEV-TGVPPREIRKRVPAALELVG-LSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502191832 185 SMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEI 230
Cdd:cd03292 170 DTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
31-240 |
1.18e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 107.14 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 31 LKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIR----MIFQDPNSSLNPQL 106
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRkkvgLVFQFPESQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 107 RVGRILEAPlrLNTDLSEEERANTVIETLRMVGMLPEhaLF--YPQMISLGQKQRVAFARALILDPKIIVADEAFSMLDV 184
Cdd:PRK13649 103 VLKDVAFGP--QNFGVSQEEAEALAREKLALVGISES--LFekNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502191832 185 SMRSQVVNLLLKLQErLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVF 240
Cdd:PRK13649 179 KGRKELMTLFKKLHQ-SGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
17-234 |
1.31e-27 |
|
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: 105.65 E-value: 1.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 17 FNRVGLFRRKQVQ-VLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIRMIF 95
Cdd:cd03244 5 FKNVSLRYRPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 96 QDPNsslnpqlrvgrILEAPLRLNTD----LSEEErantVIETLRMVGMLPEHALFYPQM----------ISLGQKQRVA 161
Cdd:cd03244 85 QDPV-----------LFSGTIRSNLDpfgeYSDEE----LWQALERVGLKEFVESLPGGLdtvveeggenLSVGQRQLLC 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502191832 162 FARALILDPKIIVADEAFSMLDVSMRSQVVNLllkLQERL-GLSYVVVANDLGLVRHiSDKVLIMHQGEIVESG 234
Cdd:cd03244 150 LARALLRKSKILVLDEATASVDPETDALIQKT---IREAFkDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFD 219
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
9-223 |
1.55e-27 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 105.00 E-value: 1.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 9 VSGINKTFFNRVglfrrkqvqVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRC 88
Cdd:TIGR03608 1 LKNISKKFGDKV---------ILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKAS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 89 KLIR----MIFQdpNSSLNPQLRVGRILEAPLrLNTDLSEEERANTVIETLRMVGMlpEHALF-YPQMISLGQKQRVAFA 163
Cdd:TIGR03608 72 KFRReklgYLFQ--NFALIENETVEENLDLGL-KYKKLSKKEKREKKKEALEKVGL--NLKLKqKIYELSGGEQQRVALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 164 RALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLgLVRHISDKVL 223
Cdd:TIGR03608 147 RAILKPPPLILADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDP-EVAKQADRVI 204
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-239 |
2.23e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 106.73 E-value: 2.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 7 LRVSGINKTFfnrvglfrrKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQK 86
Cdd:COG4152 2 LELKGLTKRF---------GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 87 -------RcklirmifqdpnsSLNPQLRVGRIL------------EAPLRLNTDLSE---EERANTVIETLrmvgmlpeh 144
Cdd:COG4152 73 igylpeeR-------------GLYPKMKVGEQLvylarlkglskaEAKRRADEWLERlglGDRANKKVEEL--------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 145 alfypqmiSLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLI 224
Cdd:COG4152 131 --------SKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVI 201
|
250
....*....|....*
gi 502191832 225 MHQGEIVESGLTSEV 239
Cdd:COG4152 202 INKGRKVLSGSVDEI 216
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
23-241 |
1.03e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 104.70 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 23 FRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIafeDTQKRCKL-----IRMIFQD 97
Cdd:PRK13638 9 FRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL---DYSKRGLLalrqqVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 98 PNSSLNpQLRVGRILEAPLRlNTDLSEEERANTVIETLRMVGmlPEHALFYP-QMISLGQKQRVAFARALILDPKIIVAD 176
Cdd:PRK13638 86 PEQQIF-YTDIDSDIAFSLR-NLGVPEAEITRRVDEALTLVD--AQHFRHQPiQCLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502191832 177 EAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFS 241
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
27-238 |
1.22e-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: 103.22 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 27 QVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRcKLIRMIFQDPnsSLNPQL 106
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVR-RRIGIVFQDL--SVDDEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 107 RVGRILEAPLRLnTDLSEEERANTVIETLRMVGMLpEHALFYPQMISLGQKQRVAFARALILDPKIIVADEAFSMLDVSM 186
Cdd:cd03265 89 TGWENLYIHARL-YGVPGAERRERIDELLDFVGLL-EAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502191832 187 RSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSE 238
Cdd:cd03265 167 RAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-234 |
2.23e-26 |
|
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: 102.45 E-value: 2.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 6 LLRVSGINKTFFNRvglfrRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAfedTQ 85
Cdd:cd03266 1 MITADALTKRFRDV-----KKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV---KE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 86 KRCKLIRMIFQDPNSSLNPQLRVGRILEAPLRLNtDLSEEE---RANTVIETLRMVGMLPEHAlfypQMISLGQKQRVAF 162
Cdd:cd03266 73 PAEARRRLGFVSDSTGLYDRLTARENLEYFAGLY-GLKGDEltaRLEELADRLGMEELLDRRV----GGFSTGMRQKVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502191832 163 ARALILDPKIIVADEAFSMLDVsMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESG 234
Cdd:cd03266 148 ARALVHDPPVLLLDEPTTGLDV-MATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
29-240 |
2.23e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 104.05 E-value: 2.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 29 QVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIR----MIFQDPNSSLNP 104
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRkkvgVVFQFPESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 105 QLRVGRILEAPlrLNTDLSEEERANTVIETLRMVGMLPEHALFYPQMISLGQKQRVAFARALILDPKIIVADEAFSMLDV 184
Cdd:PRK13643 100 ETVLKDVAFGP--QNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502191832 185 SMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVF 240
Cdd:PRK13643 178 KARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
21-234 |
2.75e-26 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 102.41 E-value: 2.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 21 GLFRRK--QVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEViAFEDTQKRCKLIRMIFQDp 98
Cdd:cd03267 25 SLFKRKyrEVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV-PWKRRKKFLRRIGVVFGQ- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 99 NSSLNPQLRVGRILEApLRLNTDLSEEERANTVIETLRMVGMlpEHALFYP-QMISLGQKQRVAFARALILDPKIIVADE 177
Cdd:cd03267 103 KTQLWWDLPVIDSFYL-LAAIYDLPPARFKKRLDELSELLDL--EELLDTPvRQLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502191832 178 AFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESG 234
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-230 |
3.36e-26 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 102.83 E-value: 3.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 5 PLLrVSGINKTFFNRvglfrrkqvQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVI--AFE 82
Cdd:PRK11247 12 PLL-LNAVSKRYGER---------TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLaeARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 83 DTqkrckliRMIFQDpnSSLNPQLRVgrILEAPLRLNTDLSEEERantviETLRMVGmLPEHALFYPQMISLGQKQRVAF 162
Cdd:PRK11247 82 DT-------RLMFQD--ARLLPWKKV--IDNVGLGLKGQWRDAAL-----QALAAVG-LADRANEWPAALSGGQKQRVAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502191832 163 ARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEI 230
Cdd:PRK11247 145 ARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
30-230 |
5.43e-26 |
|
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: 100.20 E-value: 5.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 30 VLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKL-IRMIFQDPnsslnpqLRV 108
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDR-------KRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 109 GRILEAPLRLNTDLseeerantvietlrmvgmlpehalfyPQMISLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRS 188
Cdd:cd03215 88 GLVLDLSVAENIAL--------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502191832 189 QVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEI 230
Cdd:cd03215 142 EIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-231 |
1.63e-25 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 105.19 E-value: 1.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 4 APLLRVSGINKTFFNRvglfrRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFED 83
Cdd:PRK10535 2 TALLELKDIRRSYPSG-----EEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 84 TQKRCKLIR----MIFQdpNSSLNPQLRVGRILEAPlRLNTDLSEEERANTVIETLRMVGmLPEHALFYPQMISLGQKQR 159
Cdd:PRK10535 77 ADALAQLRRehfgFIFQ--RYHLLSHLTAAQNVEVP-AVYAGLERKQRLLRAQELLQRLG-LEDRVEYQPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502191832 160 VAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDlGLVRHISDKVLIMHQGEIV 231
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHD-PQVAAQAERVIEIRDGEIV 222
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
30-212 |
1.68e-25 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 104.75 E-value: 1.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 30 VLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIRMIFQDPN---SSLNPQL 106
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHlfdTTVRENL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 107 RVGRileaplrlnTDLSEEErantVIETLRMVGM------LP--------EHAlfypQMISLGQKQRVAFARALILDPKI 172
Cdd:TIGR02868 430 RLAR---------PDATDEE----LWAALERVGLadwlraLPdgldtvlgEGG----ARLSGGERQRLALARALLADAPI 492
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502191832 173 IVADEAFSMLDVSMRSQVVNLLLKLQErlGLSYVVVANDL 212
Cdd:TIGR02868 493 LLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHHL 530
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
7-234 |
2.12e-25 |
|
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: 99.57 E-value: 2.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 7 LRVSGINKTFFNRVglfrrkqvqVLKDISFTLEPGeTLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEviafEDTQK 86
Cdd:cd03264 1 LQLENLTKRYGKKR---------ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQ----DVLKQ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 87 RCKLIRMIF---QDPNssLNPQLRVGRILEAPLRLNTDLSEEERAnTVIETLRMVGMLpEHALFYPQMISLGQKQRVAFA 163
Cdd:cd03264 67 PQKLRRRIGylpQEFG--VYPNFTVREFLDYIAWLKGIPSKEVKA-RVDEVLELVNLG-DRAKKKIGSLSGGMRRRVGIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502191832 164 RALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQErlGLSYVVVANDLGLVRHISDKVLIMHQGEIVESG 234
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
9-234 |
2.20e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 102.09 E-value: 2.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 9 VSGINKTFFNRV----------GLFRR--KQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNG 76
Cdd:COG4586 4 VENLSKTYRVYEkepglkgalkGLFRReyREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 77 EVIaFEDTQKRCKLIRMIF-QdpNSSLNPQLRVgriLEApLRLNT---DLSEEERANTVIEtlrMVGMLP-EHALFYP-- 149
Cdd:COG4586 84 YVP-FKRRKEFARRIGVVFgQ--RSQLWWDLPA---IDS-FRLLKaiyRIPDAEYKKRLDE---LVELLDlGELLDTPvr 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 150 QMiSLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGE 229
Cdd:COG4586 154 QL-SLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGR 232
|
....*
gi 502191832 230 IVESG 234
Cdd:COG4586 233 IIYDG 237
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
29-244 |
3.47e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 100.58 E-value: 3.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 29 QVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIafedTQKRCKLIR----MIFQDPNSslnp 104
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV----NAENEKWVRskvgLVFQDPDD---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 105 QLRVGRILE--APLRLNTDLSEEERANTVIETLRMVGM--LPEHAlfyPQMISLGQKQRVAFARALILDPKIIVADEAFS 180
Cdd:PRK13647 91 QVFSSTVWDdvAFGPVNMGLDKDEVERRVEEALKAVRMwdFRDKP---PYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502191832 181 MLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGlTSEVFSNPQ 244
Cdd:PRK13647 168 YLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG-DKSLLTDED 229
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
25-234 |
5.55e-25 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 103.26 E-value: 5.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 25 RKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIRMIFQDP---NSS 101
Cdd:PRK10790 351 RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPvvlADT 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 102 LNPQLRVGRileaplrlntDLSeEERANTVIETLRM---VGMLPE--HALFYPQ--MISLGQKQRVAFARALILDPKIIV 174
Cdd:PRK10790 431 FLANVTLGR----------DIS-EEQVWQALETVQLaelARSLPDglYTPLGEQgnNLSVGQKQLLALARVLVQTPQILI 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 175 ADEAFSMLDVSMRSQVVNLLLKLQERLGLsyVVVANDLGLVRHiSDKVLIMHQGEIVESG 234
Cdd:PRK10790 500 LDEATANIDSGTEQAIQQALAAVREHTTL--VVIAHRLSTIVE-ADTILVLHRGQAVEQG 556
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
27-222 |
8.90e-25 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 98.35 E-value: 8.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 27 QVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKL----IRMIFQdpNSSL 102
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqkLGFIYQ--FHHL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 103 NPQLRVGRILEAPLrLNTDLSEEERANTVIETLRMVGmLPEHALFYPQMISLGQKQRVAFARALILDPKIIVADEAFSML 182
Cdd:PRK11629 99 LPDFTALENVAMPL-LIGKKKPAEINSRALEMLAAVG-LEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502191832 183 DVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKV 222
Cdd:PRK11629 177 DARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
27-242 |
1.21e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 99.31 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 27 QVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVI-----AFEDTQKRCKLIRMIFQDPNSS 101
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkKIKEVKRLRKEIGLVFQFPEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 102 LNPQLRVGRILEAPLRLNTDlsEEERANTVIETLRMVGMLPEHALFYPQMISLGQKQRVAFARALILDPKIIVADEAFSM 181
Cdd:PRK13645 103 LFQETIEKDIAFGPVNLGEN--KQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502191832 182 LDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSN 242
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
31-243 |
1.27e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 98.91 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 31 LKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNG-EVIAFEDTQKRCKLIRMIFQDPNSSLnpqlrVG 109
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGiDTGDFSKLQGIRKLVGIVFQNPETQF-----VG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 110 RILEAPLRL---NTDLSEEERANTVIETLRMVGmLPEHALFYPQMISLGQKQRVAFARALILDPKIIVADEAFSMLDVSM 186
Cdd:PRK13644 93 RTVEEDLAFgpeNLCLPPIEIRKRVDRALAEIG-LEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502191832 187 RSQVVNLLLKLQERlGLSYVVVANDLGLVrHISDKVLIMHQGEIVESGLTSEVFSNP 243
Cdd:PRK13644 172 GIAVLERIKKLHEK-GKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
29-234 |
1.47e-24 |
|
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: 102.21 E-value: 1.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 29 QVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAfEDTQK--RcKLIRMIFQDP---NSSLN 103
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIR-DVTQAslR-AAIGIVPQDTvlfNDTIA 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 104 PQLRVGRIleaplrlntDLSEEErantVIETLRM------VGMLPEHalfYPQMI-------SLGQKQRVAFARALILDP 170
Cdd:COG5265 450 YNIAYGRP---------DASEEE----VEAAARAaqihdfIESLPDG---YDTRVgerglklSGGEKQRVAIARTLLKNP 513
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502191832 171 KIIVADEAFSMLDVSMRSQVVNLLLKL-QERLGLsyvVVANDLGLVRHiSDKVLIMHQGEIVESG 234
Cdd:COG5265 514 PILIFDEATSALDSRTERAIQAALREVaRGRTTL---VIAHRLSTIVD-ADEILVLEAGRIVERG 574
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
30-212 |
1.74e-24 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 98.23 E-value: 1.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 30 VLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRcklirMIFQdpNSSLNPQLRVG 109
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERG-----VVFQ--NEGLLPWRNVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 110 RILEAPLRLnTDLSEEERANTVIETLRMVGMLPEHALFYPQMiSLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQ 189
Cdd:PRK11248 89 DNVAFGLQL-AGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQL-SGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180
....*....|....*....|...
gi 502191832 190 VVNLLLKLQERLGLSYVVVANDL 212
Cdd:PRK11248 167 MQTLLLKLWQETGKQVLLITHDI 189
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-239 |
5.46e-24 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 100.24 E-value: 5.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 2 NSAPLLRVSGINKTFfnrvglfrrKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAF 81
Cdd:PRK09700 1 MATPYISMAGIGKSF---------GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 82 EDTQKRCKL-IRMIFQDPNS----SLNPQLRVGRIL-EAPLRLNTDLSEEERANTVIETLRmVGMLPEHALFYPQMiSLG 155
Cdd:PRK09700 72 LDHKLAAQLgIGIIYQELSVidelTVLENLYIGRHLtKKVCGVNIIDWREMRVRAAMMLLR-VGLKVDLDEKVANL-SIS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 156 QKQRVAFARALILDPKIIVADEAFSmldvSMRSQVVNLLLKLQERL---GLSYVVVANDLGLVRHISDKVLIMHQGEIVE 232
Cdd:PRK09700 150 HKQMLEIAKTLMLDAKVIIMDEPTS----SLTNKEVDYLFLIMNQLrkeGTAIVYISHKLAEIRRICDRYTVMKDGSSVC 225
|
....*..
gi 502191832 233 SGLTSEV 239
Cdd:PRK09700 226 SGMVSDV 232
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-252 |
1.18e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 96.00 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 3 SAPLLRVSGINkTFFNrvglfrrkQVQVLKDISFTLEPGETLALVGETGSGKSTLAKIL--AGVVPP---TSGEIEVNGE 77
Cdd:PRK14239 2 TEPILQVSDLS-VYYN--------KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 78 VI--AFEDTQKRCKLIRMIFQDPNS---SLNPQLRVGrileapLRLNtDLSEEERANTVIET-LRMVGM-------LPEH 144
Cdd:PRK14239 73 NIysPRTDTVDLRKEIGMVFQQPNPfpmSIYENVVYG------LRLK-GIKDKQVLDEAVEKsLKGASIwdevkdrLHDS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 145 ALfypqMISLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLsyVVVANDLGLVRHISDKVLI 224
Cdd:PRK14239 146 AL----GLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTM--LLVTRSMQQASRISDRTGF 219
|
250 260
....*....|....*....|....*...
gi 502191832 225 MHQGEIVESGLTSEVFSNPQHDVTKRLI 252
Cdd:PRK14239 220 FLDGDLIEYNDTKQMFMNPKHKETEDYI 247
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
35-241 |
1.73e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 95.03 E-value: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 35 SFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCklIRMIFQDPNssLNPQLRVGRILEA 114
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRP--VSMLFQENN--LFSHLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 115 PLRLNTDLSEEERAnTVIETLRMVGmLPEHALFYPQMISLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLL 194
Cdd:PRK10771 95 GLNPGLKLNAAQRE-KLHAIARQMG-IEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502191832 195 LKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFS 241
Cdd:PRK10771 173 SQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
5-240 |
6.92e-23 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 93.61 E-value: 6.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 5 PLLRVSGINktffnrvglFRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSG-EIEVNGEVIAFED 83
Cdd:COG1119 2 PLLELRNVT---------VRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 84 TQKRCKLIRMIfqdpNSSLNPQLRVG-RILE-------APLRLNTDLSEEERAnTVIETLRMVGMLP-EHALFypQMISL 154
Cdd:COG1119 73 VWELRKRIGLV----SPALQLRFPRDeTVLDvvlsgffDSIGLYREPTDEQRE-RARELLELLGLAHlADRPF--GTLSQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 155 GQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANdlglvrHISD------KVLIMHQG 228
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH------HVEEippgitHVLLLKDG 219
|
250
....*....|..
gi 502191832 229 EIVESGLTSEVF 240
Cdd:COG1119 220 RVVAAGPKEEVL 231
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-225 |
8.76e-23 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 96.97 E-value: 8.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 3 SAPLLRVSGINKTFFNRVglfrrkqvQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFE 82
Cdd:TIGR02857 318 PASSLEFSGVSVAYPGRR--------PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 83 DTQKRCKLIRMIFQdpnsslNPQLRVGRILEApLRLNT-DLSEEErantVIETLRMVGMLP-EHALfyPQMI-------- 152
Cdd:TIGR02857 390 DADSWRDQIAWVPQ------HPFLFAGTIAEN-IRLARpDASDAE----IREALERAGLDEfVAAL--PQGLdtpigegg 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502191832 153 ---SLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQErlGLSYVVVANDLGLVrHISDKVLIM 225
Cdd:TIGR02857 457 aglSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALA-ALADRIVVL 529
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
28-243 |
1.03e-22 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 95.30 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 28 VQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCklIRMIFQdpNSSLNPQLR 107
Cdd:PRK11650 17 TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRD--IAMVFQ--NYALYPHMS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 108 VGRILEAPLRlNTDLSEEERANTVIETLRMVGMLPehalfY----PQMISLGQKQRVAFARALILDPKIIVADEAFSMLD 183
Cdd:PRK11650 93 VRENMAYGLK-IRGMPKAEIEERVAEAARILELEP-----LldrkPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502191832 184 ----VSMRSQvvnlLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNP 243
Cdd:PRK11650 167 aklrVQMRLE----IQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKP 226
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
27-214 |
1.47e-22 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 92.53 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 27 QVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKL----IRMIFQdpNSSL 102
Cdd:PRK10584 22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLrakhVGFVFQ--SFML 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 103 NPQLRVGRILEAPLRLNTDlSEEERANTVIETLRMVGmLPEHALFYPQMISLGQKQRVAFARALILDPKIIVADEAFSML 182
Cdd:PRK10584 100 IPTLNALENVELPALLRGE-SSRQSRNGAKALLEQLG-LGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNL 177
|
170 180 190
....*....|....*....|....*....|..
gi 502191832 183 DVSMRSQVVNLLLKLQERLGLSYVVVANDLGL 214
Cdd:PRK10584 178 DRQTGDKIADLLFSLNREHGTTLILVTHDLQL 209
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
24-238 |
3.84e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 95.11 E-value: 3.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 24 RRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPP---TSGEIEVNGEVIAFEDTQKRCKLIRmifQDpnS 100
Cdd:TIGR00955 34 ERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAISAYVQ---QD--D 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 101 SLNPQLRVGRIL--EAPLRLNTDLSEEERANTVIETLRMVGMLP-EHALF----YPQMISLGQKQRVAFARALILDPKII 173
Cdd:TIGR00955 109 LFIPTLTVREHLmfQAHLRMPRRVTKKEKRERVDEVLQALGLRKcANTRIgvpgRVKGLSGGERKRLAFASELLTDPPLL 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 174 VADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVV-----ANDLGLVrhisDKVLIMHQGEIVESGLTSE 238
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTihqpsSELFELF----DKIILMAEGRVAYLGSPDQ 253
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
24-214 |
4.74e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 90.70 E-value: 4.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 24 RRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIrmifqDPNSSLN 103
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYL-----GHRNAMK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 104 PQLRVGRILE--APLRLNTDLSEEERANTVieTLRMVGMLPEHALfypqmiSLGQKQRVAFARALILDPKIIVADEAFSM 181
Cdd:PRK13539 86 PALTVAENLEfwAAFLGGEELDIAAALEAV--GLAPLAHLPFGYL------SAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170 180 190
....*....|....*....|....*....|....*
gi 502191832 182 LDVSMRSQVVNLLLKLQERLGLsyVVVA--NDLGL 214
Cdd:PRK13539 158 LDAAAVALFAELIRAHLAQGGI--VIAAthIPLGL 190
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
28-244 |
5.94e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 93.17 E-value: 5.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 28 VQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCklIRMIFQdpNSSLNPQLR 107
Cdd:PRK11000 16 VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG--VGMVFQ--SYALYPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 108 VGRILEAPLRL-NTDLSE-EERANTVIETLRMVGMLPEHalfyPQMISLGQKQRVAFARALILDPKIIVADEAFSMLDVS 185
Cdd:PRK11000 92 VAENMSFGLKLaGAKKEEiNQRVNQVAEVLQLAHLLDRK----PKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502191832 186 MRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNPQ 244
Cdd:PRK11000 168 LRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
6-243 |
7.24e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 92.61 E-value: 7.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 6 LLRVSGInKTFFNRVglfRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEV----NGEVIAF 81
Cdd:PRK13631 21 ILRVKNL-YCVFDEK---QENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 82 EDT-----QKRCK-------LIRMIFQDPNSSLNPQLRVGRILEAPLRLNtdLSEEERANTVIETLRMVGMLPEHALFYP 149
Cdd:PRK13631 97 HELitnpySKKIKnfkelrrRVSMVFQFPEYQLFKDTIEKDIMFGPVALG--VKKSEAKKLAKFYLNKMGLDDSYLERSP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 150 QMISLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGE 229
Cdd:PRK13631 175 FGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGK 253
|
250
....*....|....
gi 502191832 230 IVESGLTSEVFSNP 243
Cdd:PRK13631 254 ILKTGTPYEIFTDQ 267
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
29-234 |
9.99e-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: 89.78 E-value: 9.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 29 QVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIRMIFQDPNsslnpqlrv 108
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPT--------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 109 grILEAPLRLNTDLSEEERANTVIETLRmvgmLPEHALfypqMISLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRS 188
Cdd:cd03369 93 --LFSGTIRSNLDPFDEYSDEEIYGALR----VSEGGL----NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502191832 189 QVVNLLLKlqERLGLSYVVVANDLGLVRHIsDKVLIMHQGEIVESG 234
Cdd:cd03369 163 LIQKTIRE--EFTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYD 205
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
25-234 |
1.09e-21 |
|
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: 89.15 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 25 RKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAG--VVPPTSGEIEVNGevIAFEDTQKRCkLIRMIFQDpnSSL 102
Cdd:cd03213 19 KSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLING--RPLDKRSFRK-IIGYVPQD--DIL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 103 NPQLrvgrileaplrlntdlseeeranTVIETLRMVGMLpehalfypQMISLGQKQRVAFARALILDPKIIVADEAFSML 182
Cdd:cd03213 94 HPTL-----------------------TVRETLMFAAKL--------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502191832 183 DVSMRSQVVNLLLKL--QERLGLsyVVVANDLGLVRHISDKVLIMHQGEIVESG 234
Cdd:cd03213 143 DSSSALQVMSLLRRLadTGRTII--CSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
32-239 |
1.36e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 93.19 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 32 KDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKL-IRMIFQDPNSSlnpqlrvGR 110
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARgLVYLPEDRQSS-------GL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 111 ILEAPLRLNT------DLS---EEERANTVIETL-RMVGMLPEHALFYPQMISLGQKQRVAFARALILDPKIIVADEAFS 180
Cdd:PRK15439 353 YLDAPLAWNVcalthnRRGfwiKPARENAVLERYrRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502191832 181 MLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEV 239
Cdd:PRK15439 433 GVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAI 490
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-231 |
2.47e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.39 E-value: 2.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 4 APLLRVSGINKTffnrvglfrrkqvQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFED 83
Cdd:COG1129 254 EVVLEVEGLSVG-------------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRS 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 84 TQKRCKL-IRMIFQDpnsslnpQLRVGRILEAPLRLNTDLS---------------EEERANTVIETLR--------MVG 139
Cdd:COG1129 321 PRDAIRAgIAYVPED-------RKGEGLVLDLSIRENITLAsldrlsrgglldrrrERALAEEYIKRLRiktpspeqPVG 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 140 MLpehalfypqmiSLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHIS 219
Cdd:COG1129 394 NL-----------SGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLS 461
|
250
....*....|..
gi 502191832 220 DKVLIMHQGEIV 231
Cdd:COG1129 462 DRILVMREGRIV 473
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
7-254 |
2.51e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 90.53 E-value: 2.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 7 LRVSGINKTFFNRVGLfrrkQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIE------------- 73
Cdd:PRK13651 3 IKVKNIVKIFNKKLPT----ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwifkdeknkkktk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 74 ----VNGEVIAFEDTQKRCKLIRMI-------FQDPNSSLNPQLRVGRILEAPLRLNTDLSE-EERANTVIEtlrMVGmL 141
Cdd:PRK13651 79 ekekVLEKLVIQKTRFKKIKKIKEIrrrvgvvFQFAEYQLFEQTIEKDIIFGPVSMGVSKEEaKKRAAKYIE---LVG-L 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 142 PEHAL-FYPQMISLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISD 220
Cdd:PRK13651 155 DESYLqRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTK 233
|
250 260 270
....*....|....*....|....*....|....
gi 502191832 221 KVLIMHQGEIVESGLTSEVFSNpqhdvTKRLIQN 254
Cdd:PRK13651 234 RTIFFKDGKIIKDGDTYDILSD-----NKFLIEN 262
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
30-216 |
3.37e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 87.67 E-value: 3.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 30 VLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEV-IAFEDTQkrcklirmifqdpnSSLNPQL-- 106
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGArVAYVPQR--------------SEVPDSLpl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 107 RVGRILE----APLRLNTDLSEEERAnTVIETLRMVGM--LPEHALfypQMISLGQKQRVAFARALILDPKIIVADEAFS 180
Cdd:NF040873 73 TVRDLVAmgrwARRGLWRRLTRDDRA-AVDDALERVGLadLAGRQL---GELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 502191832 181 MLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVR 216
Cdd:NF040873 149 GLDAESRERIIALLAEEHAR-GATVVVVTHDLELVR 183
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
27-234 |
3.48e-21 |
|
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: 88.42 E-value: 3.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 27 QVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIRMIFQDPnsslnpql 106
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDV-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 107 rvgRILEAPLRLNTDL----SEEERantVIETLRMVGM---LPEHALFYPQMI-------SLGQKQRVAFARALILDPKI 172
Cdd:cd03245 88 ---TLFYGTLRDNITLgaplADDER---ILRAAELAGVtdfVNKHPNGLDLQIgergrglSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502191832 173 IVADEAFSMLDvsMRSQvVNLLLKLQERLGLSYVVVAND----LGLVrhisDKVLIMHQGEIVESG 234
Cdd:cd03245 162 LLLDEPTSAMD--MNSE-ERLKERLRQLLGDKTLIIITHrpslLDLV----DRIIVMDSGRIVADG 220
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
12-234 |
4.57e-21 |
|
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: 88.48 E-value: 4.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 12 INKTFFNRVGLFRRKQ---VQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPP---TSGEIEVNGEVIAFEDTQ 85
Cdd:cd03234 1 QRVLPWWDVGLKAKNWnkyARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPDQFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 86 KRCKLIRmifQDPNssLNPQLRVGRILE--APLRLNTDLSEEERANTV-IETLRMVGMLP-EHALFypQMISLGQKQRVA 161
Cdd:cd03234 81 KCVAYVR---QDDI--LLPGLTVRETLTytAILRLPRKSSDAIRKKRVeDVLLRDLALTRiGGNLV--KGISGGERRRVS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502191832 162 FARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESG 234
Cdd:cd03234 154 IAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-238 |
4.69e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 91.65 E-value: 4.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 1 MNSAPLLRVSGINKTFfnrvglfrrKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIA 80
Cdd:PRK15439 6 TTAPPLLCARSISKQY---------SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 81 FEDTQKRCKL-IRMIFQDPNssLNPQLRVGR-ILeapLRLNTDLSEEERANTVIETLRMVGMLPEHAlfypQMISLGQKQ 158
Cdd:PRK15439 77 RLTPAKAHQLgIYLVPQEPL--LFPNLSVKEnIL---FGLPKRQASMQKMKQLLAALGCQLDLDSSA----GSLEVADRQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 159 RVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQErLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSE 238
Cdd:PRK15439 148 IVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLA-QGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTAD 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
29-252 |
6.80e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 88.75 E-value: 6.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 29 QVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVV-----PPTSGEIEVNGEVIAFEDTQ--KRCKLIRMIFQDPNSS 101
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIYSPDVDpiEVRREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 102 lnPQLRVGRILEAPLRLNTDLSEEERANTVIETlrmvgMLPEHALF---------YPQMISLGQKQRVAFARALILDPKI 172
Cdd:PRK14267 98 --PHLTIYDNVAIGVKLNGLVKSKKELDERVEW-----ALKKAALWdevkdrlndYPSNLSGGQRQRLVIARALAMKPKI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 173 IVADEAFSMLDVSMRSQVVNLLLKLQERlgLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNPQHDVTKRLI 252
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYV 248
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-182 |
1.20e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 90.74 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 3 SAPLLRVSGINKTFfnrvglfrrKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFE 82
Cdd:PRK11288 1 SSPYLSFDGIGKTF---------PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 83 DTqkRCKL---IRMIFQD----PNSSLNPQLRVGRIleaPLRLNTdLSEEERANTVIETLRMVGML--PEHALFYpqmIS 153
Cdd:PRK11288 72 ST--TAALaagVAIIYQElhlvPEMTVAENLYLGQL---PHKGGI-VNRRLLNYEAREQLEHLGVDidPDTPLKY---LS 142
|
170 180
....*....|....*....|....*....
gi 502191832 154 LGQKQRVAFARALILDPKIIVADEAFSML 182
Cdd:PRK11288 143 IGQRQMVEIAKALARNARVIAFDEPTSSL 171
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
29-234 |
1.23e-20 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 86.43 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 29 QVLKDISFTLEPGETLALVGETGSGKSTLAKILAGV--VPPTSGEIEVNGEVIAFEDTQKRCKL-IRMIFQDPnsslnpq 105
Cdd:cd03217 14 EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLgIFLAFQYP------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 106 lrvgrileaplrlntdlsEEERANTVIETLRMVGMlpehalfypqMISLGQKQRVAFARALILDPKIIVADEAFSMLDVS 185
Cdd:cd03217 87 ------------------PEIPGVKNADFLRYVNE----------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502191832 186 MRSQVVNLLLKLQERlGLSYVVVANDLGLVRHI-SDKVLIMHQGEIVESG 234
Cdd:cd03217 139 ALRLVAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG 187
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
29-231 |
1.78e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 86.85 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 29 QVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIR---MIFQDPNSSLNPQ 105
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRqigMIFQDHHLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 106 lrVGRILEAPLRLnTDLSEEERANTVIETLRMVGMLpEHALFYPQMISLGQKQRVAFARALILDPKIIVADEAFSMLDVS 185
Cdd:PRK10908 96 --VYDNVAIPLII-AGASGDDIRRRVSAALDKVGLL-DKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502191832 186 MRSQVVNLLLKLQeRLGLSYVVVANDLGLVRHISDKVLIMHQGEIV 231
Cdd:PRK10908 172 LSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
30-209 |
3.86e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 89.10 E-value: 3.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 30 VLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEvngeviafedtqkRCKLIRMIFqdpnssLnPQ---L 106
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA-------------RPAGARVLF------L-PQrpyL 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 107 RVGRILEA---PlRLNTDLSEEErantVIETLRMVGmLPEHA--LF----YPQMISLGQKQRVAFARALILDPKIIVADE 177
Cdd:COG4178 438 PLGTLREAllyP-ATAEAFSDAE----LREALEAVG-LGHLAerLDeeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDE 511
|
170 180 190
....*....|....*....|....*....|...
gi 502191832 178 AFSMLDVSMRSQvvnLLLKLQERL-GLSYVVVA 209
Cdd:COG4178 512 ATSALDEENEAA---LYQLLREELpGTTVISVG 541
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
45-244 |
4.61e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 88.01 E-value: 4.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 45 ALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIaFEDTQKRC-----KLIRMIFQDpnSSLNPQLRVgrilEAPLRLN 119
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVL-FDAEKGIClppekRRIGYVFQD--ARLFPHYKV----RGNLRYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 120 TDLSEEERANTVIETLRMvgmlpEHAL-FYPQMISLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQ 198
Cdd:PRK11144 101 MAKSMVAQFDKIVALLGI-----EPLLdRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502191832 199 ERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNPQ 244
Cdd:PRK11144 176 REINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
27-260 |
1.41e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 84.78 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 27 QVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKrcklirmIFQDPNSSLNpql 106
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQK-------LYLDTTLPLT--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 107 rVGRILEapLRLNTdlseeeRANTVIETLRMVGmlPEHALFYP-QMISLGQKQRVAFARALILDPKIIVADEAFSMLDVS 185
Cdd:PRK09544 86 -VNRFLR--LRPGT------KKEDILPALKRVQ--AGHLIDAPmQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 186 MRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQgEIVESGlTSEVFS------------------------ 241
Cdd:PRK09544 155 GQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSG-TPEVVSlhpefismfgprgaeqlgiyrhhh 232
|
250
....*....|....*....
gi 502191832 242 NPQHDVTKRLIQNHGHEYR 260
Cdd:PRK09544 233 NHRHDLQGRIVLRRGNDRS 251
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
29-234 |
3.00e-19 |
|
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: 82.36 E-value: 3.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 29 QVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEviafedtqkrcklirmifqdPNSSLNPQLR- 107
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGV--------------------PVSDLEKALSs 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 108 -VGRILEAPLRLNTDLseeeRANtvietlrmVGmlpehalfypQMISLGQKQRVAFARALILDPKIIVADEAFSMLDVSM 186
Cdd:cd03247 76 lISVLNQRPYLFDTTL----RNN--------LG----------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPIT 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502191832 187 RSQVVNLLLKLQErlGLSYVVVANDLGLVRHIsDKVLIMHQGEIVESG 234
Cdd:cd03247 134 ERQLLSLIFEVLK--DKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
17-197 |
4.79e-19 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 81.43 E-value: 4.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 17 FNRVGLFRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEvngeviafedtqkrcklirmIFQ 96
Cdd:cd03223 3 LENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG--------------------MPE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 97 DPNSSLNPQlrvgrileaplrlntdlseeeRANTVIETLRmvgmlpeHALFYP--QMISLGQKQRVAFARALILDPKIIV 174
Cdd:cd03223 63 GEDLLFLPQ---------------------RPYLPLGTLR-------EQLIYPwdDVLSGGEQQRLAFARLLLHKPKFVF 114
|
170 180
....*....|....*....|...
gi 502191832 175 ADEAFSMLDVSMRSQVVNLLLKL 197
Cdd:cd03223 115 LDEATSALDEESEDRLYQLLKEL 137
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-232 |
6.77e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.50 E-value: 6.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 5 PLLRVSGINKTFFNRVglfrrkqvqVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEV-IAFED 83
Cdd:COG0488 314 KVLELEGLSKSYGDKT---------LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVkIGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 84 tqkrcklirmifQDpNSSLNPQLRVgriLEAPLRLNTDLSEEErantvietLRmvGMLpEHALFYPQMI-------SLGQ 156
Cdd:COG0488 385 ------------QH-QEELDPDKTV---LDELRDGAPGGTEQE--------VR--GYL-GRFLFSGDDAfkpvgvlSGGE 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 157 KQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLlklqerlgLSY----VVVANDLGLVRHISDKVLIMHQGEIVE 232
Cdd:COG0488 438 KARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEAL--------DDFpgtvLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
29-250 |
8.38e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 83.16 E-value: 8.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 29 QVLKDISFTLEPGETLALVGETGSGKSTLAKILaGVVPPTSGEIEVNGEVIAFEDT--QKRCKLIR------MIFQDPN- 99
Cdd:PRK14258 21 KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVEFFNQNiyERRVNLNRlrrqvsMVHPKPNl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 100 ---------------SSLNPQLRVGRILEAPLRlNTDLSEEERANTVIETLRMVGmlpehalfypqmislGQKQRVAFAR 164
Cdd:PRK14258 100 fpmsvydnvaygvkiVGWRPKLEIDDIVESALK-DADLWDEIKHKIHKSALDLSG---------------GQQQRLCIAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 165 ALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQ-----GEIVESGLTSEV 239
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKI 243
|
250
....*....|.
gi 502191832 240 FSNPqHDVTKR 250
Cdd:PRK14258 244 FNSP-HDSRTR 253
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-229 |
1.48e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 84.60 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 3 SAPLLRVSGINKTFfnrvglfrrKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVP--PTSGEIEVNGEVIA 80
Cdd:PRK13549 2 MEYLLEMKNITKTF---------GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 81 FE---DTQKrcKLIRMIFQDpnSSLNPQLRVGRileaplrlNTDLSEEERANTVIE----TLRMVGMLPEHALFY----P 149
Cdd:PRK13549 73 ASnirDTER--AGIAIIHQE--LALVKELSVLE--------NIFLGNEITPGGIMDydamYLRAQKLLAQLKLDInpatP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 150 QM-ISLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQG 228
Cdd:PRK13549 141 VGnLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDG 219
|
.
gi 502191832 229 E 229
Cdd:PRK13549 220 R 220
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2-249 |
2.03e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 81.96 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 2 NSAPLLRVSGINKTFFnrvGLFrrkqvqVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAF 81
Cdd:PRK11300 1 MSQPLLSVSGLMMRFG---GLL------AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 82 EDTQK--RCKLIRMiFQdpNSSLNPQLRVgriLEAPL-----RLNTDL------------SEEERANTVIETLRMVGMLp 142
Cdd:PRK11300 72 LPGHQiaRMGVVRT-FQ--HVRLFREMTV---IENLLvaqhqQLKTGLfsgllktpafrrAESEALDRAATWLERVGLL- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 143 EHALFYPQMISLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKV 222
Cdd:PRK11300 145 EHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRI 224
|
250 260
....*....|....*....|....*..
gi 502191832 223 LIMHQGEIVESGLTSEVFSNPqhDVTK 249
Cdd:PRK11300 225 YVVNQGTPLANGTPEEIRNNP--DVIK 249
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
6-252 |
4.98e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 80.83 E-value: 4.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 6 LLRVSGINKTFfnrvglfrrKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVV---PPTSGEIEVNGEVIAFE 82
Cdd:PRK09984 4 IIRVEKLAKTF---------NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 83 -----DTQKRCKLIRMIFQDPNS----SLNPQLRVGRILEAPL-RLNTDLSEEERANTVIETLRMVGMlpehALFYPQMI 152
Cdd:PRK09984 75 grlarDIRKSRANTGYIFQQFNLvnrlSVLENVLIGALGSTPFwRTCFSWFTREQKQRALQALTRVGM----VHFAHQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 153 SL---GQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGE 229
Cdd:PRK09984 151 STlsgGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGH 230
|
250 260
....*....|....*....|...
gi 502191832 230 IVESGlTSEVFSNPQHDVTKRLI 252
Cdd:PRK09984 231 VFYDG-SSQQFDNERFDHLYRSI 252
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
26-241 |
5.34e-18 |
|
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: 82.93 E-value: 5.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 26 KQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGV--VPPTSGEIEVNG---------EVIAFEDTQ-KRC----K 89
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHValcekcgyvERPSKVGEPcPVCggtlE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 90 LIRMIFQDPNSSLNPQLRvgRILEAPLRLNTDLSEEERA-NTVIETLRMVGMLPEHALFYP----QMISL---------- 154
Cdd:TIGR03269 91 PEEVDFWNLSDKLRRRIR--KRIAIMLQRTFALYGDDTVlDNVLEALEEIGYEGKEAVGRAvdliEMVQLshrithiard 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 155 ---GQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIV 231
Cdd:TIGR03269 169 lsgGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIK 248
|
250
....*....|
gi 502191832 232 ESGLTSEVFS 241
Cdd:TIGR03269 249 EEGTPDEVVA 258
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
4-243 |
5.51e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 82.58 E-value: 5.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 4 APLLRVSGINKTFfnrvglfrrKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFED 83
Cdd:PRK09536 1 MPMIDVSDLSVEF---------GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 84 TQKRCKLIRMIFQDpnSSLNPQLRVGRILE---AP--LRLNTDLSEEERAntVIETLRMVGMlpehALFYPQMI---SLG 155
Cdd:PRK09536 72 ARAASRRVASVPQD--TSLSFEFDVRQVVEmgrTPhrSRFDTWTETDRAA--VERAMERTGV----AQFADRPVtslSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 156 QKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGL 235
Cdd:PRK09536 144 ERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGP 222
|
....*...
gi 502191832 236 TSEVFSNP 243
Cdd:PRK09536 223 PADVLTAD 230
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
30-252 |
7.93e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 80.53 E-value: 7.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 30 VLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSG-----EIEVNGE-VIAFEDTQKRCKLIRMIFQDPNSSln 103
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRsIFNYRDVLEFRRRVGMLFQRPNPF-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 104 PQLRVGRILeAPLRLNTDLSEEERANTVIETLRMVGM---LPEHALFYPQMISLGQKQRVAFARALILDPKIIVADEAFS 180
Cdd:PRK14271 114 PMSIMDNVL-AGVRAHKLVPRKEFRGVAQARLTEVGLwdaVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502191832 181 MLDVSMRSQVVNLLLKLQERLglSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNPQHDVTKRLI 252
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYV 262
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-229 |
8.48e-18 |
|
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: 77.49 E-value: 8.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 7 LRVSGINKTFFNRVglfrrkqvqVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVngeviafedtqk 86
Cdd:cd03221 1 IELENLSKTYGGKL---------LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW------------ 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 87 rcklirmifqdpnsslNPQLRVGrileaplrlntdlseeerantvietlrmvgmlpehalFYPQMiSLGQKQRVAFARAL 166
Cdd:cd03221 60 ----------------GSTVKIG-------------------------------------YFEQL-SGGEKMRLALAKLL 85
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502191832 167 ILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQerlGlSYVVVANDLGLVRHISDKVLIMHQGE 229
Cdd:cd03221 86 LENPNLLLLDEPTNHLDLESIEALEEALKEYP---G-TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-233 |
9.06e-18 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 82.14 E-value: 9.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 6 LLRVSGINKTFFNrvglfrrkqVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTS--GEIEVNGEVIAFED 83
Cdd:NF040905 1 ILEMRGITKTFPG---------VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRFKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 84 TQKRCKL-IRMIFQDpnSSLNPQLRVGRileaplrlNTDLSEEERANTVI----------ETLRMVGmLPEHalfyPQM- 151
Cdd:NF040905 72 IRDSEALgIVIIHQE--LALIPYLSIAE--------NIFLGNERAKRGVIdwnetnrrarELLAKVG-LDES----PDTl 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 152 ---ISLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQG 228
Cdd:NF040905 137 vtdIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDG 215
|
....*
gi 502191832 229 EIVES 233
Cdd:NF040905 216 RTIET 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-238 |
1.16e-17 |
|
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: 81.79 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 24 RRKQVQvlkDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPT-SGEIEVNGEVIAFEDTQKRCKL-IRMIFQD-PNS 100
Cdd:TIGR02633 272 HRKRVD---DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRAgIAMVPEDrKRH 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 101 SLNPQLRVGR-ILEAPL-------RLNtDLSEEERANTVIETLRMVGMLPEHALfypQMISLGQKQRVAFARALILDPKI 172
Cdd:TIGR02633 349 GIVPILGVGKnITLSVLksfcfkmRID-AAAELQIIGSAIQRLKVKTASPFLPI---GRLSGGNQQKAVLAKMLLTNPRV 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 173 IVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEI----VESGLTSE 238
Cdd:TIGR02633 425 LILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLkgdfVNHALTQE 493
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
30-241 |
1.25e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 79.67 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 30 VLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIA-FEDTQkrckLIRMIFQDPNSSLNPQ-LR 107
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISmLSSRQ----LARRLALLPQHHLTPEgIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 108 VGRILE---AP-LRLNTDLSEEERA--NTVIETLRMVgMLPEHALfypQMISLGQKQRVAFARALILDPKIIVADEAFSM 181
Cdd:PRK11231 93 VRELVAygrSPwLSLWGRLSAEDNArvNQAMEQTRIN-HLADRRL---TDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTY 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 182 LDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFS 241
Cdd:PRK11231 169 LDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMT 227
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
24-185 |
3.23e-17 |
|
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: 77.40 E-value: 3.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 24 RRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAfEDTQKRCKLIRMIFQDPnsSLN 103
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA-EQRDEPHENILYLGHLP--GLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 104 PQLRVgriLEAPLRLNTDLSEEERanTVIETLRMVGM-----LPEHALfypqmiSLGQKQRVAFARALILDPKIIVADEA 178
Cdd:TIGR01189 86 PELSA---LENLHFWAAIHGGAQR--TIEDALAAVGLtgfedLPAAQL------SAGQQRRLALARLWLSRRPLWILDEP 154
|
....*..
gi 502191832 179 FSMLDVS 185
Cdd:TIGR01189 155 TTALDKA 161
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
29-234 |
3.33e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 80.66 E-value: 3.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 29 QVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTsGEIEVNG-EVIAFEDTQKRcKLIRMIFQdpnsslNPQLR 107
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGiELRELDPESWR-KHLSWVGQ------NPQLP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 108 VGRILEAPLRLNTDLSEEErANTVIE---TLRMVGMLPeHALFYP---QM--ISLGQKQRVAFARALILDPKIIVADEAF 179
Cdd:PRK11174 436 HGTLRDNVLLGNPDASDEQ-LQQALEnawVSEFLPLLP-QGLDTPigdQAagLSVGQAQRLALARALLQPCQLLLLDEPT 513
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502191832 180 SMLDVSMRSQVVNLLlkLQERLGLSYVVVANDLGLVRHIsDKVLIMHQGEIVESG 234
Cdd:PRK11174 514 ASLDAHSEQLVMQAL--NAASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQG 565
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
26-244 |
6.12e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 77.63 E-value: 6.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 26 KQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKliRMIFQDPN-SSLNP 104
Cdd:PRK10895 14 KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARAR--RGIGYLPQeASIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 105 QLRVGRILEAPLRLNTDLSEE---ERANTVIETLRMVGMLPEHAlfypQMISLGQKQRVAFARALILDPKIIVADEAFSM 181
Cdd:PRK10895 92 RLSVYDNLMAVLQIRDDLSAEqreDRANELMEEFHIEHLRDSMG----QSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502191832 182 LDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNPQ 244
Cdd:PRK10895 168 VDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-233 |
7.14e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 77.06 E-value: 7.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 1 MNSAPLLRVSGINktffnrvglFRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIA 80
Cdd:PRK10247 2 QENSPLLQLQNVG---------YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 81 FEDTQKRCKLIRMIFQDP---------NSSLNPQLRvgRILEAPLRLNTDLSEEErantvietlrmvgmLPEHALFYP-Q 150
Cdd:PRK10247 73 TLKPEIYRQQVSYCAQTPtlfgdtvydNLIFPWQIR--NQQPDPAIFLDDLERFA--------------LPDTILTKNiA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 151 MISLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHiSDKVLIM--HQG 228
Cdd:PRK10247 137 ELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITLqpHAG 215
|
....*
gi 502191832 229 EIVES 233
Cdd:PRK10247 216 EMQEA 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-231 |
9.04e-17 |
|
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: 79.48 E-value: 9.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 6 LLRVSGINKTFfnrvglfrrKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVP--PTSGEIEVNGEVI---A 80
Cdd:TIGR02633 1 LLEMKGIVKTF---------GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLkasN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 81 FEDTQKrcKLIRMIFQD----PNSSLNPQLRVGRILEAPLRLNTDLSEEERANTVIETLRmvgmLPEHALFYPQM-ISLG 155
Cdd:TIGR02633 72 IRDTER--AGIVIIHQEltlvPELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQ----LDADNVTRPVGdYGGG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502191832 156 QKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEIV 231
Cdd:TIGR02633 146 QQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
26-234 |
1.68e-16 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 76.60 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 26 KQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGvvPP----TSGEIEVNGEVIAFEDTQKRCKL-IRMIFQDPns 100
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPaykiLEGDILFKGESILDLEPEERAHLgIFLAFQYP-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 101 slnpqlrvgriLEAP-------LRL--NT--------DLSEEERANTVIETLRMVGMLPEhalFYPQMI----SLGQKQR 159
Cdd:CHL00131 94 -----------IEIPgvsnadfLRLayNSkrkfqglpELDPLEFLEIINEKLKLVGMDPS---FLSRNVnegfSGGEKKR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502191832 160 VAFARALILDPKIIVADEAFSMLDV-SMR--SQVVNLLLKLQErlglSYVVVANDLGLVRHIS-DKVLIMHQGEIVESG 234
Cdd:CHL00131 160 NEILQMALLDSELAILDETDSGLDIdALKiiAEGINKLMTSEN----SIILITHYQRLLDYIKpDYVHVMQNGKIIKTG 234
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
30-229 |
2.05e-16 |
|
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: 75.20 E-value: 2.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 30 VLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEvIAF--------EDTqkrcklIR--MIFQDPn 99
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-IAYvsqepwiqNGT------IRenILFGKP- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 100 ssLNPQlRVGRILEAPLrLNTDLSE-EERANTVI-E---TLrmvgmlpehalfypqmiSLGQKQRVAFARALILDPKIIV 174
Cdd:cd03250 92 --FDEE-RYEKVIKACA-LEPDLEIlPDGDLTEIgEkgiNL-----------------SGGQKQRISLARAVYSDADIYL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502191832 175 ADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHiSDKVLIMHQGE 229
Cdd:cd03250 151 LDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
26-234 |
2.10e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 78.14 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 26 KQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIafedtqKRCKLirmifqdpnSSLNPQ 105
Cdd:PRK11176 354 KEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL------RDYTL---------ASLRNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 106 LrvgrileAPLRLNTDLSEEERANT-------------VIETLRMVgmlpeHAL-FYPQM--------------ISLGQK 157
Cdd:PRK11176 419 V-------ALVSQNVHLFNDTIANNiayarteqysreqIEEAARMA-----YAMdFINKMdngldtvigengvlLSGGQR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502191832 158 QRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQ-ERLGLsyvVVANDLGLVRHiSDKVLIMHQGEIVESG 234
Cdd:PRK11176 487 QRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQkNRTSL---VIAHRLSTIEK-ADEILVVEDGEIVERG 560
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
30-234 |
2.26e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 78.22 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 30 VLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNG---EVIAFEDTQKRCKLIR---MIFQDpnsSLN 103
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDiplTKLQLDSWRSRLAVVSqtpFLFSD---TVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 104 PQLRVGRileaplrlnTDLSEEErantvIETLRMVGMLPEHALFYPQ-----------MISLGQKQRVAFARALILDPKI 172
Cdd:PRK10789 407 NNIALGR---------PDATQQE-----IEHVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLLNAEI 472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502191832 173 IVADEAFSMLDVSMRSQVVNLLlkLQERLGLSYVVVANDLGLVRHiSDKVLIMHQGEIVESG 234
Cdd:PRK10789 473 LILDDALSAVDGRTEHQILHNL--RQWGEGRTVIISAHRLSALTE-ASEILVMQHGHIAQRG 531
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
24-238 |
3.67e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 77.66 E-value: 3.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 24 RRKQVqvlKDISFTLEPGETLALVGETGSGKSTLAKILAGVVP-PTSGEIEVNGEVIAFEDTQKRCKL-IRMIFQD-PNS 100
Cdd:PRK13549 274 HIKRV---DDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQAIAQgIAMVPEDrKRD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 101 SLNPQLRVGR-ILEAPL-------RLNtDLSEEERANTVIETLRMVGMLPEHALfypQMISLGQKQRVAFARALILDPKI 172
Cdd:PRK13549 351 GIVPVMGVGKnITLAALdrftggsRID-DAAELKTILESIQRLKVKTASPELAI---ARLSGGNQQKAVLAKCLLLNPKI 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 173 IVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEI----VESGLTSE 238
Cdd:PRK13549 427 LILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKLkgdlINHNLTQE 495
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
24-232 |
3.94e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 74.99 E-value: 3.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 24 RRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVP--PTSGEIEVNGEVIafedtqkrcklirmifqDPNSS 101
Cdd:COG2401 39 RVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQF-----------------GREAS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 102 lnpqlrvgrILEAPLRLNTdlseeerANTVIETLRMVGmLPEHALF---YPQMiSLGQKQRVAFARALILDPKIIVADEA 178
Cdd:COG2401 102 ---------LIDAIGRKGD-------FKDAVELLNAVG-LSDAVLWlrrFKEL-STGQKFRFRLALLLAERPKLLVIDEF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502191832 179 FSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHIS-DKVLIMHQGEIVE 232
Cdd:COG2401 164 CSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQpDLLIFVGYGGVPE 218
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
31-256 |
6.47e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 77.09 E-value: 6.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 31 LKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTS-GEIEVNGEViafedtqkrcklirmifqdpnsSLNPQlrVG 109
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGTV----------------------AYVPQ--VS 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 110 RILEAPLRLNT------DLSEEERANTVIETLRMVGMLPEHALF----YPQMISLGQKQRVAFARALILDPKIIVADEAF 179
Cdd:PLN03130 689 WIFNATVRDNIlfgspfDPERYERAIDVTALQHDLDLLPGGDLTeigeRGVNISGGQKQRVSMARAVYSNSDVYIFDDPL 768
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502191832 180 SMLDVSMRSQVVNLLLKlQERLGLSYVVVANDLGLVRHIsDKVLIMHQGEIVESGLTSEVFSNPQhdVTKRLIQNHG 256
Cdd:PLN03130 769 SALDAHVGRQVFDKCIK-DELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNNGP--LFQKLMENAG 841
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-177 |
6.47e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.64 E-value: 6.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 9 VSGINKTFFNRVglfrrkqvqVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNG------------ 76
Cdd:COG0488 1 LENLSKSFGGRP---------LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglrigylpqepp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 77 ---------EVI-AFEDTQKRCKLIRMIFQDPNSSLNPQLRVGRILEAPLRLNT-DLseEERANTVIETLRmvgmLPEhA 145
Cdd:COG0488 72 ldddltvldTVLdGDAELRALEAELEELEAKLAEPDEDLERLAELQEEFEALGGwEA--EARAEEILSGLG----FPE-E 144
|
170 180 190
....*....|....*....|....*....|....
gi 502191832 146 LFYPQMISL--GQKQRVAFARALILDPKIIVADE 177
Cdd:COG0488 145 DLDRPVSELsgGWRRRVALARALLSEPDLLLLDE 178
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-260 |
1.01e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 76.40 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 2 NSAPLLRVSGINKTFFNRvglfrrkQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVI-A 80
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQ-------PQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIaD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 81 FEDTQKRckliRMIfqdpnsSLNPQlRVgRILEAPLRLNTDL-SEEERANTVIETLRMVGMlpEHALFYPQ--------- 150
Cdd:PRK11160 407 YSEAALR----QAI------SVVSQ-RV-HLFSATLRDNLLLaAPNASDEALIEVLQQVGL--EKLLEDDKglnawlgeg 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 151 --MISLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQErlGLSYVVVANDLGLVRHIsDKVLIMHQG 228
Cdd:PRK11160 473 grQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNG 549
|
250 260 270
....*....|....*....|....*....|..
gi 502191832 229 EIVESGltsevfsnpQHDVtkrLIQNHGHEYR 260
Cdd:PRK11160 550 QIIEQG---------THQE---LLAQQGRYYQ 569
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
33-184 |
1.39e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.91 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 33 DISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKL--------IrmifqdpNSSLNP 104
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLlylghqpgI-------KTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 105 qlrvgrilEAPLRLNTDLSEEERANTVIETLRMVG-----MLPEHALfypqmiSLGQKQRVAFARALILDPKIIVADEAF 179
Cdd:PRK13538 92 --------LENLRFYQRLHGPGDDEALWEALAQVGlagfeDVPVRQL------SAGQQRRVALARLWLTRAPLWILDEPF 157
|
....*
gi 502191832 180 SMLDV 184
Cdd:PRK13538 158 TAIDK 162
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
5-177 |
1.81e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.43 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 5 PLLRVSGINKTFfnrvglfrrKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAF--- 81
Cdd:PRK10762 3 ALLQLKGIDKAF---------PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFngp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 82 EDTQKRCklIRMIFQDPNssLNPQL--------------RVGRIL------EAPL---RLNTDLSEEerantvietlRMV 138
Cdd:PRK10762 74 KSSQEAG--IGIIHQELN--LIPQLtiaeniflgrefvnRFGRIDwkkmyaEADKllaRLNLRFSSD----------KLV 139
|
170 180 190
....*....|....*....|....*....|....*....
gi 502191832 139 GMLpehalfypqmiSLGQKQRVAFARALILDPKIIVADE 177
Cdd:PRK10762 140 GEL-----------SIGEQQMVEIAKVLSFESKVIIMDE 167
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-231 |
1.82e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.45 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 4 APLLRVSGINktffnrvgLFRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFED 83
Cdd:COG3845 255 EVVLEVENLS--------VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 84 TQKRCKL-IRMIFQDPnsslnpqLRVGRILEAPLRLNTDLSE-----------------EERANTVIETLR--------M 137
Cdd:COG3845 327 PRERRRLgVAYIPEDR-------LGRGLVPDMSVAENLILGRyrrppfsrggfldrkaiRAFAEELIEEFDvrtpgpdtP 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 138 VGMLpehalfypqmiSLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRH 217
Cdd:COG3845 400 ARSL-----------SGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILA 467
|
250
....*....|....
gi 502191832 218 ISDKVLIMHQGEIV 231
Cdd:COG3845 468 LSDRIAVMYEGRIV 481
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
18-241 |
1.86e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.15 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 18 NRVGLFRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIafeDTQKRCKLIRMIFQD 97
Cdd:PRK15056 10 NDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT---RQALQKNLVAYVPQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 98 PNSSLN-PQL--------RVGRI--LEAPlrlntdlSEEERAnTVIETLRMVGMLpEHALFYPQMISLGQKQRVAFARAL 166
Cdd:PRK15056 87 EEVDWSfPVLvedvvmmgRYGHMgwLRRA-------KKRDRQ-IVTAALARVDMV-EFRHRQIGELSGGQKKRVFLARAI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502191832 167 ILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVlIMHQGEIVESGLTSEVFS 241
Cdd:PRK15056 158 AQQGQVILLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASGPTETTFT 230
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-241 |
2.40e-15 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 75.05 E-value: 2.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 21 GLFRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIA---FEDTQKrckLIRMIFQd 97
Cdd:PRK10938 9 GTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITrlsFEQLQK---LVSDEWQ- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 98 pnsslnpqlrvgrileaplRLNTDL---SEEERANTVIETLRMVGMLPEHALFYPQM-------------ISLGQKQRVA 161
Cdd:PRK10938 85 -------------------RNNTDMlspGEDDTGRTTAEIIQDEVKDPARCEQLAQQfgitalldrrfkyLSTGETRKTL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 162 FARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFS 241
Cdd:PRK10938 146 LCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQ 224
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
25-215 |
3.74e-15 |
|
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: 71.76 E-value: 3.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 25 RKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIRMIFQDpnsSLNP 104
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAP---GIKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 105 QLRVGRILEAPLRLNTDLSEEERANTVieTLRMVGMLPEHALfypqmiSLGQKQRVAFARALILDPKIIVADEAFSMLDV 184
Cdd:cd03231 87 TLSVLENLRFWHADHSDEQVEEALARV--GLNGFEDRPVAQL------SAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170 180 190
....*....|....*....|....*....|.
gi 502191832 185 SMRSQVVNLLLKLQERLGLSYVVVANDLGLV 215
Cdd:cd03231 159 AGVARFAEAMAGHCARGGMVVLTTHQDLGLS 189
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
31-230 |
4.19e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 74.27 E-value: 4.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 31 LKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKL-IRMIFQDpnsslnpQLRVG 109
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANgIVYISED-------RKRDG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 110 RILEAPLRLNTDLseeeranTVIETLRMVGMLPEHA-----------LF---YPQM------ISLGQKQRVAFARALILD 169
Cdd:PRK10762 341 LVLGMSVKENMSL-------TALRYFSRAGGSLKHAdeqqavsdfirLFnikTPSMeqaiglLSGGNQQKVAIARGLMTR 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502191832 170 PKIIVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEI 230
Cdd:PRK10762 414 PKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
30-244 |
6.57e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 74.04 E-value: 6.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 30 VLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIRMIFQDPnsslnpqlrvg 109
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDP----------- 1393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 110 RILEAPLRLNTDLSEEERANTVIETLRMVGmLPEHALFYPQMI-----------SLGQKQRVAFARALI-LDPKIIVADE 177
Cdd:PTZ00243 1394 VLFDGTVRQNVDPFLEASSAEVWAALELVG-LRERVASESEGIdsrvleggsnySVGQRQLMCMARALLkKGSGFILMDE 1472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502191832 178 AFSMLDVSMRSQVVNLLLKLQErlglSYVV--VANDLGLVRHIsDKVLIMHQGEIVESGLTSEVFSNPQ 244
Cdd:PTZ00243 1473 ATANIDPALDRQIQATVMSAFS----AYTVitIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMNRQ 1536
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
25-258 |
7.67e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.91 E-value: 7.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 25 RKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKIL------------------------------------------- 61
Cdd:PTZ00265 1178 RPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtndmtneqdyqgdeeqnvgmknvne 1257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 62 -----------AGVVPPTSGEIEVNGEVIAFEDTQKRCKLIRMIFQDP---NSSLNPQLRVGRileaplrLNTDLSEEER 127
Cdd:PTZ00265 1258 fsltkeggsgeDSTVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPmlfNMSIYENIKFGK-------EDATREDVKR 1330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 128 ANTVIETLRMVGMLPE----HALFYPQMISLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGL 203
Cdd:PTZ00265 1331 ACKFAAIDEFIESLPNkydtNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADK 1410
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 502191832 204 SYVVVANDLGLVRHiSDKVLimhqgeivesgltseVFSNPqhDVTKRLIQNHG-HE 258
Cdd:PTZ00265 1411 TIITIAHRIASIKR-SDKIV---------------VFNNP--DRTGSFVQAHGtHE 1448
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
25-217 |
8.11e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.91 E-value: 8.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 25 RKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQK--RCKlIRMIFQDP---- 98
Cdd:PTZ00265 395 RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKwwRSK-IGVVSQDPllfs 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 99 NSSLNP------QLRVGRILEAPLRLNT----------------------DLSEEERANTVIETLR-------------- 136
Cdd:PTZ00265 474 NSIKNNikyslySLKDLEALSNYYNEDGndsqenknkrnscrakcagdlnDMSNTTDSNELIEMRKnyqtikdsevvdvs 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 137 -------MVGMLPEHalfYPQMI-------SLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLG 202
Cdd:PTZ00265 554 kkvlihdFVSALPDK---YETLVgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNEN 630
|
250
....*....|....*
gi 502191832 203 LSYVVVANDLGLVRH 217
Cdd:PTZ00265 631 RITIIIAHRLSTIRY 645
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
10-252 |
8.60e-15 |
|
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: 72.20 E-value: 8.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 10 SGINKTFFNRVGLFrrkQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEViafedtqkrck 89
Cdd:cd03291 35 SDDNNLFFSNLCLV---GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRI----------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 90 lirmifqdpnsSLNPQlrVGRILEAPLRLNTDLS---EEERANTVIETLRmvgmLPEHALFYPQ-----------MISLG 155
Cdd:cd03291 101 -----------SFSSQ--FSWIMPGTIKENIIFGvsyDEYRYKSVVKACQ----LEEDITKFPEkdntvlgeggiTLSGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 156 QKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVV-NLLLKLQErlGLSYVVVANDLGLVRhISDKVLIMHQGEIVESG 234
Cdd:cd03291 164 QRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFeSCVCKLMA--NKTRILVTSKMEHLK-KADKILILHEGSSYFYG 240
|
250
....*....|....*...
gi 502191832 235 LTSEVfSNPQHDVTKRLI 252
Cdd:cd03291 241 TFSEL-QSLRPDFSSKLM 257
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
31-251 |
9.25e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 73.47 E-value: 9.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 31 LKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIRMIFQDP---NSSLNPQlr 107
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFhlfDQLLGPE-- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 108 vgrileaplrlnTDLSEEERANTVIETLRMVGML--PEHALFYPQMiSLGQKQRVAFARALILDPKIIVADEAFSMLDVS 185
Cdd:PRK10522 417 ------------GKPANPALVEKWLERLKMAHKLelEDGRISNLKL-SKGQKKRLALLLALAEERDILLLDEWAADQDPH 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502191832 186 MRSQVVNLLLKLQERLGLSYVVVANDLGLVRHiSDKVLIMHQGEIVEsgLTSEVFSNPQHDVTKRL 251
Cdd:PRK10522 484 FRREFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSE--LTGEERDAASRDAVART 546
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
26-259 |
1.28e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.12 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 26 KQVQV---LKDISFTLEPGETLALVGETGSGKSTLAKILAGVVpPTSGEIEVNG----EVIAFEDTQKRCKLIRmifQDP 98
Cdd:PRK03695 4 NDVAVstrLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGqpleAWSAAELARHRAYLSQ---QQT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 99 NSSLNPqlrVGRILEAPLRLNTDLSEEERA-NTVIETLRMVGMLPEHAlfypQMISLGQKQRVAFA-------RALILDP 170
Cdd:PRK03695 80 PPFAMP---VFQYLTLHQPDKTRTEAVASAlNEVAEALGLDDKLGRSV----NQLSGGEWQRVRLAavvlqvwPDINPAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 171 KIIVADEAFSMLDVsmrSQVVNL--LLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSNPQ---- 244
Cdd:PRK03695 153 QLLLLDEPMNSLDV---AQQAALdrLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENlaqv 229
|
250
....*....|....*
gi 502191832 245 HDVTKRLIQNHGHEY 259
Cdd:PRK03695 230 FGVNFRRLDVEGHPM 244
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
34-231 |
1.39e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.02 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 34 ISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAF---------------EDTQKRCKL-IRMIFQD 97
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIrsprdairagimlcpEDRKAEGIIpVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 98 PN-SSLNPQLRVGRILEAPlrlntdlSEEERANTVIETLRMVGMLPEHALFYpqmISLGQKQRVAFARALILDPKIIVAD 176
Cdd:PRK11288 352 INiSARRHHLRAGCLINNR-------WEAENADRFIRSLNIKTPSREQLIMN---LSGGNQQKAILGRWLSEDMKVILLD 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502191832 177 EAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEIV 231
Cdd:PRK11288 422 EPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
13-239 |
1.61e-14 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 71.39 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 13 NKTFFnrvglfrrkqvqVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGE--VIAFedtqkrckl 90
Cdd:PRK13546 34 NKTFF------------ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvsVIAI--------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 91 irmifqdpNSSLNPQLRVGRILEAPLRLNTDLSEEERANT--VIEtlrmvgmLPEHALFYPQMI---SLGQKQRVAFARA 165
Cdd:PRK13546 93 --------SAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTpkIIE-------FSELGEFIYQPVkkySSGMRAKLGFSIN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502191832 166 LILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEV 239
Cdd:PRK13546 158 ITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-187 |
2.28e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 71.79 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 9 VSGINKTFFNRVglfrrkqvqVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRC 88
Cdd:PRK13536 44 LAGVSKSYGDKA---------VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 89 KlIRMIFQ----DPNSSLNPQLRV-GRIleapLRLNTDLSEEerantVIETLRMVGMLPEHALFYPQMISLGQKQRVAFA 163
Cdd:PRK13536 115 R-IGVVPQfdnlDLEFTVRENLLVfGRY----FGMSTREIEA-----VIPSLLEFARLESKADARVSDLSGGMKRRLTLA 184
|
170 180
....*....|....*....|....
gi 502191832 164 RALILDPKIIVADEAFSMLDVSMR 187
Cdd:PRK13536 185 RALINDPQLLILDEPTTGLDPHAR 208
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
31-256 |
5.26e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.55 E-value: 5.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 31 LKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTsgeievngeviafEDTqkrCKLIRmifqdPNSSLNPQlrVGR 110
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHA-------------ETS---SVVIR-----GSVAYVPQ--VSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 111 ILEAPLRLNTDLS---EEERANTVIETLRM---VGMLPEHALF----YPQMISLGQKQRVAFARALILDPKIIVADEAFS 180
Cdd:PLN03232 690 IFNATVRENILFGsdfESERYWRAIDVTALqhdLDLLPGRDLTeigeRGVNISGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502191832 181 MLDVSMRSQVVNLLLKlQERLGLSYVVVANDLGLVRHIsDKVLIMHQGEIVESGLTSEVFSNPQhdVTKRLIQNHG 256
Cdd:PLN03232 770 ALDAHVAHQVFDSCMK-DELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSKSGS--LFKKLMENAG 841
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
30-252 |
5.66e-14 |
|
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: 71.48 E-value: 5.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 30 VLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEViafedtqkrcklirmifqdpnsSLNPQlrVG 109
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRI----------------------SFSPQ--TS 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 110 RILEAPLRLNT--DLSEEE-RANTVIETLRM---VGMLPE--HALFYPQMISL--GQKQRVAFARALILDPKIIVADEAF 179
Cdd:TIGR01271 497 WIMPGTIKDNIifGLSYDEyRYTSVIKACQLeedIALFPEkdKTVLGEGGITLsgGQRARISLARAVYKDADLYLLDSPF 576
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502191832 180 SMLDVSMRSQVV-NLLLKLQerLGLSYVVVANDLGLVRHiSDKVLIMHQGEIVESGLTSEVfSNPQHDVTKRLI 252
Cdd:TIGR01271 577 THLDVVTEKEIFeSCLCKLM--SNKTRILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSEL-QAKRPDFSSLLL 646
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
9-234 |
5.91e-14 |
|
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: 68.44 E-value: 5.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 9 VSGINKTFFNRVGLFRRKqvqVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPT---SGEIEVNGevIAFEDTQ 85
Cdd:cd03233 4 LSWRNISFTTGKGRSKIP---ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNG--IPYKEFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 86 KRCKLiRMIFQDPNSSLNPQLRVGRILEAPLRLNTDlseeerantvietlRMVgmlpehalfypQMISLGQKQRVAFARA 165
Cdd:cd03233 79 EKYPG-EIIYVSEEDVHFPTLTVRETLDFALRCKGN--------------EFV-----------RGISGGERKRVSIAEA 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502191832 166 LILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVV---ANDlGLVrHISDKVLIMHQGEIVESG 234
Cdd:cd03233 133 LVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSlyqASD-EIY-DLFDKVLVLYEGRQIYYG 202
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
15-239 |
7.20e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 69.43 E-value: 7.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 15 TFFNRVGLFRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIRMI 94
Cdd:PRK10575 11 TFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 95 FQDPNSSLNPQLR----VGRI--LEAPLRlntdLSEEERANtVIETLRMVGMLP-EHALFypQMISLGQKQRVAFARALI 167
Cdd:PRK10575 91 PQQLPAAEGMTVRelvaIGRYpwHGALGR----FGAADREK-VEEAISLVGLKPlAHRLV--DSLSGGERQRAWIAMLVA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502191832 168 LDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEV 239
Cdd:PRK10575 164 QDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
30-241 |
1.21e-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: 70.36 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 30 VLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIA---FEDTQKRcklIRMIFQDPnsslnpql 106
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAkigLHDLRFK---ITIIPQDP-------- 1369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 107 rvgRILEAPLRLNTD----LSEEErANTVIETLRM---VGMLPEHALFY----PQMISLGQKQRVAFARALILDPKIIVA 175
Cdd:TIGR00957 1370 ---VLFSGSLRMNLDpfsqYSDEE-VWWALELAHLktfVSALPDKLDHEcaegGENLSVGQRQLVCLARALLRKTKILVL 1445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502191832 176 DEAFSMLDVSMrSQVVNLLLKLQERlGLSYVVVANDLGLVRHISdKVLIMHQGEIVESGLTSEVFS 241
Cdd:TIGR00957 1446 DEATAAVDLET-DNLIQSTIRTQFE-DCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQ 1508
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
30-253 |
1.92e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 68.09 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 30 VLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIRMIFQDPNS----SLNPQ 105
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpgdiTVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 106 LRVGRILEAPLRLNTdlsEEERANTVIETLRMVGmLPEHALFYPQMISLGQKQRVAFARALILDPKIIVADEAFSMLDVS 185
Cdd:PRK10253 102 VARGRYPHQPLFTRW---RKEDEEAVTKAMQATG-ITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502191832 186 MRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVfsnpqhdVTKRLIQ 253
Cdd:PRK10253 178 HQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI-------VTAELIE 238
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
13-242 |
2.34e-13 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 69.15 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 13 NKTFFNRVGLFRRKQVQV----LKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEViafedtqkrc 88
Cdd:PRK13545 18 NKPFDKLKDLFFRSKDGEyhyaLNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 89 KLIRMifqdpNSSLNPQLRVGRILEapLR-LNTDLSEEErantVIETLRMVGMLPEHALFYPQMI---SLGQKQRVAFAR 164
Cdd:PRK13545 88 ALIAI-----SSGLNGQLTGIENIE--LKgLMMGLTKEK----IKEIIPEIIEFADIGKFIYQPVktySSGMKSRLGFAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502191832 165 ALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFSN 242
Cdd:PRK13545 157 SVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
35-224 |
2.36e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.45 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 35 SFTLE-------PGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEV--------IAFEDTQKrcKLIRMIFQDPN 99
Cdd:PRK13409 352 DFSLEveggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKIsykpqyikPDYDGTVE--DLLRSITDDLG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 100 SS------LNPqLRVGRILEAPLrlnTDLSEEERantvietlrmvgmlpehalfypqmislgqkQRVAFARALILDPKII 173
Cdd:PRK13409 430 SSyykseiIKP-LQLERLLDKNV---KDLSGGEL------------------------------QRVAIAACLSRDADLY 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502191832 174 VADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLI 224
Cdd:PRK13409 476 LLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
30-242 |
3.49e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 69.23 E-value: 3.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 30 VLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNG-EVIAFEDTQKRcKLIRMIFQDPnsslnpqlrv 108
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDcDVAKFGLTDLR-RVLSIIPQSP---------- 1319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 109 gRILEAPLRLNTD-LSEE---------ERANTVIETLRMVGMLPEHALFYPQMISLGQKQRVAFARALILDPKIIVADEA 178
Cdd:PLN03232 1320 -VLFSGTVRFNIDpFSEHndadlwealERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEA 1398
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502191832 179 FSMLDVSMRSQVVNLLlkLQERLGLSYVVVANDLGLVRHiSDKVLIMHQGEIVESGLTSEVFSN 242
Cdd:PLN03232 1399 TASVDVRTDSLIQRTI--REEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSR 1459
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-245 |
6.30e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 66.77 E-value: 6.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 22 LFRRKQVqVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPT--------SGEIEVNGEVIAFEDTQKRCKLIRM 93
Cdd:PRK13547 9 VARRHRA-ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLRAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 94 IFQDPNS----SLNPQLRVGRILEAplRLNTDLSEEERaNTVIETLRMVGmlpEHALFYPQMISL--GQKQRVAFARAL- 166
Cdd:PRK13547 88 LPQAAQPafafSAREIVLLGRYPHA--RRAGALTHRDG-EIAWQALALAG---ATALVGRDVTTLsgGELARVQFARVLa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 167 --------ILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSE 238
Cdd:PRK13547 162 qlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPAD 241
|
....*..
gi 502191832 239 VFSnPQH 245
Cdd:PRK13547 242 VLT-PAH 247
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
30-183 |
6.64e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 65.74 E-value: 6.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 30 VLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIafedTQKRCKLIRMI-FQDPNSSLNPQLrv 108
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQKQLcFVGHRSGINPYL-- 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502191832 109 grileaPLRLNT--DLSEEERANTVIETLRMVGMlpEHALFYP-QMISLGQKQRVAFARALILDPKIIVADEAFSMLD 183
Cdd:PRK13540 90 ------TLRENClyDIHFSPGAVGITELCRLFSL--EHLIDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-224 |
7.09e-13 |
|
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: 66.28 E-value: 7.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 35 SFTLE-------PGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFE------DTQKRCK-LIRMIFQDPNS 100
Cdd:cd03237 12 EFTLEveggsisESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKpqyikaDYEGTVRdLLSSITKDFYT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 101 SlnPQLRVgRILEaPLRLNTDLSEEerantvietlrmvgmLPEhalfypqmISLGQKQRVAFARALILDPKIIVADEAFS 180
Cdd:cd03237 92 H--PYFKT-EIAK-PLQIEQILDRE---------------VPE--------LSGGELQRVAIAACLSKDADIYLLDEPSA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502191832 181 MLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLI 224
Cdd:cd03237 145 YLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
34-79 |
2.26e-12 |
|
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: 66.36 E-value: 2.26e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 502191832 34 ISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVI 79
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV 396
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
27-183 |
3.29e-12 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 66.02 E-value: 3.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 27 QVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGvvPPTSGEIEVNGEVIAFEDTQKRCKLIRMiFQDPNSSLNPQL 106
Cdd:PLN03140 892 RLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGDIRISGFPKKQETFARISG-YCEQNDIHSPQV 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 107 RVGR--ILEAPLRLNTDLSEEERANTVIETLRMVGM--LPEHALFYPQMISLG--QKQRVAFARALILDPKIIVADEAFS 180
Cdd:PLN03140 969 TVREslIYSAFLRLPKEVSKEEKMMFVDEVMELVELdnLKDAIVGLPGVTGLSteQRKRLTIAVELVANPSIIFMDEPTS 1048
|
...
gi 502191832 181 MLD 183
Cdd:PLN03140 1049 GLD 1051
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
5-230 |
3.46e-12 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 65.96 E-value: 3.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 5 PLLRVSGINKTFFNRVglfrrkqvqVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVngeviafedt 84
Cdd:PRK10636 311 PLLKMEKVSAGYGDRI---------ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL---------- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 85 qkrCKLIRMIFQDPNsslnpQLRVGRILEAPLRLNTDLSEEERANTVIETLRMVGMLPEHALFYPQMISLGQKQRVAFAR 164
Cdd:PRK10636 372 ---AKGIKLGYFAQH-----QLEFLRADESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLAL 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502191832 165 ALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLglsyVVVANDLGLVRHISDKVLIMHQGEI 230
Cdd:PRK10636 444 IVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGAL----VVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
11-234 |
3.83e-12 |
|
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: 66.19 E-value: 3.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 11 GINKTFFNR--------------VGLFRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNG 76
Cdd:TIGR01257 912 GINDSFFERelpglvpgvcvknlVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG 991
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 77 EVI-----AFEDTQKRCKLIRMIFQdpnsslnpQLRVGRILEAPLRLNTDLSEEERantvietLRMVGMLPEHALFY--- 148
Cdd:TIGR01257 992 KDIetnldAVRQSLGMCPQHNILFH--------HLTVAEHILFYAQLKGRSWEEAQ-------LEMEAMLEDTGLHHkrn 1056
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 149 --PQMISLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLqeRLGLSYVVVANDLGLVRHISDKVLIMH 226
Cdd:TIGR01257 1057 eeAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIIS 1134
|
....*...
gi 502191832 227 QGEIVESG 234
Cdd:TIGR01257 1135 QGRLYCSG 1142
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
35-224 |
6.09e-12 |
|
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: 65.19 E-value: 6.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 35 SFTLE-------PGETLALVGETGSGKSTLAKILAGVVPPTSGEIE---------------VNGEVIAFedtqkrckLIR 92
Cdd:COG1245 353 GFSLEveggeirEGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDedlkisykpqyispdYDGTVEEF--------LRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 93 MIFQDPNSS------LNPqLRVGRILEAPLRlntDLSEEERantvietlrmvgmlpehalfypqmislgqkQRVAFARAL 166
Cdd:COG1245 425 ANTDDFGSSyykteiIKP-LGLEKLLDKNVK---DLSGGEL------------------------------QRVAIAACL 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502191832 167 ILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLI 224
Cdd:COG1245 471 SRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
39-226 |
1.09e-11 |
|
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: 63.15 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 39 EPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNG---EVI-AFEDTQKRCKLIRMIFQDPNSSLNPQL-------- 106
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPdwdEILdEFRGSELQNYFTKLLEGDVKVIVKPQYvdlipkav 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 107 --RVGRILEAplrlnTDlsEEERANTVIETLRMVGMLPEHAlfypQMISLGQKQRVAFARALILDPKIIVADEAFSMLDV 184
Cdd:cd03236 104 kgKVGELLKK-----KD--ERGKLDELVDQLELRHVLDRNI----DQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502191832 185 SMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMH 226
Cdd:cd03236 173 KQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
14-242 |
1.50e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.04 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 14 KTFFNRVGLFRRKQVQVlKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIA----FEDTQKRCK 89
Cdd:PRK09700 263 ETVFEVRNVTSRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprspLDAVKKGMA 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 90 LIRMIFQD----PNSSLNPQLRVGRILE-APLRLNTDLSEEERANTVIETLRMVGMLPEHALfyPQMI---SLGQKQRVA 161
Cdd:PRK09700 342 YITESRRDngffPNFSIAQNMAISRSLKdGGYKGAMGLFHEVDEQRTAENQRELLALKCHSV--NQNItelSGGNQQKVL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 162 FARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEIvesgltSEVFS 241
Cdd:PRK09700 420 ISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRL------TQILT 492
|
.
gi 502191832 242 N 242
Cdd:PRK09700 493 N 493
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
30-256 |
3.88e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.83 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 30 VLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIA---FEDTQKRCKLIrmifqdpnsslnPQL 106
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISkfgLMDLRKVLGII------------PQA 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 107 RVgrILEAPLRLNTDLSEE----------ERANTVIETLRMVGMLPEHALFYPQMISLGQKQRVAFARALILDPKIIVAD 176
Cdd:PLN03130 1322 PV--LFSGTVRFNLDPFNEhndadlweslERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLD 1399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 177 EAFSMLDVsmRSQVvnLLLKL--QERLGLSYVVVANDLGLVRHiSDKVLIMHQGEIVESGLTSEVFSNpQHDVTKRLIQN 254
Cdd:PLN03130 1400 EATAAVDV--RTDA--LIQKTirEEFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSN-EGSAFSKMVQS 1473
|
..
gi 502191832 255 HG 256
Cdd:PLN03130 1474 TG 1475
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-187 |
6.71e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 61.36 E-value: 6.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 3 SAPLLRVSGINKTFFNRVglfrrkqvqVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFE 82
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKL---------VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 83 DTQKRCKlIRMIFQ----DPNSSLNPQLRV-GRILEAPlrlntdlSEEERAntVIETLRMVGMLPEHALFYPQMISLGQK 157
Cdd:PRK13537 75 ARHARQR-VGVVPQfdnlDPDFTVRENLLVfGRYFGLS-------AAAARA--LVPPLLEFAKLENKADAKVGELSGGMK 144
|
170 180 190
....*....|....*....|....*....|
gi 502191832 158 QRVAFARALILDPKIIVADEAFSMLDVSMR 187
Cdd:PRK13537 145 RRLTLARALVNDPDVLVLDEPTTGLDPQAR 174
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
29-234 |
9.78e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.19 E-value: 9.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 29 QVLKDISFTLEPGETLALVGETGSGKSTLAKILAGV--VPPTSGEIEVNG-EVIAFEDTQKRCKLIRMIFQDP------- 98
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGkDLLELSPEDRAGEGIFMAFQYPveipgvs 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 99 -----NSSLNpQLRVGRILEAPLRLN-TDLSEEErantvIETLRMvgmlPEHALFYPQMI--SLGQKQRVAFARALILDP 170
Cdd:PRK09580 95 nqfflQTALN-AVRSYRGQEPLDRFDfQDLMEEK-----IALLKM----PEDLLTRSVNVgfSGGEKKRNDILQMAVLEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502191832 171 KIIVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHIS-DKVLIMHQGEIVESG 234
Cdd:PRK09580 165 ELCILDESDSGLDIDALKIVADGVNSLRDG-KRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSG 228
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-183 |
1.06e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.86 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 1 MNSAPLLRVSGINktffnrvglFRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIA 80
Cdd:PRK13543 6 HTAPPLLAAHALA---------FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 81 fedTQKRCKLIRMIFQDPnsSLNPQLRVgriLEAPLRLNTdLSEEERANTVIETLRMVGmLPEHALFYPQMISLGQKQRV 160
Cdd:PRK13543 77 ---RGDRSRFMAYLGHLP--GLKADLST---LENLHFLCG-LHGRRAKQMPGSALAIVG-LAGYEDTLVRQLSAGQKKRL 146
|
170 180
....*....|....*....|...
gi 502191832 161 AFARALILDPKIIVADEAFSMLD 183
Cdd:PRK13543 147 ALARLWLSPAPLWLLDEPYANLD 169
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
30-241 |
2.12e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 60.66 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 30 VLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTS--GEIEVNGEVIafedTQKRCKLIRMIFQDpnSSLNPQLR 107
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKP----TKQILKRTGFVTQD--DILYPHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 108 VGRILE--APLRLNTDLSEEER---ANTVIETLRMVGMlpEHALF---YPQMISLGQKQRVAFARALILDPKIIVADEAF 179
Cdd:PLN03211 157 VRETLVfcSLLRLPKSLTKQEKilvAESVISELGLTKC--ENTIIgnsFIRGISGGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502191832 180 SMLDVSMRSQVVNLLLKLQERLGLSYVVVANDLGLVRHISDKVLIMHQGEIVESGLTSEVFS 241
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
31-184 |
3.56e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.96 E-value: 3.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 31 LKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEI-----------------EVNGEVIAF--EDTQKRCKLI 91
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIiyeqdlivarlqqdpprNVEGTVYDFvaEGIEEQAEYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 92 -------RMIFQDPNSSLNPQL-RVGRILEaplrlNTDLSE-EERANTVIETLrmvGMLPEHALfypQMISLGQKQRVAF 162
Cdd:PRK11147 99 kryhdisHLVETDPSEKNLNELaKLQEQLD-----HHNLWQlENRINEVLAQL---GLDPDAAL---SSLSGGWLRKAAL 167
|
170 180
....*....|....*....|..
gi 502191832 163 ARALILDPKIIVADEAFSMLDV 184
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLDI 189
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
2-239 |
5.18e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 59.74 E-value: 5.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 2 NSAPLLRVSGINKTFFNRvglfRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILA----GVVPPTSGEIEVNGe 77
Cdd:TIGR00956 52 NALLKILTRGFRKLKKFR----DTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDG- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 78 vIAFEDTQKRcKLIRMIFQDPNSSLNPQLRVGRILEAPLRLNT------DLSEEERANTVIE-TLRMVGMlpEHALF--- 147
Cdd:TIGR00956 127 -ITPEEIKKH-YRGDVVYNAETDVHFPHLTVGETLDFAARCKTpqnrpdGVSREEYAKHIADvYMATYGL--SHTRNtkv 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 148 ---YPQMISLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNlLLKLQERLGLSYVVVA------NDLGLVrhi 218
Cdd:TIGR00956 203 gndFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIR-ALKTSANILDTTPLVAiyqcsqDAYELF--- 278
|
250 260
....*....|....*....|.
gi 502191832 219 sDKVLIMHQGEIVESGLTSEV 239
Cdd:TIGR00956 279 -DKVIVLYEGYQIYFGPADKA 298
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
30-196 |
8.61e-10 |
|
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: 57.94 E-value: 8.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 30 VLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVpPTSGEIEVNGEVIAFEDTQKRCKLIRMIfqdpnsslnPQLRVg 109
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSWNSVPLQKWRKAFGVI---------PQKVF- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 110 rILEAPLRLNTD------------LSEEERANTVIEtlRMVGMLPEHALFYPQMISLGQKQRVAFARALILDPKIIVADE 177
Cdd:cd03289 88 -IFSGTFRKNLDpygkwsdeeiwkVAEEVGLKSVIE--QFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDE 164
|
170
....*....|....*....
gi 502191832 178 AFSMLDvSMRSQVVNLLLK 196
Cdd:cd03289 165 PSAHLD-PITYQVIRKTLK 182
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
29-197 |
1.64e-09 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 56.10 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 29 QVLKDISFTLEPGETLALVGETGSGKSTLAKILA-----GVVpptSGEIEVNGeviafedtqkrcKLIRMIFQdPNSSLN 103
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrktaGVI---TGEILING------------RPLDKNFQ-RSTGYV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 104 PQLrvgrileaplrlntDLSEEEraNTVIETLRMVGMLPEhalfypqmISLGQKQRVAFARALILDPKIIVADEAFSMLD 183
Cdd:cd03232 85 EQQ--------------DVHSPN--LTVREALRFSALLRG--------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
170
....*....|....
gi 502191832 184 VSMRSQVVNLLLKL 197
Cdd:cd03232 141 SQAAYNIVRFLKKL 154
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
31-249 |
1.71e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 56.71 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 31 LKDISFTLEPGETLALVGETGSGKSTLAKI---LAGVVPP--TSGEIEVNGEVIAFED-----TQKRcklIRMIFQDPNS 100
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGfrVEGKVTFHGKNLYAPDvdpveVRRR---IGMVFQKPNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 101 SlnPQLRVGRILEAPlRLN---TDLSE-EERA-------NTVIETLRMVGmlpehalfypQMISLGQKQRVAFARALILD 169
Cdd:PRK14243 103 F--PKSIYDNIAYGA-RINgykGDMDElVERSlrqaalwDEVKDKLKQSG----------LSLSGGQQQRLCIARAIAVQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 170 PKIIVADEAFSMLDVSMRSQVVNLLLKLQERlgLSYVVVANDLGLVRHISDKVLIMH---------QGEIVESGLTSEVF 240
Cdd:PRK14243 170 PEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEFDRTEKIF 247
|
....*....
gi 502191832 241 SNPQHDVTK 249
Cdd:PRK14243 248 NSPQQQATR 256
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
40-229 |
3.15e-09 |
|
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: 54.30 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 40 PGETLALVGETGSGKSTLAKILAG-VVPPTSGEIEVNGEVIAFEDTQKRCKLIRMIFQDPNSSlnpqlrvgrileaplrl 118
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSG----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 119 ntdlseeerantvietlrmvgmlpehalfypqmislGQKQRVAFARALILDPKIIVADEAFSMLDVS-----MRSQVVNL 193
Cdd:smart00382 64 ------------------------------------ELRLRLALALARKLKPDVLILDEITSLLDAEqeallLLLEELRL 107
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502191832 194 LLKLQERLGLSYVVVANDL-----GLVRHISDKVLIMHQGE 229
Cdd:smart00382 108 LLLLKSEKNLTVILTTNDEkdlgpALLRRRFDRRIVLLLIL 148
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
37-229 |
4.19e-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: 56.72 E-value: 4.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 37 TLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNG---EVI-AFEDTQKRCKLIRMIFQDPNSSLNPQL------ 106
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPswdEVLkRFRGTELQDYFKKLANGEIKVAHKPQYvdlipk 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 107 ----RVGRILEaplrlNTDlsEEERANTVIETLRMVGMLpEHALfypQMISLGQKQRVAFARALILDPKIIVADEAFSML 182
Cdd:COG1245 175 vfkgTVRELLE-----KVD--ERGKLDELAEKLGLENIL-DRDI---SELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502191832 183 DVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHqGE 229
Cdd:COG1245 244 DIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHILY-GE 288
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
30-196 |
1.09e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 55.69 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 30 VLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVpPTSGEIEVNGEVIAFEDTQKRCKLIRMIfqdpnsslnPQLRVg 109
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSVTLQTWRKAFGVI---------PQKVF- 1302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 110 rILEAPLRLNTD----LSEEE--RANTVIETLRMVGMLPEHALFYPQ----MISLGQKQRVAFARALILDPKIIVADEAF 179
Cdd:TIGR01271 1303 -IFSGTFRKNLDpyeqWSDEEiwKVAEEVGLKSVIEQFPDKLDFVLVdggyVLSNGHKQLMCLARSILSKAKILLLDEPS 1381
|
170
....*....|....*..
gi 502191832 180 SMLDvSMRSQVVNLLLK 196
Cdd:TIGR01271 1382 AHLD-PVTLQIIRKTLK 1397
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
41-226 |
1.11e-08 |
|
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: 53.34 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 41 GETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEdtqkrcklirmifqdpnsslnpqlrvgrileaplrlnt 120
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYK-------------------------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 121 dlseeerantvietlrmvgmlpehalfyPQMISL--GQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQVVNLLLKLQ 198
Cdd:cd03222 67 ----------------------------PQYIDLsgGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLS 118
|
170 180
....*....|....*....|....*...
gi 502191832 199 ERLGLSYVVVANDLGLVRHISDKVLIMH 226
Cdd:cd03222 119 EEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
28-231 |
1.78e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.74 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 28 VQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKL-IRMIFQDPN----SSL 102
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENgISMVHQELNlvlqRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 103 NPQLRVGRIleaPLR-LNTDLSEEERANTVIETLRMVGMLPEHALfypQMISLGQKQRVAFARALILDPKIIVADEAFSM 181
Cdd:PRK10982 91 MDNMWLGRY---PTKgMFVDQDKMYRDTKAIFDELDIDIDPRAKV---ATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502191832 182 LDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEIV 231
Cdd:PRK10982 165 LTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
30-241 |
2.84e-08 |
|
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: 53.37 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 30 VLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKRCKLIRMIFQDPnsslnpqlrvg 109
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDP----------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 110 RILEAPLRLNTDLSEEERANTVIETLR------MVGMLPE--HALFYP--QMISLGQKQRVAFARALILDPKIIVADEAF 179
Cdd:cd03288 105 ILFSGSIRFNLDPECKCTDDRLWEALEiaqlknMVKSLPGglDAVVTEggENFSVGQRQLFCLARAFVRKSSILIMDEAT 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502191832 180 SMLDVSMRsqvvNLLLK--LQERLGLSYVVVANdlgLVRHI--SDKVLIMHQGEIVESGLTSEVFS 241
Cdd:cd03288 185 ASIDMATE----NILQKvvMTAFADRTVVTIAH---RVSTIldADLVLVLSRGILVECDTPENLLA 243
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-72 |
3.97e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.74 E-value: 3.97e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502191832 7 LRVSGINKTFFNRVgLFrrkqvqvlKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEI 72
Cdd:PRK15064 320 LEVENLTKGFDNGP-LF--------KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
18-183 |
5.54e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 53.02 E-value: 5.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 18 NRVGLFRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEI---------------------EVNG 76
Cdd:TIGR03719 8 NRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEArpqpgikvgylpqepqldptkTVRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 77 EVIA----FEDTQKRCKLIRMIFQDPNSSLNP----QLRVGRILEAPLRLNTDlSEEERAntvIETLRMVgmlPEHALFy 148
Cdd:TIGR03719 88 NVEEgvaeIKDALDRFNEISAKYAEPDADFDKlaaeQAELQEIIDAADAWDLD-SQLEIA---MDALRCP---PWDADV- 159
|
170 180 190
....*....|....*....|....*....|....*
gi 502191832 149 pQMISLGQKQRVAFARALILDPKIIVADEAFSMLD 183
Cdd:TIGR03719 160 -TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-101 |
7.99e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 52.63 E-value: 7.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 7 LRVSGINKTFFNRVglfrrkqvqVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVnGE--VIAFEDt 84
Cdd:TIGR03719 323 IEAENLTKAFGDKL---------LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GEtvKLAYVD- 391
|
90
....*....|....*..
gi 502191832 85 QKRCKLirmifqDPNSS 101
Cdd:TIGR03719 392 QSRDAL------DPNKT 402
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
31-228 |
8.49e-08 |
|
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: 51.56 E-value: 8.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 31 LKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEI---EVNGEVIAFEDTQKRCKLIRMIFQDPNSSLNPQLR 107
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsNKNESEPSFEATRSRNRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 108 VGRILEAPLrlntdlsEEERANTVIETLRM---VGMLP--EHALFYPQMISL--GQKQRVAFARALILDPKIIVADEAFS 180
Cdd:cd03290 97 ENITFGSPF-------NKQRYKAVTDACSLqpdIDLLPfgDQTEIGERGINLsgGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502191832 181 MLDVSMRSQVVNL-LLKLQERLGLSYVVVANDLGLVRHiSDKVLIMHQG 228
Cdd:cd03290 170 ALDIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-197 |
1.71e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.03 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 29 QVLKDISFTLEPGETLALVGETGSGKSTLAKILA-----GVVppTSGEIEVNGEVI--AFEDTQKRCKLirmifQDPNSs 101
Cdd:TIGR00956 777 VILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAervttGVI--TGGDRLVNGRPLdsSFQRSIGYVQQ-----QDLHL- 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 102 lnPQLRVGRILE--APLRLNTDLSEEERANTVIETLRMVGM---------LPEHALfypqmiSLGQKQRVAFARALILDP 170
Cdd:TIGR00956 849 --PTSTVRESLRfsAYLRQPKSVSKSEKMEYVEEVIKLLEMesyadavvgVPGEGL------NVEQRKRLTIGVELVAKP 920
|
170 180
....*....|....*....|....*...
gi 502191832 171 KIIV-ADEAFSMLDVSMRSQVVNLLLKL 197
Cdd:TIGR00956 921 KLLLfLDEPTSGLDSQTAWSICKLMRKL 948
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
37-229 |
1.85e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.73 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 37 TLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNG---EVI-AFEDTQKRCKLIRMIFQDPNSSLNPQL------ 106
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPswdEVLkRFRGTELQNYFKKLYNGEIKVVHKPQYvdlipk 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 107 ----RVGRILEaplrlNTDlsEEERANTVIETLRMVGMLPEHAlfypQMISLGQKQRVAFARALILDPKIIVADEAFSML 182
Cdd:PRK13409 175 vfkgKVRELLK-----KVD--ERGKLDEVVERLGLENILDRDI----SELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502191832 183 DVSMRSQVVNLLLKLQErlGLSYVVVANDLGLVRHISDKVLIMHqGE 229
Cdd:PRK13409 244 DIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNVHIAY-GE 287
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
30-230 |
1.95e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.78 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 30 VLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIevngeviaFEDTQKRCKLIRMIFQDP-NSSLNPQLRV 108
Cdd:PLN03073 524 LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV--------FRSAKVRMAVFSQHHVDGlDLSSNPLLYM 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 109 GRILEAPLrlntdlseEERANTVIETLRMVGMLPEHALFypqMISLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRS 188
Cdd:PLN03073 596 MRCFPGVP--------EQKLRAHLGSFGVTGNLALQPMY---TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVE 664
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502191832 189 QVVNLLLKLQERLglsyVVVANDLGLVRHISDKVLIMHQGEI 230
Cdd:PLN03073 665 ALIQGLVLFQGGV----LMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
33-177 |
3.28e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.89 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 33 DISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFED--TQKRCKLIRMIFqdpnsSLNPQLRVGR 110
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDiaTRRRVGYMSQAF-----SLYGELTVRQ 358
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502191832 111 ILEAPLRLnTDLSEEERANTVIETLRMVGmLPEHALFYPQMISLGQKQRVAFARALILDPKIIVADE 177
Cdd:NF033858 359 NLELHARL-FHLPAAEIAARVAEMLERFD-LADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDE 423
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
29-184 |
4.16e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.72 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 29 QVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEV-IAFEDtQKRCKLirmifqDPnsslnpqlr 107
Cdd:PRK11147 333 QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLeVAYFD-QHRAEL------DP--------- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 108 vgrileaplrlntdlseeERanTVIETLR------MVGMLPEHALFYPQ--------------MISLGQKQRVAFARaLI 167
Cdd:PRK11147 397 ------------------EK--TVMDNLAegkqevMVNGRPRHVLGYLQdflfhpkramtpvkALSGGERNRLLLAR-LF 455
|
170
....*....|....*...
gi 502191832 168 LDP-KIIVADEAFSMLDV 184
Cdd:PRK11147 456 LKPsNLLILDEPTNDLDV 473
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
29-71 |
4.55e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.50 E-value: 4.55e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 502191832 29 QVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGE 71
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE 63
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
31-234 |
7.05e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 49.94 E-value: 7.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 31 LKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEViAFEDTQKRCKlirmifqdpNSSLNPQLRVGR 110
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSV-AYVPQQAWIQ---------NDSLRENILFGK 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 111 ILeaplrlntdlsEEERANTVIETLRMVG---MLP--EHALFYPQMISL--GQKQRVAFARALILDPKIIVADEAFSMLD 183
Cdd:TIGR00957 724 AL-----------NEKYYQQVLEACALLPdleILPsgDRTEIGEKGVNLsgGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502191832 184 VSMRSQVVNLLLKLQERL-GLSYVVVANDLGLVRHIsDKVLIMHQGEIVESG 234
Cdd:TIGR00957 793 AHVGKHIFEHVIGPEGVLkNKTRILVTHGISYLPQV-DVIIVMSGGKISEMG 843
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-87 |
7.57e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.73 E-value: 7.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 7 LRVSGINKTFFNRVglfrrkqvqVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVnGE--VIAFEDt 84
Cdd:PRK11819 325 IEAENLSKSFGDRL---------LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GEtvKLAYVD- 393
|
...
gi 502191832 85 QKR 87
Cdd:PRK11819 394 QSR 396
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
17-231 |
1.20e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 48.34 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 17 FNRVGLFRRKqVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEDTQKrcklirmIFQ 96
Cdd:PRK11614 8 FDKVSAHYGK-IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAK-------IMR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 97 DPNSSLNPQLRV-GRI-LEAPLRLNTDLSEEERANTVIEtlRMVGMLP---EHALFYPQMISLGQKQRVAFARALILDPK 171
Cdd:PRK11614 80 EAVAIVPEGRRVfSRMtVEENLAMGGFFAERDQFQERIK--WVYELFPrlhERRIQRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 172 IIVADEAFSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGEIV 231
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
31-238 |
4.60e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.42 E-value: 4.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 31 LKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVI----AFEDTQKRCKLIRM------IFQDPNS 100
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKInnhnANEAINHGFALVTEerrstgIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 101 SLNPQLRVGRILEAPLRLNTDLSEEERANTVIETLRMvgMLPEHalfYPQMISL--GQKQRVAFARALILDPKIIVADEA 178
Cdd:PRK10982 344 GFNSLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRV--KTPGH---RTQIGSLsgGNQQKVIIGRWLLTQPEILMLDEP 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502191832 179 FSMLDVSMRSQVVNLLLKLQERlGLSYVVVANDLGLVRHISDKVLIMHQGE---IVESGLTSE 238
Cdd:PRK10982 419 TRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLvagIVDTKTTTQ 480
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
38-228 |
1.44e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 46.16 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 38 LEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNGEVIAFEdtqkrcklIRMIFQD----PNSSLNPQLRVGR--- 110
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN--------ISDVHQNmgycPQFDAIDDLLTGRehl 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 111 ILEAPLRLNTDLSEEERANTVIETLRMVGMLPEHALFYpqmiSLGQKQRVAFARALILDPKIIVADEAFSMLDVSMRSQV 190
Cdd:TIGR01257 2034 YLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTY----SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRML 2109
|
170 180 190
....*....|....*....|....*....|....*...
gi 502191832 191 VNLLLKLQeRLGLSYVVVANDLGLVRHISDKVLIMHQG 228
Cdd:TIGR01257 2110 WNTIVSII-REGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
7-76 |
4.11e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.84 E-value: 4.11e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502191832 7 LRVSGINktffnrvgLFRRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPT---SGEIEVNG 76
Cdd:PLN03140 165 LGMLGIN--------LAKKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNG 229
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
46-184 |
1.23e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.96 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 46 LVGETGSGKSTLAKILAGVVPPTSGEIEV-NGEVI--------AFEDTQK------------RCKLIR-MIFQDPNSSLN 103
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLdPNERLgklrqdqfAFEEFTVldtvimghtelwEVKQERdRIYALPEMSEE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 104 PQLRVGRiLEAPLRLNTDLSEEERANtviETLRMVGmLPEHALFYP-QMISLGQKQRVAFARALILDPKIIVADEAFSML 182
Cdd:PRK15064 112 DGMKVAD-LEVKFAEMDGYTAEARAG---ELLLGVG-IPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNL 186
|
..
gi 502191832 183 DV 184
Cdd:PRK15064 187 DI 188
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
24-76 |
5.87e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.88 E-value: 5.87e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 502191832 24 RRKQVQVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEIEVNG 76
Cdd:NF033858 10 RYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLG 62
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
29-72 |
7.01e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.47 E-value: 7.01e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 502191832 29 QVLKDISFTLEPGETLALVGETGSGKSTLAKILAGVVPPTSGEI 72
Cdd:PRK13541 14 KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNI 57
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
31-169 |
3.42e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 37.48 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502191832 31 LKDISFTLEPGETLaLVGETGSGKSTLAK----ILAGVVPPTSGEIE---VNGEV-IAFEDTQKRCklIRMIFQDPNSSL 102
Cdd:pfam13476 9 FRDQTIDFSKGLTL-ITGPNGSGKTTILDaiklALYGKTSRLKRKSGggfVKGDIrIGLEGKGKAY--VEITFENNDGRY 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502191832 103 NPQLRVGRILEAPLRLNTDLSEEErantVIETLRMVGMLPEH----ALFYPQMISLGQKQRVAFARALILD 169
Cdd:pfam13476 86 TYAIERSRELSKKKGKTKKKEILE----ILEIDELQQFISELlksdKIILPLLVFLGQEREEEFERKEKKE 152
|
|
| TsaE |
pfam02367 |
Threonylcarbamoyl adenosine biosynthesis protein TsaE; This family of proteins is involved in ... |
37-68 |
4.83e-03 |
|
Threonylcarbamoyl adenosine biosynthesis protein TsaE; This family of proteins is involved in the synthesis of threonylcarbamoyl adenosine (t(6)A).
Pssm-ID: 460540 Cd Length: 127 Bit Score: 36.26 E-value: 4.83e-03
10 20 30
....*....|....*....|....*....|....*....
gi 502191832 37 TLEPGETLALVGETGSGKSTLAKILA------GVVP-PT 68
Cdd:pfam02367 17 LLKPGDVILLSGDLGAGKTTFTRGLArglgvtGPVTsPT 55
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
38-63 |
4.91e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 37.61 E-value: 4.91e-03
10 20
....*....|....*....|....*.
gi 502191832 38 LEPGETLALVGETGSGKSTLAKILAG 63
Cdd:PRK01889 192 LSGGKTVALLGSSGVGKSTLVNALLG 217
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
1-58 |
8.92e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.50 E-value: 8.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 502191832 1 MNSAPLlRVSGINktffnrvglfrrkqVQVLKDISFTLEPGETLALVGETGSGKSTLA 58
Cdd:PRK00635 1 MPSLPV-RLSGIT--------------VRNLKNISIEFCPREIVLLTGVSGSGKSSLA 43
|
|
| |
