|
Name |
Accession |
Description |
Interval |
E-value |
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
13-279 |
2.96e-131 |
|
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: 374.77 E-value: 2.96e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 13 LLDVRDLCVDFVNGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPKKARVSASrMQFANLDLLHLTEAQ 91
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRgETLGLVGESGSGKSTLARAILGLLPPPGITSGE-ILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 92 MRGVRGKRISMIMQDPKYSLNPVVCVGKQIAEAWLTHHPGRKDEAKAKALEMLEVVRIRQPERVYQLYPHEISGGQGQRI 171
Cdd:COG0444 80 LRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 172 MIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVESIAACDL- 250
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELf 239
|
250 260
....*....|....*....|....*....
gi 503996112 251 DNARHPYTQGLINSLPDMQHRRPILPVLQ 279
Cdd:COG0444 240 ENPRHPYTRALLSSIPRLDPDGRRLIPIP 268
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-273 |
3.90e-117 |
|
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: 346.67 E-value: 3.90e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 9 NNAPLLDVRDLCVDFVNGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPKKARVSASRMQFANLDLLHL 87
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAgETLALVGESGSGKSVTALSILRLLPDPAAHPSGSILFDGQDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 88 TEAQMRGVRGKRISMIMQDPKYSLNPVVCVGKQIAEAWLTHHPGRKDEAKAKALEMLEVVRIRQPERVYQLYPHEISGGQ 167
Cdd:COG4172 82 SERELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGGQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 168 GQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVESIAA 247
Cdd:COG4172 162 RQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPT 241
|
250 260
....*....|....*....|....*..
gi 503996112 248 CDL-DNARHPYTQGLINSLPDMQHRRP 273
Cdd:COG4172 242 AELfAAPQHPYTRKLLAAEPRGDPRPV 268
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-269 |
2.72e-96 |
|
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: 292.58 E-value: 2.72e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 6 PAANNAPLLDVRDLCVDF-VNGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPkkarVSASRMQFANLD 83
Cdd:COG1123 253 AAAAAEPLLEVRNLSKRYpVRGKGGVRAVDDVSLTLRRgETLGLVGESGSGKSTLARLLLGLLR----PTSGSILFDGKD 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 84 LLHLTEAQMRGVRgKRISMIMQDPKYSLNPVVCVGKQIAEAWLTHHPGRKDEAKAKALEMLEVVRIrqPERVYQLYPHEI 163
Cdd:COG1123 329 LTKLSRRSLRELR-RRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGL--PPDLADRYPHEL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 164 SGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVE 243
Cdd:COG1123 406 SGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVE 485
|
250 260
....*....|....*....|....*..
gi 503996112 244 SIAACD-LDNARHPYTQGLINSLPDMQ 269
Cdd:COG1123 486 DGPTEEvFANPQHPYTRALLAAVPSLD 512
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
7-275 |
6.69e-96 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 285.47 E-value: 6.69e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 7 AANNAPLLDVRDLCVDF-VNG------SAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPKkarvSASRMQ 78
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFpVRGglfgrtVGVVKAVDGVSFDIRRgETLGLVGESGCGKSTLGRLLLRLEEP----TSGEIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 79 FANLDLLHLTEAQMRGVRgKRISMIMQDPKYSLNPVVCVGKQIAEAWLTHHPGRKDEAKAKALEMLEVVRIRqPErVYQL 158
Cdd:COG4608 77 FDGQDITGLSGRELRPLR-RRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLR-PE-HADR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 159 YPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYA 238
Cdd:COG4608 154 YPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYL 233
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 503996112 239 GRVVESIAACDL-DNARHPYTQGLINSLP----DMQHRRPIL 275
Cdd:COG4608 234 GKIVEIAPRDELyARPLHPYTQALLSAVPvpdpERRRERIVL 275
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
13-243 |
1.32e-95 |
|
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: 280.93 E-value: 1.32e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 13 LLDVRDLCVDFVNGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHpkkARVSASRMqFANLDLLHLTEaQ 91
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKgETLGLVGESGSGKSTLARAILGLL---KPTSGSII-FDGKDLLKLSR-R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 92 MRGVRGKRISMIMQDPKYSLNPVVCVGKQIAEAWLTHHPGRKDEAKAKALeMLEVVRIRQPERVYQLYPHEISGGQGQRI 171
Cdd:cd03257 76 LRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAV-LLLLVGVGLPEEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503996112 172 MIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVE 243
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVE 226
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6-268 |
8.26e-87 |
|
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: 268.86 E-value: 8.26e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 6 PAANNAPLLDVRDLCVDFVN-----GSAVTH--AVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPkkarvSASRM 77
Cdd:COG4172 268 VPPDAPPLLEARDLKVWFPIkrglfRRTVGHvkAVDGVSLTLRRgETLGLVGESGSGKSTLGLALLRLIP-----SEGEI 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 78 QFANLDLLHLTEAQMRGVRgKRISMIMQDPKYSLNPVVCVGKQIAEAWLTHHPGR-KDEAKAKALEMLEVVRIrqPERVY 156
Cdd:COG4172 343 RFDGQDLDGLSRRALRPLR-RRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGPGLsAAERRARVAEALEEVGL--DPAAR 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 157 QLYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVM 236
Cdd:COG4172 420 HRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVM 499
|
250 260 270
....*....|....*....|....*....|....
gi 503996112 237 YAGRVVESiAACD--LDNARHPYTQGLINSLPDM 268
Cdd:COG4172 500 KDGKVVEQ-GPTEqvFDAPQHPYTRALLAAAPLL 532
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
8-266 |
1.07e-79 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 244.25 E-value: 1.07e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 8 ANNAPLLDVRDLCVDFVNGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPKKARVSASrMQFANLDLLH 86
Cdd:PRK09473 7 QQADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAgETLGIVGESGSGKSQTAFALMGLLAANGRIGGS-ATFNGREILN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 87 LTEAQMRGVRGKRISMIMQDPKYSLNPVVCVGKQIAEAWLTHHPGRKDEAKAKALEMLEVVRIRQPERVYQLYPHEISGG 166
Cdd:PRK09473 86 LPEKELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 167 QGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVESIA 246
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGN 245
|
250 260
....*....|....*....|.
gi 503996112 247 ACDL-DNARHPYTQGLINSLP 266
Cdd:PRK09473 246 ARDVfYQPSHPYSIGLLNAVP 266
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-275 |
1.66e-78 |
|
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: 246.74 E-value: 1.66e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 11 APLLDVRDLCVDFVNGSavTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPKKARVSASrMQFANLDLLHLTE 89
Cdd:COG1123 2 TPLLEVRDLSVRYPGGD--VPAVDGVSLTIAPgETVALVGESGSGKSTLALALMGLLPHGGRISGE-VLLDGRDLLELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 90 AqmrgVRGKRISMIMQDPKYSLNPVvCVGKQIAEAwLTHHPGRKDEAKAKALEMLEVVRIrqpERVYQLYPHEISGGQGQ 169
Cdd:COG1123 79 A----LRGRRIGMVFQDPMTQLNPV-TVGDQIAEA-LENLGLSRAEARARVLELLEAVGL---ERRLDRYPHQLSGGQRQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 170 RIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVES----- 244
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDgppee 229
|
250 260 270
....*....|....*....|....*....|..
gi 503996112 245 -IAACDLDNARHPYTQGLINSLPDMQHRRPIL 275
Cdd:COG1123 230 iLAAPQALAAVPRLGAARGRAAPAAAAAEPLL 261
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-284 |
2.68e-78 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 246.54 E-value: 2.68e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 12 PLLDVRDLCVDFVNGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPKKARV-SASRMQFANLDLLHLTE 89
Cdd:PRK15134 4 PLLAIENLSVAFRQQQTVRTVVNDVSLQIEAgETLALVGESGSGKSVTALSILRLLPSPPVVyPSGDIRFHGESLLHASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 90 AQMRGVRGKRISMIMQDPKYSLNPVVCVGKQIAEAWLTHHPGRKDEAKAKALEMLEVVRIRQPERVYQLYPHEISGGQGQ 169
Cdd:PRK15134 84 QTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGGERQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 170 RIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVESIAACD 249
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAAT 243
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 503996112 250 LDNA-RHPYTQGLINS------LPDMQHRRPILPVLQRQASW 284
Cdd:PRK15134 244 LFSApTHPYTQKLLNSepsgdpVPLPEPASPLLDVEQLQVAF 285
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
12-270 |
5.96e-75 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 232.10 E-value: 5.96e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 12 PLLDVRDLCVDFVNGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPKKARVSASRMQFANLDLLHLTEA 90
Cdd:COG4170 2 PLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEgEIRGLVGESGSGKSLIAKAICGITKDNWHVTADRFRWNGIDLLKLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 91 QMRGVRGKRISMIMQDPKYSLNPVVCVGKQIAEAWLTHHPG-----RKDEAKAKALEMLEVVRIRQPERVYQLYPHEISG 165
Cdd:COG4170 82 ERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIPSWTFKgkwwqRFKWRKKRAIELLHRVGIKDHKDIMNSYPHELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 166 GQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVESi 245
Cdd:COG4170 162 GECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVES- 240
|
250 260
....*....|....*....|....*..
gi 503996112 246 AACD--LDNARHPYTQGLINSLPDMQH 270
Cdd:COG4170 241 GPTEqiLKSPHHPYTKALLRSMPDFRQ 267
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
13-267 |
8.08e-75 |
|
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: 228.92 E-value: 8.08e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 13 LLDVRDLCVDFVNGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPkkarVSASRMQFANLDLLHLTEAQ 91
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPgESFGLVGESGSGKSTLLRALAGLER----PWSGEVTFDGRPVTRRRRKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 92 MRgvrgKRISMIMQDPKYSLNPVVCVGKQIAEAwLTHHpgRKDEAKAKALEMLEVVRIrqPERVYQLYPHEISGGQGQRI 171
Cdd:COG1124 77 FR----RRVQMVFQDPYASLHPRHTVDRILAEP-LRIH--GLPDREERIAELLEQVGL--PPSFLDRYPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 172 MIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVESIAACDL- 250
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLl 227
|
250
....*....|....*..
gi 503996112 251 DNARHPYTQGLINSLPD 267
Cdd:COG1124 228 AGPKHPYTRELLAASLA 244
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
13-267 |
1.32e-73 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 228.47 E-value: 1.32e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 13 LLDVRDLCVDFVNGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPKKARVSASRMQFANLDLLHLTEAQ 91
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQgEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEFNGQDLQRISEKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 92 MRGVRGKRISMIMQDPKYSLNPVVCVGKQIAEAWLTHHPGRKDEAKAKALEMLEVVRIRQPERVYQLYPHEISGGQGQRI 171
Cdd:PRK11022 83 RRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQRV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 172 MIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVESIAACDLD 251
Cdd:PRK11022 163 MIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIF 242
|
250
....*....|....*..
gi 503996112 252 NA-RHPYTQGLINSLPD 267
Cdd:PRK11022 243 RApRHPYTQALLRALPE 259
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
6-266 |
2.35e-72 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 225.36 E-value: 2.35e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 6 PAANNAPLLDVRDLCVDF--VNGSA-------VTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLhpkkarVSAS 75
Cdd:PRK15079 1 VTEGKKVLLEVADLKVHFdiKDGKQwfwqppkTLKAVDGVTLRLYEgETLGVVGESGCGKSTFARAIIGL------VKAT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 76 RMQFANL--DLLHLTEAQMRGVRgKRISMIMQDPKYSLNPVVCVGKQIAEAWLTHHPG-RKDEAKAKALEMLEVVRIRqp 152
Cdd:PRK15079 75 DGEVAWLgkDLLGMKDDEWRAVR-SDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKlSRQEVKDRVKAMMLKVGLL-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 153 ERVYQLYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDR 232
Cdd:PRK15079 152 PNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDR 231
|
250 260 270
....*....|....*....|....*....|....*.
gi 503996112 233 VLVMYAGRVVEsIAACD--LDNARHPYTQGLINSLP 266
Cdd:PRK15079 232 VLVMYLGHAVE-LGTYDevYHNPLHPYTKALMSAVP 266
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
10-273 |
9.35e-70 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 218.68 E-value: 9.35e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 10 NAPLLDVRDLC------VDFVNGSAVTHAVRGVSFQLGREK-LAIVGESGSGKSTVGRALLQLHPKkarvSASRMQFANL 82
Cdd:PRK11308 2 QQPLLQAIDLKkhypvkRGLFKPERLVKALDGVSFTLERGKtLAVVGESGCGKSTLARLLTMIETP----TGGELYYQGQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 83 DLLHLTEAQMRGVRgKRISMIMQDPKYSLNPVVCVGKQIAEAWLTHHPGRKDEAKAKALEMLEVVRIRqPERvYQLYPHE 162
Cdd:PRK11308 78 DLLKADPEAQKLLR-QKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLR-PEH-YDRYPHM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 163 ISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVV 242
Cdd:PRK11308 155 FSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCV 234
|
250 260 270
....*....|....*....|....*....|....
gi 503996112 243 ESIAACDL-DNARHPYTQGLINSLP--DMQHRRP 273
Cdd:PRK11308 235 EKGTKEQIfNNPRHPYTQALLSATPrlNPDDRRE 268
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
13-268 |
1.75e-64 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 212.79 E-value: 1.75e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 13 LLDVRDLCVDFVNGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQL-HPKKARVSASRMQFAN-----LDLL 85
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRgETLAIVGESGSGKSVTALALMRLlEQAGGLVQCDKMLLRRrsrqvIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 86 HLTEAQMRGVRGKRISMIMQDPKYSLNPVVCVGKQIAEAWLTHHPGRKDEAKAKALEMLEVVRIRQPERVYQLYPHEISG 165
Cdd:PRK10261 92 EQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 166 GQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVESI 245
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
|
250 260
....*....|....*....|....
gi 503996112 246 AACDLDNA-RHPYTQGLINSLPDM 268
Cdd:PRK10261 252 SVEQIFHApQHPYTRALLAAVPQL 275
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
12-273 |
2.42e-60 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 194.64 E-value: 2.42e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 12 PLLDVRDLCVDFVNGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPKKARVSASRMQFANLDLLHLTEA 90
Cdd:PRK15093 2 PLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEgEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDIDLLRLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 91 QMRGVRGKRISMIMQDPKYSLNPVVCVGKQIAEAWlthhPG---------RKDEAKAKALEMLEVVRIRQPERVYQLYPH 161
Cdd:PRK15093 82 ERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNI----PGwtykgrwwqRFGWRKRRAIELLHRVGIKDHKDAMRSFPY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 162 EISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRV 241
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQT 237
|
250 260 270
....*....|....*....|....*....|...
gi 503996112 242 VESIAACDLDNA-RHPYTQGLINSLPDMQHRRP 273
Cdd:PRK15093 238 VETAPSKELVTTpHHPYTQALIRAIPDFGSAMP 270
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
7-262 |
9.89e-53 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 179.90 E-value: 9.89e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 7 AANNAPLLDVRDLCVDFVNGSAV-------THAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPkkarvSASRMQ 78
Cdd:PRK15134 269 PEPASPLLDVEQLQVAFPIRKGIlkrtvdhNVVVKNISFTLRPgETLGLVGESGSGKSTTGLALLRLIN-----SQGEIW 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 79 FANLDLLHLTEAQMRGVRgKRISMIMQDPKYSLNPVVCVGKQIAEAWLTHHPG-RKDEAKAKALEMLEVVRIRQPERvyQ 157
Cdd:PRK15134 344 FDGQPLHNLNRRQLLPVR-HRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTlSAAQREQQVIAVMEEVGLDPETR--H 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 158 LYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMY 237
Cdd:PRK15134 421 RYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLR 500
|
250 260
....*....|....*....|....*.
gi 503996112 238 AGRVVESIAACDLDNA-RHPYTQGLI 262
Cdd:PRK15134 501 QGEVVEQGDCERVFAApQQEYTRQLL 526
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
12-273 |
8.83e-52 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 178.90 E-value: 8.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 12 PLLDVRDLCVDFVNGSAV-------THAVRGVSFQL-GREKLAIVGESGSGKSTVGRALLQLhpkkARVSASRMQFANLD 83
Cdd:PRK10261 312 PILQVRNLVTRFPLRSGLlnrvtreVHAVEKVSFDLwPGETLSLVGESGSGKSTTGRALLRL----VESQGGEIIFNGQR 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 84 LLHLTEAQMRGVRgKRISMIMQDPKYSLNPVVCVGKQIAEAWLTHHPGRKDEAKAKALEMLEVVRIRqPERVYQlYPHEI 163
Cdd:PRK10261 388 IDTLSPGKLQALR-RDIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLL-PEHAWR-YPHEF 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 164 SGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVE 243
Cdd:PRK10261 465 SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVE 544
|
250 260 270
....*....|....*....|....*....|...
gi 503996112 244 -SIAACDLDNARHPYTQGLINSLP--DMQHRRP 273
Cdd:PRK10261 545 iGPRRAVFENPQHPYTRKLMAAVPvaDPSRQRP 577
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
12-264 |
3.09e-51 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 169.25 E-value: 3.09e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 12 PLLDVRDLCVDFVNGSA-----VTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPKKA---RVSASRMQFANl 82
Cdd:COG4167 3 ALLEVRNLSKTFKYRTGlfrrqQFEAVKPVSFTLEAgQTLAIIGENGSGKSTLAKMLAGIIEPTSgeiLINGHKLEYGD- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 83 dllhlteaqmRGVRGKRISMIMQDPKYSLNPVVCVGkQIAEAWLTHHPGRKDEAKAKALEM-LEVVRIRqPERVYqLYPH 161
Cdd:COG4167 82 ----------YKYRCKHIRMIFQDPNTSLNPRLNIG-QILEEPLRLNTDLTAEEREERIFAtLRLVGLL-PEHAN-FYPH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 162 EISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRV 241
Cdd:COG4167 149 MLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEV 228
|
250 260
....*....|....*....|....
gi 503996112 242 VESIAACD-LDNARHPYTQGLINS 264
Cdd:COG4167 229 VEYGKTAEvFANPQHEVTKRLIES 252
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
13-274 |
4.35e-49 |
|
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: 163.44 E-value: 4.35e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 13 LLDVRDLCVDFVNGSAVTHAVR-----GVSFQLGR-EKLAIVGESGSGKSTVGRALLQLH-PKKARVSasrmqFANLDLL 85
Cdd:TIGR02769 2 LLEVRDVTHTYRTGGLFGAKQRapvltNVSLSIEEgETVGLLGRSGCGKSTLARLLLGLEkPAQGTVS-----FRGQDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 86 HLTEAQMRGVRgKRISMIMQDPKYSLNPVVCVGKQIAEAWLTHHPGRKDEAKAKALEMLEVVRIRqpERVYQLYPHEISG 165
Cdd:TIGR02769 77 QLDRKQRRAFR-RDVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLR--SEDADKLPRQLSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 166 GQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVESI 245
Cdd:TIGR02769 154 GQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEEC 233
|
250 260 270
....*....|....*....|....*....|
gi 503996112 246 AACDLDNARHPYTQGLINS-LPDMQHRRPI 274
Cdd:TIGR02769 234 DVAQLLSFKHPAGRNLQSAvLPEHPVRRSI 263
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
33-262 |
5.16e-48 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 160.64 E-value: 5.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 33 VRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPKKARVSASRMqfanldLLHLTEAQMRGVRGKRISMIMQDPKYSL 111
Cdd:PRK10418 19 VHGVSLTLQRgRVLALVGGSGSGKSLTCAAALGILPAGVRQTAGRV------LLDGKPVAPCALRGRKIATIMQNPRSAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 112 NPVVCVGKQIAEAWLTHhpGRKDEAkAKALEMLEVVRIRQPERVYQLYPHEISGGQGQRIMIAMMLITDPELIIADEPTS 191
Cdd:PRK10418 93 NPLHTMHTHARETCLAL--GKPADD-ATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503996112 192 ALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVESIAACDLDNA-RHPYTQGLI 262
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNApKHAVTRSLV 241
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
11-246 |
1.37e-47 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 158.28 E-value: 1.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 11 APLLDVRDLCVDFVNGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTvgraLLQL-----HPKKARVSasrmqFANLDL 84
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAgEFVAIVGPSGSGKST----LLNIlggldRPTSGEVL-----IDGQDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 85 LHLTEAQMRGVRGKRISMIMQDpkYSLNPVVCVGKQIAEAWLTHHPGRKdEAKAKALEMLEVVRIrqPERVYQlYPHEIS 164
Cdd:COG1136 73 SSLSERELARLRRRHIGFVFQF--FNLLPELTALENVALPLLLAGVSRK-ERRERARELLERVGL--GDRLDH-RPSQLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 165 GGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVrSFCDRVLVMYAGRVVES 244
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLRDGRIVSD 225
|
..
gi 503996112 245 IA 246
Cdd:COG1136 226 ER 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
14-241 |
4.62e-46 |
|
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: 154.18 E-value: 4.62e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 14 LDVRDLCVDFVNGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTvgraLLQLHPKKARVSASRMQFANLDLLHLTEAQM 92
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKgEFVAIVGPSGSGKST----LLNILGGLDRPTSGEVRVDGTDISKLSEKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 93 RGVRGKRISMIMQDpkYSLNPVVCVGKQIAEAwLTHHPGRKDEAKAKALEMLEVVRIrqPERVYQlYPHEISGGQGQRIM 172
Cdd:cd03255 77 AAFRRRHIGFVFQS--FNLLPDLTALENVELP-LLLAGVPKKERRERAEELLERVGL--GDRLNH-YPSELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503996112 173 IAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVrSFCDRVLVMYAGRV 241
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
8-264 |
9.75e-46 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 154.70 E-value: 9.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 8 ANNAPLLDVRDLCVDFVNGsavtHAVRGVSFQL-GREKLAIVGESGSGKSTVGRAL-LQLHPKKARVSASRMQFANLDLL 85
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPR----KGCRDVSFDLyPGEVLGIVGESGSGKTTLLNALsARLAPDAGEVHYRMRDGQLRDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 86 HLTEAQMRGVRGKRISMIMQDPKYSLNPVVCVGKQIAEAWLT---HHPGRkdeAKAKALEMLEVVRIrQPERVYQLyPHE 162
Cdd:PRK11701 77 ALSEAERRRLLRTEWGFVHQHPRDGLRMQVSAGGNIGERLMAvgaRHYGD---IRATAGDWLERVEI-DAARIDDL-PTT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 163 ISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVV 242
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
250 260
....*....|....*....|....
gi 503996112 243 ESiAACD--LDNARHPYTQGLINS 264
Cdd:PRK11701 232 ES-GLTDqvLDDPQHPYTQLLVSS 254
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
33-273 |
2.91e-43 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 148.68 E-value: 2.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 33 VRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLH-PKKARVSasrmqFANLDLLHLTEAQMRGVRGKrISMIMQDPKYS 110
Cdd:PRK10419 28 LNNVSLSLKSgETVALLGRSGCGKSTLARLLVGLEsPSQGNVS-----WRGEPLAKLNRAQRKAFRRD-IQMVFQDSISA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 111 LNPVVCVGKQIAEAwLTHHPGRKDEAK-AKALEMLEVVRIRqPERVYQLyPHEISGGQGQRIMIAMMLITDPELIIADEP 189
Cdd:PRK10419 102 VNPRKTVREIIREP-LRHLLSLDKAERlARASEMLRAVDLD-DSVLDKR-PPQLSGGQLQRVCLARALAVEPKLLILDEA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 190 TSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVESIAACDLDNARHPYTQGLINS-LPDM 268
Cdd:PRK10419 179 VSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLTFSSPAGRVLQNAvLPAF 258
|
....*
gi 503996112 269 QHRRP 273
Cdd:PRK10419 259 PVRRR 263
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
12-242 |
1.72e-41 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 143.27 E-value: 1.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 12 PLLDVRDLCVDFVNGsavTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPkkarVSASRMQFANLDLLHLTEA 90
Cdd:COG3638 1 PMLELRNLSKRYPGG---TPALDDVSLEIERgEFVALIGPSGAGKSTLLRCLNGLVE----PTSGEILVDGQDVTALRGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 91 QMRGVRGkRISMIMQDpkYSLNP---V---VCVGKqiaeawLTHHPGRK-------DEAKAKALEMLEVVRI--RQPERV 155
Cdd:COG3638 74 ALRRLRR-RIGMIFQQ--FNLVPrlsVltnVLAGR------LGRTSTWRsllglfpPEDRERALEALERVGLadKAYQRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 156 YQLypheiSGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLV 235
Cdd:COG3638 145 DQL-----SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIG 219
|
....*..
gi 503996112 236 MYAGRVV 242
Cdd:COG3638 220 LRDGRVV 226
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
16-267 |
6.15e-41 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 144.45 E-value: 6.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 16 VRDLCVDFVNGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGR--ALLQlhpkkaRVSASRMQFANLDLLHLTEAQM 92
Cdd:COG1135 4 LENLSKTFPTKGGPVTALDDVSLTIEKgEIFGIIGYSGAGKSTLIRciNLLE------RPTSGSVLVDGVDLTALSEREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 93 RGVRgKRISMIMQDpkYSL--------N---PVVCVGKqiaeawlthhpgRKDEAKAKALEMLEVV----RIRQpervyq 157
Cdd:COG1135 78 RAAR-RKIGMIFQH--FNLlssrtvaeNvalPLEIAGV------------PKAEIRKRVAELLELVglsdKADA------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 158 lYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMY 237
Cdd:COG1135 137 -YPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLE 215
|
250 260 270
....*....|....*....|....*....|.
gi 503996112 238 AGRVVESIAACDL-DNARHPYTQGLINSLPD 267
Cdd:COG1135 216 NGRIVEQGPVLDVfANPQSELTRRFLPTVLN 246
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
14-242 |
1.59e-40 |
|
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: 140.16 E-value: 1.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 14 LDVRDLCVDFVNGsavTHAVRGVSFQLGR-EKLAIVGESGSGKSTvgraLLQ-----LHPKKARVsasrmQFANLDLLHL 87
Cdd:COG1122 1 IELENLSFSYPGG---TPALDDVSLSIEKgEFVAIIGPNGSGKST----LLRllnglLKPTSGEV-----LVDGKDITKK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 88 TEAQMRgvrgKRISMIMQDPKYSLnpvVC--VGKQIAEAwLTHHPGRKDEAKAKALEMLEVVRIrqpERVYQLYPHEISG 165
Cdd:COG1122 69 NLRELR----RKVGLVFQNPDDQL---FAptVEEDVAFG-PENLGLPREEIRERVEEALELVGL---EHLADRPPHELSG 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503996112 166 GQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLvQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVV 242
Cdd:COG1122 138 GQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDDGRIV 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
16-243 |
2.14e-40 |
|
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: 140.02 E-value: 2.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 16 VRDLCVDFVNGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHpkkaRVSASRMQFANLDLLHLTEAQMRG 94
Cdd:cd03258 4 LKNVSKVFGDTGGKVTALKDVSLSVPKgEIFGIIGRSGAGKSTLIRCINGLE----RPTSGSVLVDGTDLTLLSGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 95 VRgKRISMIMQdpKYSLNPVVCVGKQIAEAwLTHHPGRKDEAKAKALEMLEVVRIRQPERVYqlyPHEISGGQGQRIMIA 174
Cdd:cd03258 80 AR-RRIGMIFQ--HFNLLSSRTVFENVALP-LEIAGVPKAEIEERVLELLELVGLEDKADAY---PAQLSGGQKQRVGIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503996112 175 MMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVE 243
Cdd:cd03258 153 RALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVE 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
16-240 |
4.78e-38 |
|
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: 133.36 E-value: 4.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 16 VRDLCVDFvnGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRAL-LQLHPKKARVsasrmQFANLDLLHLTEAQMR 93
Cdd:cd03225 2 LKNLSFSY--PDGARPALDDISLTIKKgEFVLIVGPNGSGKSTLLRLLnGLLGPTSGEV-----LVDGKDLTKLSLKELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 94 gvrgKRISMIMQDPKYSLnpvvcVGKQIAE--AW-LTHHPGRKDEAKAKALEMLEVVRIR-QPERVyqlyPHEISGGQGQ 169
Cdd:cd03225 75 ----RKVGLVFQNPDDQF-----FGPTVEEevAFgLENLGLPEEEIEERVEEALELVGLEgLRDRS----PFTLSGGQKQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503996112 170 RIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLvQSRGLGLIFISHDINLVRSFCDRVLVMYAGR 240
Cdd:cd03225 142 RVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
13-242 |
1.05e-37 |
|
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: 133.63 E-value: 1.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 13 LLDVRDLCVDFvNGSAVthaVRGVSFQLGREKL-AIVGESGSGKSTVGRALL-QLHPKKARVSasrmqFANLDLLHLTEA 90
Cdd:COG1120 1 MLEAENLSVGY-GGRPV---LDDVSLSLPPGEVtALLGPNGSGKSTLLRALAgLLKPSSGEVL-----LDGRDLASLSRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 91 QmrgvRGKRISMIMQDPK----YSLNPVVCVGKQIAEAWLtHHPGRKDEAKA-KALEMLEVVRIRqpERVYqlypHEISG 165
Cdd:COG1120 72 E----LARRIAYVPQEPPapfgLTVRELVALGRYPHLGLF-GRPSAEDREAVeEALERTGLEHLA--DRPV----DELSG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503996112 166 GQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVV 242
Cdd:COG1120 141 GERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
14-243 |
5.85e-37 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 130.72 E-value: 5.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 14 LDVRDLCVDFvnGSavTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLhpkkARVSASRMQFANLDLLHLTEAQm 92
Cdd:cd03259 1 LELKGLSKTY--GS--VRALDDLSLTVEPgEFLALLGPSGCGKTTLLRLIAGL----ERPDSGEILIDGRDVTGVPPER- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 93 rgvrgKRISMIMQDpkYSLNPVVCVGKQIAEAwLTHHPGRKDEAKAKALEMLEVVRIRQPErvyQLYPHEISGGQGQRIM 172
Cdd:cd03259 72 -----RNIGMVFQD--YALFPHLTVAENIAFG-LKLRGVPKAEIRARVRELLELVGLEGLL---NRYPHELSGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503996112 173 IAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVE 243
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
14-257 |
8.23e-37 |
|
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: 130.70 E-value: 8.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 14 LDVRDLCVDFvnGSAVTHavRGVSFQLGR-EKLAIVGESGSGKSTVGRALL-QLHPKKARVsasrmQFANLDLLHLTEAQ 91
Cdd:cd03261 1 IELRGLTKSF--GGRTVL--KGVDLDVRRgEILAIIGPSGSGKSTLLRLIVgLLRPDSGEV-----LIDGEDISGLSEAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 92 MRGVRgKRISMIMQDPKY--SLNpvvcVGKQIAEAWLTHHPGRKDEAKAKALEMLEVVRIRQPErvyQLYPHEISGGQGQ 169
Cdd:cd03261 72 LYRLR-RRMGMLFQSGALfdSLT----VFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAE---DLYPAELSGGMKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 170 RIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVESIAACD 249
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEE 223
|
....*...
gi 503996112 250 LDNARHPY 257
Cdd:cd03261 224 LRASDDPL 231
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
10-259 |
4.35e-36 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 128.94 E-value: 4.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 10 NAPLLDVRDLCVDFvnGSAVTHavRGVSFQLGR-EKLAIVGESGSGKSTVGRALL-QLHPKKARVsasrmQFANLDLLHL 87
Cdd:COG1127 2 SEPMIEVRNLTKSF--GDRVVL--DGVSLDVPRgEILAIIGGSGSGKSVLLKLIIgLLRPDSGEI-----LVDGQDITGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 88 TEAQMRGVRgKRISMIMQ-----DpkySLNpvvcVGKQIAeAWLTHHPG-RKDEAKAKALEMLEVVRIRQperVYQLYPH 161
Cdd:COG1127 73 SEKELYELR-RRIGMLFQggalfD---SLT----VFENVA-FPLREHTDlSEAEIRELVLEKLELVGLPG---AADKMPS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 162 EISGGQGQRIMIAMMLITDPELIIADEPTSALD-VSVRlQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGR 240
Cdd:COG1127 141 ELSGGMRKRVALARALALDPEILLYDEPTAGLDpITSA-VIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGK 219
|
250
....*....|....*....
gi 503996112 241 VVESIAACDLDNARHPYTQ 259
Cdd:COG1127 220 IIAEGTPEELLASDDPWVR 238
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
13-259 |
4.14e-35 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 126.26 E-value: 4.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 13 LLDVRDLCVDFvnGSavTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPkkarVSASRMQFANLDLlHLTEAQ 91
Cdd:COG1126 1 MIEIENLHKSF--GD--LEVLKGISLDVEKgEVVVIIGPSGSGKSTLLRCINLLEE----PDSGTITVDGEDL-TDSKKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 92 MRGVRgKRISMIMQDpkYSLNPVVCVGKQIAEAWLTHHPGRKDEAKAKALEMLEVVRIrqPERVYQlYPHEISGGQGQRI 171
Cdd:COG1126 72 INKLR-RKVGMVFQQ--FNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGL--ADKADA-YPAQLSGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 172 MIAMMLITDPELIIADEPTSALD---VSvrlQVLGLLDDLVQSrGLGLIFISHDINLVRSFCDRVLVMYAGRVVESIAAC 248
Cdd:COG1126 146 AIARALAMEPKVMLFDEPTSALDpelVG---EVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPE 221
|
250
....*....|..
gi 503996112 249 DL-DNARHPYTQ 259
Cdd:COG1126 222 EFfENPQHERTR 233
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
13-264 |
7.40e-35 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 126.83 E-value: 7.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 13 LLDVRDLCVDFVNGSAVTH-----AVRGVSFQLG-REKLAIVGESGSGKSTVGRALL-QLHPKKARVSASRMQFANLDLl 85
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGWFRrqtveAVKPLSFTLReGQTLAIIGENGSGKSTLAKMLAgMIEPTSGELLIDDHPLHFGDY- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 86 hlteaqmrGVRGKRISMIMQDPKYSLNPVVCVGkQIAEAWLTHHPGRKDEAKAKAL-EMLEVVRIRqPERVYqLYPHEIS 164
Cdd:PRK15112 83 --------SYRSQRIRMIFQDPSTSLNPRQRIS-QILDFPLRLNTDLEPEQREKQIiETLRQVGLL-PDHAS-YYPHMLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 165 GGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVES 244
Cdd:PRK15112 152 PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVER 231
|
250 260
....*....|....*....|.
gi 503996112 245 IAACD-LDNARHPYTQGLINS 264
Cdd:PRK15112 232 GSTADvLASPLHELTKRLIAG 252
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
14-245 |
9.36e-35 |
|
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: 124.89 E-value: 9.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 14 LDVRDLCVDFVNGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHpkkaRVSASRMQFANldllhlteAQM 92
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEgEFVALVGPSGCGKSTLLRIIAGLE----RPTSGEVLVDG--------EPV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 93 RGVrGKRISMIMQDpkYSLNPVVCVGKQIAEAwLTHHPGRKDEAKAKALEMLEVVRIRQPERvyqLYPHEISGGQGQRIM 172
Cdd:cd03293 69 TGP-GPDRGYVFQQ--DALLPWLTVLDNVALG-LELQGVPKAEARERAEELLELVGLSGFEN---AYPHQLSGGMRQRVA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503996112 173 IAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYA--GRVVESI 245
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAEV 216
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
14-254 |
1.28e-34 |
|
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: 125.37 E-value: 1.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 14 LDVRDLCVDFVNGsavTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHpkkaRVSASRMQFANLDLLHLTEAQM 92
Cdd:cd03256 1 IEVENLSKTYPNG---KKALKDVSLSINPgEFVALIGPSGAGKSTLLRCLNGLV----EPTSGSVLIDGTDINKLKGKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 93 RGVRgKRISMIMQDpkYSLNPVVCVGKQIAEAWLTHHP------GR-KDEAKAKALEMLEVVRIRqpERVYQlYPHEISG 165
Cdd:cd03256 74 RQLR-RQIGMIFQQ--FNLIERLSVLENVLSGRLGRRStwrslfGLfPKEEKQRALAALERVGLL--DKAYQ-RADQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 166 GQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVESI 245
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDG 227
|
....*....
gi 503996112 246 AACDLDNAR 254
Cdd:cd03256 228 PPAELTDEV 236
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
30-242 |
2.35e-34 |
|
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 downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 125.64 E-value: 2.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 30 THAVRGVSFQLGR-EKLAIVGESGSGKSTvgraLLQ-----LHPKKARVsasrmQFANLDLLHLTEAQMRGVRgKRISMI 103
Cdd:TIGR04521 18 KKALDDVSLTIEDgEFVAIIGHTGSGKST----LIQhlnglLKPTSGTV-----TIDGRDITAKKKKKLKDLR-KKVGLV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 104 MQDPKYSL---NpvvcVGKQIAEAwlthhPGR----KDEAKAKALEMLEVVRIrqPERVYQLYPHEISGGQGQRIMIAMM 176
Cdd:TIGR04521 88 FQFPEHQLfeeT----VYKDIAFG-----PKNlglsEEEAEERVKEALELVGL--DEEYLERSPFELSGGQMRRVAIAGV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503996112 177 LITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVV 242
Cdd:TIGR04521 157 LAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIV 222
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
13-257 |
1.25e-32 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 120.10 E-value: 1.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 13 LLDVRDLCVDFVNGsavTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHpkkaRVSASRMQFANLDLLHLTEAQ 91
Cdd:TIGR02315 1 MLEVENLSKVYPNG---KQALKNINLNINPgEFVAIIGPSGAGKSTLLRCINRLV----EPSSGSILLEGTDITKLRGKK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 92 MRGVRgKRISMIMQDpkYSLNPVVCVGKQIAEAWLTHHPGRK-------DEAKAKALEMLEVVRIRQP--ERVYQLyphe 162
Cdd:TIGR02315 74 LRKLR-RRIGMIFQH--YNLIERLTVLENVLHGRLGYKPTWRsllgrfsEEDKERALSALERVGLADKayQRADQL---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 163 iSGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVV 242
Cdd:TIGR02315 147 -SGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIV 225
|
250
....*....|....*..
gi 503996112 243 ESIAACDLDNA--RHPY 257
Cdd:TIGR02315 226 FDGAPSELDDEvlRHIY 242
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
31-241 |
1.91e-32 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 118.79 E-value: 1.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 31 HAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHpkkaRVSASRMQFANLDLLHlTEAQMRGVRgKRISMIMQDpkY 109
Cdd:cd03262 14 HVLKGIDLTVKKgEVVVIIGPSGSGKSTLLRCINLLE----EPDSGTIIIDGLKLTD-DKKNINELR-QKVGMVFQQ--F 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 110 SLNPVVCVGKQIAEAWLTHHPGRKDEAKAKALEMLEVVRIrqPERVYQlYPHEISGGQGQRIMIAMMLITDPELIIADEP 189
Cdd:cd03262 86 NLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGL--ADKADA-YPAQLSGGQQQRVAIARALAMNPKVMLFDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503996112 190 TSALDVSVRLQVLGLLDDLVQSrGLGLIFISHDINLVRSFCDRVLVMYAGRV 241
Cdd:cd03262 163 TSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
8-245 |
1.97e-32 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 120.19 E-value: 1.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 8 ANNAPLLDVRDLCVDFVNGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQL-HPKKARVSasrmqfanLDLL 85
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAgEFVALVGPSGCGKSTLLRLIAGLeKPTSGEVL--------VDGK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 86 HLTEAqmrgvrGKRISMIMQDPkySLNPvvcvgkqiaeaWLT----------HHPGRKDEAKAKALEMLEVVRIRQPErv 155
Cdd:COG1116 74 PVTGP------GPDRGVVFQEP--ALLP-----------WLTvldnvalgleLRGVPKAERRERARELLELVGLAGFE-- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 156 yQLYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDIN----LvrsfCD 231
Cdd:COG1116 133 -DAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDeavfL----AD 207
|
250
....*....|....*.
gi 503996112 232 RVLVMYA--GRVVESI 245
Cdd:COG1116 208 RVVVLSArpGRIVEEI 223
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
15-242 |
2.32e-32 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 117.54 E-value: 2.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 15 DVRDLCVDFVNgsavTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLH-PKKARVSasrmqFANLDLLHLTEAQm 92
Cdd:cd03214 1 EVENLSVGYGG----RTVLDDLSLSIEAgEIVGILGPNGAGKSTLLKTLAGLLkPSSGEIL-----LDGKDLASLSPKE- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 93 rgvRGKRISMIMQdpkyslnpvvcvgkqiaeawlthhpgrkdeakakALEMLEVVRIRqpERVYqlypHEISGGQGQRIM 172
Cdd:cd03214 71 ---LARKIAYVPQ----------------------------------ALELLGLAHLA--DRPF----NELSGGERQRVL 107
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 173 IAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVV 242
Cdd:cd03214 108 LARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
12-240 |
2.81e-32 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 118.69 E-value: 2.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 12 PLLDVRDLCVDFVN---GSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLqlhpKKARVSASRM----QFANLD 83
Cdd:COG4778 3 TLLEVENLSKTFTLhlqGGKRLPVLDGVSFSVAAgECVALTGPSGAGKSTLLKCIY----GNYLPDSGSIlvrhDGGWVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 84 LLHLTEAQMRGVRGKRISMIMQ----DPKYSLNPVVcvgkqiAEAwLTHHPGRKDEAKAKALEMLEvvRIRQPERVYQLY 159
Cdd:COG4778 79 LAQASPREILALRRRTIGYVSQflrvIPRVSALDVV------AEP-LLERGVDREEARARARELLA--RLNLPERLWDLP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 160 PHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLvQSRGLGLIFISHDINLVRSFCDRVLVMYAG 239
Cdd:COG4778 150 PATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
.
gi 503996112 240 R 240
Cdd:COG4778 229 S 229
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
7-247 |
5.39e-32 |
|
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: 118.31 E-value: 5.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 7 AANNAPLLDVRDLCVDFVNGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTvgraLLQLHPKKARVSASRMQFANLDLL 85
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTGAGELTILKGISLEVEAgESVAIVGASGSGKST----LLGLLAGLDRPTSGTVRLAGQDLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 86 HLTEAQMRGVRGKRISMIMQD----PkySLNPV--VCVGKQIAeawlthhpGRKDeAKAKALEMLEVV----RIRQperv 155
Cdd:COG4181 78 ALDEDARARLRARHVGFVFQSfqllP--TLTALenVMLPLELA--------GRRD-ARARARALLERVglghRLDH---- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 156 yqlYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSfCDRVLV 235
Cdd:COG4181 143 ---YPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLR 218
|
250
....*....|..
gi 503996112 236 MYAGRVVESIAA 247
Cdd:COG4181 219 LRAGRLVEDTAA 230
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
14-244 |
7.97e-30 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 112.46 E-value: 7.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 14 LDVRDLCVDFvnGSavTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLhpkkARVSASRMQFANLDLLHLTEAqm 92
Cdd:COG1131 1 IEVRGLTKRY--GD--KTALDGVSLTVEPgEIFGLLGPNGAGKTTTIRMLLGL----LRPTSGEVRVLGEDVARDPAE-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 93 rgVRgKRISMIMQDPkySLNPVVCVgKQIAEAWLTHHPGRKDEAKAKALEMLEVVRI--RQPERVYQLypheiSGGQGQR 170
Cdd:COG1131 71 --VR-RRIGYVPQEP--ALYPDLTV-RENLRFFARLYGLPRKEARERIDELLELFGLtdAADRKVGTL-----SGGMKQR 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503996112 171 IMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQsRGLGLIFISHDINLVRSFCDRVLVMYAGRVVES 244
Cdd:COG1131 140 LGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAERLCDRVAIIDKGRIVAD 212
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
10-242 |
1.84e-29 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 114.42 E-value: 1.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 10 NAPLLDVRDLCVDFvnGSavTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPkkarVSASRMQFANLDLLHLt 88
Cdd:COG3842 2 AMPALELENVSKRY--GD--VTALDDVSLSIEPgEFVALLGPSGCGKTTLLRMIAGFET----PDSGRILLDGRDVTGL- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 89 EAQMRGvrgkrISMIMQDpkYSLNPVVCVGKQIAEAwLTHHPGRKDEAKAKALEMLEVVRIrqpERVYQLYPHEISGGQG 168
Cdd:COG3842 73 PPEKRN-----VGMVFQD--YALFPHLTVAENVAFG-LRMRGVPKAEIRARVAELLELVGL---EGLADRYPHQLSGGQQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503996112 169 QRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDinlvR----SFCDRVLVMYAGRVV 242
Cdd:COG3842 142 QRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHD----QeealALADRIAVMNDGRIE 215
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
9-242 |
5.02e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 110.56 E-value: 5.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 9 NNAPLLDVRDLCVDFVNgsavTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPkkarVSASRMQFANLDLlhl 87
Cdd:COG1121 2 MMMPAIELENLTVSYGG----RPVLEDVSLTIPPgEFVAIVGPNGAGKSTLLKAILGLLP----PTSGTVRLFGKPP--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 88 teaqmrGVRGKRISMIMQdpKYSLNP--------VVCVGKQIAEAWLtHHPGRKDeaKAKALEMLEVVRIRQPE--RVYQ 157
Cdd:COG1121 71 ------RRARRRIGYVPQ--RAEVDWdfpitvrdVVLMGRYGRRGLF-RRPSRAD--REAVDEALERVGLEDLAdrPIGE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 158 LypheiSGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQsRGLGLIFISHDINLVRSFCDRVLVMy 237
Cdd:COG1121 140 L-----SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDLGAVREYFDRVLLL- 212
|
....*
gi 503996112 238 AGRVV 242
Cdd:COG1121 213 NRGLV 217
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
16-242 |
5.21e-29 |
|
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: 109.93 E-value: 5.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 16 VRDLCVDFVNgsavTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALL-QLHPKKARVSasrmqfanLDLLHLTEAQmr 93
Cdd:cd03235 2 VEDLTVSYGG----HPVLEDVSFEVKPgEFLAIVGPNGAGKSTLLKAILgLLKPTSGSIR--------VFGKPLEKER-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 94 gvrgKRISMIMQdpKYSLNP--------VVCVGKQiAEAWLTHHPGRKDeaKAKALEMLEVVRIRQPERvYQLypHEISG 165
Cdd:cd03235 68 ----KRIGYVPQ--RRSIDRdfpisvrdVVLMGLY-GHKGLFRRLSKAD--KAKVDEALERVGLSELAD-RQI--GELSG 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503996112 166 GQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLvQSRGLGLIFISHDINLVRSFCDRVLVMyAGRVV 242
Cdd:cd03235 136 GQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVLLL-NRTVV 210
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
32-247 |
6.75e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 109.76 E-value: 6.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 32 AVRGVSFQLGR-EKLAIVGESGSGKSTvgraLLQLHPKKARVSASRMQFANLDLLHLTEAQMRGVRgKRISMIMQDPK-- 108
Cdd:COG2884 17 ALSDVSLEIEKgEFVFLTGPSGAGKST----LLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLR-RRIGVVFQDFRll 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 109 YSLN-------PVVCVGKqiaeawlthhpgRKDEAKAKALEMLEVVRIRQPERVYqlyPHEISGGQGQRIMIAMMLITDP 181
Cdd:COG2884 92 PDRTvyenvalPLRVTGK------------SRKEIRRRVREVLDLVGLSDKAKAL---PHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503996112 182 ELIIADEPTSALDVSVRLQVLGLLDDLVQsRGLGLIFISHDINLVRSFCDRVLVMYAGRVVESIAA 247
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEAR 221
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
14-241 |
2.19e-28 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 107.98 E-value: 2.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 14 LDVRDLCVDFVNgsavTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPkkarVSASRMQFANLDLLHLTEAQM 92
Cdd:COG4619 1 LELEGLSFRVGG----KPILSPVSLTLEAgECVAITGPSGSGKSTLLRALADLDP----PTSGEIYLDGKPLSAMPPPEW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 93 RgvrgKRISMIMQDPKYSLNPVvcvGKQIAEAWLTHHPGRKDEAKAKALEMLEVvrirqPERVYQLYPHEISGGQGQRIM 172
Cdd:COG4619 73 R----RQVAYVPQEPALWGGTV---RDNLPFPFQLRERKFDRERALELLERLGL-----PPDILDKPVERLSGGERQRLA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503996112 173 IAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRV 241
Cdd:COG4619 141 LIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
12-243 |
3.55e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 109.33 E-value: 3.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 12 PLLDVRDLcvDFVNGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQL-HPKKARVSASRMQfanldllhLTE 89
Cdd:PRK13635 4 EIIRVEHI--SFRYPDAATYALKDVSFSVYEgEWVAIVGHNGSGKSTLAKLLNGLlLPEAGTITVGGMV--------LSE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 90 AQMRGVRgKRISMIMQDPKyslNPVV--CVGKQIAEAwLTHHPGRKDEAKAKALEMLEVVRIrqpERVYQLYPHEISGGQ 167
Cdd:PRK13635 74 ETVWDVR-RQVGMVFQNPD---NQFVgaTVQDDVAFG-LENIGVPREEMVERVDQALRQVGM---EDFLNREPHRLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503996112 168 GQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVrSFCDRVLVMYAGRVVE 243
Cdd:PRK13635 146 KQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILE 220
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
32-243 |
4.17e-28 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 108.88 E-value: 4.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 32 AVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPKkarvSASRMQFANLDLLHLTEAQMRGVRGKRISMIMQdpKYS 110
Cdd:cd03294 39 GVNDVSLDVREgEIFVIMGLSGSGKSTLLRCINRLIEP----TSGKVLIDGQDIAAMSRKELRELRRKKISMVFQ--SFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 111 LNPVVCVGKQIAEAWLTHHPGRKdEAKAKALEMLEVVRIRQPErvyQLYPHEISGGQGQRIMIAMMLITDPELIIADEPT 190
Cdd:cd03294 113 LLPHRTVLENVAFGLEVQGVPRA-EREERAAEALELVGLEGWE---HKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503996112 191 SALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVE 243
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQ 241
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
16-240 |
4.81e-28 |
|
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: 105.40 E-value: 4.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 16 VRDLCVDFVNGsavtHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHpkkaRVSASRMQFANLDLLHLTEAQMRg 94
Cdd:cd00267 2 IENLSFRYGGR----TALDNVSLTLKAgEIVALVGPNGSGKSTLLRAIAGLL----KPTSGEILIDGKDIAKLPLEELR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 95 vrgKRISMIMQdpkyslnpvvcvgkqiaeawlthhpgrkdeakakalemlevvrirqpervyqlypheISGGQGQRIMIA 174
Cdd:cd00267 73 ---RRIGYVPQ---------------------------------------------------------LSGGQRQRVALA 92
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503996112 175 MMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQsRGLGLIFISHDINLVRSFCDRVLVMYAGR 240
Cdd:cd00267 93 RALLLNPDLLLLDEPTSGLDPASRERLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
14-241 |
7.58e-28 |
|
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: 105.56 E-value: 7.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 14 LDVRDLCVDFvngsAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPKkarvSASRMQFANLDLLHLTEAQM 92
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKgEIYGLLGPNGAGKTTLIKIILGLLKP----DSGEIKVLGKDIKKEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 93 RgvrgkRISMIMQDPkySLNPvvcvgkqiaeaWLThhpgrkdeakakALEMLEVvrirqpervyqlypheiSGGQGQRIM 172
Cdd:cd03230 73 R-----RIGYLPEEP--SLYE-----------NLT------------VRENLKL-----------------SGGMKQRLA 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503996112 173 IAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQsRGLGLIFISHDINLVRSFCDRVLVMYAGRV 241
Cdd:cd03230 106 LAQALLHDPELLILDEPTSGLDPESRREFWELLRELKK-EGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
14-243 |
8.44e-28 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 109.85 E-value: 8.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 14 LDVRDLCVDFvnGSavTHAVRGVSFQL-GREKLAIVGESGSGKSTvgraLLQL-----HPKKARVSasrmqFANLDLL-H 86
Cdd:COG1118 3 IEVRNISKRF--GS--FTLLDDVSLEIaSGELVALLGPSGSGKTT----LLRIiagleTPDSGRIV-----LNGRDLFtN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 87 LTeaqmrgVRGKRISMIMQDpkYSLNPVVCVGKQIAEAwLTHHPGRKDEAKAKALEMLEVVRIRQPERVYqlyPHEISGG 166
Cdd:COG1118 70 LP------PRERRVGFVFQH--YALFPHMTVAENIAFG-LRVRPPSKAEIRARVEELLELVQLEGLADRY---PSQLSGG 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503996112 167 QGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVE 243
Cdd:COG1118 138 QRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQ 214
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
23-264 |
1.45e-27 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 109.12 E-value: 1.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 23 FVNGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHpkkaRVSASRMQFANLDLLHLTEAQMRGVRgKRIS 101
Cdd:PRK11153 11 FPQGGRTIHALNNVSLHIPAgEIFGVIGASGAGKSTLIRCINLLE----RPTSGRVLVDGQDLTALSEKELRKAR-RQIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 102 MIMQdpKYSLNPVVCVGKQIAEAwLTHHPGRKDEAKAKALEMLEVVRIRQPERVYqlyPHEISGGQGQRIMIAMMLITDP 181
Cdd:PRK11153 86 MIFQ--HFNLLSSRTVFDNVALP-LELAGTPKAEIKARVTELLELVGLSDKADRY---PAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 182 ELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVESIAACDL-DNARHPYTQG 260
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVfSHPKHPLTRE 239
|
....
gi 503996112 261 LINS 264
Cdd:PRK11153 240 FIQS 243
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
36-242 |
1.52e-27 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 105.84 E-value: 1.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 36 VSFQLGREKLAIVGESGSGKSTVGRALLQLHpkkaRVSASRMQFaNLDLLHLTEAQMR-GVRGKRISMIMQDpkYSLNPV 114
Cdd:cd03297 17 IDFDLNEEVTGIFGASGAGKSTLLRCIAGLE----KPDGGTIVL-NGTVLFDSRKKINlPPQQRKIGLVFQQ--YALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 115 VCVGKQIAEAWLTHHPGrkdEAKAKALEMLEVVRIRQperVYQLYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALD 194
Cdd:cd03297 90 LNVRENLAFGLKRKRNR---EDRISVDELLDLLGLDH---LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503996112 195 VSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVV 242
Cdd:cd03297 164 RALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
9-241 |
2.11e-27 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 106.05 E-value: 2.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 9 NNAPLLDVRDLCVDFVNGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTvgraLLQLHPKKARVSASRMQFANLDLLHL 87
Cdd:PRK11629 1 MNKILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEgEMMAIVGSSGSGKST----LLHLLGGLDTPTSGDVIFNGQPMSKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 88 TEAQMRGVRGKRISMIMQdpKYSLNPVVCVGKQIAEAWLTHHPGRKdEAKAKALEMLEVVRIrqpERVYQLYPHEISGGQ 167
Cdd:PRK11629 77 SSAAKAELRNQKLGFIYQ--FHHLLPDFTALENVAMPLLIGKKKPA-EINSRALEMLAAVGL---EHRANHRPSELSGGE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503996112 168 GQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFcDRVLVMYAGRV 241
Cdd:PRK11629 151 RQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRL 223
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
14-240 |
2.61e-27 |
|
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: 104.19 E-value: 2.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 14 LDVRDLCVDFvngsAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLhpkkarVSASRMQFANLDLLHLTEAQM 92
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAgEIVALLGPSGSGKSTLLRCIAGL------EEPDSGSILIDGEDLTDLEDE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 93 RGVRGKRISMIMQDpkYSLNPVVCVGKQIAEAwlthhpgrkdeakakalemlevvrirqpervyqlypheISGGQGQRIM 172
Cdd:cd03229 71 LPPLRRRIGMVFQD--FALFPHLTVLENIALG--------------------------------------LSGGQQQRVA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503996112 173 IAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGR 240
Cdd:cd03229 111 LARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
33-191 |
2.93e-27 |
|
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: 103.50 E-value: 2.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 33 VRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPKkarvSASRMQFANLDLLHLTEAQMRgvrgKRISMIMQDPkySL 111
Cdd:pfam00005 1 LKNVSLTLNPgEILALVGPNGAGKSTLLKLIAGLLSP----TEGTILLDGQDLTDDERKSLR----KEIGYVFQDP--QL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 112 NPVVCVGKQIAEAWLTHHPGrKDEAKAKALEMLEVVRIR-QPERVYQLYPHEISGGQGQRIMIAMMLITDPELIIADEPT 190
Cdd:pfam00005 71 FPRLTVRENLRLGLLLKGLS-KREKDARAEEALEKLGLGdLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
.
gi 503996112 191 S 191
Cdd:pfam00005 150 A 150
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
8-244 |
4.57e-27 |
|
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: 109.85 E-value: 4.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 8 ANNAPLLDVRDLCVDFVNGSAVTHavrGVSFQL-GREKLAIVGESGSGKSTVGRALLQLHPkkarVSASRMQFANLDLLH 86
Cdd:COG4988 331 AAGPPSIELEDVSFSYPGGRPALD---GLSLTIpPGERVALVGPSGAGKSTLLNLLLGFLP----PYSGSILINGVDLSD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 87 LTEAQMRgvrgKRISMIMQDPkyslnpvVCVGKQIAEAWLTHHPGRKDEAKAKALE---MLEVVRiRQP--------ERV 155
Cdd:COG4988 404 LDPASWR----RQIAWVPQNP-------YLFAGTIRENLRLGRPDASDEELEAALEaagLDEFVA-ALPdgldtplgEGG 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 156 YQLypheiSGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLvqSRGLGLIFISHDINLVRsFCDRVLV 235
Cdd:COG4988 472 RGL-----SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL--AKGRTVILITHRLALLA-QADRILV 543
|
....*....
gi 503996112 236 MYAGRVVES 244
Cdd:COG4988 544 LDDGRIVEQ 552
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
14-242 |
1.19e-26 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 104.06 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 14 LDVRDLCVDFvnGSavTHAVRGVSFQLGR-EKLAIVGESGSGKSTvgraLLQLHPKKARVSASRMQFANLDLLHLTEAQm 92
Cdd:cd03219 1 LEVRGLTKRF--GG--LVALDDVSFSVRPgEIHGLIGPNGAGKTT----LFNLISGFLRPTSGSVLFDGEDITGLPPHE- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 93 RGVRGkrISMIMQD----PKYSLNPVVCVGKQIAE---AWLTHHPGRKDEAKAKALEMLEVVRIrqpERVYQLYPHEISG 165
Cdd:cd03219 72 IARLG--IGRTFQIprlfPELTVLENVMVAAQARTgsgLLLARARREEREARERAEELLERVGL---ADLADRPAGELSY 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503996112 166 GQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQsRGLGLIFISHDINLVRSFCDRVLVMYAGRVV 242
Cdd:cd03219 147 GQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
14-243 |
1.24e-26 |
|
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: 103.95 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 14 LDVRDLCVDFVNGSavthaVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLH-PKKARVSASRMQFANLdllhltEAQ 91
Cdd:cd03299 1 LKVENLSKDWKEFK-----LKNVSLEVERgDYFVILGPTGSGKSVLLETIAGFIkPDSGKILLNGKDITNL------PPE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 92 MRGvrgkrISMIMQDpkYSLNPVVCVGKQIAEAwLTHHPGRKDEAKAKALEMLEVVRIRQperVYQLYPHEISGGQGQRI 171
Cdd:cd03299 70 KRD-----ISYVPQN--YALFPHMTVYKNIAYG-LKKRKVDKKEIERKVLEIAEMLGIDH---LLNRKPETLSGGEQQRV 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503996112 172 MIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVE 243
Cdd:cd03299 139 AIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQ 210
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
30-243 |
3.72e-26 |
|
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: 102.70 E-value: 3.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 30 THAVRGVSFQLGR-EKLAIVGESGSGKSTvgraLLQLHPKKARVSASRMQFANLDLLHLTEAQmrgvrgKRISMIMQdpK 108
Cdd:cd03300 13 FVALDGVSLDIKEgEFFTLLGPSGCGKTT----LLRLIAGFETPTSGEILLDGKDITNLPPHK------RPVNTVFQ--N 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 109 YSLNPVVCVGKQIAEAwLTHHPGRKDEAKAKALEMLEVVRIRQPERvyqLYPHEISGGQGQRIMIAMMLITDPELIIADE 188
Cdd:cd03300 81 YALFPHLTVFENIAFG-LRLKKLPKAEIKERVAEALDLVQLEGYAN---RKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503996112 189 PTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVE 243
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQ 211
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
32-244 |
3.85e-26 |
|
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: 107.61 E-value: 3.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 32 AVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPkkarVSASRMQFANLDLLHLTEAQMRgvrgKRISMIMQDPK-Y 109
Cdd:COG2274 490 VLDNISLTIKPgERVAIVGRSGSGKSTLLKLLLGLYE----PTSGRILIDGIDLRQIDPASLR----RQIGVVLQDVFlF 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 110 SLNpvvcvgkqIAEAWLTHHPGRKDEAKAKALEM---LEVVRiRQPERvYQLYPHE----ISGGQGQRIMIAMMLITDPE 182
Cdd:COG2274 562 SGT--------IRENITLGDPDATDEEIIEAARLaglHDFIE-ALPMG-YDTVVGEggsnLSGGQRQRLAIARALLRNPR 631
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503996112 183 LIIADEPTSALDVSVRLQVLGLLDDLVQSRglGLIFISHDINLVRSfCDRVLVMYAGRVVES 244
Cdd:COG2274 632 ILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAHRLSTIRL-ADRIIVLDKGRIVED 690
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-242 |
4.68e-26 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 100.58 E-value: 4.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 14 LDVRDLCVDFvngsAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPKkarvsasrmqfanldllhlTEAQM 92
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRgEVHALLGENGAGKSTLMKILSGLYKP-------------------DSGEI 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 93 RgVRGKRISMimqdpkysLNPvvcvgkqiaeawlthhpgrkDEAKAKALEMlevvrirqperVYQLypheiSGGQGQRIM 172
Cdd:cd03216 58 L-VDGKEVSF--------ASP--------------------RDARRAGIAM-----------VYQL-----SVGERQMVE 92
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 173 IAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLvQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVV 242
Cdd:cd03216 93 IARALARNARLLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
32-244 |
1.81e-25 |
|
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: 101.74 E-value: 1.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 32 AVRGVSFQLGR-EKLAIVGESGSGKSTVGR---ALLQlhPKKARVSASrmqfanlDLLHLTEAQMRGVRgKRISMIMQDP 107
Cdd:TIGR04520 17 ALKNVSLSIEKgEFVAIIGHNGSGKSTLAKllnGLLL--PTSGKVTVD-------GLDTLDEENLWEIR-KKVGMVFQNP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 108 KyslNPVVC--VGKQIA-----------EAWLthhpgRKDEAkAKALEMLEvvrIRQPErvyqlyPHEISGGQGQRIMIA 174
Cdd:TIGR04520 87 D---NQFVGatVEDDVAfglenlgvpreEMRK-----RVDEA-LKLVGMED---FRDRE------PHLLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 175 MMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVrSFCDRVLVMYAGRVVES 244
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAE 217
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
43-250 |
8.08e-25 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 99.06 E-value: 8.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 43 EKLAIVGESGSGKSTvgraLLQL-----HPKKARVSasrmqFANLDLLHLTEAQmRGVrgkriSMIMQDpkYSLNPVVCV 117
Cdd:COG3840 26 ERVAILGPSGAGKST----LLNLiagflPPDSGRIL-----WNGQDLTALPPAE-RPV-----SMLFQE--NNLFPHLTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 118 GKQIAeawLTHHPGRK--DEAKAKALEMLEVVRIrqpERVYQLYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDV 195
Cdd:COG3840 89 AQNIG---LGLRPGLKltAEQRAQVEQALERVGL---AGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503996112 196 SVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVESIAACDL 250
Cdd:COG3840 163 ALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
15-242 |
2.67e-24 |
|
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: 96.94 E-value: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 15 DVRDLCVDFVNGSAVthaVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQL-HPKKARVSASRMQFAnldllhlteaqm 92
Cdd:cd03226 1 RIENISFSYKKGTEI---LDDLSLDLYAgEIIALTGKNGAGKTTLAKILAGLiKESSGSILLNGKPIK------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 93 RGVRGKRISMIMQDPKYSLnpvvcvGKQIAEAWLTHHPGRKDEAKAKALEMLEVVRIRQPErvyQLYPHEISGGQGQRIM 172
Cdd:cd03226 66 AKERRKSIGYVMQDVDYQL------FTDSVREELLLGLKELDAGNEQAETVLKDLDLYALK---ERHPLSLSGGQKQRLA 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 173 IAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLvQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVV 242
Cdd:cd03226 137 IAAALLSGKDLLIFDEPTSGLDYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
21-240 |
3.05e-24 |
|
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: 95.91 E-value: 3.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 21 VDFVNGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPkkarVSASRMQFANLDLLHLTEAQMRgvrgKR 99
Cdd:cd03228 6 VSFSYPGRPKPVLKDVSLTIKPgEKVAIVGPSGSGKSTLLKLLLRLYD----PTSGEILIDGVDLRDLDLESLR----KN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 100 ISMIMQDPkyslnpvvcvgkqiaeawlthhpgrkdeakakalemlevvrirqpervyQLYPHEI-----SGGQGQRIMIA 174
Cdd:cd03228 78 IAYVPQDP-------------------------------------------------FLFSGTIrenilSGGQRQRIAIA 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503996112 175 MMLITDPELIIADEPTSALDVSVRLQVLGLLDDLvqSRGLGLIFISHDINLVRsFCDRVLVMYAGR 240
Cdd:cd03228 109 RALLRDPPILILDEATSALDPETEALILEALRAL--AKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
32-243 |
3.33e-24 |
|
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: 97.76 E-value: 3.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 32 AVRGVSFQL-GREKLAIVGESGSGKSTVGRALLQL-HPKKARVsasrmQFANLDLLHLTEAQMRgvrgKRISMIMQdpKY 109
Cdd:cd03295 16 AVNNLNLEIaKGEFLVLIGPSGSGKTTTMKMINRLiEPTSGEI-----FIDGEDIREQDPVELR----RKIGYVIQ--QI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 110 SLNPVVCVGKQIA-----EAWLthhpgrKDEAKAKALEMLEVVRIrQPERVYQLYPHEISGGQGQRIMIAMMLITDPELI 184
Cdd:cd03295 85 GLFPHMTVEENIAlvpklLKWP------KEKIRERADELLALVGL-DPAEFADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503996112 185 IADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVE 243
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQ 216
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
43-243 |
3.91e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 97.78 E-value: 3.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 43 EKLAIVGESGSGKSTVGRALLQLH-PKKARVSASRMQFanlDLLHLT-EAQMRGVRgKRISMIMQdpKYSLNPVVCVGKQ 120
Cdd:PRK11124 29 ETLVLLGPSGAGKSSLLRVLNLLEmPRSGTLNIAGNHF---DFSKTPsDKAIRELR-RNVGMVFQ--QYNLWPHLTVQQN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 121 IAEAwlthhPGR-----KDEAKAKALEMLEVVRIRQ-PERvyqlYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALD 194
Cdd:PRK11124 103 LIEA-----PCRvlglsKDQALARAEKLLERLRLKPyADR----FPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503996112 195 VSVRLQVLGLLDDLVQSrGLGLIFISHDINLVRSFCDRVLVMYAGRVVE 243
Cdd:PRK11124 174 PEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVE 221
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
46-244 |
1.57e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 97.01 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 46 AIVGESGSGKSTvgraLLQ-----LHPKKARVSASRMQFANldllHLTEAQMRGVRgKRISMIMQDPKYSLNPVVcVGKQ 120
Cdd:PRK13634 37 AIIGHTGSGKST----LLQhlnglLQPTSGTVTIGERVITA----GKKNKKLKPLR-KKVGIVFQFPEHQLFEET-VEKD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 121 IAEAwlthhPG----RKDEAKAKALEMLEVVRIrqPERVYQLYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVS 196
Cdd:PRK13634 107 ICFG-----PMnfgvSEEDAKQKAREMIELVGL--PEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503996112 197 VRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVES 244
Cdd:PRK13634 180 GRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQ 227
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
32-243 |
2.55e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 96.39 E-value: 2.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 32 AVRGVSFQLGREKL-AIVGESGSGKSTvgraLLQLHPKKARVSASRMQFANLDLLHLT-EAQMRGVRgKRISMIMQDPKY 109
Cdd:PRK13646 22 AIHDVNTEFEQGKYyAIVGQTGSGKST----LIQNINALLKPTTGTVTVDDITITHKTkDKYIRPVR-KRIGMVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 110 SLNPVVcVGKQIAEawlthhpGRK------DEAKAKALEMLevVRIRQPERVYQLYPHEISGGQGQRIMIAMMLITDPEL 183
Cdd:PRK13646 97 QLFEDT-VEREIIF-------GPKnfkmnlDEVKNYAHRLL--MDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 184 IIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVE 243
Cdd:PRK13646 167 IVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVS 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-254 |
1.14e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.01 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 10 NAPLLDVRDLCVDFvngSAVtHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPKKA---RVSASRMQFANLdll 85
Cdd:COG1129 1 AEPLLEMRGISKSF---GGV-KALDGVSLELRPgEVHALLGENGAGKSTLMKILSGVYQPDSgeiLLDGEPVRFRSP--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 86 hlTEAQMRGvrgkrISMIMQDpkysLNPV--------VCVGKQIAEAWLTHHPGRKDEAKAkALEMLEV-VRIRQPERvy 156
Cdd:COG1129 74 --RDAQAAG-----IAIIHQE----LNLVpnlsvaenIFLGREPRRGGLIDWRAMRRRARE-LLARLGLdIDPDTPVG-- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 157 qlyphEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLvQSRGLGLIFISHDINLVRSFCDRVLVM 236
Cdd:COG1129 140 -----DLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVL 213
|
250
....*....|....*...
gi 503996112 237 YAGRVVESIAACDLDNAR 254
Cdd:COG1129 214 RDGRLVGTGPVAELTEDE 231
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
6-244 |
1.15e-22 |
|
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: 97.14 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 6 PAANNAPLLDVRDLCVDFVNGSAvtHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPkkarVSASRMQFANLDL 84
Cdd:COG4987 326 APAPGGPSLELEDVSFRYPGAGR--PVLDGLSLTLPPgERVAIVGPSGSGKSTLLALLLRFLD----PQSGSITLGGVDL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 85 LHLTEAQMRgvrgKRISMIMQDPkyslnpvvcvgkqiaeawltH----------HPGRKDEAKAKALEMLEVVRI----- 149
Cdd:COG4987 400 RDLDEDDLR----RRIAVVPQRP--------------------HlfdttlrenlRLARPDATDEELWAALERVGLgdwla 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 150 RQPERvYQLYPHE----ISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRglGLIFISHDINL 225
Cdd:COG4987 456 ALPDG-LDTWLGEggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAG 532
|
250
....*....|....*....
gi 503996112 226 VRSFcDRVLVMYAGRVVES 244
Cdd:COG4987 533 LERM-DRILVLEDGRIVEQ 550
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
14-244 |
1.71e-22 |
|
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: 93.01 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 14 LDVRDLCVDFVNGsavtHAVRGVSFQL-GREKLAIVGESGSGKSTVGRAL--LQLHPKKARVSASRMqFANLDLLHLTEA 90
Cdd:cd03260 1 IELRDLNVYYGDK----HALKDISLDIpKGEITALIGPSGCGKSTLLRLLnrLNDLIPGAPDEGEVL-LDGKDIYDLDVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 91 QMRgVRgKRISMIMQDPkyslNPV-------VCVGKQIAEAWLTHHPgrkDEAKAKALEMLEVvrirqPERVY-QLYPHE 162
Cdd:cd03260 76 VLE-LR-RRVGMVFQKP----NPFpgsiydnVAYGLRLHGIKLKEEL---DERVEEALRKAAL-----WDEVKdRLHALG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 163 ISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLvqSRGLGLIFISHDINLVRSFCDRVLVMYAGRVV 242
Cdd:cd03260 142 LSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGRLV 219
|
..
gi 503996112 243 ES 244
Cdd:cd03260 220 EF 221
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
31-243 |
3.21e-22 |
|
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: 92.61 E-value: 3.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 31 HAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALL-QLHPKKARVsasrmQFANLDLLHLTeaqmRGVRgKRISMIMQDPK 108
Cdd:COG4555 15 PALKDVSFTAKDgEITGLLGPNGAGKTTLLRMLAgLLKPDSGSI-----LIDGEDVRKEP----REAR-RQIGVLPDERG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 109 YSLNPVVcvgKQIAEAWLTHHPGRKDEAKAKALEMLEVVRIRQP--ERVyqlypHEISGGQGQRIMIAMMLITDPELIIA 186
Cdd:COG4555 85 LYDRLTV---RENIRYFAELYGLFDEELKKRIEELIELLGLEEFldRRV-----GELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503996112 187 DEPTSALDVSVRLQVLGLLDDLVQSrGLGLIFISHDINLVRSFCDRVLVMYAGRVVE 243
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVA 212
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
16-241 |
3.93e-22 |
|
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: 92.02 E-value: 3.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 16 VRDLCVDFvnGSAVthAVRGVSFQL-GREKLAIVGESGSGKSTVGRALLQL-HPKKARVsasrmqfanldLLHLTEAQMR 93
Cdd:cd03296 5 VRNVSKRF--GDFV--ALDDVSLDIpSGELVALLGPSGSGKTTLLRLIAGLeRPDSGTI-----------LFGGEDATDV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 94 GVRGKRISMIMQDpkYSLNPVVCVGKQIAEAwLTHHPGR----KDEAKAKALEMLEVVRIrqpERVYQLYPHEISGGQGQ 169
Cdd:cd03296 70 PVQERNVGFVFQH--YALFRHMTVFDNVAFG-LRVKPRSerppEAEIRAKVHELLKLVQL---DWLADRYPAQLSGGQRQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503996112 170 RIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRV 241
Cdd:cd03296 144 RVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
14-263 |
4.00e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 92.51 E-value: 4.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 14 LDVRDLCVDFvNGSAVTHAVrGVSFQLGrEKLAIVGESGSGKSTVGRAL-LQLHPKKARVSASRMQFANLDLLHLTEAQM 92
Cdd:PRK11264 4 IEVKNLVKKF-HGQTVLHGI-DLEVKPG-EVVAIIGPSGSGKTTLLRCInLLEQPEAGTIRVGDITIDTARSLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 93 RGVRgKRISMIMQDpkYSLNPVVCVGKQIAEAWLTHHPGRKDEAKAKALEMLEVVRIRQPERVYqlyPHEISGGQGQRIM 172
Cdd:PRK11264 81 RQLR-QHVGFVFQN--FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSY---PRRLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 173 IAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLgLIFISHDINLVRSFCDRVLVMYAGRVVESIAACDL-D 251
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALfA 233
|
250
....*....|..
gi 503996112 252 NARHPYTQGLIN 263
Cdd:PRK11264 234 DPQQPRTRQFLE 245
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
32-242 |
6.76e-22 |
|
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: 90.80 E-value: 6.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 32 AVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPK---KARVSASRMQFANLDLL-HLTEAqmrgvRGkrismimqd 106
Cdd:cd03269 15 ALDDISFSVEKgEIFGLLGPNGAGKTTTIRMILGIILPdsgEVLFDGKPLDIAARNRIgYLPEE-----RG--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 107 pkysLNPVVCVGKQIAeaWLTHHPG-RKDEAKAKALEMLEVVRI--RQPERVYQLypheiSGGQGQRIMIAMMLITDPEL 183
Cdd:cd03269 81 ----LYPKMKVIDQLV--YLAQLKGlKKEEARRRIDEWLERLELseYANKRVEEL-----SKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 184 IIADEPTSALD-VSVRLqVLGLLDDLvQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVV 242
Cdd:cd03269 150 LILDEPFSGLDpVNVEL-LKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
9-244 |
7.23e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 91.98 E-value: 7.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 9 NNAPLLDVRDLCvdFVNGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQL-HPKKARVSasrmqfanLDLLH 86
Cdd:PRK13632 3 NKSVMIKVENVS--FSYPNSENNALKNVSFEINEgEYVAILGHNGSGKSTISKILTGLlKPQSGEIK--------IDGIT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 87 LTEAQMRGVRGKrISMIMQDPKyslNPVV--CVGKQIAEAwLTHHPGRKDEAKAKALEMLEVVRIrqpERVYQLYPHEIS 164
Cdd:PRK13632 73 ISKENLKEIRKK-IGIIFQNPD---NQFIgaTVEDDIAFG-LENKKVPPKKMKDIIDDLAKKVGM---EDYLDKEPQNLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 165 GGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVrSFCDRVLVMYAGRVVES 244
Cdd:PRK13632 145 GGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQ 223
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
12-242 |
7.87e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 91.76 E-value: 7.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 12 PLLDVRDLCVDfVNGSAVTHavrGVSFQLGR-EKLAIVGESGSGKSTVGRALLQ-LHPkkarvSASRMQFANLDLLHLTE 89
Cdd:PRK13548 1 AMLEARNLSVR-LGGRTLLD---DVSLTLRPgEVVAILGPNGAGKSTLLRALSGeLSP-----DSGEVRLNGRPLADWSP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 90 AQMrgvrGKRISMIMQDPK----YSLNPVVCVGkqiaeawLTHHPGRKDEAKAKALEMLEVVRIRQ-PERVYQlyphEIS 164
Cdd:PRK13548 72 AEL----ARRRAVLPQHSSlsfpFTVEEVVAMG-------RAPHGLSRAEDDALVAAALAQVDLAHlAGRDYP----QLS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 165 GGQGQRIMIAMMLI------TDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYA 238
Cdd:PRK13548 137 GGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQ 216
|
....
gi 503996112 239 GRVV 242
Cdd:PRK13548 217 GRLV 220
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
43-243 |
8.06e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 91.23 E-value: 8.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 43 EKLAIVGESGSGKSTVGRALLQLH-PKKARVSASRMQFanlDL-LHLTEAQMRGVRGKrISMIMQdpKYSLNPVVCVGKQ 120
Cdd:COG4161 29 ETLVLLGPSGAGKSSLLRVLNLLEtPDSGQLNIAGHQF---DFsQKPSEKAIRLLRQK-VGMVFQ--QYNLWPHLTVMEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 121 IAEAwlthhPGR-----KDEAKAKALEMLEVVRIrqpERVYQLYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDV 195
Cdd:COG4161 103 LIEA-----PCKvlglsKEQAREKAMKLLARLRL---TDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDP 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503996112 196 SVRLQVLGLLDDLVQSrGLGLIFISHDINLVRSFCDRVLVMYAGRVVE 243
Cdd:COG4161 175 EITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIE 221
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
34-243 |
9.47e-22 |
|
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: 91.14 E-value: 9.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 34 RGVSFQL-GREKLAIVGESGSGKSTVGRALLQLHPkkarVSASRMQFANLDLLHLTEAQMRgvrgKRISMIMQDpkysln 112
Cdd:cd03253 18 KDVSFTIpAGKKVAIVGPSGSGKSTILRLLFRFYD----VSSGSILIDGQDIREVTLDSLR----RAIGVVPQD------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 113 pVVCVGKQIAEAWLTHHPGRKDE---AKAKALEMLEVVrIRQPERvYQLYPHE----ISGGQGQRIMIAMMLITDPELII 185
Cdd:cd03253 84 -TVLFNDTIGYNIRYGRPDATDEeviEAAKAAQIHDKI-MRFPDG-YDTIVGErglkLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503996112 186 ADEPTSALDVSVRLQVLGLLDDLVQSRglGLIFISHDINLVRSfCDRVLVMYAGRVVE 243
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGR--TTIVIAHRLSTIVN-ADKIIVLKDGRIVE 215
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
43-243 |
1.72e-21 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 90.54 E-value: 1.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 43 EKLAIVGESGSGKSTVGRALLQLHPkkarVSASRMQFANLDLLHlTEAQMRGVRgKRISMIMQdpKYSLNPVVCVGKQIA 122
Cdd:PRK09493 28 EVVVIIGPSGSGKSTLLRCINKLEE----ITSGDLIVDGLKVND-PKVDERLIR-QEAGMVFQ--QFYLFPHLTALENVM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 123 EAWLTHHPGRKDEAKAKALEMLEVVRIRqpERVYQlYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVL 202
Cdd:PRK09493 100 FGPLRVRGASKEEAEKQARELLAKVGLA--ERAHH-YPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 503996112 203 GLLDDLVQSrGLGLIFISHDINLVRSFCDRVLVMYAGRVVE 243
Cdd:PRK09493 177 KVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAE 216
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
12-243 |
2.70e-21 |
|
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: 93.33 E-value: 2.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 12 PLLDVRDLCVDFVN-GSAVTHAVRGVSFQL-GREKLAIVGESGSGKSTVGRALLQ-LHPKKARVSASrmqfANLDLLHLT 88
Cdd:TIGR03269 278 PIIKVRNVSKRYISvDRGVVKAVDNVSLEVkEGEIFGIVGTSGAGKTTLSKIIAGvLEPTSGEVNVR----VGDEWVDMT 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 89 E--AQMRGVRGKRISMIMQDpkYSLNPVVCVGKQIAEAWLTHHPgrKDEAKAKALEMLEVVRI--RQPERVYQLYPHEIS 164
Cdd:TIGR03269 354 KpgPDGRGRAKRYIGILHQE--YDLYPHRTVLDNLTEAIGLELP--DELARMKAVITLKMVGFdeEKAEEILDKYPDELS 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 165 GGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVlglLDDLVQSR---GLGLIFISHDINLVRSFCDRVLVMYAGRV 241
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDV---THSILKAReemEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
..
gi 503996112 242 VE 243
Cdd:TIGR03269 507 VK 508
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
30-243 |
2.75e-21 |
|
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: 89.24 E-value: 2.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 30 THAVRGVSFQLG-REKLAIVGESGSGKSTVGRALLQLHPkkarVSASRMQFANLDLLHLtEAQMRGvrgkrISMIMQDpk 108
Cdd:cd03301 13 VTALDDLNLDIAdGEFVVLLGPSGCGKTTTLRMIAGLEE----PTSGRIYIGGRDVTDL-PPKDRD-----IAMVFQN-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 109 YSLNPVVCVGKQIAEAwLTHHPGRKDEAKAKALEMLEVVRIrqpERVYQLYPHEISGGQGQRIMIAMMLITDPELIIADE 188
Cdd:cd03301 81 YALYPHMTVYDNIAFG-LKLRKVPKDEIDERVREVAELLQI---EHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503996112 189 PTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVE 243
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQ 211
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
47-243 |
4.90e-21 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 91.02 E-value: 4.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 47 IVGESGSGKSTVGRALLQLHpkkaRVSASRMQFANLDLLHLTeAQMRGvrgkrISMIMQDpkYSLNPVVCVGKQIAEAwL 126
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFE----QPDSGSIMLDGEDVTNVP-PHLRH-----INMVFQS--YALFPHMTVEENVAFG-L 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 127 THHPGRKDEAKAKALEMLEVVrirQPERVYQLYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLD 206
Cdd:TIGR01187 68 KMRKVPRAEIKPRVLEALRLV---QLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELK 144
|
170 180 190
....*....|....*....|....*....|....*..
gi 503996112 207 DLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVE 243
Cdd:TIGR01187 145 TIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQ 181
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
32-244 |
6.63e-21 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 92.15 E-value: 6.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 32 AVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPkkarVSASRMQFANLDLLHLTEAQMRgvrgKRISMIMQDPK-Y 109
Cdd:COG1132 355 VLKDISLTIPPgETVALVGPSGSGKSTLVNLLLRFYD----PTSGRILIDGVDIRDLTLESLR----RQIGVVPQDTFlF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 110 SLNpvvcvgkqIAE--AWlthhpGRKD------EAKAKALEMLEVVRiRQP--------ERVYQLypheiSGGQGQRIMI 173
Cdd:COG1132 427 SGT--------IREniRY-----GRPDatdeevEEAAKAAQAHEFIE-ALPdgydtvvgERGVNL-----SGGQRQRIAI 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503996112 174 AMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRglGLIFISHDINLVRSfCDRVLVMYAGRVVES 244
Cdd:COG1132 488 ARALLKDPPILILDEATSALDTETEALIQEALERLMKGR--TTIVIAHRLSTIRN-ADRILVLDDGRIVEQ 555
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
13-244 |
9.05e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 89.37 E-value: 9.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 13 LLDVRDLCVDFVNGsavTHAVRGVSFQLGR-EKLAIVGESGSGKSTvgralLQLH------PKKARV--SASRMQFANLD 83
Cdd:PRK13639 1 ILETRDLKYSYPDG---TEALKGINFKAEKgEMVALLGPNGAGKST-----LFLHfngilkPTSGEVliKGEPIKYDKKS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 84 LLHlteaqmrgVRgKRISMIMQDPKYSL-NPVVcvGKQIAEAWLTHHPgRKDEAKAKALEMLEVVRIRQPERVYqlyPHE 162
Cdd:PRK13639 73 LLE--------VR-KTVGIVFQNPDDQLfAPTV--EEDVAFGPLNLGL-SKEEVEKRVKEALKAVGMEGFENKP---PHH 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 163 ISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLvQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVV 242
Cdd:PRK13639 138 LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDL-NKEGITIIISTHDVDLVPVYADKVYVMSDGKII 216
|
..
gi 503996112 243 ES 244
Cdd:PRK13639 217 KE 218
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
13-242 |
9.10e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 89.48 E-value: 9.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 13 LLDVRDLCVDFvngSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQ-LHPKKARVSASRMQfanldllhLTEA 90
Cdd:PRK13652 3 LIETRDLCYSY---SGSKEALNNINFIAPRnSRIAVIGPNGAGKSTLFRHFNGiLKPTSGSVLIRGEP--------ITKE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 91 QMRGVRgKRISMIMQDPKYSL-NPVVcvGKQIA---------EAWLTHhpgRKDEAkakaLEMLEVVRIRqpERVyqlyP 160
Cdd:PRK13652 72 NIREVR-KFVGLVFQNPDDQIfSPTV--EQDIAfgpinlgldEETVAH---RVSSA----LHMLGLEELR--DRV----P 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 161 HEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGR 240
Cdd:PRK13652 136 HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGR 215
|
..
gi 503996112 241 VV 242
Cdd:PRK13652 216 IV 217
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
12-243 |
2.75e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 89.51 E-value: 2.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 12 PLLDVRDLCVDFvNGSavtHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPKkarvSASRMQFANLDLLHLTEA 90
Cdd:PRK11607 18 PLLEIRNLTKSF-DGQ---HAVDDVSLTIYKgEIFALLGASGCGKSTLLRMLAGFEQP----TAGQIMLDGVDLSHVPPY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 91 QmrgvrgKRISMIMQdpKYSLNPVVCVGKQIAEAwLTHHPGRKDEAKAKALEMLEVVRIRQperVYQLYPHEISGGQGQR 170
Cdd:PRK11607 90 Q------RPINMMFQ--SYALFPHMTVEQNIAFG-LKQDKLPKAEIASRVNEMLGLVHMQE---FAKRKPHQLSGGQRQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503996112 171 IMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVE 243
Cdd:PRK11607 158 VALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQ 230
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
10-241 |
3.33e-20 |
|
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: 85.56 E-value: 3.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 10 NAPLLDVRDLCVDfvngsavtHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPkkarVSASRMQFANLDLLHLT 88
Cdd:cd03215 1 GEPVLEVRGLSVK--------GAVRDVSFEVRAgEIVGIAGLVGNGQTELAEALFGLRP----PASGEITLDGKPVTRRS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 89 EAQMRGvrgKRISMIMQDpkyslnpvvcvgkqiaeawlthhpgRKDEAKAKALEMLEVVRIRQpervyQLypheiSGGQG 168
Cdd:cd03215 69 PRDAIR---AGIAYVPED-------------------------RKREGLVLDLSVAENIALSS-----LL-----SGGNQ 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503996112 169 QRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQsRGLGLIFISHDINLVRSFCDRVLVMYAGRV 241
Cdd:cd03215 111 QKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAD-AGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-251 |
4.30e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 89.69 E-value: 4.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 6 PAANNAPLLDVRDLCVDfvngsavtHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPKKA-RVsasrmqfanld 83
Cdd:COG1129 249 AAAPGEVVLEVEGLSVG--------GVVRDVSFSVRAgEILGIAGLVGAGRTELARALFGADPADSgEI----------- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 84 LLHLTEAQMRGVR---GKRISMIMQDPK-YSLNPVVCVGKQIAEAWL--THHPGRKDEAKAKAL--EMLEVVRIRQP--- 152
Cdd:COG1129 310 RLDGKPVRIRSPRdaiRAGIAYVPEDRKgEGLVLDLSIRENITLASLdrLSRGGLLDRRRERALaeEYIKRLRIKTPspe 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 153 ERVYQLypheiSGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQsRGLGLIFISHDINLVRSFCDR 232
Cdd:COG1129 390 QPVGNL-----SGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAA-EGKAVIVISSELPELLGLSDR 463
|
250
....*....|....*....
gi 503996112 233 VLVMYAGRVVESIAACDLD 251
Cdd:COG1129 464 ILVMREGRIVGELDREEAT 482
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
30-241 |
7.26e-20 |
|
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: 85.54 E-value: 7.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 30 THAVRGVSFQLGR-EKLAIVGESGSGKSTvgraLLQLHPKKARVSASRMQFANLDLLHLTEAQMRGVRgKRISMIMQDPK 108
Cdd:cd03292 14 TAALDGINISISAgEFVFLVGPSGAGKST----LLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR-RKIGVVFQDFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 109 ysLNPVVCVGKQIAEAW-LTHHPGRkdEAKAKALEMLEVVRIRQPERVYqlyPHEISGGQGQRIMIAMMLITDPELIIAD 187
Cdd:cd03292 89 --LLPDRNVYENVAFALeVTGVPPR--EIRKRVPAALELVGLSHKHRAL---PAELSGGEQQRVAIARAIVNSPTILIAD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503996112 188 EPTSALDVSVRLQVLGLLDDlVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRV 241
Cdd:cd03292 162 EPTGNLDPDTTWEIMNLLKK-INKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
30-242 |
1.10e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 86.64 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 30 THAVRGVSFQL-GREKLAIVGESGSGKSTvgraLLQ-----LHPKKARVSasrmqfanLDLLHLTE--AQMRGVRgKRIS 101
Cdd:PRK13637 20 KKALDNVNIEIeDGEFVGLIGHTGSGKST----LIQhlnglLKPTSGKII--------IDGVDITDkkVKLSDIR-KKVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 102 MIMQDPKYSLNPVVcVGKQIAeawltHHPGR----KDEAKAKALEMLEVVRIRqpervYQLY----PHEISGGQGQRIMI 173
Cdd:PRK13637 87 LVFQYPEYQLFEET-IEKDIA-----FGPINlglsEEEIENRVKRAMNIVGLD-----YEDYkdksPFELSGGQKRRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503996112 174 AMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVV 242
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
32-242 |
1.22e-19 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 85.11 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 32 AVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLhpkkARVSASRMQFANLDLLhlteAQMRGVRgKRISMIMQDPkyS 110
Cdd:cd03265 15 AVRGVSFRVRRgEIFGLLGPNGAGKTTTIKMLTTL----LKPTSGRATVAGHDVV----REPREVR-RRIGIVFQDL--S 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 111 LNPVVCVGKQIA-EAWLTHHPGrkDEAKAKALEMLEVVRIRQ-PERVYQLYpheiSGGQGQRIMIAMMLITDPELIIADE 188
Cdd:cd03265 84 VDDELTGWENLYiHARLYGVPG--AERRERIDELLDFVGLLEaADRLVKTY----SGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503996112 189 PTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVV 242
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
14-252 |
1.27e-19 |
|
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: 84.79 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 14 LDVRDLCVdfvnGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPkkarVSASRMQFANLDLLHLTeAQM 92
Cdd:cd03224 1 LEVENLNA----GYGKSQILFGVSLTVPEgEIVALLGRNGAGKTTLLKTIMGLLP----PRSGSIRFDGRDITGLP-PHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 93 RGVRGkrISMIMQDPKysLNPVVCVGKQIAEAWLTHHPGRKDEAKAKALEMLEVVRIRQPERVYQLypheiSGGQGQRIM 172
Cdd:cd03224 72 RARAG--IGYVPEGRR--IFPELTVEENLLLGAYARRRAKRKARLERVYELFPRLKERRKQLAGTL-----SGGEQQMLA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 173 IAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLvQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVESIAACDLDN 252
Cdd:cd03224 143 IARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
13-242 |
1.50e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 86.05 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 13 LLDVRDLCVDFVNGsavTHAVRGVSFQLGR-EKLAIVGESGSGKSTvgraLLQLHPKKARVSASRMQFANLDLLHLTEAQ 91
Cdd:PRK13636 5 ILKVEELNYNYSDG---THALKGININIKKgEVTAILGGNGAGKST----LFQNLNGILKPSSGRILFDGKPIDYSRKGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 92 MRgVRgKRISMIMQDPKYSLNPVvCVGKQIAEAWLTHH-PgrKDEAKAKALEMLEVVRIrqpERVYQLYPHEISGGQGQR 170
Cdd:PRK13636 78 MK-LR-ESVGMVFQDPDNQLFSA-SVYQDVSFGAVNLKlP--EDEVRKRVDNALKRTGI---EHLKDKPTHCLSFGQKKR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503996112 171 IMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVV 242
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
33-243 |
2.40e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 85.02 E-value: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 33 VRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLH-PKKARVSASRmqfANLDLLHLTEAQMRGVRGK-------RISMI 103
Cdd:PRK10619 21 LKGVSLQANAgDVISIIGSSGSGKSTFLRCINFLEkPSEGSIVVNG---QTINLVRDKDGQLKVADKNqlrllrtRLTMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 104 MQdpKYSLNPVVCVGKQIAEAWLTHHPGRKDEAKAKALEMLEVVRIrqPERVYQLYPHEISGGQGQRIMIAMMLITDPEL 183
Cdd:PRK10619 98 FQ--HFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGI--DERAQGKYPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 184 IIADEPTSALDVSVRLQVLGLLDDLVQsRGLGLIFISHDINLVRSFCDRVLVMYAGRVVE 243
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFARHVSSHVIFLHQGKIEE 232
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
30-242 |
2.74e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 85.14 E-value: 2.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 30 THAVRGVSFQLGR-EKLAIVGESGSGKSTVGR---ALLQlhPKKARVSASRMQfaNLDLLHLTEaqmrgVRgKRISMIMQ 105
Cdd:PRK13633 23 KLALDDVNLEVKKgEFLVILGRNGSGKSTIAKhmnALLI--PSEGKVYVDGLD--TSDEENLWD-----IR-NKAGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 106 DPKyslNPVVCVgkqIAEAWLTHHPGR----KDEAKAKALEMLEVVRIRQpervYQLY-PHEISGGQGQRIMIAMMLITD 180
Cdd:PRK13633 93 NPD---NQIVAT---IVEEDVAFGPENlgipPEEIRERVDESLKKVGMYE----YRRHaPHLLSGGQKQRVAIAGILAMR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503996112 181 PELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSfCDRVLVMYAGRVV 242
Cdd:PRK13633 163 PECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVV 223
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
32-244 |
2.91e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 85.24 E-value: 2.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 32 AVRGVSFQLGREK-LAIVGESGSGKSTVGRaLLQ--LHPKKArvSASRMqfaNLDLLHLTEAQMRGVRgKRISMIMQDPK 108
Cdd:PRK13640 22 ALNDISFSIPRGSwTALIGHNGSGKSTISK-LINglLLPDDN--PNSKI---TVDGITLTAKTVWDIR-EKVGIVFQNPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 109 yslNPVV--CVGKQIAEawlthhpGRKDEAKAKAlEMLEVVRiRQPERVYQL-----YPHEISGGQGQRIMIAMMLITDP 181
Cdd:PRK13640 95 ---NQFVgaTVGDDVAF-------GLENRAVPRP-EMIKIVR-DVLADVGMLdyidsEPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503996112 182 ELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVrSFCDRVLVMYAGRVVES 244
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQ 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
33-246 |
3.01e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 85.17 E-value: 3.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 33 VRGVSFQLGR-EKLAIVGESGSGKSTVGR---ALLQLHPKKARVSASRmqfanldllhLTEAQMRGVRGKrISMIMQDPK 108
Cdd:PRK13650 23 LNDVSFHVKQgEWLSIIGHNGSGKSTTVRlidGLLEAESGQIIIDGDL----------LTEENVWDIRHK-IGMVFQNPD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 109 YSLnpvvcVGKQIAE--AWLTHHPG-RKDEAKAKALEMLEVV-----RIRQPERvyqlypheISGGQGQRIMIAMMLITD 180
Cdd:PRK13650 92 NQF-----VGATVEDdvAFGLENKGiPHEEMKERVNEALELVgmqdfKEREPAR--------LSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503996112 181 PELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVrSFCDRVLVMYAGRvVESIA 246
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQ-VESTS 222
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
13-250 |
3.05e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 85.14 E-value: 3.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 13 LLDVRDLCVDFVNGSAVTHaVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPKKARVsasrmqfANLDLLHLTEAQ 91
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQ-LNGVSFSITKgEWVSIIGQNGSGKSTTARLIDGLFEEFEGK-------VKIDGELLTAEN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 92 MRGVRgKRISMIMQDPKYSLnpvvcVGKQIAE--AWLTHHPG--------RKDEAKAkALEMLEVvRIRQPERvyqlyph 161
Cdd:PRK13642 76 VWNLR-RKIGMVFQNPDNQF-----VGATVEDdvAFGMENQGipreemikRVDEALL-AVNMLDF-KTREPAR------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 162 eISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSfCDRVLVMYAGRV 241
Cdd:PRK13642 141 -LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEI 218
|
....*....
gi 503996112 242 VESIAACDL 250
Cdd:PRK13642 219 IKEAAPSEL 227
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
14-242 |
5.41e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 84.40 E-value: 5.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 14 LDVRDLCVDFVNGsavTHAVRGVSFQLGR-EKLAIVGESGSGKSTVgraLLQLH----PKKARVSASRMQfanldllhLT 88
Cdd:PRK13647 5 IEVEDLHFRYKDG---TKALKGLSLSIPEgSKTALLGPNGAGKSTL---LLHLNgiylPQRGRVKVMGRE--------VN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 89 EAQMRGVRGKrISMIMQDPKyslnpvvcvgKQI--AEAW--LTHHPG----RKDEAKAKALEMLEVVRIrqpERVYQLYP 160
Cdd:PRK13647 71 AENEKWVRSK-VGLVFQDPD----------DQVfsSTVWddVAFGPVnmglDKDEVERRVEEALKAVRM---WDFRDKPP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 161 HEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQsRGLGLIFISHDINLVRSFCDRVLVMYAGR 240
Cdd:PRK13647 137 YHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHN-QGKTVIVATHDVDLAAEWADQVIVLKEGR 215
|
..
gi 503996112 241 VV 242
Cdd:PRK13647 216 VL 217
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
36-243 |
6.63e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 84.50 E-value: 6.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 36 VSFQLGREK-LAIVGESGSGKSTvgraLLQ-----LHPKKARVSASRMQFAnldlLHLTEAQMRGVRgKRISMIMQDPKY 109
Cdd:PRK13641 26 ISFELEEGSfVALVGHTGSGKST----LMQhfnalLKPSSGTITIAGYHIT----PETGNKNLKKLR-KKVSLVFQFPEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 110 SL--NPVVcvgKQIaEAWLTHHPGRKDEAKAKALEMLEVVRIrqPERVYQLYPHEISGGQGQRIMIAMMLITDPELIIAD 187
Cdd:PRK13641 97 QLfeNTVL---KDV-EFGPKNFGFSEDEAKEKALKWLKKVGL--SEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503996112 188 EPTSALDVSVRLQVLGLLDDLvQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVE 243
Cdd:PRK13641 171 EPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIK 225
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
21-242 |
1.02e-18 |
|
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: 82.64 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 21 VDFVNGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHpkkaRVSASRMQFANLDLLHLTEAQMRgvrgKR 99
Cdd:cd03245 8 VSFSYPNQEIPALDNVSLTIRAgEKVAIIGRVGSGKSTLLKLLAGLY----KPTSGSVLLDGTDIRQLDPADLR----RN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 100 ISMIMQDP---KYSLNPVVCVGKQIAEawlthhpgrkDEakakalEMLEVVRI--------RQP--------ERVYQLyp 160
Cdd:cd03245 80 IGYVPQDVtlfYGTLRDNITLGAPLAD----------DE------RILRAAELagvtdfvnKHPngldlqigERGRGL-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 161 heiSGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRglGLIFISHDINLVrSFCDRVLVMYAGR 240
Cdd:cd03245 142 ---SGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLL-DLVDRIIVMDSGR 215
|
..
gi 503996112 241 VV 242
Cdd:cd03245 216 IV 217
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
36-241 |
1.20e-18 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 84.39 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 36 VSFQL-GREKLAIVGESGSGKSTVGRALLQL-HPKKARVS-ASRMQFANLDLLHLTEAQmrgvrgKRISMIMQDPkySLN 112
Cdd:TIGR02142 16 ADFTLpGQGVTAIFGRSGSGKTTLIRLIAGLtRPDEGEIVlNGRTLFDSRKGIFLPPEK------RRIGYVFQEA--RLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 113 PVVCVGKQIAEAWLTHHPGRKDEAKAKALEMLEVvrirqpERVYQLYPHEISGGQGQRIMIAMMLITDPELIIADEPTSA 192
Cdd:TIGR02142 88 PHLSVRGNLRYGMKRARPSERRISFERVIELLGI------GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503996112 193 LDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRV 241
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRV 210
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
12-244 |
1.37e-18 |
|
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: 82.83 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 12 PLLDVRDLCVDFvNGSAVthaVRGVSFQLGR-EKLAIVGESGSGKSTvgraLLQL----HPKKARVSASRM--QFANLDL 84
Cdd:COG1119 2 PLLELRNVTVRR-GGKTI---LDDISWTVKPgEHWAILGPNGAGKST----LLSLitgdLPPTYGNDVRLFgeRRGGEDV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 85 LHLteaqmrgvRgKRI---SMIMQDpKYSLNP----VVCVGK--QIAeawLTHHPGRKDEAKAKA-LEMLEVVRIRqpER 154
Cdd:COG1119 74 WEL--------R-KRIglvSPALQL-RFPRDEtvldVVLSGFfdSIG---LYREPTDEQRERARElLELLGLAHLA--DR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 155 VYqlypHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVL 234
Cdd:COG1119 139 PF----GTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVL 214
|
250
....*....|
gi 503996112 235 VMYAGRVVES 244
Cdd:COG1119 215 LLKDGRVVAA 224
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
43-243 |
1.69e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 84.70 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 43 EKLAIVGESGSGKSTVGRALLQL-HPKKARVSASrmqfaNLDLLHLTEAQMRGVRGKRISMIMQdpKYSLNPVVCVGKQI 121
Cdd:PRK10070 55 EIFVIMGLSGSGKSTMVRLLNRLiEPTRGQVLID-----GVDIAKISDAELREVRRKKIAMVFQ--SFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 122 AEAW-LTHHPGrkDEAKAKALEMLEVVRIrqpERVYQLYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQ 200
Cdd:PRK10070 128 AFGMeLAGINA--EERREKALDALRQVGL---ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 503996112 201 VLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVE 243
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
31-244 |
1.83e-18 |
|
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: 81.47 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 31 HAVRGVSFQLGREKLAIVGESGSGKSTVGRALLQLhpkkARVSASRMQFANLDLLhlteAQMRGVRgKRISMIMQDPKYS 110
Cdd:cd03264 14 RALDGVSLTLGPGMYGLLGPNGAGKTTLMRILATL----TPPSSGTIRIDGQDVL----KQPQKLR-RRIGYLPQEFGVY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 111 lnPVVCVGKQIAE-AWLTHHPGRkdEAKAKALEMLEVVRI--RQPERVYQLypheiSGGQGQRIMIAMMLITDPELIIAD 187
Cdd:cd03264 85 --PNFTVREFLDYiAWLKGIPSK--EVKARVDEVLELVNLgdRAKKKIGSL-----SGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503996112 188 EPTSALDVSVRLQVLGLLDDLVQSRglglIFI--SHDINLVRSFCDRVLVMYAGRVVES 244
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELGEDR----IVIlsTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
14-254 |
2.33e-18 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 81.80 E-value: 2.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 14 LDVRDLCVdFVNGSavtHAVRGVSFQLGREK-LAIVGESGSGKSTVGRALLQLHPkkarVSASRMQFANLDLLHLtEAQM 92
Cdd:TIGR03410 1 LEVSNLNV-YYGQS---HILRGVSLEVPKGEvTCVLGRNGVGKTTLLKTLMGLLP----VKSGSIRLDGEDITKL-PPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 93 RGVRGkrISMIMQdpkyslnpvvcvGKQI------AEAWLTHHPGRKDEAKakalemlevvriRQPERVYQLYP--HE-- 162
Cdd:TIGR03410 72 RARAG--IAYVPQ------------GREIfprltvEENLLTGLAALPRRSR------------KIPDEIYELFPvlKEml 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 163 ------ISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVM 236
Cdd:TIGR03410 126 grrggdLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVM 205
|
250
....*....|....*...
gi 503996112 237 YAGRVVESIAACDLDNAR 254
Cdd:TIGR03410 206 ERGRVVASGAGDELDEDK 223
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
32-244 |
3.17e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 84.24 E-value: 3.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 32 AVRGVSFQ-LGREKLAIVGESGSGKSTVgRALLQlhpkkaRV---SASRMQFANLDLLHLTEAQMRgvrgKRISMIMQDP 107
Cdd:PRK13657 350 GVEDVSFEaKPGQTVAIVGPTGAGKSTL-INLLQ------RVfdpQSGRILIDGTDIRTVTRASLR----RNIAVVFQDA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 108 ---KYSLNPVVCVGKQIAeawlTHHPGRKDEAKAKALEMLEvvriRQP--------ERVYQLypheiSGGQGQRIMIAMM 176
Cdd:PRK13657 419 glfNRSIEDNIRVGRPDA----TDEEMRAAAERAQAHDFIE----RKPdgydtvvgERGRQL-----SGGERQRLAIARA 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503996112 177 LITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRglGLIFISHDINLVRSfCDRVLVMYAGRVVES 244
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVKAALDELMKGR--TTFIIAHRLSTVRN-ADRILVFDNGRVVES 550
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
12-272 |
4.23e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 81.45 E-value: 4.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 12 PLLDVRDLCVDFVNGSAVTHAVRGVSFQLG-REKLAIVGESGSGKSTvgraLLQL-----HPKKARVSasrmqfanldll 85
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIEsGEFVVALGASGCGKTT----LLNLiagflAPSSGEIT------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 86 hLTEAQMRGVRGKRiSMIMQdpKYSLNPVVCVGKQIAEAwLTHHPGRKDEAKAKALEMLEVVRIRQPER--VYQLyphei 163
Cdd:COG4525 66 -LDGVPVTGPGADR-GVVFQ--KDALLPWLNVLDNVAFG-LRLRGVPKAERRARAEELLALVGLADFARrrIWQL----- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 164 SGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVM--YAGRV 241
Cdd:COG4525 136 SGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRI 215
|
250 260 270
....*....|....*....|....*....|....*
gi 503996112 242 VESIaacDLDNARHpYTQG----LINSLPDMQHRR 272
Cdd:COG4525 216 VERL---ELDFSRR-FLAGedarAIKSDPAFIALR 246
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
21-243 |
4.92e-18 |
|
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: 80.74 E-value: 4.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 21 VDFVNGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTvgraLLQLHPKKARVSASRMQFANLDLLHLTEAQMRgvrgKR 99
Cdd:cd03251 6 VTFRYPGDGPPVLRDISLDIPAgETVALVGPSGSGKST----LVNLIPRFYDVDSGRILIDGHDVRDYTLASLR----RQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 100 ISMIMQDpkyslnpVVCVGKQIAE--AWLTHHPGRKD-EAKAKALEMLEVVRiRQP--------ERVYQLypheiSGGQG 168
Cdd:cd03251 78 IGLVSQD-------VFLFNDTVAEniAYGRPGATREEvEEAARAANAHEFIM-ELPegydtvigERGVKL-----SGGQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503996112 169 QRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRglGLIFISHDINLVRSfCDRVLVMYAGRVVE 243
Cdd:cd03251 145 QRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNR--TTFVIAHRLSTIEN-ADRIVVLEDGKIVE 216
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-251 |
7.27e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 83.15 E-value: 7.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 6 PAANNAPLLDVRDLCVDfvnGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLhpkkARVSASRMQFANLDL 84
Cdd:COG3845 250 PAEPGEVVLEVENLSVR---DDRGVPALKDVSLEVRAgEILGIAGVAGNGQSELAEALAGL----RPPASGSIRLDGEDI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 85 LHLTEAQMRGvrgKRISMIMQD-------PKYSL--NPVVcvgKQIAEAWLTHHPG-RKDEAKAKALEMLEV--VRIRQP 152
Cdd:COG3845 323 TGLSPRERRR---LGVAYIPEDrlgrglvPDMSVaeNLIL---GRYRRPPFSRGGFlDRKAIRAFAEELIEEfdVRTPGP 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 153 E-RVYQLypheiSGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLvQSRGLGLIFISHDINLVRSFCD 231
Cdd:COG3845 397 DtPARSL-----SGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSD 470
|
250 260
....*....|....*....|
gi 503996112 232 RVLVMYAGRVVESIAACDLD 251
Cdd:COG3845 471 RIAVMYEGRIVGEVPAAEAT 490
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
30-242 |
8.46e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 82.04 E-value: 8.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 30 THAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHpkkaRVSASRMQFANLDLLHLtEAQMRGvrgkrISMIMQDpk 108
Cdd:COG3839 16 VEALKDIDLDIEDgEFLVLLGPSGCGKSTLLRMIAGLE----DPTSGEILIGGRDVTDL-PPKDRN-----IAMVFQS-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 109 YSLNPVVCVGKQIAEA-WLTHHPgrKDEAKAKALEMLEVVRIrqpERVYQLYPHEISGGQGQRIMIAMMLITDPELIIAD 187
Cdd:COG3839 84 YALYPHMTVYENIAFPlKLRKVP--KAEIDRRVREAAELLGL---EDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503996112 188 EPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVV 242
Cdd:COG3839 159 EPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQ 213
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
7-243 |
8.50e-18 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 80.62 E-value: 8.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 7 AANNAPLLDVRDLCVDFvnGSavtHAV-RGVSFQLGR-EKLAIVGESGSGKST-----------------VGRALLQLHP 67
Cdd:COG4598 2 TDTAPPALEVRDLHKSF--GD---LEVlKGVSLTARKgDVISIIGSSGSGKSTflrcinlletpdsgeirVGGEEIRLKP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 68 KK--ARVSASRMQFAnldllhlteaQMRGvrgkRISMIMQDpkYSLNPVVCVGKQIAEAWLtHHPGR-KDEAKAKALEML 144
Cdd:COG4598 77 DRdgELVPADRRQLQ----------RIRT----RLGMVFQS--FNLWSHMTVLENVIEAPV-HVLGRpKAEAIERAEALL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 145 EVVRIrqpERVYQLYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQsRGLGLIFISHDIN 224
Cdd:COG4598 140 AKVGL---ADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAE-EGRTMLVVTHEMG 215
|
250
....*....|....*....
gi 503996112 225 LVRSFCDRVLVMYAGRVVE 243
Cdd:COG4598 216 FARDVSSHVVFLHQGRIEE 234
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
21-243 |
9.35e-18 |
|
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: 80.22 E-value: 9.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 21 VDFVNGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLH-PKKARVSASRMQFANLDLLHLTeaqmrgvrgK 98
Cdd:cd03252 6 VRFRYKPDGPVILDNISLRIKPgEVVGIVGRSGSGKSTLTKLIQRFYvPENGRVLVDGHDLALADPAWLR---------R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 99 RISMIMQDPkyslnpvVCVGKQIAEAWLTHHPG---RKDEAKAKALEMLEVVRiRQPERVYQLYPHE---ISGGQGQRIM 172
Cdd:cd03252 77 QVGVVLQEN-------VLFNRSIRDNIALADPGmsmERVIEAAKLAGAHDFIS-ELPEGYDTIVGEQgagLSGGQRQRIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503996112 173 IAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRglGLIFISHDINLVRSfCDRVLVMYAGRVVE 243
Cdd:cd03252 149 IARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGR--TVIIIAHRLSTVKN-ADRIIVMEKGRIVE 216
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
46-244 |
1.04e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 80.94 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 46 AIVGESGSGKSTVGRALLQLH-PKKARVSASRMQFANldllHLTEAQMRGVRgKRISMIMQDPKYSL--NPV---VCVGK 119
Cdd:PRK13649 37 AFIGHTGSGKSTIMQLLNGLHvPTQGSVRVDDTLITS----TSKNKDIKQIR-KKVGLVFQFPESQLfeETVlkdVAFGP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 120 QiaeawltHHPGRKDEAKAKALEMLEVVRIrqPERVYQLYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRL 199
Cdd:PRK13649 112 Q-------NFGVSQEEAEALAREKLALVGI--SESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRK 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503996112 200 QVLGLLDDLVQSrGLGLIFISHDINLVRSFCDRVLVMYAGRVVES 244
Cdd:PRK13649 183 ELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLS 226
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
43-242 |
1.25e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 79.63 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 43 EKLAIVGESGSGKSTvgraLLQLHPKKARVSASRMQFANLDLLHLTEAQmrgvrgKRISMIMQDpkYSLNPVVCVGKQIA 122
Cdd:PRK10771 26 ERVAILGPSGAGKST----LLNLIAGFLTPASGSLTLNGQDHTTTPPSR------RPVSMLFQE--NNLFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 123 eawLTHHPGRK--DEAKAKALEMLEVVRIrqpERVYQLYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQ 200
Cdd:PRK10771 94 ---LGLNPGLKlnAAQREKLHAIARQMGI---EDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 503996112 201 VLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVV 242
Cdd:PRK10771 168 MLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIA 209
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
11-241 |
2.61e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 81.04 E-value: 2.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 11 APLLDVRDLCVDFvngsAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALL-QLHPKKARVSASRMQFANLDLlhlT 88
Cdd:PRK09536 1 MPMIDVSDLSVEF----GDTTVLDGVDLSVREgSLVGLVGPNGAGKTTLLRAINgTLTPTAGTVLVAGDDVEALSA---R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 89 EAqmrgvrGKRISMIMQDPKYSLNPVVcvgKQIAEAWLTHHPGR-------KDEAKAKALEMLEVVRIrqPERVYQlyph 161
Cdd:PRK09536 74 AA------SRRVASVPQDTSLSFEFDV---RQVVEMGRTPHRSRfdtwtetDRAAVERAMERTGVAQF--ADRPVT---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 162 EISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSrGLGLIFISHDINLVRSFCDRVLVMYAGRV 241
Cdd:PRK09536 139 SLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
46-250 |
3.41e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 79.78 E-value: 3.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 46 AIVGESGSGKSTvgraLLQ-----LHPKKARVSASRMQFANLDllhlTEAQMRGVRgKRISMIMQDPKYSLNPVVcVGKQ 120
Cdd:PRK13643 36 ALIGHTGSGKST----LLQhlnglLQPTEGKVTVGDIVVSSTS----KQKEIKPVR-KKVGVVFQFPESQLFEET-VLKD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 121 IAeaWLTHHPG-RKDEAKAKALEMLEVVRIRQpeRVYQLYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRL 199
Cdd:PRK13643 106 VA--FGPQNFGiPKEKAEKIAAEKLEMVGLAD--EFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 503996112 200 QVLGLLDDLVQSrGLGLIFISHDINLVRSFCDRVLVMYAGRVVESIAACDL 250
Cdd:PRK13643 182 EMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
34-244 |
3.97e-17 |
|
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: 78.35 E-value: 3.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 34 RGVSFQL-GREKLAIVGESGSGKSTVGRALLQLH-PKKARVSasrmqfanLDLLHLTEAQMRGVRGKrISMIMQDP---- 107
Cdd:cd03249 20 KGLSLTIpPGKTVALVGSSGCGKSTVVSLLERFYdPTSGEIL--------LDGVDIRDLNLRWLRSQ-IGLVSQEPvlfd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 108 -------KYSLNPVVCVgkqiaeawlthhpgrKDEAKAKALEMLEVVrIRQPERVY-QLYPH--EISGGQGQRIMIAMML 177
Cdd:cd03249 91 gtiaeniRYGKPDATDE---------------EVEEAAKKANIHDFI-MSLPDGYDtLVGERgsQLSGGQKQRIAIARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503996112 178 ITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRglGLIFISHDINLVRSfCDRVLVMYAGRVVES 244
Cdd:cd03249 155 LRNPKILLLDEATSALDAESEKLVQEALDRAMKGR--TTIVIAHRLSTIRN-ADLIAVLQNGQVVEQ 218
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
33-274 |
4.02e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 78.90 E-value: 4.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 33 VRGVSFQLGREKL-AIVGESGSGKSTVGRALL-QLHPKKARVSasrmqFANLDLLHLTEAQMrgvrGKRISMImqdPKYS 110
Cdd:PRK11231 18 LNDLSLSLPTGKItALIGPNGCGKSTLLKCFArLLTPQSGTVF-----LGDKPISMLSSRQL----ARRLALL---PQHH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 111 LNPV-VCVGKQIA---EAWLTHHpGR---KDEAK-AKALEMLEVVRIRQpERVYQLypheiSGGQGQRIMIAMMLITDPE 182
Cdd:PRK11231 86 LTPEgITVRELVAygrSPWLSLW-GRlsaEDNARvNQAMEQTRINHLAD-RRLTDL-----SGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 183 LIIADEPTSALDVSVRLQVLGLLDDLvQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVESIAACDLdnarhpYTQGLI 262
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMREL-NTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV------MTPGLL 231
|
250
....*....|....*
gi 503996112 263 NSLPDMQ---HRRPI 274
Cdd:PRK11231 232 RTVFDVEaeiHPEPV 246
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-236 |
4.51e-17 |
|
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: 80.79 E-value: 4.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 3 SSIPAANNAPLLDVRDLCVDFVNGSAV----THAVRGVSFQL-GREKLAIVGESGSGKSTVGRALLQLhpkkARVSASRM 77
Cdd:TIGR02857 304 APRPLAGKAPVTAAPASSLEFSGVSVAypgrRPALRPVSFTVpPGERVALVGPSGAGKSTLLNLLLGF----VDPTEGSI 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 78 QFANLDLLHLTEAQMRgvrgKRISMIMQDPkyslnpvVCVGKQIAEAWLTHHPGRKDEAKAKALE---MLEVVRIRQPER 154
Cdd:TIGR02857 380 AVNGVPLADADADSWR----DQIAWVPQHP-------FLFAGTIAENIRLARPDASDAEIREALEragLDEFVAALPQGL 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 155 VYQLYPH--EISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRglGLIFISHDINLVRSfCDR 232
Cdd:TIGR02857 449 DTPIGEGgaGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR--TVLLVTHRLALAAL-ADR 525
|
....
gi 503996112 233 VLVM 236
Cdd:TIGR02857 526 IVVL 529
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
32-242 |
5.50e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 79.36 E-value: 5.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 32 AVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQL-------------HPKKARVSASRMQFANLDLLHLTEA----QMR 93
Cdd:PRK13651 22 ALDNVSVEINQgEFIAIIGQTGSGKTTFIEHLNALllpdtgtiewifkDEKNKKKTKEKEKVLEKLVIQKTRFkkikKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 94 GVRgKRISMIMQDPKYSLNpvvcvgKQIAEAWLTHHP---G-RKDEAKAKALEMLEVVRIrqPERVYQLYPHEISGGQGQ 169
Cdd:PRK13651 102 EIR-RRVGVVFQFAEYQLF------EQTIEKDIIFGPvsmGvSKEEAKKRAAKYIELVGL--DESYLQRSPFELSGGQKR 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503996112 170 RIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSrGLGLIFISHDINLVRSFCDRVLVMYAGRVV 242
Cdd:PRK13651 173 RVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKII 244
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
36-244 |
6.30e-17 |
|
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: 79.76 E-value: 6.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 36 VSFQL-GREKLAIVGESGSGKSTVGRALLQLHpkkaRVSASRMQFANLDLLHLTEAQMRGVRGKRISMIMQDPkySLNPv 114
Cdd:COG4148 18 VDFTLpGRGVTALFGPSGSGKTTLLRAIAGLE----RPDSGRIRLGGEVLQDSARGIFLPPHRRRIGYVFQEA--RLFP- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 115 vcvgkqiaeaWLT--------HHPGRKDEAKAKALEMLEVVRIrqpERVYQLYPHEISGGQGQRIMIAMMLITDPELIIA 186
Cdd:COG4148 91 ----------HLSvrgnllygRKRAPRAERRISFDEVVELLGI---GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503996112 187 DEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVES 244
Cdd:COG4148 158 DEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVAS 215
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
43-241 |
6.86e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 79.36 E-value: 6.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 43 EKLAIVGESGSGKSTVGRALLQLHPKkarvSASRMQFANLDLLHLTeaqmrgVRGKRISMIMQDpkYSLNPVVCVGKQIA 122
Cdd:PRK10851 29 QMVALLGPSGSGKTTLLRIIAGLEHQ----TSGHIRFHGTDVSRLH------ARDRKVGFVFQH--YALFRHMTVFDNIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 123 EAwLTHHPGRK----DEAKAKALEMLEVVrirQPERVYQLYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVR 198
Cdd:PRK10851 97 FG-LTVLPRRErpnaAAIKAKVTQLLEMV---QLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVR 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 503996112 199 LQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRV 241
Cdd:PRK10851 173 KELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
43-244 |
6.95e-17 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 80.56 E-value: 6.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 43 EKLAIVGESGSGKSTVGRALLQLH-PKKARVSASRMQFANLDllhltEAQMRgvrgKRISMIMQDPkyslnpvVCVGKQI 121
Cdd:TIGR01846 484 EFIGIVGPSGSGKSTLTKLLQRLYtPQHGQVLVDGVDLAIAD-----PAWLR----RQMGVVLQEN-------VLFSRSI 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 122 AEAWLTHHPGRKDE---AKAKALEMLEVVrIRQPERvYQLYPHE----ISGGQGQRIMIAMMLITDPELIIADEPTSALD 194
Cdd:TIGR01846 548 RDNIALCNPGAPFEhviHAAKLAGAHDFI-SELPQG-YNTEVGEkganLSGGQRQRIAIARALVGNPRILIFDEATSALD 625
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503996112 195 VSVRLQVLGLLDDLvqSRGLGLIFISHDINLVRSfCDRVLVMYAGRVVES 244
Cdd:TIGR01846 626 YESEALIMRNMREI--CRGRTVIIIAHRLSTVRA-CDRIIVLEKGQIAES 672
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-259 |
7.22e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 78.03 E-value: 7.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 14 LDVRDLCVDFVNgsavTHAVRGVSFQL-GREKLAIVGESGSGKSTVGRA---LLQLHPKkARVSASRMqFANLDLLHLTE 89
Cdd:PRK14247 4 IEIRDLKVSFGQ----VEVLDGVNLEIpDNTITALMGPSGSGKSTLLRVfnrLIELYPE-ARVSGEVY-LDGQDIFKMDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 90 AQMRgvrgKRISMIMQDPkyslNPVVCVgkqiaEAWLTHHPGRKDEAKAKALEMLEVvRIRQPERVYQLYPH-------- 161
Cdd:PRK14247 78 IELR----RRVQMVFQIP----NPIPNL-----SIFENVALGLKLNRLVKSKKELQE-RVRWALEKAQLWDEvkdrldap 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 162 --EISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLvqSRGLGLIFISHDINLVRSFCDRVLVMYAG 239
Cdd:PRK14247 144 agKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARISDYVAFLYKG 221
|
250 260
....*....|....*....|.
gi 503996112 240 RVVESIAACDL-DNARHPYTQ 259
Cdd:PRK14247 222 QIVEWGPTREVfTNPRHELTE 242
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
32-243 |
8.62e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 78.51 E-value: 8.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 32 AVRGVSFQLGREKLA-IVGESGSGKST---VGRALLQLHPKKARVSASRMQfANLDLLHlteaQMRGVRgKRISMIMQDP 107
Cdd:PRK13645 26 ALNNTSLTFKKNKVTcVIGTTGSGKSTmiqLTNGLIISETGQTIVGDYAIP-ANLKKIK----EVKRLR-KEIGLVFQFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 108 KYSLNPVVcVGKQIAEAWLtHHPGRKDEAKAKALEMLEVVRIrqPERVYQLYPHEISGGQGQRIMIAMMLITDPELIIAD 187
Cdd:PRK13645 100 EYQLFQET-IEKDIAFGPV-NLGENKQEAYKKVPELLKLVQL--PEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503996112 188 EPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVE 243
Cdd:PRK13645 176 EPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVIS 231
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
30-254 |
1.01e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 78.23 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 30 THAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQ-LHPKKARVSasrmqfanLDLLHLTEAQMRGV------RGkris 101
Cdd:COG4152 14 KTAVDDVSFTVPKgEIFGLLGPNGAGKTTTIRIILGiLAPDSGEVL--------WDGEPLDPEDRRRIgylpeeRG---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 102 mimqdpkysLNPVVCVGKQIAeaWLthhpGR-----KDEAKAKALEMLEVVRI--RQPERVYQLypheiSGGQGQRIMIA 174
Cdd:COG4152 82 ---------LYPKMKVGEQLV--YL----ARlkglsKAEAKRRADEWLERLGLgdRANKKVEEL-----SKGNQQKVQLI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 175 MMLITDPELIIADEPTSALD-VSVRLqVLGLLDDLVQsRGLGLIFISHDINLVRSFCDRVLVMYAGRVVesiAACDLDNA 253
Cdd:COG4152 142 AALLHDPELLILDEPFSGLDpVNVEL-LKDVIRELAA-KGTTVIFSSHQMELVEELCDRIVIINKGRKV---LSGSVDEI 216
|
.
gi 503996112 254 R 254
Cdd:COG4152 217 R 217
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
21-242 |
1.02e-16 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 79.91 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 21 VDFVNGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHpkkaRVSASRMQFANLDLLHLTEAQMRgvrgKR 99
Cdd:TIGR03375 469 VSFAYPGQETPALDNVSLTIRPgEKVAIIGRIGSGKSTLLKLLLGLY----QPTEGSVLLDGVDIRQIDPADLR----RN 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 100 ISMIMQDPKY---SLNPVVCVGKQIAEawlthhpgrkDEakakalEMLEVVRIRQPERVYQLYPH-----------EISG 165
Cdd:TIGR03375 541 IGYVPQDPRLfygTLRDNIALGAPYAD----------DE------EILRAAELAGVTEFVRRHPDgldmqigergrSLSG 604
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503996112 166 GQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRglGLIFISHDINLVrSFCDRVLVMYAGRVV 242
Cdd:TIGR03375 605 GQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGK--TLVLVTHRTSLL-DLVDRIIVMDNGRIV 678
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
33-224 |
1.06e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 76.75 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 33 VRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPkkARVSAS-RMQFANLDLLHL-TEAqmrgvrgKRISMIMQDPKy 109
Cdd:COG4136 17 LAPLSLTVAPgEILTLMGPSGSGKSTLLAAIAGTLS--PAFSASgEVLLNGRRLTALpAEQ-------RRIGILFQDDL- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 110 sLNPVVCVGKQIAEAwLTHHPGRKdEAKAKALEMLEVVRIrqpERVYQLYPHEISGGQGQRIMIAMMLITDPELIIADEP 189
Cdd:COG4136 87 -LFPHLSVGENLAFA-LPPTIGRA-QRRARVEQALEEAGL---AGFADRDPATLSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190
....*....|....*....|....*....|....*
gi 503996112 190 TSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDIN 224
Cdd:COG4136 161 FSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEE 195
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-241 |
1.11e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 79.59 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 1 MTSSIPAANNAP---LLDVRDL-CVDFVNgsavTHA--VRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHP--KKAR 71
Cdd:PRK13549 244 LTALYPREPHTIgevILEVRNLtAWDPVN----PHIkrVDDVSFSLRRgEILGIAGLVGAGRTELVQCLFGAYPgrWEGE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 72 VsasRMQFANLDLLHLTEAQMRGvrgkrISMIMQDPK-YSLNPVVCVGKQIAEAWLTH--HPGRKDEAK--AKALEMLEV 146
Cdd:PRK13549 320 I---FIDGKPVKIRNPQQAIAQG-----IAMVPEDRKrDGIVPVMGVGKNITLAALDRftGGSRIDDAAelKTILESIQR 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 147 VRIRQPE---RVYQLypheiSGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQsRGLGLIFISHDI 223
Cdd:PRK13549 392 LKVKTASpelAIARL-----SGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQ-QGVAIIVISSEL 465
|
250
....*....|....*...
gi 503996112 224 NLVRSFCDRVLVMYAGRV 241
Cdd:PRK13549 466 PEVLGLSDRVLVMHEGKL 483
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
21-241 |
1.25e-16 |
|
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: 75.72 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 21 VDFVNGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQL-HPKKARVsasRMQFANLDLLHLTEaqmrgvRGK 98
Cdd:cd03246 6 VSFRYPGAEPPVLRNVSFSIEPgESLAIIGPSGSGKSTLARLILGLlRPTSGRV---RLDGADISQWDPNE------LGD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 99 RISMIMQDpkyslnpVVCVGKQIAEAWLthhpgrkdeakakalemlevvrirqpervyqlypheiSGGQGQRIMIAMMLI 178
Cdd:cd03246 77 HVGYLPQD-------DELFSGSIAENIL-------------------------------------SGGQRQRLGLARALY 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503996112 179 TDPELIIADEPTSALDVSVRLQVLGLLDDLvQSRGLGLIFISHDINLVRSfCDRVLVMYAGRV 241
Cdd:cd03246 113 GNPRILVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
31-244 |
1.33e-16 |
|
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: 76.88 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 31 HAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPkkarVSASRMQFANLDLLHLTEAQMRgvrgKRISMIMQDPkY 109
Cdd:cd03254 17 PVLKDINFSIKPgETVAIVGPTGAGKTTLINLLMRFYD----PQKGQILIDGIDIRDISRKSLR----SMIGVVLQDT-F 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 110 SLNpvvcvgKQIAEAWLTHHPGRKDE---AKAKALEMLEVvrIRQPERVYQLYPHE----ISGGQGQRIMIAMMLITDPE 182
Cdd:cd03254 88 LFS------GTIMENIRLGRPNATDEeviEAAKEAGAHDF--IMKLPNGYDTVLGEnggnLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503996112 183 LIIADEPTSALDVSVRLQVLGLLDDLVQSRglGLIFISHDINLVRsFCDRVLVMYAGRVVES 244
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGR--TSIIIAHRLSTIK-NADKILVLDDGKIIEE 218
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
163-242 |
1.39e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.52 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 163 ISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVV 242
Cdd:PRK10575 148 LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMI 227
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
32-244 |
1.55e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 78.35 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 32 AVRGVSFQLGREKL-AIVGESGSGKST-VGRALLQLHPKKARV------SASRMQFANLDLLHLTEAQMRGVR-GKRISM 102
Cdd:PRK13631 41 ALNNISYTFEKNKIyFIIGNSGSGKSTlVTHFNGLIKSKYGTIqvgdiyIGDKKNNHELITNPYSKKIKNFKElRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 103 IMQDPKYSLNpvvcvgKQIAEAWLTHHP----GRKDEAKAKALEMLEVVRIRQP--ERvyqlYPHEISGGQGQRIMIAMM 176
Cdd:PRK13631 121 VFQFPEYQLF------KDTIEKDIMFGPvalgVKKSEAKKLAKFYLNKMGLDDSylER----SPFGLSGGQKRRVAIAGI 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503996112 177 LITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSrGLGLIFISHDINLVRSFCDRVLVMYAGRVVES 244
Cdd:PRK13631 191 LAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKT 257
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
32-242 |
1.85e-16 |
|
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: 76.60 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 32 AVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQ-LHPKKARVSAS-------RMQFAnldllhlteAQMRGVRGKRISM 102
Cdd:cd03267 36 ALKGISFTIEKgEIVGFIGPNGAGKTTTLKILSGlLQPTSGEVRVAglvpwkrRKKFL---------RRIGVVFGQKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 103 IMQDPkyslnpvvcvgkqIAEAWLTHH------PGRKDEAKAKALEMLEVVRI-RQPERvyqlyphEISGGQGQRIMIAM 175
Cdd:cd03267 107 WWDLP-------------VIDSFYLLAaiydlpPARFKKRLDELSELLDLEELlDTPVR-------QLSLGQRMRAEIAA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503996112 176 MLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVV 242
Cdd:cd03267 167 ALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
8-243 |
2.28e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 77.10 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 8 ANNAPLLDVRDlcVDFVNGSAVTHAVRGVSFQLGREK-LAIVGESGSGKSTVGRALLQLHpkkaRVSASRMQFANLdllH 86
Cdd:PRK13648 2 EDKNSIIVFKN--VSFQYQSDASFTLKDVSFNIPKGQwTSIVGHNGSGKSTIAKLMIGIE----KVKSGEIFYNNQ---A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 87 LTEAQMRGVRgKRISMIMQDPKyslNPVVCVGKQIAEAW-LTHHPGRKDEAK---AKALEMLEVVRIRQPErvyqlyPHE 162
Cdd:PRK13648 73 ITDDNFEKLR-KHIGIVFQNPD---NQFVGSIVKYDVAFgLENHAVPYDEMHrrvSEALKQVDMLERADYE------PNA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 163 ISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSfCDRVLVMYAGRVV 242
Cdd:PRK13648 143 LSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVY 221
|
.
gi 503996112 243 E 243
Cdd:PRK13648 222 K 222
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
26-242 |
2.93e-16 |
|
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: 75.62 E-value: 2.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 26 GSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPKkarvSASRMQFANLDLLhlteAQMRGVRgKRISMIM 104
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKgEIFGLLGHNGAGKTTTLKMLTGELRP----TSGTAYINGYSIR----TDRKAAR-QSLGYCP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 105 QDpkySLNPVVCVGKQIAE--AWLTHHPgrKDEAKAKALEMLEVVRIRQPE--RVYQLypheiSGGQGQRIMIAMMLITD 180
Cdd:cd03263 82 QF---DALFDELTVREHLRfyARLKGLP--KSEIKEEVELLLRVLGLTDKAnkRARTL-----SGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503996112 181 PELIIADEPTSALDVSVRLQVLGLLDDLVQSRglGLIFISHDINLVRSFCDRVLVMYAGRVV 242
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
43-243 |
4.45e-16 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 77.34 E-value: 4.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 43 EKLAIVGESGSGKSTVGRALLQLhpKKARVSASRMQFANLDLLHLTEAQmrgvrgKRISMIMQDpkYSLNPVVCVGKQIA 122
Cdd:TIGR03258 32 ELLALIGKSGCGKTTLLRAIAGF--VKAAGLTGRIAIADRDLTHAPPHK------RGLALLFQN--YALFPHLKVEDNVA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 123 EAWLTHHPGRKDEAKakalemlevvRIRQPERVYQL------YPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVS 196
Cdd:TIGR03258 102 FGLRAQKMPKADIAE----------RVADALKLVGLgdaaahLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSALDAN 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503996112 197 VRLQVLGLLDDLVQS-RGLGLIFISHDINLVRSFCDRVLVMYAGRVVE 243
Cdd:TIGR03258 172 IRANMREEIAALHEElPELTILCVTHDQDDALTLADKAGIMKDGRLAA 219
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
30-242 |
4.83e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 76.18 E-value: 4.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 30 THAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQL-HPKKARVSASRMQFANLdllhlteAQMRGVRgKRISMIMQDP 107
Cdd:PRK13644 15 TPALENINLVIKKgEYIGIIGKNGSGKSTLALHLNGLlRPQKGKVLVSGIDTGDF-------SKLQGIR-KLVGIVFQNP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 108 KYSLnpvvcVGKQIAEAwLTHHPG---------RKDEAKAKALEMLEVVRIRQPErvyqlyphEISGGQGQRIMIAMMLI 178
Cdd:PRK13644 87 ETQF-----VGRTVEED-LAFGPEnlclppieiRKRVDRALAEIGLEKYRHRSPK--------TLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503996112 179 TDPELIIADEPTSALDVSVRLQVLGLLDDLvQSRGLGLIFISHDINLVRSfCDRVLVMYAGRVV 242
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKL-HEKGKTIVYITHNLEELHD-ADRIIVMDRGKIV 214
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
33-241 |
5.40e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 77.56 E-value: 5.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 33 VRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPKKARVSASrMQFANLDLLHLTEAQMRGvrgkrISMIMQDPK-YS 110
Cdd:TIGR02633 276 VDDVSFSLRRgEILGVAGLVGAGRTELVQALFGAYPGKFEGNVF-INGKPVDIRNPAQAIRAG-----IAMVPEDRKrHG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 111 LNPVVCVGKQIAEAWLTHHP--GRKDEAKAKALEMLEVVRIRQPERVYQLYPHEISGGQGQRIMIAMMLITDPELIIADE 188
Cdd:TIGR02633 350 IVPILGVGKNITLSVLKSFCfkMRIDAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503996112 189 PTSALDVSVRLQVLGLLDDLVQsRGLGLIFISHDINLVRSFCDRVLVMYAGRV 241
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLAQ-EGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
11-242 |
7.44e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 77.46 E-value: 7.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 11 APLLDVRDLCVDFVNGSAVTHAVRGVSFQL-GREKLAIVGESGSGKSTVGRALLQLHpkkaRVSASRMQFANLDLLHLTE 89
Cdd:PRK10535 2 TALLELKDIRRSYPSGEEQVEVLKGISLDIyAGEMVAIVGASGSGKSTLMNILGCLD----KPTSGTYRVAGQDVATLDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 90 AQMRGVRGKRISMIMQdpKYSLNPVVcVGKQIAEAWLTHHPGRKDEAKAKALEMLevVRIRQPERV-YQlyPHEISGGQG 168
Cdd:PRK10535 78 DALAQLRREHFGFIFQ--RYHLLSHL-TAAQNVEVPAVYAGLERKQRLLRAQELL--QRLGLEDRVeYQ--PSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503996112 169 QRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLvQSRGLGLIFISHDiNLVRSFCDRVLVMYAGRVV 242
Cdd:PRK10535 151 QRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIV 222
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
32-243 |
7.71e-16 |
|
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: 74.45 E-value: 7.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 32 AVRGVSFQL-GREKLAIVGESGSGKSTVGRALLQLHPkkarVSASRMQFANLDLLHLTEAQMRgvrgKRISMIMQDP--- 107
Cdd:cd03244 19 VLKNISFSIkPGEKVGIVGRTGSGKSSLLLALFRLVE----LSSGSILIDGVDISKIGLHDLR----SRISIIPQDPvlf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 108 ----KYSLNPvvcvgkqiaeawLTHHPgrkDEAKAKALE---MLEVVRirqpERVYQLYPHEISGG----QGQR--IMIA 174
Cdd:cd03244 91 sgtiRSNLDP------------FGEYS---DEELWQALErvgLKEFVE----SLPGGLDTVVEEGGenlsVGQRqlLCLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503996112 175 MMLITDPELIIADEPTSALDVSvrlqvlglLDDLVQS------RGLGLIFISHDINLVRSfCDRVLVMYAGRVVE 243
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPE--------TDALIQKtireafKDCTVLTIAHRLDTIID-SDRILVLDKGRVVE 217
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
43-241 |
1.80e-15 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 73.36 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 43 EKLAIVGESGSGKSTvgraLLQL-----HPKKARVSASrmqfanlDLLHLTEAQMRgvrgKRISMIMQDpkYSLNPVVCV 117
Cdd:TIGR01277 25 EIVAIMGPSGAGKST----LLNLiagfiEPASGSIKVN-------DQSHTGLAPYQ----RPVSMLFQE--NNLFAHLTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 118 GKQIAeawLTHHPGRKDEAKAKAlEMLEVVRIRQPERVYQLYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSV 197
Cdd:TIGR01277 88 RQNIG---LGLHPGLKLNAEQQE-KVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 503996112 198 RLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRV 241
Cdd:TIGR01277 164 REEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
11-252 |
1.83e-15 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 73.86 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 11 APLLDVRDLCVdFVNGSavtHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPkkarVSASRMQFANLDLLHL-T 88
Cdd:COG0410 1 MPMLEVENLHA-GYGGI---HVLHGVSLEVEEgEIVALLGRNGAGKTTLLKAISGLLP----PRSGSIRFDGEDITGLpP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 89 EAQMRgvRGkrISMIMQdpkyslnpvvcvGKQI------AE-----AWLthhpgRKDEAKAKAlemlevvrirQPERVYQ 157
Cdd:COG0410 73 HRIAR--LG--IGYVPE------------GRRIfpsltvEEnlllgAYA-----RRDRAEVRA----------DLERVYE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 158 LYPH----------EISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLvQSRGLGLIFISHDINLVR 227
Cdd:COG0410 122 LFPRlkerrrqragTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFAL 200
|
250 260
....*....|....*....|....*
gi 503996112 228 SFCDRVLVMYAGRVVESIAACDLDN 252
Cdd:COG0410 201 EIADRAYVLERGRIVLEGTAAELLA 225
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
32-250 |
1.90e-15 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 76.28 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 32 AVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLH-PKKARVSasrmqfanLDLLHLTEAQMRGVRgKRISMIMQDPKY 109
Cdd:TIGR02204 355 ALDGLNLTVRPgETVALVGPSGAGKSTLFQLLLRFYdPQSGRIL--------LDGVDLRQLDPAELR-ARMALVPQDPVL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 110 SLNPVVcvgKQIAEawlthhpGRKD------EAKAKALEMLEVvrIRQPERVYQLYPHE----ISGGQGQRIMIAMMLIT 179
Cdd:TIGR02204 426 FAASVM---ENIRY-------GRPDatdeevEAAARAAHAHEF--ISALPEGYDTYLGErgvtLSGGQRQRIAIARAILK 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503996112 180 DPELIIADEPTSALDVSVRLQVLGLLDDLVQSRglGLIFISHDINLVRSfCDRVLVMYAGRVVES------IAACDL 250
Cdd:TIGR02204 494 DAPILLLDEATSALDAESEQLVQQALETLMKGR--TTLIIAHRLATVLK-ADRIVVMDQGRIVAQgthaelIAKGGL 567
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
33-244 |
2.14e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 73.96 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 33 VRGVSFQLGREKL-AIVGESGSGKST----VGRallqLHPKkarvSASRMQFANLDLlhlteAQMRG-VRGKRISMIMQD 106
Cdd:COG4604 17 LDDVSLTIPKGGItALIGPNGAGKSTllsmISR----LLPP----DSGEVLVDGLDV-----ATTPSrELAKRLAILRQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 107 PKYSLNpvvcvgkqiaeawLT-----------HHPGR---KDEAK-AKALEMLEVVRIRqpERvyqlYPHEISGGQGQRI 171
Cdd:COG4604 84 NHINSR-------------LTvrelvafgrfpYSKGRltaEDREIiDEAIAYLDLEDLA--DR----YLDELSGGQRQRA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503996112 172 MIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVES 244
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQ 217
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
13-242 |
2.75e-15 |
|
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: 73.17 E-value: 2.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 13 LLDVRDLCVDFVNGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLhpkkARVSASRMQFANLDLLHLTEAQ 91
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPgEVTGLLGPNGAGKTTTLRMLAGL----LEPDAGFATVDGFDVVKEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 92 MRGV------RG--KRISmimqdpkyslnpvvcvGKQIAEAWLTHHPGRKDEAKAKALEMLEVVRIRQ--PERVyqlypH 161
Cdd:cd03266 77 RRRLgfvsdsTGlyDRLT----------------ARENLEYFAGLYGLKGDELTARLEELADRLGMEEllDRRV-----G 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 162 EISGGQGQRIMIAMMLITDPELIIADEPTSALDVsvrLQVLGLLDDLVQSRGLG--LIFISHDINLVRSFCDRVLVMYAG 239
Cdd:cd03266 136 GFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV---MATRALREFIRQLRALGkcILFSTHIMQEVERLCDRVVVLHRG 212
|
...
gi 503996112 240 RVV 242
Cdd:cd03266 213 RVV 215
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
43-241 |
3.89e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 74.60 E-value: 3.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 43 EKLAIVGESGSGKSTVGRALLQLHpkkaRVSASRMQFANLDLLHLTeAQMRGVrgkriSMIMQDpkYSLNPVVCVGKQIA 122
Cdd:PRK09452 41 EFLTLLGPSGCGKTTVLRLIAGFE----TPDSGRIMLDGQDITHVP-AENRHV-----NTVFQS--YALFPHMTVFENVA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 123 EAwLTHHPGRKDEAKAKALEMLEVVRIrqpERVYQLYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVL 202
Cdd:PRK09452 109 FG-LRMQKTPAAEITPRVMEALRMVQL---EEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQ 184
|
170 180 190
....*....|....*....|....*....|....*....
gi 503996112 203 GLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRV 241
Cdd:PRK09452 185 NELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
43-242 |
5.03e-15 |
|
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: 72.14 E-value: 5.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 43 EKLAIVGESGSGKSTvgraLLQLHPKKARVSASRMQFANLDLLHLTEAQmrgvrgKRISMIMQDPkySLNPVVCVGKQIA 122
Cdd:cd03298 25 EITAIVGPSGSGKST----LLNLIAGFETPQSGRVLINGVDVTAAPPAD------RPVSMLFQEN--NLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 123 eawLTHHPG-------RKDEAKAKALEMLEVVRIRQPErvyqlyphEISGGQGQRIMIAMMLITDPELIIADEPTSALDV 195
Cdd:cd03298 93 ---LGLSPGlkltaedRQAIEVALARVGLAGLEKRLPG--------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 503996112 196 SVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVV 242
Cdd:cd03298 162 ALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-240 |
5.84e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 73.71 E-value: 5.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 4 SIPAANNAPLLDVRDLCVDFVN------GSAVthaVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLH---------- 66
Cdd:PRK13536 25 GISEAKASIPGSMSTVAIDLAGvsksygDKAV---VNGLSFTVASgECFGLLGPNGAGKSTIARMILGMTspdagkitvl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 67 ----PKKARVSASRM----QFANLDLlHLTEAQMRGVRGKRISMimqdpkyslnpvvcvgkqiaeawlthhPGRKDEAKA 138
Cdd:PRK13536 102 gvpvPARARLARARIgvvpQFDNLDL-EFTVRENLLVFGRYFGM---------------------------STREIEAVI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 139 KALemLEVVRIrqpERVYQLYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVqSRGLGLIF 218
Cdd:PRK13536 154 PSL--LEFARL---ESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLL-ARGKTILL 227
|
250 260
....*....|....*....|..
gi 503996112 219 ISHDINLVRSFCDRVLVMYAGR 240
Cdd:PRK13536 228 TTHFMEEAERLCDRLCVLEAGR 249
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
10-251 |
5.93e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.58 E-value: 5.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 10 NAPLLDVRDLCVDFvngSAVThAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPK-----KARVSASRMQFANL- 82
Cdd:PRK13549 2 MEYLLEMKNITKTF---GGVK-ALDNVSLKVRAgEIVSLCGENGAGKSTLMKVLSGVYPHgtyegEIIFEGEELQASNIr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 83 DllhlTEAqmrgvrgKRISMIMQDpkYSLNPVVCVGKQI---AEawLTHHpGRKDEAK--AKALEMLEVVR--IRQPERV 155
Cdd:PRK13549 78 D----TER-------AGIAIIHQE--LALVKELSVLENIflgNE--ITPG-GIMDYDAmyLRAQKLLAQLKldINPATPV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 156 YQLypheiSGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLvQSRGLGLIFISHDINLVRSFCDRVLV 235
Cdd:PRK13549 142 GNL-----GLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICV 215
|
250
....*....|....*.
gi 503996112 236 MYAGRVVESIAACDLD 251
Cdd:PRK13549 216 IRDGRHIGTRPAAGMT 231
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
43-244 |
6.59e-15 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 74.78 E-value: 6.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 43 EKLAIVGESGSGKSTVGRALLQLH-PKKARVSASRMQFANLDllhlteaqmRGVRGKRISMIMQDPkyslnpVVCVGKQI 121
Cdd:TIGR01193 501 SKTTIVGMSGSGKSTLAKLLVGFFqARSGEILLNGFSLKDID---------RHTLRQFINYLPQEP------YIFSGSIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 122 AEAWLTHHPGRKDEAKAKALEMLEV-VRIRQPERVYQ--LYPH--EISGGQGQRIMIAMMLITDPELIIADEPTSALDVS 196
Cdd:TIGR01193 566 ENLLLGAKENVSQDEIWAACEIAEIkDDIENMPLGYQteLSEEgsSISGGQKQRIALARALLTDSKVLILDESTSNLDTI 645
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503996112 197 VRLQVlglLDDLVQSRGLGLIFISHDINlVRSFCDRVLVMYAGRVVES 244
Cdd:TIGR01193 646 TEKKI---VNNLLNLQDKTIIFVAHRLS-VAKQSDKIIVLDHGKIIEQ 689
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
46-241 |
8.64e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 72.40 E-value: 8.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 46 AIVGESGSGKSTVGRALLQL-HPKKARVSASRMQfanldllhLTEAQmrgvrgKRISMIMQDPKysLNPVVCVgkqIAEA 124
Cdd:PRK11247 42 AVVGRSGCGKSTLLRLLAGLeTPSAGELLAGTAP--------LAEAR------EDTRLMFQDAR--LLPWKKV---IDNV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 125 WLthhpGRKDEAKAKALEMLEVVRI--RQPErvyqlYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVL 202
Cdd:PRK11247 103 GL----GLKGQWRDAALQALAAVGLadRANE-----WPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQ 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 503996112 203 GLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRV 241
Cdd:PRK11247 174 DLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
23-242 |
9.09e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 73.93 E-value: 9.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 23 FVNGSAVTHAVRGVS--FQLGrEKLAIVGESGSGKSTVGRALLQLHPKKARVSASRMqfanLDLLHLTEAQMRgvrgKRI 100
Cdd:TIGR00955 31 FCRERPRKHLLKNVSgvAKPG-ELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVL----LNGMPIDAKEMR----AIS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 101 SMIMQDPKYslnpvvcVGKQIAEAWLT-------HHPGRKDEAKAKALEMLEVV--------RIRQPERVYQLypheiSG 165
Cdd:TIGR00955 102 AYVQQDDLF-------IPTLTVREHLMfqahlrmPRRVTKKEKRERVDEVLQALglrkcantRIGVPGRVKGL-----SG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 166 GQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFI---SHDInlvrsFC--DRVLVMYAGR 240
Cdd:TIGR00955 170 GERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIhqpSSEL-----FElfDKIILMAEGR 244
|
..
gi 503996112 241 VV 242
Cdd:TIGR00955 245 VA 246
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
9-253 |
1.38e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 73.52 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 9 NNAPLLDVRDLCVDFvnGSavTHAVRGVSFQLGR-EKLAIVGESGSGKSTV-----Grallqlhpkkarvsasrmqfanl 82
Cdd:COG3845 1 MMPPALELRGITKRF--GG--VVANDDVSLTVRPgEIHALLGENGAGKSTLmkilyG----------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 83 dLLHLTEAQMRgVRGKR-------------ISMIMQDPKysLNPVVCVGKQIAEAWLTHHPGRKDEAKAKAlemlevvRI 149
Cdd:COG3845 54 -LYQPDSGEIL-IDGKPvrirsprdaialgIGMVHQHFM--LVPNLTVAENIVLGLEPTKGGRLDRKAARA-------RI 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 150 RQPERVYQL------YPHEISGGQGQRIMIAMMLITDPELIIADEPTSAL-----DvsvrlQVLGLLDDLVqSRGLGLIF 218
Cdd:COG3845 123 RELSERYGLdvdpdaKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLtpqeaD-----ELFEILRRLA-AEGKSIIF 196
|
250 260 270
....*....|....*....|....*....|....*
gi 503996112 219 ISHDINLVRSFCDRVLVMYAGRVVESIAACDLDNA 253
Cdd:COG3845 197 ITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEE 231
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
31-243 |
1.45e-14 |
|
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: 71.02 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 31 HAVRGVSFQLGR-EKLAIVGESGSGKSTvgraLLQL-----HPKKARVSasrmqfanldllhlteaqmrgVRGKRISMIm 104
Cdd:cd03220 36 WALKDVSFEVPRgERIGLIGRNGAGKST----LLRLlagiyPPDSGTVT---------------------VRGRVSSLL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 105 qDPKYSLNP-------VVCVGkqiaeAWLTHhpgRKDEAKAKALEMLEVV----RIRQPERVYqlypheiSGGQGQRIMI 173
Cdd:cd03220 90 -GLGGGFNPeltgrenIYLNG-----RLLGL---SRKEIDEKIDEIIEFSelgdFIDLPVKTY-------SSGMKARLAF 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 174 AMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQsRGLGLIFISHDINLVRSFCDRVLVMYAGRVVE 243
Cdd:cd03220 154 AIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLK-QGKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-243 |
1.47e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 71.61 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 1 MTSSIPAANNAplLDVRDLCVDFVNgsavTHAVRGVSFQLGREK-LAIVGESGSGKSTVGRAL---LQLHPKkARVSAsR 76
Cdd:COG1117 1 MTAPASTLEPK--IEVRNLNVYYGD----KQALKDINLDIPENKvTALIGPSGCGKSTLLRCLnrmNDLIPG-ARVEG-E 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 77 MQFANLDLLH----LTEaqmrgVRgKRISMIMQDPkyslNPVVcvgKQIAE--AW-LTHHpGRKDEAKA-----KALEML 144
Cdd:COG1117 73 ILLDGEDIYDpdvdVVE-----LR-RRVGMVFQKP----NPFP---KSIYDnvAYgLRLH-GIKSKSELdeiveESLRKA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 145 ----EVV-RIRQPervyqlyPHEISGGQGQRIMIAMMLITDPELIIADEPTSALD-VSVrLQVLGLLDDLVQSrgLGLIF 218
Cdd:COG1117 139 alwdEVKdRLKKS-------ALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpIST-AKIEELILELKKD--YTIVI 208
|
250 260
....*....|....*....|....*
gi 503996112 219 ISHDINLVRSFCDRVLVMYAGRVVE 243
Cdd:COG1117 209 VTHNMQQAARVSDYTAFFYLGELVE 233
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-243 |
1.66e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 73.34 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 6 PAANNAPL-LDVRDLCVDFVNGSAVTHAVrgvSFQL-GREKLAIVGESGSGKSTVGRALLQLHPKKARVSASRMQFANLD 83
Cdd:PRK11174 341 ELASNDPVtIEAEDLEILSPDGKTLAGPL---NFTLpAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKINGIELRELD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 84 LlhlteAQMRgvrgKRISMIMQDP---KYSLNPVVCVGK-QIAEAWLTHHPgrkdeAKAKALEMLEvvriRQPervyQLY 159
Cdd:PRK11174 418 P-----ESWR----KHLSWVGQNPqlpHGTLRDNVLLGNpDASDEQLQQAL-----ENAWVSEFLP----LLP----QGL 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 160 PHEI-------SGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLvqSRGLGLIFISHDINLVRSfCDR 232
Cdd:PRK11174 476 DTPIgdqaaglSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAA--SRRQTTLMVTHQLEDLAQ-WDQ 552
|
250
....*....|.
gi 503996112 233 VLVMYAGRVVE 243
Cdd:PRK11174 553 IWVMQDGQIVQ 563
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
31-252 |
2.62e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.51 E-value: 2.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 31 HAVRGVSFQL-GREKLAIVGESGSGKSTVGRALLQLH-PKKARVSASRMQFANLDllHLTEAQMRgvrgkrISMIMQDpk 108
Cdd:PRK09700 19 HALKSVNLTVyPGEIHALLGENGAGKSTLMKVLSGIHePTKGTITINNINYNKLD--HKLAAQLG------IGIIYQE-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 109 YSLNPVVCVGKQIaeaWLTHHPGRK---------DEAKAKALEMLEVVRIRQP--ERVYQLypheiSGGQGQRIMIAMML 177
Cdd:PRK09700 89 LSVIDELTVLENL---YIGRHLTKKvcgvniidwREMRVRAAMMLLRVGLKVDldEKVANL-----SISHKQMLEIAKTL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503996112 178 ITDPELIIADEPTSALDVSVRLQVLGLLDDLvQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVESIAACDLDN 252
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSN 234
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
30-241 |
3.01e-14 |
|
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: 70.19 E-value: 3.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 30 THAVRGVSFQLGREKL-AIVGESGSGKSTVGRALLQLH-PKKARVSasrmqfanLDLLHLTEAQMRGVRGKrISMIMQDP 107
Cdd:cd03248 27 TLVLQDVSFTLHPGEVtALVGPSGSGKSTVVALLENFYqPQGGQVL--------LDGKPISQYEHKYLHSK-VSLVGQEP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 108 KY---SLNPVVCVGKQIAEAWLTHHPGRKDEAKAKALEMLEVVRIRQPERVYQLypheiSGGQGQRIMIAMMLITDPELI 184
Cdd:cd03248 98 VLfarSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQL-----SGGQKQRVAIARALIRNPQVL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503996112 185 IADEPTSALDVSVRLQVLGLLDDLVQSRglGLIFISHDINLVRSfCDRVLVMYAGRV 241
Cdd:cd03248 173 ILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
31-242 |
4.22e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 69.90 E-value: 4.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 31 HAVRGVSFQLGREKLA-IVGESGSGKSTvgraLLQLHPKKARVSASRMQFANLDLLHLTEAQMRGVRgKRISMIMQDPKY 109
Cdd:PRK10908 16 QALQGVTFHMRPGEMAfLTGHSGAGKST----LLKLICGIERPSAGKIWFSGHDITRLKNREVPFLR-RQIGMIFQDHHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 110 SLNPVVCVGKQIAeawLTHHPGRKDEAKAKALEMLEVVRIRQPERVYqlyPHEISGGQGQRIMIAMMLITDPELIIADEP 189
Cdd:PRK10908 91 LMDRTVYDNVAIP---LIIAGASGDDIRRRVSAALDKVGLLDKAKNF---PIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503996112 190 TSALDVSVRLQVLGLLDDLvQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVV 242
Cdd:PRK10908 165 TGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
31-243 |
4.58e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 70.11 E-value: 4.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 31 HAVRGVSFQLGR-EKLAIVGESGSGKSTvgraLLQL-----HPKKARVSasrmqfanldllhlteaqmrgVRGkRISMIM 104
Cdd:COG1134 40 WALKDVSFEVERgESVGIIGRNGAGKST----LLKLiagilEPTSGRVE---------------------VNG-RVSALL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 105 Q-----DPKYSlnpvvcvgkqiaeawlthhpGR-------------KDEAKAKaleMLEVVR-------IRQPERVYqly 159
Cdd:COG1134 94 ElgagfHPELT--------------------GReniylngrllglsRKEIDEK---FDEIVEfaelgdfIDQPVKTY--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 160 pheiSGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQsRGLGLIFISHDINLVRSFCDRVLVMYAG 239
Cdd:COG1134 148 ----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRE-SGRTVIFVSHSMGAVRRLCDRAIWLEKG 222
|
....
gi 503996112 240 RVVE 243
Cdd:COG1134 223 RLVM 226
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
45-243 |
4.71e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 70.46 E-value: 4.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 45 LAIVGESGSGKSTVGRAL---LQLHPKKARVSASRMQFANlDLLHLTEAQMRgvrgKRISMIMQDPkySLNPVVCVGKQI 121
Cdd:PRK14246 39 FGIMGPSGSGKSTLLKVLnrlIEIYDSKIKVDGKVLYFGK-DIFQIDAIKLR----KEVGMVFQQP--NPFPHLSIYDNI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 122 AEAWLTHHPGRKDEAKAKALEMLEVV--------RIRQPERvyqlyphEISGGQGQRIMIAMMLITDPELIIADEPTSAL 193
Cdd:PRK14246 112 AYPLKSHGIKEKREIKKIVEECLRKVglwkevydRLNSPAS-------QLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503996112 194 DVSVRLQVLGLLDDLvqSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVE 243
Cdd:PRK14246 185 DIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVE 232
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
9-240 |
8.13e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 69.63 E-value: 8.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 9 NNAPLLDVRDLCVDFvnGSAVthAVRGVSFQLG-REKLAIVGESGSGKSTV------------GRALLQLHP-------K 68
Cdd:PRK11300 1 MSQPLLSVSGLMMRF--GGLL--AVNNVNLEVReQEIVSLIGPNGAGKTTVfncltgfykptgGTILLRGQHieglpghQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 69 KARVSASRMqFANLDLL-------HLTEAQMRGVRGKRISMIMQDPKYslnpvvcvgkqiaeawlthhpgRKDEAKA--K 139
Cdd:PRK11300 77 IARMGVVRT-FQHVRLFremtvieNLLVAQHQQLKTGLFSGLLKTPAF----------------------RRAESEAldR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 140 ALEMLEVVRIRQperVYQLYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFI 219
Cdd:PRK11300 134 AATWLERVGLLE---HANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLI 210
|
250 260
....*....|....*....|.
gi 503996112 220 SHDINLVRSFCDRVLVMYAGR 240
Cdd:PRK11300 211 EHDMKLVMGISDRIYVVNQGT 231
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
13-254 |
9.44e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 69.34 E-value: 9.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 13 LLDVRDLCVDFvngsAVTHAVRGVSFQLGREKLAIV-GESGSGKSTvgraLLQLHPKKARVSASRMQFANLDLLhlTEAQ 91
Cdd:PRK11248 1 MLQISHLYADY----GGKPALEDINLTLESGELLVVlGPSGCGKTT----LLNLIAGFVPYQHGSITLDGKPVE--GPGA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 92 MRGVrgkrismIMQD----PKYSLNPVVCVGKQIAEAwlthhpgRKDEAKAKALEMLEVVRIRQPErvyQLYPHEISGGQ 167
Cdd:PRK11248 71 ERGV-------VFQNegllPWRNVQDNVAFGLQLAGV-------EKMQRLEIAHQMLKKVGLEGAE---KRYIWQLSGGQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 168 GQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVrSFCDRVLVMYA---GRVVES 244
Cdd:PRK11248 134 RQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEA-VFMATELVLLSpgpGRVVER 212
|
250
....*....|
gi 503996112 245 IAacdLDNAR 254
Cdd:PRK11248 213 LP---LNFAR 219
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
12-243 |
1.19e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 69.03 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 12 PLLDVRDLCVDFVNgsavTHAVRGVSFQL-GREKLAIVGESGSGKSTVGRALLQ---LHPKKARVSASRMQFANLDLLHL 87
Cdd:PRK14239 4 PILQVSDLSVYYNK----KKALNSVSLDFyPNEITALIGPSGSGKSTLLRSINRmndLNPEVTITGSIVYNGHNIYSPRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 88 TEAQMRgvrgKRISMIMQDPK---YSLNPVVCVGKQIAEawlTHHPGRKDEAKAKALE---MLEVVRIRQPERVYQLyph 161
Cdd:PRK14239 80 DTVDLR----KEIGMVFQQPNpfpMSIYENVVYGLRLKG---IKDKQVLDEAVEKSLKgasIWDEVKDRLHDSALGL--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 162 eiSGGQGQRIMIAMMLITDPELIIADEPTSALD-VS---VRLQVLGLLDDLVqsrglgLIFISHDINLVRSFCDRVLVMY 237
Cdd:PRK14239 150 --SGGQQQRVCIARVLATSPKIILLDEPTSALDpISagkIEETLLGLKDDYT------MLLVTRSMQQASRISDRTGFFL 221
|
....*.
gi 503996112 238 AGRVVE 243
Cdd:PRK14239 222 DGDLIE 227
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
12-222 |
1.27e-13 |
|
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: 68.27 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 12 PLLDVRDLCVDFvNGSAVthaVRGVSFQLGR-EKLAIVGESGSGKSTvgraLLqlhpkkaRVSASrmqfanldLLHLTEA 90
Cdd:COG4133 1 MMLEAENLSCRR-GERLL---FSGLSFTLAAgEALALTGPNGSGKTT----LL-------RILAG--------LLPPSAG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 91 QMRgVRGKRISMIMQDPKYSLnpvvcvgkqiaeAWLTHHPGRKDE------------------AKAKALEMLEVVRI--R 150
Cdd:COG4133 58 EVL-WNGEPIRDAREDYRRRL------------AYLGHADGLKPEltvrenlrfwaalyglraDREAIDEALEAVGLagL 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503996112 151 QPERVYQLypheiSGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLgLIFISHD 222
Cdd:COG4133 125 ADLPVRQL-----SAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGA-VLLTTHQ 190
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
14-243 |
1.52e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 70.22 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 14 LDVRDLCVDFvNGSAVthaVRGVSFQLGR-EKLAIVGESGSGKST---VGRALLQLHPKKARV----------------- 72
Cdd:TIGR03269 1 IEVKNLTKKF-DGKEV---LKNISFTIEEgEVLGILGRSGAGKSVlmhVLRGMDQYEPTSGRIiyhvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 73 --------SASRMQFANLDLLHLTEAQMRGVRgKRISmIMQDPKYSLNPVVCVGKQIAEAwlTHHPGRK-DEAKAKALEM 143
Cdd:TIGR03269 77 kvgepcpvCGGTLEPEEVDFWNLSDKLRRRIR-KRIA-IMLQRTFALYGDDTVLDNVLEA--LEEIGYEgKEAVGRAVDL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 144 LEVVRIRQpeRVYQLyPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDI 223
Cdd:TIGR03269 153 IEMVQLSH--RITHI-ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWP 229
|
250 260
....*....|....*....|
gi 503996112 224 NLVRSFCDRVLVMYAGRVVE 243
Cdd:TIGR03269 230 EVIEDLSDKAIWLENGEIKE 249
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
46-242 |
2.03e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 68.47 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 46 AIVGESGSGKSTVGRALLQLH-PKKARVSasrmqfanLDLLHLTEAQMRGVrGKRISMIMQDPKYSLNpvVCVGKQIAEA 124
Cdd:PRK10253 37 AIIGPNGCGKSTLLRTLSRLMtPAHGHVW--------LDGEHIQHYASKEV-ARRIGLLAQNATTPGD--ITVQELVARG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 125 WLTHHP----GRKDEAKAkalemleVVRIRQPERVYQLYPHEI---SGGQGQRIMIAMMLITDPELIIADEPTSALDVSV 197
Cdd:PRK10253 106 RYPHQPlftrWRKEDEEA-------VTKAMQATGITHLADQSVdtlSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISH 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503996112 198 RLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVV 242
Cdd:PRK10253 179 QIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIV 223
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-222 |
2.13e-13 |
|
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: 70.08 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 6 PAANNAPLLDVRDLCVDFVNGSAVthaVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQ-LHPKKARVSasrmqfanLD 83
Cdd:TIGR02868 327 AVGLGKPTLELRDLSAGYPGAPPV---LDGVSLDLPPgERVAILGPSGSGKSTLLATLAGlLDPLQGEVT--------LD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 84 LLHLTEAQMRGVRgKRISMIMQDPKYslnpvvcVGKQIAEAWLThhpGRKDEAKAKALEMLEVVR----IRQPERVYQLY 159
Cdd:TIGR02868 396 GVPVSSLDQDEVR-RRVSVCAQDAHL-------FDTTVRENLRL---ARPDATDEELWAALERVGladwLRALPDGLDTV 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503996112 160 PHE----ISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQvlgLLDDLVQ-SRGLGLIFISHD 222
Cdd:TIGR02868 465 LGEggarLSGGERQRLALARALLADAPILLLDEPTEHLDAETADE---LLEDLLAaLSGRTVVLITHH 529
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
43-243 |
2.49e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 67.88 E-value: 2.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 43 EKLAIVGESGSGKSTvgraLLQLHPKKARVSASRMQFANLDLLHLTEAQMRGVRGKRISMIMQdpKYSLNPVVCVGKQIA 122
Cdd:PRK10584 37 ETIALIGESGSGKST----LLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQ--SFMLIPTLNALENVE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 123 EAWLTHhpGRKD-EAKAKALEMLEVVRIrqPERVYQLyPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQV 201
Cdd:PRK10584 111 LPALLR--GESSrQSRNGAKALLEQLGL--GKRLDHL-PAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 503996112 202 LGLLDDLVQSRGLGLIFISHDINLVrSFCDRVLVMYAGRVVE 243
Cdd:PRK10584 186 ADLLFSLNREHGTTLILVTHDLQLA-ARCDRRLRLVNGQLQE 226
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-251 |
3.10e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 69.47 E-value: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 13 LLDVRDLCVDFvngSAVThAVRGVSFQL-GREKLAIVGESGSGKSTVGRALLQLHPKKARVSASRMQFANLDLLHLTEAQ 91
Cdd:TIGR02633 1 LLEMKGIVKTF---GGVK-ALDGIDLEVrPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSGSPLKASNIRDTE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 92 MRGvrgkrISMIMQD----PKYSLNPVVCVGKQIaeawlTHHPGRKDEAKA--KALEMLEVVRIrqPERVYQLYPHEISG 165
Cdd:TIGR02633 77 RAG-----IVIIHQEltlvPELSVAENIFLGNEI-----TLPGGRMAYNAMylRAKNLLRELQL--DADNVTRPVGDYGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 166 GQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLvQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVESI 245
Cdd:TIGR02633 145 GQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATK 223
|
....*.
gi 503996112 246 AACDLD 251
Cdd:TIGR02633 224 DMSTMS 229
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
149-236 |
4.02e-13 |
|
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: 65.16 E-value: 4.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 149 IRQPERVYQLYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQvlgLLDDLVQSRGlGLIFISHDINLVRS 228
Cdd:cd03221 57 VTWGSTVKIGYFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEA---LEEALKEYPG-TVILVSHDRYFLDQ 132
|
....*...
gi 503996112 229 FCDRVLVM 236
Cdd:cd03221 133 VATKIIEL 140
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
47-256 |
4.70e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 68.21 E-value: 4.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 47 IVGESGSGKSTVGRALLQLH-PKKARVsasrmqFanLDLLHLTEaqmRGVRGKRISMIMQdpKYSLNPVVCVGKQIAEAw 125
Cdd:PRK11432 37 LLGPSGCGKTTVLRLVAGLEkPTEGQI------F--IDGEDVTH---RSIQQRDICMVFQ--SYALFPHMSLGENVGYG- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 126 LTHHPGRKDEAKAKALEMLEVVRIRQPErvyQLYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLL 205
Cdd:PRK11432 103 LKMLGVPKEERKQRVKEALELVDLAGFE---DRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKI 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 503996112 206 DDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVESIAACDLdnARHP 256
Cdd:PRK11432 180 RELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL--YRQP 228
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
163-242 |
6.00e-13 |
|
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: 66.04 E-value: 6.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 163 ISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSrGLGLIFISHDI-NLVRSFCDRVLVMYAGRV 241
Cdd:cd03213 112 LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPsSEIFELFDKLLLLSQGRV 190
|
.
gi 503996112 242 V 242
Cdd:cd03213 191 I 191
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
163-255 |
9.59e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.77 E-value: 9.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 163 ISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQsRGLGLIFISHDINLVRSFCDRVLVMYAGRVV 242
Cdd:PRK15439 404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAA-QNVAVLFISSDLEEIEQMADRVLVMHQGEIS 482
|
90
....*....|....*
gi 503996112 243 ESIA--ACDLDNARH 255
Cdd:PRK15439 483 GALTgaAINVDTIMR 497
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
34-243 |
1.04e-12 |
|
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: 67.92 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 34 RGVSFQLG-REKLAIVGESGSGKSTVGRALLQLHpkkaRVSASRMQFANLDLLHLTEAQMRGVrgkrISMIMQDpkysln 112
Cdd:COG5265 375 KGVSFEVPaGKTVAIVGPSGAGKSTLARLLFRFY----DVTSGRILIDGQDIRDVTQASLRAA----IGIVPQD------ 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 113 pVVCVGKQIAE--AWlthhpGRKD------EAKAKALEMLEVVRiRQP--------ERVYQLypheiSGGQGQRIMIAMM 176
Cdd:COG5265 441 -TVLFNDTIAYniAY-----GRPDaseeevEAAARAAQIHDFIE-SLPdgydtrvgERGLKL-----SGGEKQRVAIART 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503996112 177 LITDPELIIADEPTSALDVSVRLQVLGLLDDLvqSRGLGLIFISHDINLVRSfCDRVLVMYAGRVVE 243
Cdd:COG5265 509 LLKNPPILIFDEATSALDSRTERAIQAALREV--ARGRTTLVIAHRLSTIVD-ADEILVLEAGRIVE 572
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
14-244 |
1.27e-12 |
|
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: 65.24 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 14 LDVRDLCVDfVNGSAVthaVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQlHPKkARVSASRMQFANLDLLHLtEAQM 92
Cdd:cd03217 1 LEIKDLHVS-VGGKEI---LKGVNLTIKKgEVHALMGPNGSGKSTLAKTIMG-HPK-YEVTEGEILFKGEDITDL-PPEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 93 RGVRGkrISMIMQDPkyslnpvvcvgkqiAEAwlthhPGRKdeakakaleMLEVVRirqpervyqlYPHE-ISGGQGQRI 171
Cdd:cd03217 74 RARLG--IFLAFQYP--------------PEI-----PGVK---------NADFLR----------YVNEgFSGGEKKRN 113
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503996112 172 MIAMMLITDPELIIADEPTSALDV-SVRLqVLGLLDDLVqSRGLGLIFISHD---INLVRSfcDRVLVMYAGRVVES 244
Cdd:cd03217 114 EILQLLLLEPDLAILDEPDSGLDIdALRL-VAEVINKLR-EEGKSVLIITHYqrlLDYIKP--DRVHVLYDGRIVKS 186
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
33-231 |
1.31e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 66.21 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 33 VRGVSFQLGREKL-AIVGESGSGKSTVGRALLQLHPKKARVSAS-RMQFANLDLLhltEAQMRGVRGKR-ISMIMqdPKY 109
Cdd:PRK14258 23 LEGVSMEIYQSKVtAIIGPSGCGKSTFLKCLNRMNELESEVRVEgRVEFFNQNIY---ERRVNLNRLRRqVSMVH--PKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 110 SLNPV-----VCVGKQIAeAWlthHPGRK----DEAKAKALEMLEVVRIRQPERVYqlyphEISGGQGQRIMIAMMLITD 180
Cdd:PRK14258 98 NLFPMsvydnVAYGVKIV-GW---RPKLEiddiVESALKDADLWDEIKHKIHKSAL-----DLSGGQQQRLCIARALAVK 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 503996112 181 PELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCD 231
Cdd:PRK14258 169 PKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
43-239 |
2.13e-12 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 65.18 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 43 EKLAIVGESGSGKSTvgraLLQLHPKKARVSASRMQfanLDLLHLTEAqmrgvrGKRISMIMQDpkYSLNPVVCVGKQIA 122
Cdd:TIGR01184 12 EFISLIGHSGCGKST----LLNLISGLAQPTSGGVI---LEGKQITEP------GPDRMVVFQN--YSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 123 EAW-LTHHPGRKDEAKAKALEMLEVVRIRqpeRVYQLYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQV 201
Cdd:TIGR01184 77 LAVdRVLPDLSKSERRAIVEEHIALVGLT---EAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 503996112 202 LGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAG 239
Cdd:TIGR01184 154 QEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-246 |
2.39e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 65.49 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 14 LDVRDLCVDFVNGSAV-THAVRGVSFQLGR-EKLAIVGESGSGKSTvgraLLQLHPKKARVSASRMQFANLDLLHLTEAQ 91
Cdd:COG1101 2 LELKNLSKTFNPGTVNeKRALDGLNLTIEEgDFVTVIGSNGAGKST----LLNAIAGSLPPDSGSILIDGKDVTKLPEYK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 92 mrgvRGKRISMIMQDPK----YSLnpvvcvgkQIAE----AWLTHHP---------GRKDEAKA--KALEM-LEVvRIRQ 151
Cdd:COG1101 78 ----RAKYIGRVFQDPMmgtaPSM--------TIEEnlalAYRRGKRrglrrgltkKRRELFREllATLGLgLEN-RLDT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 152 PerVYQLypheiSGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCD 231
Cdd:COG1101 145 K--VGLL-----SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGN 217
|
250
....*....|....*
gi 503996112 232 RVLVMYAGRVVESIA 246
Cdd:COG1101 218 RLIMMHEGRIILDVS 232
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
31-242 |
2.51e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 65.88 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 31 HAVRGVSFQLGR-EKLAIVGESGSGKSTvgraLLQ-----LHPK--KARV-----SASRMQFAnldllhlteaqmrgvrg 97
Cdd:COG4586 36 EAVDDISFTIEPgEIVGFIGPNGAGKST----TIKmltgiLVPTsgEVRVlgyvpFKRRKEFA----------------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 98 KRISMIM------------QDpKYSLNPVV-CVGKQIAEAWLthhpgrkDEAKakalEMLEVVRI-RQPERvyQLyphei 163
Cdd:COG4586 95 RRIGVVFgqrsqlwwdlpaID-SFRLLKAIyRIPDAEYKKRL-------DELV----ELLDLGELlDTPVR--QL----- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503996112 164 SGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVV 242
Cdd:COG4586 156 SLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRII 234
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
34-258 |
2.62e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 66.63 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 34 RGVSFQLGR-EKLAIVGESGSGKSTVGRALL-QLHPKKARVSASRmqfanldllhlteaqmrgvrGKRISMIMQDPKY-- 109
Cdd:COG0488 15 DDVSLSINPgDRIGLVGRNGAGKSTLLKILAgELEPDSGEVSIPK--------------------GLRIGYLPQEPPLdd 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 110 ----------SLNPVVCVGKQIAE---------------AWLTHHPGRKD--EAKAKALEMLEVVRIrqPERVYQLYPHE 162
Cdd:COG0488 75 dltvldtvldGDAELRALEAELEEleaklaepdedlerlAELQEEFEALGgwEAEARAEEILSGLGF--PEEDLDRPVSE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 163 ISGGQGQRIMIAMMLITDPELIIADEPTSALDV-SVRlqvlgLLDDLVQSRGLGLIFISHDinlvRSFCDRVlvmyAGRV 241
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLeSIE-----WLEEFLKNYPGTVLVVSHD----RYFLDRV----ATRI 219
|
250
....*....|....*...
gi 503996112 242 VEsiaacdLDNAR-HPYT 258
Cdd:COG0488 220 LE------LDRGKlTLYP 231
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
11-244 |
2.85e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 65.29 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 11 APLLDVRDLCVDFVNGSAvthAVRGVSFQL-GREKLAIVGESGSGKSTVGRALlqlhpkkarvsasrMQFANLDLLHLTE 89
Cdd:PRK15056 4 QAGIVVNDVTVTWRNGHT---ALRDASFTVpGGSIAALVGVNGSGKSTLFKAL--------------MGFVRLASGKISI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 90 AQMRGVRGKRISMIMQDPKYS---------LNPVVCVGKQIAEAWLTHHPGRKDEAKAKALEMLEVVRIRQPErvyqlyP 160
Cdd:PRK15056 67 LGQPTRQALQKNLVAYVPQSEevdwsfpvlVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQ------I 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 161 HEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLvQSRGLGLIFISHDINLVRSFCDRVlVMYAGR 240
Cdd:PRK15056 141 GELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYT-VMVKGT 218
|
....
gi 503996112 241 VVES 244
Cdd:PRK15056 219 VLAS 222
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
43-263 |
4.13e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 64.65 E-value: 4.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 43 EKLAIVGESGSGKSTVGRALLQLhpkkarVSASRMQFANLDLLHLT---EAQM-RGVRGKRISMIMQDPKYSLNPVVCVG 118
Cdd:PRK09984 31 EMVALLGPSGSGKSTLLRHLSGL------ITGDKSAGSHIELLGRTvqrEGRLaRDIRKSRANTGYIFQQFNLVNRLSVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 119 KQI-------AEAWLTHHPGRKDEAKAKALEMLevVRIRQPERVYQLYPhEISGGQGQRIMIAMMLITDPELIIADEPTS 191
Cdd:PRK09984 105 ENVligalgsTPFWRTCFSWFTREQKQRALQAL--TRVGMVHFAHQRVS-TLSGGQQQRVAIARALMQQAKVILADEPIA 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503996112 192 ALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVESIAACDLDNARHPYTQGLIN 263
Cdd:PRK09984 182 SLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDNERFDHLYRSIN 253
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
14-243 |
4.67e-12 |
|
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: 63.59 E-value: 4.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 14 LDVRDLCVDFvnGSAVTHAVRGVSFQL-GREKLAIVGESGSGKSTVGRALLQ-LHPKKARVSASRMQFANLDLLHLTEaq 91
Cdd:cd03369 7 IEVENLSVRY--APDLPPVLKNVSFKVkAGEKIGIVGRTGAGKSTLILALFRfLEAEEGKIEIDGIDISTIPLEDLRS-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 92 mrgvrgkRISMIMQDP-------KYSLNPVvcvgkqiaeawlthhpGRKDEAkakalEMLEVVRIRQPErvyqlypHEIS 164
Cdd:cd03369 83 -------SLTIIPQDPtlfsgtiRSNLDPF----------------DEYSDE-----EIYGALRVSEGG-------LNLS 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 165 GGQGQRIMIAMMLITDPELIIADEPTSALDVSVrlqvlgllDDLVQS------RGLGLIFISHDINLVRSfCDRVLVMYA 238
Cdd:cd03369 128 QGQRQLLCLARALLKRPRVLVLDEATASIDYAT--------DALIQKtireefTNSTILTIAHRLRTIID-YDKILVMDA 198
|
....*
gi 503996112 239 GRVVE 243
Cdd:cd03369 199 GEVKE 203
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
21-241 |
5.82e-12 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 65.45 E-value: 5.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 21 VDFVNGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPKKA-RVSASRMQFANLDllhlteaqmRGVRGK 98
Cdd:TIGR01842 322 VTIVPPGGKKPTLRGISFSLQAgEALAIIGPSGSGKSTLARLIVGIWPPTSgSVRLDGADLKQWD---------RETFGK 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 99 RISMIMQDpkYSLNPVVcVGKQIAeawlthhpgRKDEaKAKALEMLEVVRIRQPERVYQLYPH-----------EISGGQ 167
Cdd:TIGR01842 393 HIGYLPQD--VELFPGT-VAENIA---------RFGE-NADPEKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQ 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503996112 168 GQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLvQSRGLGLIFISHDINLVRSfCDRVLVMYAGRV 241
Cdd:TIGR01842 460 RQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKAL-KARGITVVVITHRPSLLGC-VDKILVLQDGRI 531
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
43-243 |
5.95e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 65.90 E-value: 5.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 43 EKLAIVGESGSGKSTVGrALLQlhpkkarvsasrmqfanlDLLHLTEAQMRgVRGKRISMImqDPKYSLNPVVCVGKQ-- 120
Cdd:TIGR00958 508 EVVALVGPSGSGKSTVA-ALLQ------------------NLYQPTGGQVL-LDGVPLVQY--DHHYLHRQVALVGQEpv 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 121 ---------IAEAwLTHHPGRKDEAKAKA-------LEMLEVVRIRQPERVYQLypheiSGGQGQRIMIAMMLITDPELI 184
Cdd:TIGR00958 566 lfsgsvrenIAYG-LTDTPDEEIMAAAKAanahdfiMEFPNGYDTEVGEKGSQL-----SGGQKQRIAIARALVRKPRVL 639
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503996112 185 IADEPTSALDVsvrlQVLGLLDDLVQSRGLGLIFISHDINLVRSfCDRVLVMYAGRVVE 243
Cdd:TIGR00958 640 ILDEATSALDA----ECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVE 693
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
14-244 |
6.82e-12 |
|
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: 62.72 E-value: 6.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 14 LDVRDlcVDFVNGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTvgraLLQLHPKKARVSASRMQFANLDLlHLTEAQM 92
Cdd:cd03247 1 LSINN--VSFSYPEQEQQVLKNLSLELKQgEKIALLGRSGSGKST----LLQLLTGDLKPQQGEITLDGVPV-SDLEKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 93 RgvrgKRISMIMQDPkYSLNpvvcvgkqiaeAWLTHHPGRKdeakakalemlevvrirqpervyqlypheISGGQGQRIM 172
Cdd:cd03247 74 S----SLISVLNQRP-YLFD-----------TTLRNNLGRR-----------------------------FSGGERQRLA 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503996112 173 IAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDlvQSRGLGLIFISHDINLVRSFcDRVLVMYAGRVVES 244
Cdd:cd03247 109 LARILLQDAPIVLLDEPTVGLDPITERQLLSLIFE--VLKDKTLIWITHHLTGIEHM-DKILFLENGKIIMQ 177
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
33-249 |
1.09e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.81 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 33 VRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPKKA---RVSASRMQFAN-LDLLHlteaqmrgvrgKRISMIMQD- 106
Cdd:PRK09700 279 VRDISFSVCRgEILGFAGLVGSGRTELMNCLFGVDKRAGgeiRLNGKDISPRSpLDAVK-----------KGMAYITESr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 107 ------PKYSLNPVVCVGKQIAE-----AW--LTHHPGRKDEAKAKALEMLEVVRIRQPervyqlyPHEISGGQGQRIMI 173
Cdd:PRK09700 348 rdngffPNFSIAQNMAISRSLKDggykgAMglFHEVDEQRTAENQRELLALKCHSVNQN-------ITELSGGNQQKVLI 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503996112 174 AMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSrGLGLIFISHDINLVRSFCDRVLVMYAGRVVESIAACD 249
Cdd:PRK09700 421 SKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD 495
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
9-267 |
2.02e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 62.86 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 9 NNAPLLDVRDlcVDFVNGSAVTHAvrGVSFQLGREKL-AIVGESGSGKSTvgraLLQLHPKKARVSASRMQFANLDLLHL 87
Cdd:PRK11831 3 SVANLVDMRG--VSFTRGNRCIFD--NISLTVPRGKItAIMGPSGIGKTT----LLRLIGGQIAPDHGEILFDGENIPAM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 88 TEAQMRGVRgKRISMIMQDPkySLNPVVCVGKQIAEAWLTHHPGRKDEAKAKALEMLEVVRIRQPErvyQLYPHEISGGQ 167
Cdd:PRK11831 75 SRSRLYTVR-KRMSMLFQSG--ALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAA---KLMPSELSGGM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 168 GQRIMIAMMLITDPELIIADEPTSALDvSVRLQVL-GLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVESIA 246
Cdd:PRK11831 149 ARRAALARAIALEPDLIMFDEPFVGQD-PITMGVLvKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGS 227
|
250 260
....*....|....*....|.
gi 503996112 247 ACDLDNARHPYTQGLINSLPD 267
Cdd:PRK11831 228 AQALQANPDPRVRQFLDGIAD 248
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
14-244 |
2.69e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 62.01 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 14 LDVRDLCVDfVNGSAVthaVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQlHPKKaRVSASRMQFANLDLLHLtEAQM 92
Cdd:COG0396 1 LEIKNLHVS-VEGKEI---LKGVNLTIKPgEVHAIMGPNGSGKSTLAKVLMG-HPKY-EVTSGSILLDGEDILEL-SPDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 93 RGVRGkrISMIMQDP------------KYSLNPVVcvGKQIAEAwlthhpgrkdEAKAKALEMLEVVRIRQ--PERvyql 158
Cdd:COG0396 74 RARAG--IFLAFQYPveipgvsvsnflRTALNARR--GEELSAR----------EFLKLLKEKMKELGLDEdfLDR---- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 159 YPHE-ISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVrLQVLGLLDDLVQSRGLGLIFISHD---INLVRsfCDRVL 234
Cdd:COG0396 136 YVNEgFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDA-LRIVAEGVNKLRSPDRGILIITHYqriLDYIK--PDFVH 212
|
250
....*....|
gi 503996112 235 VMYAGRVVES 244
Cdd:COG0396 213 VLVDGRIVKS 222
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-244 |
2.71e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 63.69 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 6 PAANNAPLLDVRDLCVDFVNGSavTHAVRGVSFQLGR-EKLAIVGESGSGKSTvgraLLQLHPKKARVSASRMQFANLDL 84
Cdd:PRK11160 331 TAAADQVSLTLNNVSFTYPDQP--QPVLKGLSLQIKAgEKVALLGRTGCGKST----LLQLLTRAWDPQQGEILLNGQPI 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 85 LHLTEAQMRgvrgKRISMIMQDPkYSLNPVVCVGKQIAEawlthhPGRKDEAKAKALEMLEVVRIRQPERVYQLYPHE-- 162
Cdd:PRK11160 405 ADYSEAALR----QAISVVSQRV-HLFSATLRDNLLLAA------PNASDEALIEVLQQVGLEKLLEDDKGLNAWLGEgg 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 163 --ISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRglGLIFISHDINLVRSFcDRVLVMYAGR 240
Cdd:PRK11160 474 rqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLTGLEQF-DRICVMDNGQ 550
|
....
gi 503996112 241 VVES 244
Cdd:PRK11160 551 IIEQ 554
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
36-234 |
3.01e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.05 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 36 VSFQLGREK-LAIVGESGSGKSTVGRALLqlhpkkarvsasrmqfanlDLLHLTEAQMRGVRGKRISMIMQdpKYSLNPV 114
Cdd:PRK09544 23 VSLELKPGKiLTLLGPNGAGKSTLVRVVL-------------------GLVAPDEGVIKRNGKLRIGYVPQ--KLYLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 115 VCVgkqIAEAWLTHHPGRKdeaKAKALEMLEVVrirQPERVYQLYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALD 194
Cdd:PRK09544 82 LPL---TVNRFLRLRPGTK---KEDILPALKRV---QAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 503996112 195 VSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVL 234
Cdd:PRK09544 153 VNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
10-242 |
3.62e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 62.33 E-value: 3.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 10 NAPLLdvRDLCVDFVngsavTHAVRGvsfqlgreklaIVGESGSGKSTVGRALLQL-HPKKARV--SASRMQFANLDLLH 86
Cdd:PRK13638 13 DEPVL--KGLNLDFS-----LSPVTG-----------LVGANGCGKSTLFMNLSGLlRPQKGAVlwQGKPLDYSKRGLLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 87 LTEaqmrgvrgkRISMIMQDPK-------------YSLNPVvcvgkQIAEAWLTHhpgRKDEAkakaLEMLEVVRIR-QP 152
Cdd:PRK13638 75 LRQ---------QVATVFQDPEqqifytdidsdiaFSLRNL-----GVPEAEITR---RVDEA----LTLVDAQHFRhQP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 153 ERVyqlypheISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQsRGLGLIFISHDINLVRSFCDR 232
Cdd:PRK13638 134 IQC-------LSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVA-QGNHVIISSHDIDLIYEISDA 205
|
250
....*....|
gi 503996112 233 VLVMYAGRVV 242
Cdd:PRK13638 206 VYVLRQGQIL 215
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
31-243 |
5.19e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 61.40 E-value: 5.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 31 HAVRGVSFQLGREKL-AIVGESGSGKSTVGRA---LLQLHPKkARVSAS-RMQFANLDLLHLTEAQMRgvrgKRISMIMQ 105
Cdd:PRK14267 18 HVIKGVDLKIPQNGVfALMGPSGCGKSTLLRTfnrLLELNEE-ARVEGEvRLFGRNIYSPDVDPIEVR----REVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 106 DPkyslNPV--------VCVGKQIAEawLTHHPGRKDEAKAKALE---MLEVVRIRQPErvyqlYPHEISGGQGQRIMIA 174
Cdd:PRK14267 93 YP----NPFphltiydnVAIGVKLNG--LVKSKKELDERVEWALKkaaLWDEVKDRLND-----YPSNLSGGQRQRLVIA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503996112 175 MMLITDPELIIADEPTSALDVSVRLQVLGLLDDLvqSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVE 243
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIE 228
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-243 |
5.65e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 61.65 E-value: 5.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 11 APLLDVRDLCVDFVNGSAVTHAVRGVSfqlGREKLAIVGESGSGKSTVGRALLQLHPKKA--RVSAS-----RMQFANLD 83
Cdd:PRK14271 19 APAMAAVNLTLGFAGKTVLDQVSMGFP---ARAVTSLMGPTGSGKTTFLRTLNRMNDKVSgyRYSGDvllggRSIFNYRD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 84 LLHLTeaqmrgvrgKRISMIMQDPkySLNPVVCVGKQIAEAWLTHHPGRKD-----EAKAKALEMLEVVRIRQPERvyql 158
Cdd:PRK14271 96 VLEFR---------RRVGMLFQRP--NPFPMSIMDNVLAGVRAHKLVPRKEfrgvaQARLTEVGLWDAVKDRLSDS---- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 159 yPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSrgLGLIFISHDINLVRSFCDRVLVMYA 238
Cdd:PRK14271 161 -PFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFD 237
|
....*
gi 503996112 239 GRVVE 243
Cdd:PRK14271 238 GRLVE 242
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
163-241 |
6.85e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.44 E-value: 6.85e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503996112 163 ISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQsRGLGLIFISHDINLVRSFCDRVLVMYAGRV 241
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAK-KDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
12-243 |
8.26e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 62.00 E-value: 8.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 12 PLLDVRDLCVDFvNGSAVthaVRGVSFQLGR-EKLAIVGESGSGKSTVGRALL-QLHPKKARVS-ASRMQFANLDllhlt 88
Cdd:COG0488 314 KVLELEGLSKSY-GDKTL---LDDLSLRIDRgDRIGLIGPNGAGKSTLLKLLAgELEPDSGTVKlGETVKIGYFD----- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 89 eaQMRGvrgkrismimqdpkySLNPvvcvGKQIAEaWLTHhpGRKDEAKAKALEMLEvvriR---QPERVYQlYPHEISG 165
Cdd:COG0488 385 --QHQE---------------ELDP----DKTVLD-ELRD--GAPGGTEQEVRGYLG----RflfSGDDAFK-PVGVLSG 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503996112 166 GQGQRIMIAMMLITDPELIIADEPTSALDvsvrLQVLGLLDDLVQS-RGlGLIFISHDINLVRSFCDRVLVMYAGRVVE 243
Cdd:COG0488 436 GEKARLALAKLLLSPPNVLLLDEPTNHLD----IETLEALEEALDDfPG-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
145-235 |
1.78e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 61.34 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 145 EVVRIRQPERVYQLYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDIN 224
Cdd:COG1245 438 EIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIY 517
|
90
....*....|.
gi 503996112 225 LVRSFCDRVLV 235
Cdd:COG1245 518 LIDYISDRLMV 528
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-236 |
1.91e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 60.98 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 2 TSSIPAANNAPLLDVRDLCVDFVNGSAVthaVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPkkarvSAS-RMQF 79
Cdd:COG4178 351 AASRIETSEDGALALEDLTLRTPDGRPL---LEDLSLSLKPgERLLITGPSGSGKSTLLRAIAGLWP-----YGSgRIAR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 80 AnldllhlteaqmrgvRGKRISMIMQDPkY----SLNPVVCvgkqiaeawLTHHPGRKDEAKAKALemLEVVRIrqPERV 155
Cdd:COG4178 423 P---------------AGARVLFLPQRP-YlplgTLREALL---------YPATAEAFSDAELREA--LEAVGL--GHLA 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 156 YQLY-----PHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDlvQSRGLGLIFISHDINLVRsFC 230
Cdd:COG4178 474 ERLDeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGHRSTLAA-FH 550
|
....*.
gi 503996112 231 DRVLVM 236
Cdd:COG4178 551 DRVLEL 556
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
48-241 |
2.29e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 60.43 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 48 VGESGSGKSTvgraLLqlhpkkaRVSASRMQFANLDLLhLTEAQMRGV----RGkrISMIMQdpKYSLNPVVCVGKQIAE 123
Cdd:PRK11000 35 VGPSGCGKST----LL-------RMIAGLEDITSGDLF-IGEKRMNDVppaeRG--VGMVFQ--SYALYPHLSVAENMSF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 124 awlthhpGRKdEAKAKALEMLEvvRIRQPERVYQL------YPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSV 197
Cdd:PRK11000 99 -------GLK-LAGAKKEEINQ--RVNQVAEVLQLahlldrKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAAL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 503996112 198 RLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRV 241
Cdd:PRK11000 169 RVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
159-242 |
3.46e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 59.89 E-value: 3.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 159 YPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYA 238
Cdd:PRK11144 125 YPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQ 204
|
....
gi 503996112 239 GRVV 242
Cdd:PRK11144 205 GKVK 208
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-242 |
4.10e-10 |
|
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: 58.44 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 18 DLCVDFVNGSAVTHAVRGVSFQL-GREKLAIVGESGSGKSTVGRALLQLHPKKARVSAsRMQFANLDLlhlTEAQMRgvr 96
Cdd:cd03234 8 DVGLKAKNWNKYARILNDVSLHVeSGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSG-QILFNGQPR---KPDQFQ--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 97 gKRISMIMQDPkySLNPVVCVgkqiAEAWL--THHPGRKDEAKAKALEMLEVVRIRQ--PERVYQLYPHEISGGQGQRIM 172
Cdd:cd03234 81 -KCVAYVRQDD--ILLPGLTV----RETLTytAILRLPRKSSDAIRKKRVEDVLLRDlaLTRIGGNLVKGISGGERRRVS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503996112 173 IAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLvqSRGLGLIFIShdINLVRS----FCDRVLVMYAGRVV 242
Cdd:cd03234 154 IAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQL--ARRNRIVILT--IHQPRSdlfrLFDRILLLSSGEIV 223
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
46-243 |
6.48e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.05 E-value: 6.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 46 AIVGESGSGKSTVGRALLqlhpkkarvsasrmqfanldllhlteAQMRGVRGKRISMIMQDPKYSLNPVV-CVGkqiaea 124
Cdd:COG2401 60 LIVGASGSGKSTLLRLLA--------------------------GALKGTPVAGCVDVPDNQFGREASLIdAIG------ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 125 wlthhpgRKDEAKAkALEMLEVVRIRQPervyQLY---PHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQV 201
Cdd:COG2401 108 -------RKGDFKD-AVELLNAVGLSDA----VLWlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 503996112 202 LGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVM--YAGRVVE 243
Cdd:COG2401 176 ARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIFvgYGGVPEE 219
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
161-234 |
7.69e-10 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 57.24 E-value: 7.69e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503996112 161 HEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVqSRGLGLIFISHDINLVRSFCDRVL 234
Cdd:NF040873 118 GELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEH-ARGATVVVVTHDLELVRRADPCVL 190
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
148-242 |
1.04e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 58.65 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 148 RIRQP---ERVYQLypheiSGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVqSRGLGLIFISHDIN 224
Cdd:NF040905 392 NIKTPsvfQKVGNL-----SGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELA-AEGKGVIVISSELP 465
|
90
....*....|....*...
gi 503996112 225 LVRSFCDRVLVMYAGRVV 242
Cdd:NF040905 466 ELLGMCDRIYVMNEGRIT 483
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
9-255 |
1.05e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 57.42 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 9 NNAPLLDVRDlcVDFVNGSAVThaVRGVSFQL--GREKLaIVGESGSGKSTvgraLLQLHPKKARVSASRMQFANLDLLH 86
Cdd:PRK10247 3 ENSPLLQLQN--VGYLAGDAKI--LNNISFSLraGEFKL-ITGPSGCGKST----LLKIVASLISPTSGTLLFEGEDIST 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 87 LTEAQMRgvrgKRISMIMQDPkyslnpvVCVGKQIAEAWLTHHPGRKDEAKAKALeMLEVVRIRQPERVYQLYPHEISGG 166
Cdd:PRK10247 74 LKPEIYR----QQVSYCAQTP-------TLFGDTVYDNLIFPWQIRNQQPDPAIF-LDDLERFALPDTILTKNIAELSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 167 QGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVrSFCDRVLVMYAgrvvesiA 246
Cdd:PRK10247 142 EKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEI-NHADKVITLQP-------H 213
|
....*....
gi 503996112 247 ACDLDNARH 255
Cdd:PRK10247 214 AGEMQEARY 222
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
24-244 |
1.48e-09 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 57.16 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 24 VNGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPKKARVSASRMQFANLDLLHLteAQMRGVRGKRism 102
Cdd:COG4138 3 LNDVAVAGRLGPISAQVNAgELIHLIGPNGAGKSTLLARMAGLLPGQGEILLNGRPLSDWSAAEL--ARHRAYLSQQ--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 103 imQDPKyslnPVVCVGKQIAeawLTHHPGRKDEAKAKALEML-EVVRI-----RQperVYQLypheiSGGQGQRIMIAMM 176
Cdd:COG4138 78 --QSPP----FAMPVFQYLA---LHQPAGASSEAVEQLLAQLaEALGLedklsRP---LTQL-----SGGEWQRVRLAAV 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503996112 177 LI-----TDPE--LIIADEPTSALDVSVRLQVLGLLDDLVQSrGLGLIFISHDINLVRSFCDRVLVMYAGRVVES 244
Cdd:COG4138 141 LLqvwptINPEgqLLLLDEPMNSLDVAQQAALDRLLRELCQQ-GITVVMSSHDLNHTLRHADRVWLLKQGKLVAS 214
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
32-245 |
1.52e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 58.26 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 32 AVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPK-----KARVSASRMQFANLdllHLTEAqmrgvRGkrISMIMQ 105
Cdd:NF040905 16 ALDDVNLSVREgEIHALCGENGAGKSTLMKVLSGVYPHgsyegEILFDGEVCRFKDI---RDSEA-----LG--IVIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 106 DpkYSLNPVVCVGKQIaeaWLTHHPGRK-----DEAKAKALEMLEVVRIRQPervyqlyPH----EISGGQGQRIMIAMM 176
Cdd:NF040905 86 E--LALIPYLSIAENI---FLGNERAKRgvidwNETNRRARELLAKVGLDES-------PDtlvtDIGVGKQQLVEIAKA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503996112 177 LITDPELIIADEPTSAL--DVSVRLqvLGLLDDLvQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVESI 245
Cdd:NF040905 154 LSKDVKLLILDEPTAALneEDSAAL--LDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIETL 221
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
163-241 |
2.05e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.71 E-value: 2.05e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503996112 163 ISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQsRGLGLIFISHDINLVRSFCDRVLVMYAGRV 241
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKA-EGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
33-242 |
3.03e-09 |
|
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: 57.45 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 33 VRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPkkarVSASRMQFANLDLLHLTeaqmRGVRGKRISMIMQDpkysl 111
Cdd:COG4618 348 LRGVSFSLEPgEVLGVIGPSGSGKSTLARLLVGVWP----PTAGSVRLDGADLSQWD----REELGRHIGYLPQD----- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 112 npVVCVGKQIAE--AWLTHHPGRKDEAKAKALEMLEVVRiRQPERvyqlYPHEI-------SGGQGQRIMIAMMLITDPE 182
Cdd:COG4618 415 --VELFDGTIAEniARFGDADPEKVVAAAKLAGVHEMIL-RLPDG----YDTRIgeggarlSGGQRQRIGLARALYGDPR 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 183 LIIADEPTSALDVSVRLQVLGLLDDLvQSRGLGLIFISHDINLVRSfCDRVLVMYAGRVV 242
Cdd:COG4618 488 LVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLAA-VDKLLVLRDGRVQ 545
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
32-223 |
3.66e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 56.33 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 32 AVRGVSFQLGREKL-AIVGESGSGKSTVGRALLQLHP--KKARVSASRMQFA-NLDLLHLTEAQMRgvrgKRISMIMQDP 107
Cdd:PRK14243 25 AVKNVWLDIPKNQItAFIGPSGCGKSTILRCFNRLNDliPGFRVEGKVTFHGkNLYAPDVDPVEVR----RRIGMVFQKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 108 kyslNPVvcvGKQIAE-----AWLTHHPGRKDEAKAKALEML----EVV-RIRQPERvyqlyphEISGGQGQRIMIAMML 177
Cdd:PRK14243 101 ----NPF---PKSIYDniaygARINGYKGDMDELVERSLRQAalwdEVKdKLKQSGL-------SLSGGQQQRLCIARAI 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 503996112 178 ITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSrgLGLIFISHDI 223
Cdd:PRK14243 167 AVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNM 210
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
158-234 |
4.11e-09 |
|
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: 54.47 E-value: 4.11e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503996112 158 LYP--HEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLglldDLVQSRGLGLIFISHDINLvRSFCDRVL 234
Cdd:cd03223 85 IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY----QLLKELGITVISVGHRPSL-WKFHDRVL 158
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
145-235 |
5.11e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.74 E-value: 5.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 145 EVVRIRQPERVYQLYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDIN 224
Cdd:PRK13409 436 EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIY 515
|
90
....*....|.
gi 503996112 225 LVRSFCDRVLV 235
Cdd:PRK13409 516 MIDYISDRLMV 526
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
30-243 |
5.37e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 56.57 E-value: 5.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 30 THAVRGVSFQLGREK-LAIVGESGSGKSTV------------GRALLQLHP-KKARVSASRMQFA----NLDLLHLTEAQ 91
Cdd:PRK11176 356 VPALRNINFKIPAGKtVALVGRSGSGKSTIanlltrfydideGEILLDGHDlRDYTLASLRNQVAlvsqNVHLFNDTIAN 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 92 mrgvrgkRISMIMQDpKYSLnpvvcvgKQIAEAwlthhpgrkdeAK-AKALEMlevvrIRQPERVYQLYPHE----ISGG 166
Cdd:PRK11176 436 -------NIAYARTE-QYSR-------EQIEEA-----------ARmAYAMDF-----INKMDNGLDTVIGEngvlLSGG 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503996112 167 QGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRglGLIFISHDINLVRSfCDRVLVMYAGRVVE 243
Cdd:PRK11176 485 QRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEK-ADEILVVEDGEIVE 558
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
33-250 |
1.60e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 54.81 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 33 VRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLH--------------PKKARVSASRM----QFANLDLLHLTEAQMR 93
Cdd:PRK13537 23 VDGLSFHVQRgECFGLLGPNGAGKTTTLRMLLGLThpdagsislcgepvPSRARHARQRVgvvpQFDNLDPDFTVRENLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 94 gVRGKRISMIMQDPKYSLNPVVCVGKQiaeawlthhpgrkdEAKAKAlemlevvRIRqpervyqlyphEISGGQGQRIMI 173
Cdd:PRK13537 103 -VFGRYFGLSAAAARALVPPLLEFAKL--------------ENKADA-------KVG-----------ELSGGMKRRLTL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 174 AMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVqSRGLGLIFISHDINLVRSFCDRVLVMYAGR---------VVES 244
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLL-ARGKTILLTTHFMEEAERLCDRLCVIEEGRkiaegaphaLIES 228
|
....*.
gi 503996112 245 IAACDL 250
Cdd:PRK13537 229 EIGCDV 234
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
164-242 |
3.26e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.15 E-value: 3.26e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503996112 164 SGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQsRGLGLIFISHDINLVRSFCDRVLVMYAGRVV 242
Cdd:PRK11288 398 SGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAA-QGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
31-245 |
5.38e-08 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 52.22 E-value: 5.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 31 HAVRGVSFQLGREKL-AIVGESGSGKSTVGRALLQLhpkkARVSASRMQFANLDLLHLTEAQmrgvrgKRISMIMQDPky 109
Cdd:cd03268 14 RVLDDISLHVKKGEIyGFLGPNGAGKTTTMKIILGL----IKPDSGEITFDGKSYQKNIEAL------RRIGALIEAP-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 110 slnpvvcvgkqiaeAWLTHHPGRKD-EAKAKAL--------EMLEVVRIRQPERV----YQLypheisgGQGQRIMIAMM 176
Cdd:cd03268 82 --------------GFYPNLTARENlRLLARLLgirkkridEVLDVVGLKDSAKKkvkgFSL-------GMKQRLGIALA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503996112 177 LITDPELIIADEPTSALDVSVRLQVLGLLDDLvQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVESI 245
Cdd:cd03268 141 LLGNPDLLILDEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
8-253 |
6.22e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.52 E-value: 6.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 8 ANNAPLLDVRDLCVDFvngSAVThAVRGVSFQL-GREKLAIVGESGSGKSTVGRALLQLHPKkarvSASRMQFANLDLLH 86
Cdd:PRK15439 6 TTAPPLLCARSISKQY---SGVE-VLKGIDFTLhAGEVHALLGGNGAGKSTLMKIIAGIVPP----DSGTLEIGGNPCAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 87 LT--EAQMRGvrgkrISMIMQDPKysLNPVVCVGKQIAEAwLTHHPGRKDEAKAKaLEMLEVvrirqpervyQLYPH--- 161
Cdd:PRK15439 78 LTpaKAHQLG-----IYLVPQEPL--LFPNLSVKENILFG-LPKRQASMQKMKQL-LAALGC----------QLDLDssa 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 162 ---EISGGQGQRIMIAMMliTDPELIIADEPTSALDVSVRLQVLGLLDDLvQSRGLGLIFISHDINLVRSFCDRVLVMYA 238
Cdd:PRK15439 139 gslEVADRQIVEILRGLM--RDSRILILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRD 215
|
250
....*....|....*
gi 503996112 239 GRVVESIAACDLDNA 253
Cdd:PRK15439 216 GTIALSGKTADLSTD 230
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
33-243 |
8.19e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.44 E-value: 8.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 33 VRGVSFQLG-REKLAIVGESGSGKSTVGRALLQLhpkkARVSASRMQFANLDLLHLTEAQMRGVrgkrISMIMQDP---- 107
Cdd:PLN03232 1252 LHGLSFFVSpSEKVGVVGRTGAGKSSMLNALFRI----VELEKGRIMIDDCDVAKFGLTDLRRV----LSIIPQSPvlfs 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 108 ---KYSLNPvvcvgkqiaeawLTHHpgrKDEAKAKALE---MLEVVRiRQPervYQLYPHEISGGQ----GQR--IMIAM 175
Cdd:PLN03232 1324 gtvRFNIDP------------FSEH---NDADLWEALErahIKDVID-RNP---FGLDAEVSEGGEnfsvGQRqlLSLAR 1384
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503996112 176 MLITDPELIIADEPTSALDVSVrlqvlgllDDLVQS------RGLGLIFISHDINLVRSfCDRVLVMYAGRVVE 243
Cdd:PLN03232 1385 ALLRRSKILVLDEATASVDVRT--------DSLIQRtireefKSCTMLVIAHRLNTIID-CDKILVLSSGQVLE 1449
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
45-237 |
1.00e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 51.98 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 45 LAIVGESGSGKSTVGRALL-QLHPKKARVSASRMQFANLDLLHLTEAQ--MRGVRGKRISMIMQdPKY-SLNPVVCVGKQ 120
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAgKLKPNLGKFDDPPDWDEILDEFRGSELQnyFTKLLEGDVKVIVK-PQYvDLIPKAVKGKV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 121 IAEAWLTHHPGRKDEAkAKALEmLEVVRIRQPErvyqlyphEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQ 200
Cdd:cd03236 108 GELLKKKDERGKLDEL-VDQLE-LRHVLDRNID--------QLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLN 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 503996112 201 VLGLLDDLVQSrGLGLIFISHDINLVRSFCDRVLVMY 237
Cdd:cd03236 178 AARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCLY 213
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
14-244 |
1.40e-07 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 51.00 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 14 LDVRDLCVDFVNgsavTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLhpkkARVSASRMQFANLDLLHLTEAQm 92
Cdd:cd03218 1 LRAENLSKRYGK----RKVVNGVSLSVKQgEIVGLLGPNGAGKTTTFYMIVGL----VKPDSGKILLDGQDITKLPMHK- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 93 RGVRGkrISMIMQDPkySLNPVVCVGKQIaEAWLTHHPGRKDEAKAKALEMLEVVRIrqpERVYQLYPHEISGGQGQRIM 172
Cdd:cd03218 72 RARLG--IGYLPQEA--SIFRKLTVEENI-LAVLEIRGLSKKEREEKLEELLEEFHI---THLRKSKASSLSGGERRRVE 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503996112 173 IAMMLITDPELIIADEPTSALD-VSVRlQVLGLLDDLVQsRGLGLIFISHDINLVRSFCDRVLVMYAGRVVES 244
Cdd:cd03218 144 IARALATNPKFLLLDEPFAGVDpIAVQ-DIQKIIKILKD-RGIGVLITDHNVRETLSITDRAYIIYEGKVLAE 214
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
10-243 |
1.67e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.20 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 10 NAPLLDVRDLCvdFVNGSAVTH-AVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQL-HPKKARV----SASRMQFA-- 80
Cdd:PRK13545 18 NKPFDKLKDLF--FRSKDGEYHyALNNISFEVPEgEIVGIIGLNGSGKSTLSNLIAGVtMPNKGTVdikgSAALIAISsg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 81 -NLDLLHLTEAQMRGvrgkrisMIMQDPKyslnpvvcvgKQIaeawlthhpgrkDEAKAKALEMLEVVR-IRQPERVYql 158
Cdd:PRK13545 96 lNGQLTGIENIELKG-------LMMGLTK----------EKI------------KEIIPEIIEFADIGKfIYQPVKTY-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 159 ypheiSGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLvQSRGLGLIFISHDINLVRSFCDRVLVMYA 238
Cdd:PRK13545 145 -----SSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEF-KEQGKTIFFISHSLSQVKSFCTKALWLHY 218
|
....*
gi 503996112 239 GRVVE 243
Cdd:PRK13545 219 GQVKE 223
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
35-243 |
1.75e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.43 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 35 GVSFQL-GREKLAIVGESGSGKSTVGRALLQL-HPKKARVSASRMQFANLDLLHLTeaqmrgvrgKRISMIMQDP----- 107
Cdd:PLN03130 1257 GLSFEIsPSEKVGIVGRTGAGKSSMLNALFRIvELERGRILIDGCDISKFGLMDLR---------KVLGIIPQAPvlfsg 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 108 --KYSLNPvvcvgkqiaeawLTHHpgrKDEAKAKALE---MLEVVRiRQP----ERVYQlYPHEISGGQGQRIMIAMMLI 178
Cdd:PLN03130 1328 tvRFNLDP------------FNEH---NDADLWESLErahLKDVIR-RNSlgldAEVSE-AGENFSVGQRQLLSLARALL 1390
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503996112 179 TDPELIIADEPTSALDVSVrlqvlgllDDLVQS------RGLGLIFISHDINLVRSfCDRVLVMYAGRVVE 243
Cdd:PLN03130 1391 RRSKILVLDEATAAVDVRT--------DALIQKtireefKSCTMLIIAHRLNTIID-CDRILVLDAGRVVE 1452
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
43-240 |
2.63e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 51.42 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 43 EKLAIVGESGSGKSTVGRALlqlhpkkarvsASRMQFANLDLLHLT-EAQMRGVRGKRISMIMQDPkySLNPVVCVGKQI 121
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNAL-----------AGRIQGNNFTGTILAnNRKPTKQILKRTGFVTQDD--ILYPHLTVRETL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 122 AEAWLTHHPGR--KDEAKAKALEMLEVVRIRQPER--VYQLYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSV 197
Cdd:PLN03211 162 VFCSLLRLPKSltKQEKILVAESVISELGLTKCENtiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATA 241
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 503996112 198 RLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGR 240
Cdd:PLN03211 242 AYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGR 284
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
45-251 |
2.94e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.16 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 45 LAIVGESGSGKSTVGRALLQLHPKKA---RVSASRMQFANLdllhlTEAQMRGvrgkrISMIMQD----PKYSLNPVVCV 117
Cdd:PRK10762 33 MALVGENGAGKSTMMKVLTGIYTRDAgsiLYLGKEVTFNGP-----KSSQEAG-----IGIIHQElnliPQLTIAENIFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 118 GKQIAEAWlthhpGRKDEAK--AKALEMLEVVRIRQPERvyQLYpHEISGGQGQRIMIAMMLITDPELIIADEPTSALDV 195
Cdd:PRK10762 103 GREFVNRF-----GRIDWKKmyAEADKLLARLNLRFSSD--KLV-GELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503996112 196 SVRLQVLGLLDDLvQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVESIAACDLD 251
Cdd:PRK10762 175 TETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLT 229
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
145-235 |
3.38e-07 |
|
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: 50.10 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 145 EVVRIRQPERVYQLYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDIN 224
Cdd:cd03237 98 EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDII 177
|
90
....*....|.
gi 503996112 225 LVRSFCDRVLV 235
Cdd:cd03237 178 MIDYLADRLIV 188
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
32-226 |
3.76e-07 |
|
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: 49.66 E-value: 3.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 32 AVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQL-HPKKARVSasrmqfanLDLLHLteAQMRGVRGKRIsmimqdpky 109
Cdd:TIGR01189 15 LFEGLSFTLNAgEALQVTGPNGIGKTTLLRILAGLlRPDSGEVR--------WNGTPL--AEQRDEPHENI--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 110 slnpvvcvgkqiaeAWLTHHPGRKDE----------------AKAKALEMLEVVRIRQPErvyQLYPHEISGGQGQRIMI 173
Cdd:TIGR01189 76 --------------LYLGHLPGLKPElsalenlhfwaaihggAQRTIEDALAAVGLTGFE---DLPAAQLSAGQQRRLAL 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503996112 174 AMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLV 226
Cdd:TIGR01189 139 ARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLV 191
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
32-243 |
4.03e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 50.87 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 32 AVRGVSFQLGR-EKLAIVGESGSGKSTVgRALLQLHpkkARVSASRMQFANLDLLHLTEAQMRGvrgkRISMIMQDP-KY 109
Cdd:PRK10789 330 ALENVNFTLKPgQMLGICGPTGSGKSTL-LSLIQRH---FDVSEGDIRFHDIPLTKLQLDSWRS----RLAVVSQTPfLF 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 110 SLNpvvcVGKQIAEawlthhpGRKDeakAKALEMLEVVRIRQPE----RVYQLYPHEI-------SGGQGQRIMIAMMLI 178
Cdd:PRK10789 402 SDT----VANNIAL-------GRPD---ATQQEIEHVARLASVHddilRLPQGYDTEVgergvmlSGGQKQRISIARALL 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503996112 179 TDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRglGLIFISHDINLVrSFCDRVLVMYAGRVVE 243
Cdd:PRK10789 468 LNAEILILDDALSAVDGRTEHQILHNLRQWGEGR--TVIISAHRLSAL-TEASEILVMQHGHIAQ 529
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
14-254 |
5.52e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 50.71 E-value: 5.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 14 LDVRDLCVDFVNGsaVTHAVRGVSFQL-GREKLAIVGESGSGKSTVGRALLqlhpkkaRVSASRMQFANLDLLHLTEAQM 92
Cdd:TIGR00957 1285 VEFRNYCLRYRED--LDLVLRHINVTIhGGEKVGIVGRTGAGKSSLTLGLF-------RINESAEGEIIIDGLNIAKIGL 1355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 93 RGVRGKrISMIMQDP-------KYSLNPVVCVGKQiaEAWLthhpgrkdeakakALEM--LEVVRIRQPERVyqlyPHE- 162
Cdd:TIGR00957 1356 HDLRFK-ITIIPQDPvlfsgslRMNLDPFSQYSDE--EVWW-------------ALELahLKTFVSALPDKL----DHEc 1415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 163 ------ISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVrlqvlgllDDLVQS------RGLGLIFISHDINLVRSFC 230
Cdd:TIGR00957 1416 aeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET--------DNLIQStirtqfEDCTVLTIAHRLNTIMDYT 1487
|
250 260
....*....|....*....|....
gi 503996112 231 dRVLVMYAGRVVESIAACDLDNAR 254
Cdd:TIGR00957 1488 -RVIVLDKGEVAEFGAPSNLLQQR 1510
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
10-244 |
6.06e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 49.64 E-value: 6.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 10 NAPLLDVRDLCVDfVNGSAVthaVRGVSFQLGR-EKLAIVGESGSGKSTVGRaLLQLHPKkARVSASRMQFANLDLLHLt 88
Cdd:CHL00131 4 NKPILEIKNLHAS-VNENEI---LKGLNLSINKgEIHAIMGPNGSGKSTLSK-VIAGHPA-YKILEGDILFKGESILDL- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 89 EAQMRGVRGkrISMIMQdpkyslNPVVCVGKQIAEAW-LTHHPGRKDEAKAK--ALEMLEVvrIRQPERVYQLYPHEI-- 163
Cdd:CHL00131 77 EPEERAHLG--IFLAFQ------YPIEIPGVSNADFLrLAYNSKRKFQGLPEldPLEFLEI--INEKLKLVGMDPSFLsr 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 164 ------SGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGlGLIFISHDINLVRSFC-DRVLVM 236
Cdd:CHL00131 147 nvnegfSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSEN-SIILITHYQRLLDYIKpDYVHVM 225
|
....*...
gi 503996112 237 YAGRVVES 244
Cdd:CHL00131 226 QNGKIIKT 233
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
14-240 |
7.29e-07 |
|
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: 48.62 E-value: 7.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 14 LDVRDLCVDFVNGSAVTHAV-RGVSFQLGREKL-AIVGESGSGKSTVGRALL-QLHPKKARVS-ASRMQFAnldllhlte 89
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTlKDINLEVPKGELvAIVGPVGSGKSSLLSALLgELEKLSGSVSvPGSIAYV--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 90 AQmrgvrgkrISMIMQDpkySLNPVVCVGKQIAEAWLthhpgrkdeakakalemLEVVRIRQPERVYQLYPH----EI-- 163
Cdd:cd03250 72 SQ--------EPWIQNG---TIRENILFGKPFDEERY-----------------EKVIKACALEPDLEILPDgdltEIge 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 164 -----SGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQvlgLLDDLVQSRGLGL---IFISHDINLVRSfCDRVLV 235
Cdd:cd03250 124 kginlSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRH---IFENCILGLLLNNktrILVTHQLQLLPH-ADQIVV 199
|
....*
gi 503996112 236 MYAGR 240
Cdd:cd03250 200 LDNGR 204
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
33-231 |
7.82e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.95 E-value: 7.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 33 VRGVSFQLGR-EKLAIVGESGSGKSTVGRALL-QLHPKKARV-SASRMQFANLDllhlteaQMRGVrgkrismimQDPKY 109
Cdd:PRK11147 335 VKDFSAQVQRgDKIALIGPNGCGKTTLLKLMLgQLQADSGRIhCGTKLEVAYFD-------QHRAE---------LDPEK 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 110 SLNPVVCVGKQIAEAwlthhPGRKDEAKAKALEML-EVVRIRQPERVyqlypheISGGQGQRIMIAMMLITDPELIIADE 188
Cdd:PRK11147 399 TVMDNLAEGKQEVMV-----NGRPRHVLGYLQDFLfHPKRAMTPVKA-------LSGGERNRLLLARLFLKPSNLLILDE 466
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 503996112 189 PTSALDVsvrlQVLGLLDDLVQSRGLGLIFISHDinlvRSFCD 231
Cdd:PRK11147 467 PTNDLDV----ETLELLEELLDSYQGTVLLVSHD----RQFVD 501
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
163-242 |
8.64e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.05 E-value: 8.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 163 ISGGQGQRIMIAMML---------ITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRV 233
Cdd:PRK13547 146 LSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRI 225
|
....*....
gi 503996112 234 LVMYAGRVV 242
Cdd:PRK13547 226 AMLADGAIV 234
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
32-244 |
1.16e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.52 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 32 AVRGVSFQLGREKL-AIVGESGSGKSTVGRAL---LQLHPKKARVSASRMQFANLdllhlTEAQMRGvrgkrISMIMQDp 107
Cdd:PRK11288 19 ALDDISFDCRAGQVhALMGENGAGKSTLLKILsgnYQPDAGSILIDGQEMRFAST-----TAALAAG-----VAIIYQE- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 108 kYSLNPVVCVGKQIaeaWLTHHPGR-----KDEAKAKALEMLEV--VRIRQPERVYQLypheiSGGQGQRIMIAMMLITD 180
Cdd:PRK11288 88 -LHLVPEMTVAENL---YLGQLPHKggivnRRLLNYEAREQLEHlgVDIDPDTPLKYL-----SIGQRQMVEIAKALARN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503996112 181 PELIIADEPTSALDVSVRLQVLGLLDDLvQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVVES 244
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDGRYVAT 221
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
46-236 |
1.30e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 46 AIVGESGSGKSTVGRALlqlHPKKARVSASRM-QFANLDLLHLTEAQmrgvrgKRISMIMQDPKYSLNPVVC--VGKQIA 122
Cdd:PRK10938 33 AFVGANGSGKSALARAL---AGELPLLSGERQsQFSHITRLSFEQLQ------KLVSDEWQRNNTDMLSPGEddTGRTTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 123 EAWLTHHpgrKDEAKAKALEMLEVVRIRQPERVYQLypheiSGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVL 202
Cdd:PRK10938 104 EIIQDEV---KDPARCEQLAQQFGITALLDRRFKYL-----STGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLA 175
|
170 180 190
....*....|....*....|....*....|....
gi 503996112 203 GLLDDLvQSRGLGLIFISHDINLVRSFCDRVLVM 236
Cdd:PRK10938 176 ELLASL-HQSGITLVLVLNRFDEIPDFVQFAGVL 208
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
32-243 |
1.40e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 49.33 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 32 AVRGVSFQLGREKL---------------AIVGESGSGKSTVGRALLQLHPkkarVSASRMQFANLDLLHLTEAQMRgvr 96
Cdd:PRK10790 342 DIDNVSFAYRDDNLvlqninlsvpsrgfvALVGHTGSGKSTLASLLMGYYP----LTEGEIRLDGRPLSSLSHSVLR--- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 97 gKRISMIMQDpkyslnPVVCVGKQIAEAWLthhpGRkDEAKAKALEMLEVVRIRQ-----PERVYQLYPHE---ISGGQG 168
Cdd:PRK10790 415 -QGVAMVQQD------PVVLADTFLANVTL----GR-DISEEQVWQALETVQLAElarslPDGLYTPLGEQgnnLSVGQK 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503996112 169 QRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLdDLVQSRGLgLIFISHDINLVRSfCDRVLVMYAGRVVE 243
Cdd:PRK10790 483 QLLALARVLVQTPQILILDEATANIDSGTEQAIQQAL-AAVREHTT-LVVIAHRLSTIVE-ADTILVLHRGQAVE 554
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
46-251 |
2.05e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.57 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 46 AIVGESGSGKSTVGRALLQLHPKkarvSASRMQFAN--LDLLHLTEAQMRGVrgkriSMIMQDpkysLNPVvcvgKQ--- 120
Cdd:PRK10982 28 ALMGENGAGKSTLLKCLFGIYQK----DSGSILFQGkeIDFKSSKEALENGI-----SMVHQE----LNLV----LQrsv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 121 IAEAWLTHHPGRK---DEAK----AKALEMLEVVRIRQPERVYQLypheiSGGQGQRIMIAMMLITDPELIIADEPTSAL 193
Cdd:PRK10982 91 MDNMWLGRYPTKGmfvDQDKmyrdTKAIFDELDIDIDPRAKVATL-----SVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503996112 194 ---DVSVRLQVLGLLDDlvqsRGLGLIFISHDINLVRSFCDRVLVMYAGRVVESIAACDLD 251
Cdd:PRK10982 166 tekEVNHLFTIIRKLKE----RGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLT 222
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-244 |
2.15e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.97 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 22 DFVngsavthAVRGVSFQLGR-EKLAIVGESGSGKSTV------------GRALLQLHPKKARVSASRMQ-------F-- 79
Cdd:NF033858 278 DFT-------AVDHVSFRIRRgEIFGFLGSNGCGKSTTmkmltgllpaseGEAWLFGQPVDAGDIATRRRvgymsqaFsl 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 80 -------ANLDL----LHLTEAQmrgvRGKRISMIMQDpkYSLNPVVcvgkqiaeawlthhpgrkdEAKAKALEMlevvr 148
Cdd:NF033858 351 ygeltvrQNLELharlFHLPAAE----IAARVAEMLER--FDLADVA-------------------DALPDSLPL----- 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 149 irqpervyqlypheisgGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLvqSRGLGL-IFIS-HDIN-L 225
Cdd:NF033858 401 -----------------GIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIEL--SREDGVtIFIStHFMNeA 461
|
250
....*....|....*....
gi 503996112 226 VRsfCDRVLVMYAGRVVES 244
Cdd:NF033858 462 ER--CDRISLMHAGRVLAS 478
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
163-242 |
2.28e-06 |
|
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: 47.26 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 163 ISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFI----SHDI-NLVrsfcDRVLVMY 237
Cdd:cd03233 119 ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSlyqaSDEIyDLF----DKVLVLY 194
|
....*
gi 503996112 238 AGRVV 242
Cdd:cd03233 195 EGRQI 199
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
162-246 |
2.79e-06 |
|
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: 46.80 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 162 EISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRV 241
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEGEPG 150
|
....*
gi 503996112 242 VESIA 246
Cdd:cd03222 151 VYGIA 155
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
164-241 |
3.36e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.24 E-value: 3.36e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503996112 164 SGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRlqvLGLLDDLVQSRGlGLIFISHDINLVRSFCDRVLVMYAGRV 241
Cdd:PRK10636 432 SGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMR---QALTEALIDFEG-ALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
34-227 |
3.46e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.49 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 34 RGVSFQLGREK-LAIVGESGSGKSTVGRALLQLH-PKKARVSASrmqfanlDLLHLTEAQMRGVRGKrISMIMQDPK--- 108
Cdd:PTZ00265 402 KDLNFTLTEGKtYAFVGESGCGKSTILKLIERLYdPTEGDIIIN-------DSHNLKDINLKWWRSK-IGVVSQDPLlfs 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 109 -----------YSLNPVVCVGKQIAEAWLTHHPGRKDEAKAKA---------------------------LEMLEVVRIR 150
Cdd:PTZ00265 474 nsiknnikyslYSLKDLEALSNYYNEDGNDSQENKNKRNSCRAkcagdlndmsnttdsneliemrknyqtIKDSEVVDVS 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 151 Q-----------PERVYQLY---PHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGL 216
Cdd:PTZ00265 554 KkvlihdfvsalPDKYETLVgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRIT 633
|
250
....*....|.
gi 503996112 217 IFISHDINLVR 227
Cdd:PTZ00265 634 IIIAHRLSTIR 644
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
31-244 |
3.85e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.16 E-value: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 31 HAVRGVSFQLGREKL-AIVGESGSGKSTVGRALLQlhpkkarvsasrmqfanldllhlTEAQMRGVRGKrismimqdPKY 109
Cdd:cd03238 9 HNLQNLDVSIPLNVLvVVTGVSGSGKSTLVNEGLY-----------------------ASGKARLISFL--------PKF 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 110 SLNPVVCVGK-----QIAEAWLThhPGRKdeakakaLEMLevvrirqpervyqlypheiSGGQGQRIMIAMMLITDPE-- 182
Cdd:cd03238 58 SRNKLIFIDQlqfliDVGLGYLT--LGQK-------LSTL-------------------SGGELQRVKLASELFSEPPgt 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503996112 183 LIIADEPTSALDVSVRLQVLGLLDDLVQSrGLGLIFISHDINLVRSfCDRVLVM------YAGRVVES 244
Cdd:cd03238 110 LFILDEPSTGLHQQDINQLLEVIKGLIDL-GNTVILIEHNLDVLSS-ADWIIDFgpgsgkSGGKVVFS 175
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
153-242 |
3.96e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 46.80 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 153 ERVYQLYP--HE--------ISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLvQSRGLGLIFISHD 222
Cdd:PRK11614 118 KWVYELFPrlHErriqragtMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQN 196
|
90 100
....*....|....*....|
gi 503996112 223 INLVRSFCDRVLVMYAGRVV 242
Cdd:PRK11614 197 ANQALKLADRGYVLENGHVV 216
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
35-228 |
4.08e-06 |
|
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: 46.72 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 35 GVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPKKArvsasrmqfanldllhlteaqmrgvrgKRISMIMQdpkyslnP 113
Cdd:cd03231 18 GLSFTLAAgEALQVTGPNGSGKTTLLRILAGLSPPLA---------------------------GRVLLNGG-------P 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 114 VVCVGKQIAEA--WLTHHPGRK--------------DEAKAKALEMLEVVRIRQPErvyQLYPHEISGGQGQRIMIAMML 177
Cdd:cd03231 64 LDFQRDSIARGllYLGHAPGIKttlsvlenlrfwhaDHSDEQVEEALARVGLNGFE---DRPVAQLSAGQQRRVALARLL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 503996112 178 ITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRS 228
Cdd:cd03231 141 LSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEA 191
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
162-237 |
5.07e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.47 E-value: 5.07e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503996112 162 EISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSrGLGLIFISHDINLVRSFCDRVLVMY 237
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHILY 286
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-244 |
8.40e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 46.08 E-value: 8.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 24 VNGSAVTHAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPKKARVsasrmQFANLDLLHLTEAQMRGVRGkriSM 102
Cdd:PRK03695 3 LNDVAVSTRLGPLSAEVRAgEILHLVGPNGAGKSTLLARMAGLLPGSGSI-----QFAGQPLEAWSAAELARHRA---YL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 103 IMQDPKYSLNPVvcvgkqiaeaW----LTHHPGRKDEAKAKALEML-EVVRI--RQPERVYQLypheiSGGQGQRI-MIA 174
Cdd:PRK03695 75 SQQQTPPFAMPV----------FqyltLHQPDKTRTEAVASALNEVaEALGLddKLGRSVNQL-----SGGEWQRVrLAA 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503996112 175 MMLITDPE------LIIADEPTSALDVSvrlQVlGLLDDLVQ---SRGLGLIFISHDINLVRSFCDRVLVMYAGRVVES 244
Cdd:PRK03695 140 VVLQVWPDinpagqLLLLDEPMNSLDVA---QQ-AALDRLLSelcQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLAS 214
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
42-235 |
1.24e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.56 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 42 REKLAIVGESGSGKSTVGRALLQLH------------PKKARVSASRMQ------------------------------F 79
Cdd:PTZ00265 1194 KKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknEHTNDMTNEQDYqgdeeqnvgmknvnefsltkeggsgedstvF 1273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 80 AN-----LDLLHLTEAQMRGVRgKRISMIMQDP---KYSLNPVVCVGKQIAEawlthhpgRKDEAKAKAL----EMLEVV 147
Cdd:PTZ00265 1274 KNsgkilLDGVDICDYNLKDLR-NLFSIVSQEPmlfNMSIYENIKFGKEDAT--------REDVKRACKFaaidEFIESL 1344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 148 RIRQPERVYQlYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVR 227
Cdd:PTZ00265 1345 PNKYDTNVGP-YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIK 1423
|
....*...
gi 503996112 228 SfCDRVLV 235
Cdd:PTZ00265 1424 R-SDKIVV 1430
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
162-251 |
1.40e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.10 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 162 EISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSrglgLIFISHDinlvRSFCDRVlvmyAGRV 241
Cdd:PRK11147 156 SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGS----IIFISHD----RSFIRNM----ATRI 223
|
90
....*....|
gi 503996112 242 VesiaacDLD 251
Cdd:PRK11147 224 V------DLD 227
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
33-242 |
2.26e-05 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 44.88 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 33 VRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHPKKA-RVSasrMQFANLDLLHLTEAQMRGvrgkrISMIMQDPkyS 110
Cdd:PRK10895 19 VEDVSLTVNSgEIVGLLGPNGAGKTTTFYMVVGIVPRDAgNII---IDDEDISLLPLHARARRG-----IGYLPQEA--S 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 111 LNPVVCVGKQIAEAWLTHHPGRKDEAKAKALEMLEVVRIrqpERVYQLYPHEISGGQGQRIMIAMMLITDPELIIADEPT 190
Cdd:PRK10895 89 IFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHI---EHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503996112 191 SALDVSVRLQVLGLLDDLvQSRGLGLIFISHDINLVRSFCDRVLVMYAGRVV 242
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLI 216
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
250-278 |
2.32e-05 |
|
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid.
Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 41.62 E-value: 2.32e-05
10 20
....*....|....*....|....*....
gi 503996112 250 LDNARHPYTQGLINSLPDMQHRRPILPVL 278
Cdd:pfam08352 10 LENPLHPYTRALLNSVPRLDPPKRPLYTI 38
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
163-241 |
2.46e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.62 E-value: 2.46e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503996112 163 ISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVrlqVLGLLDDLVQSRGlGLIFISHDINLVRSFCDRVLVMYAGRV 241
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA---VEALIQGLVLFQG-GVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
162-237 |
2.61e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.18 E-value: 2.61e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503996112 162 EISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRglGLIFISHDINLVRSFCDRVLVMY 237
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGK--YVLVVEHDLAVLDYLADNVHIAY 285
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
151-233 |
3.25e-05 |
|
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: 44.93 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 151 QPERVYQLypheiSGGQGQRIMIAMMLITDPELIIADEPTSALDVsvrlQVLGLLDDLVQSRGLGLIFISHDinlvRSFC 230
Cdd:TIGR03719 437 QQKKVGQL-----SGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV----ETLRALEEALLNFAGCAVVISHD----RWFL 503
|
...
gi 503996112 231 DRV 233
Cdd:TIGR03719 504 DRI 506
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
30-247 |
3.53e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 44.45 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 30 THAVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQLHpkkaRVSASRMQFANLDLLHLTEAQmrgvRGkrISMIMQDpk 108
Cdd:PRK11650 17 TQVIKGIDLDVADgEFIVLVGPSGCGKSTLLRMVAGLE----RITSGEIWIGGRVVNELEPAD----RD--IAMVFQN-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 109 YSLNPVVCV-------------GK-QIAEawlthhpgRKDEAkAKALE---MLEvvriRQPErvyqlyphEISGGQGQRI 171
Cdd:PRK11650 85 YALYPHMSVrenmayglkirgmPKaEIEE--------RVAEA-ARILElepLLD----RKPR--------ELSGGQRQRV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503996112 172 MIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGRvVESIAA 247
Cdd:PRK11650 144 AMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGV-AEQIGT 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
164-239 |
5.71e-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: 44.62 E-value: 5.71e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503996112 164 SGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQsRGLGLIFISHDINLVRSFCDRVLVMYAG 239
Cdd:TIGR01257 2072 SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIR-EGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
42-228 |
6.16e-05 |
|
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: 42.36 E-value: 6.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 42 REKLAIVGESGSGKSTVGRALLQlhpkkarvsasrmqfanldllhltEAQMRGVRGKRISMImqdpkyslnpvvcvgkqi 121
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALAR------------------------ELGPPGGGVIYIDGE------------------ 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 122 aeawlthhpgrkdeakakalEMLEVVRIRQPERVYQLYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDVS----- 196
Cdd:smart00382 40 --------------------DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEqeall 99
|
170 180 190
....*....|....*....|....*....|..
gi 503996112 197 VRLQVLGLLDDLVQSRGLGLIFISHDINLVRS 228
Cdd:smart00382 100 LLLEELRLLLLLKSEKNLTVILTTNDEKDLGP 131
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
161-241 |
1.19e-04 |
|
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: 43.46 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 161 HEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLddLVQSRGLGLIFISHDINLVRSFCDRVLVMYAGR 240
Cdd:TIGR01257 1060 QDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
.
gi 503996112 241 V 241
Cdd:TIGR01257 1138 L 1138
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
13-244 |
1.44e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.47 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 13 LLDVRDLCVDfVNGSAVthaVRGVSFQLGR-EKLAIVGESGSGKSTVGRALLQlhPKKARVSASRMQFANLDLLHLtEAQ 91
Cdd:PRK09580 1 MLSIKDLHVS-VEDKAI---LRGLNLEVRPgEVHAIMGPNGSGKSTLSATLAG--REDYEVTGGTVEFKGKDLLEL-SPE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 92 MRGvrGKRISMIMQDP--------KYSLNPVV-CVGKQIAEAWLThhpgRKD-----EAKAKALEMLEVVRIRQPERVYq 157
Cdd:PRK09580 74 DRA--GEGIFMAFQYPveipgvsnQFFLQTALnAVRSYRGQEPLD----RFDfqdlmEEKIALLKMPEDLLTRSVNVGF- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 158 lypheiSGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLvQSRGLGLIFISHD---INLVRSfcDRVL 234
Cdd:PRK09580 147 ------SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTHYqriLDYIKP--DYVH 217
|
250
....*....|
gi 503996112 235 VMYAGRVVES 244
Cdd:PRK09580 218 VLYQGRIVKS 227
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
133-244 |
1.49e-04 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 42.32 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 133 KDEAKAKALEMLEVVRIrqpERVYQLYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALD-VSV-RLQvlGLLDDLVQ 210
Cdd:COG1137 110 KKEREERLEELLEEFGI---THLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDpIAVaDIQ--KIIRHLKE 184
|
90 100 110
....*....|....*....|....*....|....*..
gi 503996112 211 sRGLGlIFIShDINlVR---SFCDRVLVMYAGRVVES 244
Cdd:COG1137 185 -RGIG-VLIT-DHN-VRetlGICDRAYIISEGKVLAE 217
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
33-265 |
2.27e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.84 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 33 VRGVSFQLG-REKLAIVGESGSGKSTvgraLLQLHPKKARVSASRMQFANLDLLHLTEAQMRgvrgKRISMIMQDP---- 107
Cdd:PTZ00243 1326 LRGVSFRIApREKVGIVGRTGSGKST----LLLTFMRMVEVCGGEIRVNGREIGAYGLRELR----RQFSMIPQDPvlfd 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 108 ---KYSLNPVVCVGKqiAEAWLThhpgrkdeakakalemLEVVRIRqpERVYQ----LYPHEISGGQ----GQRIMIAM- 175
Cdd:PTZ00243 1398 gtvRQNVDPFLEASS--AEVWAA----------------LELVGLR--ERVASesegIDSRVLEGGSnysvGQRQLMCMa 1457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 176 --MLITDPELIIADEPTSALDVSvrlqvlglLDDLVQSRGLG------LIFISHDINLVRSfCDRVLVMYAGRVVESIAA 247
Cdd:PTZ00243 1458 raLLKKGSGFILMDEATANIDPA--------LDRQIQATVMSafsaytVITIAHRLHTVAQ-YDKIIVMDHGAVAEMGSP 1528
|
250
....*....|....*...
gi 503996112 248 CDLDNARHPYTQGLINSL 265
Cdd:PTZ00243 1529 RELVMNRQSIFHSMVEAL 1546
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
161-221 |
3.43e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.92 E-value: 3.43e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503996112 161 HEISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQSRGLGLIFISH 221
Cdd:PRK10938 400 HSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
163-243 |
4.31e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 41.65 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 163 ISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLG--LLDDLVQ-SRGL---GLIFISHdinlvrsfCDRVLVM 236
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDkcIKDELRGkTRVLvtnQLHFLSQ--------VDRIILV 812
|
....*..
gi 503996112 237 YAGRVVE 243
Cdd:PLN03130 813 HEGMIKE 819
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
136-230 |
6.55e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.03 E-value: 6.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 136 AKAKALEMLEVVRIrqPERVYQLYPHEISGGQGQRIMIAMMLITDPELIIADEPTSALDV-SVRlqvlgLLDDLVQSRGL 214
Cdd:PRK15064 131 AEARAGELLLGVGI--PEEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDInTIR-----WLEDVLNERNS 203
|
90
....*....|....*.
gi 503996112 215 GLIFISHDINLVRSFC 230
Cdd:PRK15064 204 TMIIISHDRHFLNSVC 219
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
164-233 |
6.73e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.87 E-value: 6.73e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503996112 164 SGGQGQRIMIAMMLITDPELIIADEPTSALDVsvrlQVLGLLDD-LVQSRGLGLIfISHDinlvRSFCDRV 233
Cdd:PRK11819 447 SGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV----ETLRALEEaLLEFPGCAVV-ISHD----RWFLDRI 508
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
46-228 |
8.47e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.51 E-value: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 46 AIVGESGSGKSTVGRALlqlhpkkaRVSASRMQFANLDLLHlteaqmrgvrgkrismimQDPKyslnpVVCVGKQIAEAW 125
Cdd:cd03240 26 LIVGQNGAGKTTIIEAL--------KYALTGELPPNSKGGA------------------HDPK-----LIREGEVRAQVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 126 LT--HHPGRKDEAKaKALEMLE-VVRIRQPERVYQLYPH--EISGGQGQ------RIMIAMMLITDPELIIADEPTSALD 194
Cdd:cd03240 75 LAfeNANGKKYTIT-RSLAILEnVIFCHQGESNWPLLDMrgRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLD 153
|
170 180 190
....*....|....*....|....*....|....*
gi 503996112 195 V-SVRLQVLGLLDDLVQSRGLGLIFISHDINLVRS 228
Cdd:cd03240 154 EeNIEESLAEIIEERKSQKNFQLIVITHDEELVDA 188
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
163-202 |
1.13e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 40.34 E-value: 1.13e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 503996112 163 ISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVL 202
Cdd:PLN03232 741 ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVF 780
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
162-221 |
1.19e-03 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 40.12 E-value: 1.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 162 EISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRlqvlGLLDDLVQSRGLGLIFISH 221
Cdd:TIGR00954 582 VLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVE----GYMYRLCREFGITLFSVSH 637
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
144-228 |
1.21e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.38 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 144 LEVVRIRQPerVYQLypheiSGGQGQRIMIAMML---ITDPELIIADEPTSAL---DVSVRLQVLGLLDDLvqsrGLGLI 217
Cdd:TIGR00630 818 LGYIRLGQP--ATTL-----SGGEAQRIKLAKELskrSTGRTLYILDEPTTGLhfdDIKKLLEVLQRLVDK----GNTVV 886
|
90
....*....|.
gi 503996112 218 FISHDINLVRS 228
Cdd:TIGR00630 887 VIEHNLDVIKT 897
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
132-242 |
1.33e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 39.72 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 132 RKDeAKAKALEMLEVVRIRQPE-RVYQLYpheiSGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVLGLLDDLVQ 210
Cdd:NF000106 118 RKD-ARARADELLERFSLTEAAgRAAAKY----SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVR 192
|
90 100 110
....*....|....*....|....*....|..
gi 503996112 211 SrGLGLIFISHDINLVRSFCDRVLVMYAGRVV 242
Cdd:NF000106 193 D-GATVLLTTQYMEEAEQLAHELTVIDRGRVI 223
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
163-242 |
1.69e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.49 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 163 ISGGQGQRIMIAMMLITDPELIIADEPTSALDVSvRLQVLGLLDDLVQSRglgLIFISHDINLVRSFCDRVLVMYAGRVV 242
Cdd:PRK15064 439 LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDME-SIESLNMALEKYEGT---LIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
163-243 |
1.71e-03 |
|
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: 39.93 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 163 ISGGQGQRIMIAMMLITDPELIIADEPTSALDVSVRLQVlglLDDLVQSRGL----GLIFISHDINLVRSfCDRVLVMYA 238
Cdd:TIGR00957 761 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI---FEHVIGPEGVlknkTRILVTHGISYLPQ-VDVIIVMSG 836
|
....*
gi 503996112 239 GRVVE 243
Cdd:TIGR00957 837 GKISE 841
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
163-239 |
1.99e-03 |
|
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: 38.85 E-value: 1.99e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503996112 163 ISGGQGQRIMIAMMLITDPELIIADEPTSALDV--SVRLQVLGLLdDLVQSRGLGLIFISHDINLVrSFCDRVLVMYAG 239
Cdd:cd03290 141 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIhlSDHLMQEGIL-KFLQDDKRTLVLVTHKLQYL-PHADWIIAMKDG 217
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
162-234 |
2.45e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 38.75 E-value: 2.45e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503996112 162 EISGGQGQRIMIAMMLI---TDPELIIADEPTSAL---DVSVRLQVLGLLDDlvqsRGLGLIFISHDINLVRSfCDRVL 234
Cdd:cd03271 169 TLSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLhfhDVKKLLEVLQRLVD----KGNTVVVIEHNLDVIKC-ADWII 242
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
60-234 |
4.25e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.66 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 60 RALLQLHPKKARVSASRMQFA-NLDLLHLTEAQMRGvrgkriSMIMQDPKYSLNPVVCVGKQIAEAWLTHHPGRKDeaKA 138
Cdd:PRK00635 695 RELFAEQPRSKRLGLTKSHFSfNTPLGACAECQGLG------SITTTDNRTSIPCPSCLGKRFLPQVLEVRYKGKN--IA 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503996112 139 KALEML----EVVRIRQP---ERVYQL-------YP-----HEISGGQGQRIMIAMMLIT---DPELIIADEPTSAL--- 193
Cdd:PRK00635 767 DILEMTayeaEKFFLDEPsihEKIHALcslgldyLPlgrplSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLhth 846
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 503996112 194 DVSVRLQVLGLLDDLvqsrGLGLIFISHDINLVRsFCDRVL 234
Cdd:PRK00635 847 DIKALIYVLQSLTHQ----GHTVVIIEHNMHVVK-VADYVL 882
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
164-234 |
8.93e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 37.46 E-value: 8.93e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503996112 164 SGGQGQRIMIAMMLITDPELIIADEPTSALDvsvrLQVLGLLDDLVQSRGLGLIFISHDINLVRSFCDRVL 234
Cdd:PRK10636 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLD----LDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKII 217
|
|
| |
