|
Name |
Accession |
Description |
Interval |
E-value |
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
5-254 |
0e+00 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 553.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 5 DKIKMSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEDVTIKGNISVDGEDIYTSD-DV 83
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGARVEGEILLDGEDIYDPDvDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 84 INLRTKVGMVFQKPNPFPMSIYDNVAYGPRTHGLRDKKQLDKIVEESLKGAAIWDEVKDRLKSSALGLSGGQQQRICIAR 163
Cdd:COG1117 88 VELRRRVGMVFQKPNPFPKSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDEVKDRLKKSALGLSGGQQQRLCIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 164 AIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTPVDK 243
Cdd:COG1117 168 ALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDK 247
|
250
....*....|.
gi 489527602 244 RTEDYITGRFG 254
Cdd:COG1117 248 RTEDYITGRFG 258
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
8-253 |
1.55e-170 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 470.24 E-value: 1.55e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 8 KMSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEDVTIKGNISVDGEDIYTSD-DVINL 86
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPGVRIEGKVLFDGQDIYDKKiDVVEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 87 RTKVGMVFQKPNPFPMSIYDNVAYGPRTHGLRDKKQLDKIVEESLKGAAIWDEVKDRLKSSALGLSGGQQQRICIARAIA 166
Cdd:TIGR00972 81 RRRVGMVFQKPNPFPMSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALWDEVKDRLHDSALGLSGGQQQRLCIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 167 MRPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTPVDKRTE 246
Cdd:TIGR00972 161 VEPEVLLLDEPTSALDPIATGKIEELIQELKKKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKRTE 240
|
....*..
gi 489527602 247 DYITGRF 253
Cdd:TIGR00972 241 DYISGRF 247
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
9-235 |
7.57e-147 |
|
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: 409.26 E-value: 7.57e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEDVTIKGNISVDGEDIYTSD-DVINLR 87
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIYDLDvDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 88 TKVGMVFQKPNPFPMSIYDNVAYGPRTHGLRDKKQLDKIVEESLKGAAIWDEVKDRLKssALGLSGGQQQRICIARAIAM 167
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRLH--ALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489527602 168 RPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKT 235
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQ 226
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
9-254 |
2.05e-140 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 394.14 E-value: 2.05e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEDVTIKGNISVDGEDIYT-SDDVINLR 87
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSpRTDTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 88 TKVGMVFQKPNPFPMSIYDNVAYGPRTHGLRDKKQLDKIVEESLKGAAIWDEVKDRLKSSALGLSGGQQQRICIARAIAM 167
Cdd:PRK14239 86 KEIGMVFQQPNPFPMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIARVLAT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 168 RPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTPVDKRTED 247
Cdd:PRK14239 166 SPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETED 245
|
....*..
gi 489527602 248 YITGRFG 254
Cdd:PRK14239 246 YISGKFG 252
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
7-254 |
2.10e-126 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 359.10 E-value: 2.10e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 7 IKMSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEDVTIKGNISVDGEDIYTSD-DVIN 85
Cdd:PRK14243 9 TVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFHGKNLYAPDvDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 86 LRTKVGMVFQKPNPFPMSIYDNVAYGPRTHGLrdKKQLDKIVEESLKGAAIWDEVKDRLKSSALGLSGGQQQRICIARAI 165
Cdd:PRK14243 89 VRRRIGMVFQKPNPFPKSIYDNIAYGARINGY--KGDMDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 166 AMRPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHNMQQAARISDETAFF---------LNGEVIEFSDTKTM 236
Cdd:PRK14243 167 AVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKI 246
|
250
....*....|....*...
gi 489527602 237 FTTPVDKRTEDYITGRFG 254
Cdd:PRK14243 247 FNSPQQQATRDYVSGRFG 264
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-254 |
2.30e-103 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 300.80 E-value: 2.30e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 2 ELIDKIKmsVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEDVTIKGNISVDGEDIYTSD 81
Cdd:PRK14258 3 KLIPAIK--VNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIYERR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 82 DVIN-LRTKVGMVFQKPNPFPMSIYDNVAYGPRTHGLRDKKQLDKIVEESLKGAAIWDEVKDRLKSSALGLSGGQQQRIC 160
Cdd:PRK14258 81 VNLNrLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 161 IARAIAMRPEVILMDEPTSALDPISTLKVEELIED--LKKDYTIVIVTHNMQQAARISDETAFFLN-----GEVIEFSDT 233
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSlrLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLT 240
|
250 260
....*....|....*....|.
gi 489527602 234 KTMFTTPVDKRTEDYITGRFG 254
Cdd:PRK14258 241 KKIFNSPHDSRTREYVLSRLG 261
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-254 |
3.84e-99 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 289.82 E-value: 3.84e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 6 KIKMSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEDVTIKGNISVDGEDIYTSD-DVI 84
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSPDvDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 85 NLRTKVGMVFQKPNPFP-MSIYDNVAYGPRTHGL-RDKKQLDKIVEESLKGAAIWDEVKDRLKSSALGLSGGQQQRICIA 162
Cdd:PRK14267 82 EVRREVGMVFQYPNPFPhLTIYDNVAIGVKLNGLvKSKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 163 RAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTPVD 242
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEH 241
|
250
....*....|..
gi 489527602 243 KRTEDYITGRFG 254
Cdd:PRK14267 242 ELTEKYVTGALG 253
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-252 |
5.17e-95 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 279.11 E-value: 5.17e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 8 KMSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEDVTIKGNISVDGEDIYTSDdVINLR 87
Cdd:PRK14247 3 KIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIFKMD-VIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 88 TKVGMVFQKPNPFP-MSIYDNVAYGPRTHGL-RDKKQLDKIVEESLKGAAIWDEVKDRLKSSALGLSGGQQQRICIARAI 165
Cdd:PRK14247 82 RRVQMVFQIPNPIPnLSIFENVALGLKLNRLvKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 166 AMRPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTPVDKRT 245
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELT 241
|
....*..
gi 489527602 246 EDYITGR 252
Cdd:PRK14247 242 EKYVTGR 248
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
10-249 |
1.06e-81 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 244.90 E-value: 1.06e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndliEDVTiKGNISVDGEDIYTSDDVIN-LRT 88
Cdd:COG1126 3 EIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLL----EEPD-SGTITVDGEDLTDSKKDINkLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 89 KVGMVFQKPNPFP-MSIYDNVAYGPRTHGLRDKKQLDKIVEESLkgaaiwDEV--KDRLKSSALGLSGGQQQRICIARAI 165
Cdd:COG1126 78 KVGMVFQQFNLFPhLTVLENVTLAPIKVKKMSKAEAEERAMELL------ERVglADKADAYPAQLSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 166 AMRPEVILMDEPTSALDPISTLKVEELIEDLKKD-YTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTPVDKR 244
Cdd:COG1126 152 AMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEgMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHER 231
|
....*
gi 489527602 245 TEDYI 249
Cdd:COG1126 232 TRAFL 236
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-254 |
1.43e-81 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 245.78 E-value: 1.43e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEDVTIKGNISVDGEDIYTSDDVINLRT 88
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDVLEFRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 89 KVGMVFQKPNPFPMSIYDNVAYGPRTHGLRDKKQLDKIVEESLKGAAIWDEVKDRLKSSALGLSGGQQQRICIARAIAMR 168
Cdd:PRK14271 102 RVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVN 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 169 PEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTPVDKRTEDY 248
Cdd:PRK14271 182 PEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARY 261
|
....*.
gi 489527602 249 ITGRFG 254
Cdd:PRK14271 262 VAGLSG 267
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-252 |
4.95e-80 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 241.49 E-value: 4.95e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIED-VTIKGNISVDGEDIYTSDdVINLRT 88
Cdd:PRK14246 12 NISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSkIKVDGKVLYFGKDIFQID-AIKLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 89 KVGMVFQKPNPFP-MSIYDNVAYGPRTHGLRDKKQLDKIVEESLKGAAIWDEVKDRLKSSALGLSGGQQQRICIARAIAM 167
Cdd:PRK14246 91 EVGMVFQQPNPFPhLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 168 RPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTPVDKRTED 247
Cdd:PRK14246 171 KPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEK 250
|
....*
gi 489527602 248 YITGR 252
Cdd:PRK14246 251 YVIGR 255
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
10-227 |
8.44e-67 |
|
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: 205.84 E-value: 8.44e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndliEDVTiKGNISVDGEDIY-TSDDVINLRT 88
Cdd:cd03262 2 EIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLL----EEPD-SGTIIIDGLKLTdDKKNINELRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 89 KVGMVFQKPNPFP-MSIYDNVAYGPRTHGLRDKKQLDKIVEESLKGAAIwdevKDRLKSSALGLSGGQQQRICIARAIAM 167
Cdd:cd03262 77 KVGMVFQQFNLFPhLTVLENITLAPIKVKGMSKAEAEERALELLEKVGL----ADKADAYPAQLSGGQQQRVAIARALAM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527602 168 RPEVILMDEPTSALDPISTLKVEELIEDLKKD-YTIVIVTHNMQQAARISDETAFFLNGEV 227
Cdd:cd03262 153 NPKVMLFDEPTSALDPELVGEVLDVMKDLAEEgMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
10-238 |
5.27e-64 |
|
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: 199.48 E-value: 5.27e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFY-GDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRmndLIEDVtiKGNISVDGEDIyTSDDVINLRT 88
Cdd:COG1122 2 ELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNG---LLKPT--SGEVLVDGKDI-TKKNLRELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 89 KVGMVFQkpNP----FPMSIYDNVAYGPRTHGLrDKKQLDKIVEESLKGAAIWDeVKDRlksSALGLSGGQQQRICIARA 164
Cdd:COG1122 76 KVGLVFQ--NPddqlFAPTVEEDVAFGPENLGL-PREEIRERVEEALELVGLEH-LADR---PPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489527602 165 IAMRPEVILMDEPTSALDPISTLKVEELIEDLKKD-YTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFT 238
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEgKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
11-226 |
2.61e-63 |
|
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: 195.87 E-value: 2.61e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 11 VKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndlieDVTIKGNISVDGEDIYT-SDDVINLRTK 89
Cdd:cd03229 3 LKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGL-----EEPDSGSILIDGEDLTDlEDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 90 VGMVFQKPNPFP-MSIYDNVAYGprthglrdkkqldkiveeslkgaaiwdevkdrlkssalgLSGGQQQRICIARAIAMR 168
Cdd:cd03229 78 IGMVFQDFALFPhLTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 169 PEVILMDEPTSALDPISTLKVEELIEDLKKD--YTIVIVTHNMQQAARISDETAFFLNGE 226
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
10-240 |
1.20e-62 |
|
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: 196.18 E-value: 1.20e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTlnrMNDLIEDVtiKGNISVDGEDIY--TSDDVINLR 87
Cdd:cd03261 2 ELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRL---IVGLLRPD--SGEVLIDGEDISglSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 88 TKVGMVFQKPNPF-PMSIYDNVAYGPRTHGLRDKKQLDKIVEE-----SLKGAAiwdevkDRLKSSalgLSGGQQQRICI 161
Cdd:cd03261 77 RRMGMLFQSGALFdSLTVFENVAFPLREHTRLSEEEIREIVLEkleavGLRGAE------DLYPAE---LSGGMKKRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 162 ARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTT 239
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELglTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAS 227
|
.
gi 489527602 240 P 240
Cdd:cd03261 228 D 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
10-240 |
2.87e-62 |
|
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: 203.21 E-value: 2.87e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFY-----GDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRmndlIEDVTiKGNISVDGEDI--YTSDD 82
Cdd:COG1123 262 EVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLG----LLRPT-SGSILFDGKDLtkLSRRS 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 83 VINLRTKVGMVFQKP----NPFpMSIYDNVAYGPRTHGLRDKKQLDKIVEESLkgaaiwDEVkdRLKSSALG-----LSG 153
Cdd:COG1123 337 LRELRRRVQMVFQDPysslNPR-MTVGDIIAEPLRLHGLLSRAERRERVAELL------ERV--GLPPDLADrypheLSG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 154 GQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARISDETAFFLNGEVIEFS 231
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYLFISHDLAVVRYIADRVAVMYDGRIVEDG 487
|
....*....
gi 489527602 232 DTKTMFTTP 240
Cdd:COG1123 488 PTEEVFANP 496
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
10-249 |
3.35e-61 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 192.50 E-value: 3.35e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRmndLIE-DvtiKGNISVDGEDIYTSDDV--INL 86
Cdd:COG1127 7 EVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIG---LLRpD---SGEILVDGQDITGLSEKelYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 87 RTKVGMVFQKPNPF-PMSIYDNVAYGPRTHGLRDKKQLDKIVEESLK-----GAAiwdevkDRLKSSalgLSGGQQQRIC 160
Cdd:COG1127 81 RRRIGMLFQGGALFdSLTVFENVAFPLREHTDLSEAEIRELVLEKLElvglpGAA------DKMPSE---LSGGMRKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 161 IARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFT 238
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
250
....*....|.
gi 489527602 239 TPvDKRTEDYI 249
Cdd:COG1127 232 SD-DPWVRQFL 241
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
9-230 |
4.41e-59 |
|
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: 186.19 E-value: 4.41e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRmndlIEDVTiKGNISVDGEDIYtsdDVINLRT 88
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAG----LERPD-SGEILIDGRDVT---GVPPERR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 89 KVGMVFQKPNPFP-MSIYDNVAYGPRtHGLRDKKQLDKIVEESLKGAAIwdevKDRLKSSALGLSGGQQQRICIARAIAM 167
Cdd:cd03259 73 NIGMVFQDYALFPhLTVAENIAFGLK-LRGVPKAEIRARVRELLELVGL----EGLLNRYPHELSGGQQQRVALARALAR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489527602 168 RPEVILMDEPTSALDPISTlkvEELIEDLKK-----DYTIVIVTHNMQQAARISDETAFFLNGEVIEF 230
Cdd:cd03259 148 EPSLLLLDEPLSALDAKLR---EELREELKElqrelGITTIYVTHDQEEALALADRIAVMNEGRIVQV 212
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
10-226 |
1.30e-57 |
|
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: 182.28 E-value: 1.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGD--KQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNdliedVTIKGNISVDGEDIyTSDDVINLR 87
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL-----GPTSGEVLVDGKDL-TKLSLKELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 88 TKVGMVFQKPNP--FPMSIYDNVAYGPRTHGLrDKKQLDKIVEESLKGAAIWDevkdRLKSSALGLSGGQQQRICIARAI 165
Cdd:cd03225 75 RKVGLVFQNPDDqfFGPTVEEEVAFGLENLGL-PEEEIEERVEEALELVGLEG----LRDRSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489527602 166 AMRPEVILMDEPTSALDPISTLKVEELIEDLKKD-YTIVIVTHNMQQAARISDETAFFLNGE 226
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
10-242 |
3.34e-55 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 180.68 E-value: 3.34e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRtlnrmndLI---EDVTiKGNISVDGEDIytSDDVINL 86
Cdd:COG3842 7 ELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLR-------MIagfETPD-SGRILLDGRDV--TGLPPEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 87 RtKVGMVFQKPNPFP-MSIYDNVAYGPRTHGLrDKKQLDKIVEESLkgaaiwdevkDRLKSSALG------LSGGQQQRI 159
Cdd:COG3842 77 R-NVGMVFQDYALFPhLTVAENVAFGLRMRGV-PKAEIRARVAELL----------ELVGLEGLAdryphqLSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 160 CIARAIAMRPEVILMDEPTSALDPisTLKvEELIEDLKK-----DYTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTK 234
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDA--KLR-EEMREELRRlqrelGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPE 221
|
....*...
gi 489527602 235 TMFTTPVD 242
Cdd:COG3842 222 EIYERPAT 229
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
10-240 |
5.00e-55 |
|
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: 176.92 E-value: 5.00e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYG----DKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDliEDvtiKGNISVDGEDIYTSDDViN 85
Cdd:COG1124 3 EVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLER--PW---SGEVTFDGRPVTRRRRK-A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 86 LRTKVGMVFQKP----NPFpMSIYDNVAYGPRTHGLRDKkqlDKIVEESLKGAAIWDEVKDRLKSSalgLSGGQQQRICI 161
Cdd:COG1124 77 FRRRVQMVFQDPyaslHPR-HTVDRILAEPLRIHGLPDR---EERIAELLEQVGLPPSFLDRYPHQ---LSGGQRQRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 162 ARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTT 239
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAG 229
|
.
gi 489527602 240 P 240
Cdd:COG1124 230 P 230
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
9-238 |
1.07e-54 |
|
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: 176.39 E-value: 1.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIedvtiKGNISVDGEDIYTsddvinLRT 88
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPS-----SGEVLLDGRDLAS------LSR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 89 K-----VGMVFQKPN-PFPMSIYDNVAYG--PRTHGL-RDKKQLDKIVEESLKGAAIWDeVKDRLKSSalgLSGGQQQRI 159
Cdd:COG1120 71 RelarrIAYVPQEPPaPFGLTVRELVALGryPHLGLFgRPSAEDREAVEEALERTGLEH-LADRPVDE---LSGGERQRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 160 CIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMF 237
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERgrTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
.
gi 489527602 238 T 238
Cdd:COG1120 227 T 227
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
10-230 |
5.00e-54 |
|
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: 173.85 E-value: 5.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDK----QALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIedvtiKGNISVDGEDIYTSDDVI- 84
Cdd:cd03257 3 EVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPT-----SGSIIFDGKDLLKLSRRLr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 85 -NLRTKVGMVFQKP----NPFpMSIYDNVAYGPRTHG-LRDKKQLDKIVEESLKGAaiwDEVKDRLKSSALGLSGGQQQR 158
Cdd:cd03257 78 kIRRKEIQMVFQDPmsslNPR-MTIGEQIAEPLRIHGkLSKKEARKEAVLLLLVGV---GLPEEVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489527602 159 ICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARISDETAFFLNGEVIEF 230
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
10-238 |
1.66e-53 |
|
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: 174.18 E-value: 1.66e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYG-----DKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNrmnDLIEdvTIKGNISVDGEDIYTSD--D 82
Cdd:TIGR04521 2 KLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLN---GLLK--PTSGTVTIDGRDITAKKkkK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 83 VINLRTKVGMVFQKPNP--FPMSIYDNVAYGPRTHGLrDKKQLDKIVEESLKGAAIWDEVKDRlksSALGLSGGQQQRIC 160
Cdd:TIGR04521 77 LKDLRKKVGLVFQFPEHqlFEETVYKDIAFGPKNLGL-SEEEAEERVKEALELVGLDEEYLER---SPFELSGGQMRRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 161 IARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFT 238
Cdd:TIGR04521 153 IAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKglTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFS 232
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
10-228 |
1.84e-53 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 172.56 E-value: 1.84e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLnrMNDLIEDvtiKGNISVDGEDIYTsdDVINLRTK 89
Cdd:COG1131 2 EVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRML--LGLLRPT---SGEVRVLGEDVAR--DPAEVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 90 VGMVFQKPNPFP-MSIYDNVAYGPRTHGLrDKKQLDKIVEESLKGAAIWDEVKDRLKSsalgLSGGQQQRICIARAIAMR 168
Cdd:COG1131 75 IGYVPQEPALYPdLTVRENLRFFARLYGL-PRKEARERIDELLELFGLTDAADRKVGT----LSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527602 169 PEVILMDEPTSALDPISTLKVEELIEDLKKD-YTIVIVTHNMQQAARISDETAFFLNGEVI 228
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLCDRVAIIDKGRIV 210
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
10-227 |
5.54e-53 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 170.38 E-value: 5.54e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEdvtikGNISVDGEDIyTSDDVINLRTK 89
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTS-----GEIYLDGKPL-SAMPPPEWRRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 90 VGMVFQKPNPFPMSIYDNVAYGPRthgLRDKKQLDKIVEESLKGAAIWDEVKDRlksSALGLSGGQQQRICIARAIAMRP 169
Cdd:COG4619 76 VAYVPQEPALWGGTVRDNLPFPFQ---LRERKFDRERALELLERLGLPPDILDK---PVERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 170 EVILMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARISDETAFFLNGEV 227
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAEEgrAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
18-249 |
7.69e-53 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 173.35 E-value: 7.69e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 18 YGDKQ-ALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEdvtikGNISVDGEDIyTSDDVINLRTKVGMVFQK 96
Cdd:COG1125 11 YPDGTvAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTS-----GRILIDGEDI-RDLDPVELRRRIGYVIQQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 97 PNPFP-MSIYDNVAYGPRTHGlRDKKQLDKIVEE-----SLKGaaiwDEVKDRLKSSalgLSGGQQQRICIARAIAMRPE 170
Cdd:COG1125 85 IGLFPhMTVAENIATVPRLLG-WDKERIRARVDEllelvGLDP----EEYRDRYPHE---LSGGQQQRVGVARALAADPP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 171 VILMDEPTSALDPIS--TLKvEELI---EDLKKdyTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTPVDKRT 245
Cdd:COG1125 157 ILLMDEPFGALDPITreQLQ-DELLrlqRELGK--TIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFV 233
|
....
gi 489527602 246 EDYI 249
Cdd:COG1125 234 ADFV 237
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
5-217 |
8.10e-53 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 171.81 E-value: 8.10e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 5 DKIKMSVKDLDLFY----GDKQALKKINMDIKENKVTALIGPSGCGKSTFIRtlnrmndLI---EDVTiKGNISVDGEDi 77
Cdd:COG1116 4 AAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLR-------LIaglEKPT-SGEVLVDGKP- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 78 ytsddVINLRTKVGMVFQKPNPFP-MSIYDNVAYGPRTHGLrDKKQLDKIVEES-----LKGAAiwdevkDRLKSSalgL 151
Cdd:COG1116 75 -----VTGPGPDRGVVFQEPALLPwLTVLDNVALGLELRGV-PKAERRERARELlelvgLAGFE------DAYPHQ---L 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489527602 152 SGGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARISD 217
Cdd:COG1116 140 SGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETgkTVLFVTHDVDEAVFLAD 207
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
10-240 |
9.87e-53 |
|
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: 178.17 E-value: 9.87e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFY--GDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndLIEDVTIKGNISVDGEDIYTSDDVInLR 87
Cdd:COG1123 6 EVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGL--LPHGGRISGEVLLDGRDLLELSEAL-RG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 88 TKVGMVFQKP--NPFPMSIYDNVAYGPRTHGLrDKKQLDKIVEESLKGAAIwdevKDRLKSSALGLSGGQQQRICIARAI 165
Cdd:COG1123 83 RRIGMVFQDPmtQLNPVTVGDQIAEALENLGL-SRAEARARVLELLEAVGL----ERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489527602 166 AMRPEVILMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTP 240
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP 234
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
10-227 |
2.25e-52 |
|
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: 169.21 E-value: 2.25e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGD----KQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNrmndLIEDVTiKGNISVDGEDIYTSDDV-- 83
Cdd:cd03255 2 ELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILG----GLDRPT-SGEVRVDGTDISKLSEKel 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 84 INLR-TKVGMVFQKPNPFP-MSIYDNVAYGPRTHGLRDKKQLDKIvEESLKGAAIwdevKDRLKSSALGLSGGQQQRICI 161
Cdd:cd03255 77 AAFRrRHIGFVFQSFNLLPdLTALENVELPLLLAGVPKKERRERA-EELLERVGL----GDRLNHYPSELSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489527602 162 ARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMqQAARISDETAFFLNGEV 227
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
17-249 |
2.94e-52 |
|
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: 169.79 E-value: 2.94e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 17 FYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRmndLIEDVTikGNISVDGEDIyTSDDVINLRTKVGMVFQK 96
Cdd:cd03295 10 YGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINR---LIEPTS--GEIFIDGEDI-REQDPVELRRKIGYVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 97 PNPFP-MSIYDNVAYGPRTHGLrDKKQLDKIVEESLKGAAIWD-EVKDRLKSSalgLSGGQQQRICIARAIAMRPEVILM 174
Cdd:cd03295 84 IGLFPhMTVEENIALVPKLLKW-PKEKIRERADELLALVGLDPaEFADRYPHE---LSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489527602 175 DEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTPVDKRTEDYI 249
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQELgkTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFV 236
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
9-217 |
2.24e-51 |
|
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: 166.88 E-value: 2.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGDKQ----ALKKINMDIKENKVTALIGPSGCGKSTFIRtlnrmndLI---EDVTiKGNISVDGEDIytsd 81
Cdd:cd03293 1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLR-------IIaglERPT-SGEVLVDGEPV---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 82 dvINLRTKVGMVFQKPNPFP-MSIYDNVAYGPRTHGLrDKKQLDKIVEE-----SLKGAAiwdevkDRLKSSalgLSGGQ 155
Cdd:cd03293 69 --TGPGPDRGYVFQQDALLPwLTVLDNVALGLELQGV-PKAEARERAEEllelvGLSGFE------NAYPHQ---LSGGM 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489527602 156 QQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARISD 217
Cdd:cd03293 137 RQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDEAVFLAD 200
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
10-240 |
3.30e-51 |
|
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: 169.46 E-value: 3.30e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFY----GDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRmndLIEDVTI-KGNISVDGEDI--YTSDD 82
Cdd:COG0444 3 EVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILG---LLPPPGItSGEILFDGEDLlkLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 83 VINLRTK-VGMVFQKP----NPFpMSIYDNVAYGPRTHGLRDKKQLDKIVEESLKGAAIwDEVKDRLKSSALGLSGGQQQ 157
Cdd:COG0444 80 LRKIRGReIQMIFQDPmtslNPV-MTVGDQIAEPLRIHGGLSKAEARERAIELLERVGL-PDPERRLDRYPHELSGGMRQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 158 RICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKT 235
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELglAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEE 237
|
....*
gi 489527602 236 MFTTP 240
Cdd:COG0444 238 LFENP 242
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-229 |
3.65e-51 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 166.37 E-value: 3.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 1 MELIdkikMSVKDLDLFYGDK----QALKKINMDIKENKVTALIGPSGCGKSTFIRTLNrmndLIEDVTiKGNISVDGED 76
Cdd:COG1136 1 MSPL----LELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILG----GLDRPT-SGEVLIDGQD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 77 IYT-SDDVINL--RTKVGMVFQKPNPFP-MSIYDNVAYGPRTHGlRDKKQLDKIVEESLkgaaiwDEV--KDRLKSSALG 150
Cdd:COG1136 72 ISSlSERELARlrRRHIGFVFQFFNLLPeLTALENVALPLLLAG-VSRKERRERARELL------ERVglGDRLDHRPSQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 151 LSGGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARiSDETAFFLNGEVI 228
Cdd:COG1136 145 LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgtTIVMVTHDPELAAR-ADRVIRLRDGRIV 223
|
.
gi 489527602 229 E 229
Cdd:COG1136 224 S 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
19-240 |
2.74e-50 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 167.56 E-value: 2.74e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 19 GDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNrmndLIEDVTiKGNISVDGEDI--YTSDDVINLRTKVGMVFQK 96
Cdd:COG1135 16 GPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCIN----LLERPT-SGSVLVDGVDLtaLSERELRAARRKIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 97 PNPFP-MSIYDNVAYGPRTHGLrDKKQLDKIVEESLkgaaiwDEV--KDRLKSSALGLSGGQQQRICIARAIAMRPEVIL 173
Cdd:COG1135 91 FNLLSsRTVAENVALPLEIAGV-PKAEIRKRVAELL------ELVglSDKADAYPSQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489527602 174 MDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTP 240
Cdd:COG1135 164 CDEATSALDPETTRSILDLLKDINRELglTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANP 232
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
12-249 |
3.73e-50 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 164.50 E-value: 3.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 12 KDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndliEDVTiKGNISVDGEDIY-TSDDVINLRTKV 90
Cdd:PRK09493 5 KNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKL----EEIT-SGDLIVDGLKVNdPKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 91 GMVFQKPNPFP-MSIYDNVAYGP-RTHGLRdKKQLDKIVEESLKGAAIwdevKDRLKSSALGLSGGQQQRICIARAIAMR 168
Cdd:PRK09493 80 GMVFQQFYLFPhLTALENVMFGPlRVRGAS-KEEAEKQARELLAKVGL----AERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 169 PEVILMDEPTSALDPISTLKVEELIEDLKKD-YTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTPVDKRTED 247
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQE 234
|
..
gi 489527602 248 YI 249
Cdd:PRK09493 235 FL 236
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
9-250 |
3.94e-49 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 161.72 E-value: 3.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNrmndLIEdVTIKGNISVDGE--DIYTSDD---V 83
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLN----LLE-MPRSGTLNIAGNhfDFSKTPSdkaI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 84 INLRTKVGMVFQKPNPFP-MSIYDNVAYGP-RTHGLrDKKQLDKIVEESLKgaaiwdevKDRLKSSA----LGLSGGQQQ 157
Cdd:PRK11124 78 RELRRNVGMVFQQYNLWPhLTVQQNLIEAPcRVLGL-SKDQALARAEKLLE--------RLRLKPYAdrfpLHLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 158 RICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKD-YTIVIVTHNMQQAARISDETAFFLNGEVIEFSDtKTM 236
Cdd:PRK11124 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETgITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASC 227
|
250
....*....|....
gi 489527602 237 FTTPVDKRTEDYIT 250
Cdd:PRK11124 228 FTQPQTEAFKNYLS 241
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
10-245 |
4.15e-49 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 161.80 E-value: 4.15e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTlnrMNDLIEDVTikGNISVDGEDIYTSddvinlRTK 89
Cdd:COG1121 8 ELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKA---ILGLLPPTS--GTVRLFGKPPRRA------RRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 90 VGMVFQKPN---PFPMSIYDNVAYG--PRTHGLRDKKQLDK-IVEESLK--GAAiwdEVKDRLkssaLG-LSGGQQQRIC 160
Cdd:COG1121 77 IGYVPQRAEvdwDFPITVRDVVLMGryGRRGLFRRPSRADReAVDEALErvGLE---DLADRP----IGeLSGGQQQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 161 IARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKK-DYTIVIVTHNMQQAARISDETAfFLNGEVIEFSDTKTMFTT 239
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRReGKTILVVTHDLGAVREYFDRVL-LLNRGLVAHGPPEEVLTP 228
|
....*.
gi 489527602 240 PVDKRT 245
Cdd:COG1121 229 ENLSRA 234
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
9-249 |
1.84e-48 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 160.18 E-value: 1.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MS--VKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndlieDVTIKGNISVDGEDIYTSDD---- 82
Cdd:COG4161 1 MSiqLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLL-----ETPDSGQLNIAGHQFDFSQKpsek 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 83 -VINLRTKVGMVFQKPNPFP-MSIYDNVAYGP-RTHGLrDKKQLDKIVEESLKGAAIwDEVKDRLkssALGLSGGQQQRI 159
Cdd:COG4161 76 aIRLLRQKVGMVFQQYNLWPhLTVMENLIEAPcKVLGL-SKEQAREKAMKLLARLRL-TDKADRF---PLHLSGGQQQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 160 CIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKK-DYTIVIVTHNMQQAARISDETAFFLNGEVIEFSDtKTMFT 238
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFT 229
|
250
....*....|.
gi 489527602 239 TPVDKRTEDYI 249
Cdd:COG4161 230 QPQTEAFAHYL 240
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
10-242 |
2.05e-48 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 162.93 E-value: 2.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTfirTLnRMNDLIEDVTiKGNISVDGEDiytsddVINLRTK 89
Cdd:COG3839 5 ELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKST---LL-RMIAGLEDPT-SGEILIGGRD------VTDLPPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 90 ---VGMVFQKPNPFP-MSIYDNVAYGPRTHGLrDKKQLDKIVEEslkgAA----IwDEVKDRLkssALGLSGGQQQRICI 161
Cdd:COG3839 74 drnIAMVFQSYALYPhMTVYENIAFPLKLRKV-PKAEIDRRVRE----AAellgL-EDLLDRK---PKQLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 162 ARAIAMRPEVILMDEPTSALDPisTLKVeELIEDLKK-----DYTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTM 236
Cdd:COG3839 145 GRALVREPKVFLLDEPLSNLDA--KLRV-EMRAEIKRlhrrlGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
....*.
gi 489527602 237 FTTPVD 242
Cdd:COG3839 222 YDRPAN 227
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
9-215 |
4.34e-48 |
|
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: 156.77 E-value: 4.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGD--KQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDliedVTiKGNISVDGEDIyTSDDVINL 86
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYD----PT-SGEILIDGVDL-RDLDLESL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 87 RTKVGMVFQKPNPFPMSIYDNVaygprthglrdkkqldkiveeslkgaaiwdevkdrlkssalgLSGGQQQRICIARAIA 166
Cdd:cd03228 75 RKNIAYVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALL 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489527602 167 MRPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHN---MQQAARI 215
Cdd:cd03228 113 RDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRlstIRDADRI 164
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-253 |
5.84e-48 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 159.20 E-value: 5.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 1 MELIDKIKMSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNrmndLIEDVTiKGNISVDGEDIYTS 80
Cdd:COG4598 1 MTDTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCIN----LLETPD-SGEIRVGGEEIRLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 81 DD------------VINLRTKVGMVFQKPNPFP-MSIYDNVAYGPrTHGL-RDKKQLDKIVEESLKGAAIWDeVKDRLKS 146
Cdd:COG4598 76 PDrdgelvpadrrqLQRIRTRLGMVFQSFNLWShMTVLENVIEAP-VHVLgRPKAEAIERAEALLAKVGLAD-KRDAYPA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 147 SalgLSGGQQQRICIARAIAMRPEVILMDEPTSALDPI---STLKVeelIEDLKKD-YTIVIVTHNMQQAARISDETAFF 222
Cdd:COG4598 154 H---LSGGQQQRAAIARALAMEPEVMLFDEPTSALDPElvgEVLKV---MRDLAEEgRTMLVVTHEMGFARDVSSHVVFL 227
|
250 260 270
....*....|....*....|....*....|.
gi 489527602 223 LNGEVIEFSDTKTMFTTPVDKRTEDYITGRF 253
Cdd:COG4598 228 HQGRIEEQGPPAEVFGNPKSERLRQFLSSSL 258
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
10-228 |
1.83e-47 |
|
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: 158.36 E-value: 1.83e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFY--GDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndLIEDvtiKGNISVDGEDIYTSDDVINLR 87
Cdd:TIGR04520 2 EVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGL--LLPT---SGKVTVDGLDTLDEENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 88 TKVGMVFQKP-NPFPMSIY-DNVAYGPRTHGLrDKKQLDKIVEESLKgaaiwdEV--KDRLKSSALGLSGGQQQRICIAR 163
Cdd:TIGR04520 77 KKVGMVFQNPdNQFVGATVeDDVAFGLENLGV-PREEMRKRVDEALK------LVgmEDFRDREPHLLSGGQKQRVAIAG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489527602 164 AIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARiSDETAFFLNGEVI 228
Cdd:TIGR04520 150 VLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEAVL-ADRVIVMNKGKIV 215
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
19-240 |
1.85e-46 |
|
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: 154.66 E-value: 1.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 19 GDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNrmndLIEDVTiKGNISVDGEDIYTSD--DVINLRTKVGMVFQK 96
Cdd:cd03258 16 GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCIN----GLERPT-SGSVLVDGTDLTLLSgkELRKARRRIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 97 PNPF-PMSIYDNVAYGPRTHGLrDKKQLDKIVEESLK--GAAiwdevkDRLKSSALGLSGGQQQRICIARAIAMRPEVIL 173
Cdd:cd03258 91 FNLLsSRTVFENVALPLEIAGV-PKAEIEERVLELLElvGLE------DKADAYPAQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489527602 174 MDEPTSALDPISTLKVEELIEDLKK--DYTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTP 240
Cdd:cd03258 164 CDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
9-249 |
3.15e-46 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 154.52 E-value: 3.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMnDLIEDVTIK-GNISVDGEDIYTSDD--VIN 85
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLL-EQPEAGTIRvGDITIDTARSLSQQKglIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 86 LRTKVGMVFQKPNPFP-MSIYDNVAYGPrthglrdkkqldKIVEESLKGAAIwDEVKDRLKSSALG---------LSGGQ 155
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPhRTVLENIIEGP------------VIVKGEPKEEAT-ARARELLAKVGLAgketsyprrLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 156 QQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKD-YTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTK 234
Cdd:PRK11264 150 QQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAK 229
|
250
....*....|....*
gi 489527602 235 TMFTTPVDKRTEDYI 249
Cdd:PRK11264 230 ALFADPQQPRTRQFL 244
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
9-240 |
1.89e-45 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 155.30 E-value: 1.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MS--VKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRtlnrmndLI---EDVTiKGNISVDGEDIYTsddv 83
Cdd:COG1118 1 MSieVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLR-------IIaglETPD-SGRIVLNGRDLFT---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 84 iNLRT---KVGMVFQKPNPFP-MSIYDNVAYGPRtHGLRDKKQLDKIVEESLkgaaiwDEVK-----DRLKSSalgLSGG 154
Cdd:COG1118 69 -NLPPrerRVGFVFQHYALFPhMTVAENIAFGLR-VRPPSKAEIRARVEELL------ELVQleglaDRYPSQ---LSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 155 QQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARISDETAFFLNGEVIEFSD 232
Cdd:COG1118 138 QRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELggTTVFVTHDQEEALELADRVVVMNQGRIEQVGT 217
|
....*...
gi 489527602 233 TKTMFTTP 240
Cdd:COG1118 218 PDEVYDRP 225
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
10-227 |
3.52e-45 |
|
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: 149.47 E-value: 3.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLnrMNDLIEDvtiKGNISVDGEDIytSDDVINLRTK 89
Cdd:cd03230 2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKII--LGLLKPD---SGEIKVLGKDI--KKEPEEVKRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 90 VGMVFQKPNPFP-MSIYDNvaygprthglrdkkqldkiveeslkgaaiwdevkdrlkssaLGLSGGQQQRICIARAIAMR 168
Cdd:cd03230 75 IGYLPEEPSLYEnLTVREN-----------------------------------------LKLSGGMKQRLALAQALLHD 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 169 PEVILMDEPTSALDPISTLKVEELIEDLKKDY-TIVIVTHNMQQAARISDETAFFLNGEV 227
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRELKKEGkTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
11-217 |
4.98e-45 |
|
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: 151.18 E-value: 4.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 11 VKDLDLFYGD-KQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRmndLIEDVtiKGNISVDGEDI--YTSDDVINLR 87
Cdd:cd03256 3 VENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNG---LVEPT--SGSVLIDGTDInkLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 88 TKVGMVFQKPNPFP-MSIYDNVAYG--PRTHGLRDKKQLDKiVEESLKGAAIWDEV--KDRLKSSALGLSGGQQQRICIA 162
Cdd:cd03256 78 RQIGMIFQQFNLIErLSVLENVLSGrlGRRSTWRSLFGLFP-KEEKQRALAALERVglLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489527602 163 RAIAMRPEVILMDEPTSALDPISTLKVEELIEDL--KKDYTIVIVTHNMQQAARISD 217
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREYAD 213
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
10-217 |
5.89e-45 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 151.36 E-value: 5.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDL-FYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndliEDVTiKGNISVDGEDI--YTSDDVINL 86
Cdd:COG3638 4 ELRNLSKrYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGL----VEPT-SGEILVDGQDVtaLRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 87 RTKVGMVFQKPNPFP-MSIYDNVAYG--PRTHGLRdkkQLDKIVEESLKGAAIW--DEV--KDRLKSSALGLSGGQQQRI 159
Cdd:COG3638 79 RRRIGMIFQQFNLVPrLSVLTNVLAGrlGRTSTWR---SLLGLFPPEDRERALEalERVglADKAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 160 CIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARISD 217
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgiTVVVNLHQVDLARRYAD 215
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
19-229 |
7.78e-45 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 158.40 E-value: 7.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 19 GDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDliedVTiKGNISVDGEDI--YTSDDvinLRTKVGMVFQK 96
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD----PT-SGRILIDGVDIrdLTLES---LRRQIGVVPQD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 97 PNPFPMSIYDNVAYGpRTHGLRDKkqldkiVEESLKGAAIWDEVkDRLKS---SALG-----LSGGQQQRICIARAIAMR 168
Cdd:COG1132 423 TFLFSGTIRENIRYG-RPDATDEE------VEEAAKAAQAHEFI-EALPDgydTVVGergvnLSGGQRQRIAIARALLKD 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489527602 169 PEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHnmqqaaRIS-----DETAFFLNGEVIE 229
Cdd:COG1132 495 PPILILDEATSALDTETEALIQEALERLMKGRTTIVIAH------RLStirnaDRILVLDDGRIVE 554
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
10-229 |
1.13e-44 |
|
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: 159.23 E-value: 1.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGD--KQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEdvtikGNISVDGEDIyTSDDVINLR 87
Cdd:COG2274 475 ELENVSFRYPGdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTS-----GRILIDGIDL-RQIDPASLR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 88 TKVGMVFQKPNPFPMSIYDNVAYGprtHGLRDKKQldkiVEESLKGAAIWDEVKD-------RLKSSALGLSGGQQQRIC 160
Cdd:COG2274 549 RQIGVVLQDVFLFSGTIRENITLG---DPDATDEE----IIEAARLAGLHDFIEAlpmgydtVVGEGGSNLSGGQRQRLA 621
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489527602 161 IARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHNMqQAARISDETAFFLNGEVIE 229
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRL-STIRLADRIIVLDKGRIVE 689
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
23-251 |
1.26e-44 |
|
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: 150.87 E-value: 1.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 23 ALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRmndLIEDVTikGNISVDGEDIYTSDD--VINLR-TKVGMVFQKPNP 99
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINR---LIEPTS--GKVLIDGQDIAAMSRkeLRELRrKKISMVFQSFAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 100 FP-MSIYDNVAYGPRTHGLRDKKQLDKiVEESLK--GAAIWdevKDRLKSSalgLSGGQQQRICIARAIAMRPEVILMDE 176
Cdd:cd03294 114 LPhRTVLENVAFGLEVQGVPRAEREER-AAEALElvGLEGW---EHKYPDE---LSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489527602 177 PTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTPVDKRTEDYITG 251
Cdd:cd03294 187 AFSALDPLIRREMQDELLRLQAELqkTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRG 263
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
17-227 |
1.60e-44 |
|
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: 149.69 E-value: 1.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 17 FYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndliEDVTiKGNISVDGEDIytsddvINL---RTKVGMV 93
Cdd:cd03300 9 FYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGF----ETPT-SGEILLDGKDI------TNLpphKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 94 FQKPNPFP-MSIYDNVAYGPRTHGLrDKKQLDKIVEESLKGAAIwDEVKDRLKSSalgLSGGQQQRICIARAIAMRPEVI 172
Cdd:cd03300 78 FQNYALFPhLTVFENIAFGLRLKKL-PKAEIKERVAEALDLVQL-EGYANRKPSQ---LSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527602 173 LMDEPTSALDpistLKV-EELIEDLKK-----DYTIVIVTHNMQQAARISDETAFFLNGEV 227
Cdd:cd03300 153 LLDEPLGALD----LKLrKDMQLELKRlqkelGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
19-251 |
1.74e-44 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 153.47 E-value: 1.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 19 GDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRmndLIEDVtiKGNISVDGEDIYTSDDV---INLRTKVGMVFQ 95
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNR---LIEPT--AGQIFIDGENIMKQSPVelrEVRRKKIGMVFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 96 KPNPFP-MSIYDNVAYGPRTHGLRDKKQLDKiVEESLKGAAIwDEVKDRLKSSalgLSGGQQQRICIARAIAMRPEVILM 174
Cdd:TIGR01186 79 QFALFPhMTILQNTSLGPELLGWPEQERKEK-ALELLKLVGL-EEYEHRYPDE---LSGGMQQRVGLARALAAEPDILLM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489527602 175 DEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTPVDKRTEDYITG 251
Cdd:TIGR01186 154 DEAFSALDPLIRDSMQDELKKLQATLqkTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGK 232
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
12-210 |
1.90e-44 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 149.05 E-value: 1.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 12 KDLDLFY-GDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndliEDVTiKGNISVDGEDIYT--SDDVINLRT 88
Cdd:COG2884 5 ENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGE----ERPT-SGQVLVNGQDLSRlkRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 89 KVGMVFQK----PNpfpMSIYDNVAYGPRTHGlRDKKQLDKIVEESLkgaaiwDEV--KDRLKSSALGLSGGQQQRICIA 162
Cdd:COG2884 80 RIGVVFQDfrllPD---RTVYENVALPLRVTG-KSRKEIRRRVREVL------DLVglSDKAKALPHELSGGEQQRVAIA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489527602 163 RAIAMRPEVILMDEPTSALDPISTLKVEELIEDL-KKDYTIVIVTHNMQ 210
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLE 198
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
10-226 |
1.91e-44 |
|
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: 147.01 E-value: 1.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEdvtikGNISVDGEDIyTSDDVINLRTK 89
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTS-----GEILIDGKDI-AKLPLEELRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 90 VGMVFQkpnpfpmsiydnvaygprthglrdkkqldkiveeslkgaaiwdevkdrlkssalgLSGGQQQRICIARAIAMRP 169
Cdd:cd00267 75 IGYVPQ-------------------------------------------------------LSGGQRQRVALARALLLNP 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489527602 170 EVILMDEPTSALDPISTLKVEELIEDL-KKDYTIVIVTHNMQQAARISDETAFFLNGE 226
Cdd:cd00267 100 DLLLLDEPTSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
24-179 |
2.98e-44 |
|
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: 146.25 E-value: 2.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 24 LKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEdvtikGNISVDGEDIyTSDDVINLRTKVGMVFQKPNPFP-M 102
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTE-----GTILLDGQDL-TDDERKSLRKEIGYVFQDPQLFPrL 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489527602 103 SIYDNVAYGPRTHGLRDKKQLDKiVEESLKGAAIWDEVKDRLKSSALGLSGGQQQRICIARAIAMRPEVILMDEPTS 179
Cdd:pfam00005 75 TVRENLRLGLLLKGLSKREKDAR-AEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
20-229 |
4.52e-44 |
|
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: 148.46 E-value: 4.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 20 DKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEdvtikGNISVDGEDIYTsddvIN---LRTKVGMVFQK 96
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTS-----GEILLDGVDIRD----LNlrwLRSQIGLVSQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 97 PNPFPMSIYDNVAYGprthglrDKKQLDKIVEESLKGAAIWDEVKD-------RLKSSALGLSGGQQQRICIARAIAMRP 169
Cdd:cd03249 86 PVLFDGTIAENIRYG-------KPDATDEEVEEAAKKANIHDFIMSlpdgydtLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 170 EVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHNMqQAARISDETAFFLNGEVIE 229
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRL-STIRNADLIAVLQNGQVVE 217
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
10-233 |
9.86e-43 |
|
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: 144.50 E-value: 9.86e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndliedVTIK-GNISVDGEDI--YTSDDVInl 86
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGL------LPPRsGSIRFDGRDItgLPPHERA-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 87 RTKVGMVFQKPNPFP-MSIYDN--VAYGPRTHGlRDKKQLDKIVEeslkgaaIWDEVKDRLKSSALGLSGGQQQRICIAR 163
Cdd:cd03224 74 RAGIGYVPEGRRIFPeLTVEENllLGAYARRRA-KRKARLERVYE-------LFPRLKERRKQLAGTLSGGEQQMLAIAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527602 164 AIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKD-YTIVIVTHNMQQAARISDETAFFLNGEVIeFSDT 233
Cdd:cd03224 146 ALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEgVTILLVEQNARFALEIADRAYVLERGRVV-LEGT 215
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
10-228 |
2.54e-42 |
|
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: 143.44 E-value: 2.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNrmnDLIEdvTIKGNISVDGEDIYtsddviNLRTK 89
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAIL---GLLK--PTSGSIRVFGKPLE------KERKR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 90 VGMVFQKPN---PFPMSIYDNVA---YGPRTHGLRDKKQLDKIVEESLK--GAAiwdEVKDRLKSSalgLSGGQQQRICI 161
Cdd:cd03235 70 IGYVPQRRSidrDFPISVRDVVLmglYGHKGLFRRLSKADKAKVDEALErvGLS---ELADRQIGE---LSGGQQQRVLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489527602 162 ARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKD-YTIVIVTHNMQQAARISDETAfFLNGEVI 228
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEYFDRVL-LLNRTVV 210
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
10-229 |
4.12e-42 |
|
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: 150.68 E-value: 4.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGD-KQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEdvtikGNISVDGEDIyTSDDVINLRT 88
Cdd:COG4988 338 ELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYS-----GSILINGVDL-SDLDPASWRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 89 KVGMVFQKPNPFPMSIYDNVA-YGPRThglrDKKQLdkivEESLKGAAIWDEVKD-------RLKSSALGLSGGQQQRIC 160
Cdd:COG4988 412 QIAWVPQNPYLFAGTIRENLRlGRPDA----SDEEL----EAALEAAGLDEFVAAlpdgldtPLGEGGRGLSGGQAQRLA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489527602 161 IARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTH---NMQQAARIsdetaFFL-NGEVIE 229
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHrlaLLAQADRI-----LVLdDGRIVE 551
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-232 |
1.88e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 142.95 E-value: 1.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 1 MELIdkikMSVKDLDLFYGD-KQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNdliedVTIKGNISVDGEDIyT 79
Cdd:PRK13647 1 MDNI----IEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIY-----LPQRGRVKVMGREV-N 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 80 SDDVINLRTKVGMVFQKPNP--FPMSIYDNVAYGPRTHGLrDKKQLDKIVEESLKGAAIWDeVKDRlksSALGLSGGQQQ 157
Cdd:PRK13647 71 AENEKWVRSKVGLVFQDPDDqvFSSTVWDDVAFGPVNMGL-DKDEVERRVEEALKAVRMWD-FRDK---PPYHLSYGQKK 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489527602 158 RICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKD-YTIVIVTHNMQQAARISDETAFFLNGEVIEFSD 232
Cdd:PRK13647 146 RVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGD 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
11-249 |
1.98e-41 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 141.43 E-value: 1.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 11 VKDLDLFYGDKqaLKKINMDIKENKVTALIGPSGCGKSTFIrtlnrmnDLIE--DVTIKGNISVDGEDIytSDDVINLRt 88
Cdd:COG3840 4 LDDLTYRYGDF--PLRFDLTIAAGERVAILGPSGAGKSTLL-------NLIAgfLPPDSGRILWNGQDL--TALPPAER- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 89 KVGMVFQKPNPFP-MSIYDNVAYGPRThGLR----DKKQLDKIVEE-SLKGaaiwdeVKDRLKSSalgLSGGQQQRICIA 162
Cdd:COG3840 72 PVSMLFQENNLFPhLTVAQNIGLGLRP-GLKltaeQRAQVEQALERvGLAG------LLDRLPGQ---LSGGQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 163 RAIAMRPEVILMDEPTSALDPIstLKVE--ELIEDLKKDY--TIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFT 238
Cdd:COG3840 142 RCLVRKRPILLLDEPFSALDPA--LRQEmlDLVDELCRERglTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLD 219
|
250
....*....|.
gi 489527602 239 TPVDKRTEDYI 249
Cdd:COG3840 220 GEPPPALAAYL 230
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
11-249 |
2.18e-41 |
|
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: 141.70 E-value: 2.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 11 VKDLDLFYGDKQaLKKINMDIKENKVTALIGPSGCGKSTFIRTLnrMNDLIEDvtiKGNISVDGEDIytsddvINL---R 87
Cdd:cd03299 3 VENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETI--AGFIKPD---SGKILLNGKDI------TNLppeK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 88 TKVGMVFQKPNPFP-MSIYDNVAYGPRtHGLRDKKQLDKIVEESLKGAAIwDEVKDRlksSALGLSGGQQQRICIARAIA 166
Cdd:cd03299 71 RDISYVPQNYALFPhMTVYKNIAYGLK-KRKVDKKEIERKVLEIAEMLGI-DHLLNR---KPETLSGGEQQRVAIARALV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 167 MRPEVILMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTPVDKR 244
Cdd:cd03299 146 VNPKILLLDEPFSALDVRTKEKLREELKKIRKEFgvTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEF 225
|
....*
gi 489527602 245 TEDYI 249
Cdd:cd03299 226 VAEFL 230
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
10-228 |
2.39e-41 |
|
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: 139.88 E-value: 2.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIedvtiKGNISVDGEDIyTSDDVINLRTK 89
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPS-----SGEILLDGKDL-ASLSPKELARK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 90 VGMVFQkpnpfpmsIYDNVaygprthGLRDKKqlDKIVEEslkgaaiwdevkdrlkssalgLSGGQQQRICIARAIAMRP 169
Cdd:cd03214 75 IAYVPQ--------ALELL-------GLAHLA--DRPFNE---------------------LSGGERQRVLLARALAQEP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527602 170 EVILMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARISDETAFFLNGEVI 228
Cdd:cd03214 117 PILLLDEPTSHLDIAHQIELLELLRRLARERgkTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
6-228 |
4.07e-41 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 144.86 E-value: 4.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 6 KIKMSVKDLDLFYGD--KQALKKI----------------------NMDIKENKVTALIGPSGCGKSTFIRTLNRmndLI 61
Cdd:COG4175 1 MPKIEVRNLYKIFGKrpERALKLLdqgkskdeilektgqtvgvndaSFDVEEGEIFVIMGLSGSGKSTLVRCLNR---LI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 62 EdVTiKGNISVDGEDIYTSDD--VINLR-TKVGMVFQKPNPFP-MSIYDNVAYGPRTHGLrDKKQLDKIVEESLK--GAA 135
Cdd:COG4175 78 E-PT-AGEVLIDGEDITKLSKkeLRELRrKKMSMVFQHFALLPhRTVLENVAFGLEIQGV-PKAERRERAREALElvGLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 136 IWdevKDRLKSSalgLSGGQQQRICIARAIAMRPEVILMDEPTSALDP-ISTLKVEELIE---DLKKdyTIVIVTHNMQQ 211
Cdd:COG4175 155 GW---EDSYPDE---LSGGMQQRVGLARALATDPDILLMDEAFSALDPlIRREMQDELLElqaKLKK--TIVFITHDLDE 226
|
250
....*....|....*..
gi 489527602 212 AARISDETAFFLNGEVI 228
Cdd:COG4175 227 ALRLGDRIAIMKDGRIV 243
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
8-251 |
2.71e-40 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 139.72 E-value: 2.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 8 KMSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEdvtikGNISVDGEDIYTSDD----- 82
Cdd:PRK10619 5 KLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSE-----GSIVVNGQTINLVRDkdgql 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 83 -------VINLRTKVGMVFQKPNPFP-MSIYDNVAYGP-RTHGLRDKKQLDKIVEeSLKGAAIWDEVKDRLKSSalgLSG 153
Cdd:PRK10619 80 kvadknqLRLLRTRLTMVFQHFNLWShMTVLENVMEAPiQVLGLSKQEARERAVK-YLAKVGIDERAQGKYPVH---LSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 154 GQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKD-YTIVIVTHNMQQAARISDETAFFLNGEVIEFSD 232
Cdd:PRK10619 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGA 235
|
250
....*....|....*....
gi 489527602 233 TKTMFTTPVDKRTEDYITG 251
Cdd:PRK10619 236 PEQLFGNPQSPRLQQFLKG 254
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
19-249 |
2.75e-40 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 141.86 E-value: 2.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 19 GDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndliEDVTiKGNISVDGEDIYT--SDDVINLRTKVGMVFQK 96
Cdd:PRK11153 16 RTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLL----ERPT-SGRVLVDGQDLTAlsEKELRKARRQIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 97 PNPfpMS---IYDNVAYGPRTHGlRDKKQLDKIVEESLKGAAIWDEvKDRLKSSalgLSGGQQQRICIARAIAMRPEVIL 173
Cdd:PRK11153 91 FNL--LSsrtVFDNVALPLELAG-TPKAEIKARVTELLELVGLSDK-ADRYPAQ---LSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489527602 174 MDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTPVDKRTEDYI 249
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDINRELglTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFI 241
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
26-228 |
5.76e-40 |
|
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: 137.43 E-value: 5.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 26 KINMDIKENkVTALIGPSGCGKSTFIRTLNRmndlIEDVTiKGNISVDGEDIYTSDDVINL---RTKVGMVFQKPNPFP- 101
Cdd:cd03297 16 KIDFDLNEE-VTGIFGASGAGKSTLLRCIAG----LEKPD-GGTIVLNGTVLFDSRKKINLppqQRKIGLVFQQYALFPh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 102 MSIYDNVAYGPRTHGLRDKKQLdkiVEESLKGAAIwDEVKDRlksSALGLSGGQQQRICIARAIAMRPEVILMDEPTSAL 181
Cdd:cd03297 90 LNVRENLAFGLKRKRNREDRIS---VDELLDLLGL-DHLLNR---YPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489527602 182 DPISTLKVEELIEDLKKDYTI--VIVTHNMQQAARISDETAFFLNGEVI 228
Cdd:cd03297 163 DRALRLQLLPELKQIKKNLNIpvIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-228 |
6.31e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 139.41 E-value: 6.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 20 DKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNrmnDLIEDVTikGNISVDGEDIytSDDVINL---RTKVGMVFQK 96
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLN---GLLKPTS--GKIIIDGVDI--TDKKVKLsdiRKKVGLVFQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 97 P--NPFPMSIYDNVAYGPRTHGLRDKkQLDKIVEESLKGAAI-WDEVKDRlksSALGLSGGQQQRICIARAIAMRPEVIL 173
Cdd:PRK13637 92 PeyQLFEETIEKDIAFGPINLGLSEE-EIENRVKRAMNIVGLdYEDYKDK---SPFELSGGQKRRVAIAGVVAMEPKILI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489527602 174 MDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARISDETAFFLNGEVI 228
Cdd:PRK13637 168 LDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
11-244 |
6.41e-40 |
|
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: 138.20 E-value: 6.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 11 VKDLDLFYG-DKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEdvtikGNISVDGEDI--YTSDDVINLR 87
Cdd:TIGR02315 4 VENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSS-----GSILLEGTDItkLRGKKLRKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 88 TKVGMVFQKPNPFP-MSIYDNV-----AYGPRTHGL--RDKKQLDKIVEESLKGAAIWDEVKDRLKSsalgLSGGQQQRI 159
Cdd:TIGR02315 79 RRIGMIFQHYNLIErLTVLENVlhgrlGYKPTWRSLlgRFSEEDKERALSALERVGLADKAYQRADQ----LSGGQQQRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 160 CIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDL--KKDYTIVIVTHNMQQAARISDETAFFLNGEVIeFSDTKTMF 237
Cdd:TIGR02315 155 AIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRInkEDGITVIINLHQVDLAKKYADRIVGLKAGEIV-FDGAPSEL 233
|
....*..
gi 489527602 238 TTPVDKR 244
Cdd:TIGR02315 234 DDEVLRH 240
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
17-212 |
1.04e-39 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 136.01 E-value: 1.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 17 FYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNrmnDLIEDVtiKGNISVDGEDI-YTSDDVINLRTKVGMVFQ 95
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLN---GLLRPQ--SGAVLIDGEPLdYSRKGLLERRQRVGLVFQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 96 KPNP--FPMSIYDNVAYGPRTHGLRDKkQLDKIVEESLKGAAIwDEVKDRLKSSalgLSGGQQQRICIARAIAMRPEVIL 173
Cdd:TIGR01166 76 DPDDqlFAADVDQDVAFGPLNLGLSEA-EVERRVREALTAVGA-SGLRERPTHC---LSGGEKKRVAIAGAVAMRPDVLL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489527602 174 MDEPTSALDPISTLKVEELIEDLKKD-YTIVIVTHNMQQA 212
Cdd:TIGR01166 151 LDEPTAGLDPAGREQMLAILRRLRAEgMTVVISTHDVDLA 190
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
9-227 |
2.21e-39 |
|
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: 135.85 E-value: 2.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRmndlIEDVTiKGNISVDGEDiytsddVINLRT 88
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAG----LEEPT-SGRIYIGGRD------VTDLPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 89 K---VGMVFQKPNPFP-MSIYDNVAYGPRTHGlRDKKQLDKIVEESLKGAAIwDEVKDRLKSSalgLSGGQQQRICIARA 164
Cdd:cd03301 70 KdrdIAMVFQNYALYPhMTVYDNIAFGLKLRK-VPKDEIDERVREVAELLQI-EHLLDRKPKQ---LSGGQRQRVALGRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489527602 165 IAMRPEVILMDEPTSALDpiSTLKVEELIEdLKK-----DYTIVIVTHNMQQAARISDETAFFLNGEV 227
Cdd:cd03301 145 IVREPKVFLMDEPLSNLD--AKLRVQMRAE-LKRlqqrlGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
22-240 |
3.31e-39 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 138.71 E-value: 3.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 22 QALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRmndlIEDVTiKGNISVDGEDIYTSD--DVINLRTKVGMVFQKP-- 97
Cdd:COG4608 32 KAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLR----LEEPT-SGEILFDGQDITGLSgrELRPLRRRMQMVFQDPya 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 98 --NPfPMSIYDNVAYGPRTHGLRDKKQLDKIVEESLkgaaiwDEVkdRLKSSALG-----LSGGQQQRICIARAIAMRPE 170
Cdd:COG4608 107 slNP-RMTVGDIIAEPLRIHGLASKAERRERVAELL------ELV--GLRPEHADrypheFSGGQRQRIGIARALALNPK 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489527602 171 VILMDEPTSALDpIStlkVE----ELIEDLKKDY--TIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTP 240
Cdd:COG4608 178 LIVCDEPVSALD-VS---IQaqvlNLLEDLQDELglTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARP 249
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
11-240 |
1.06e-37 |
|
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: 132.08 E-value: 1.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 11 VKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndliEDVTiKGNISVDGEDIyTSDDVinLRTKV 90
Cdd:cd03296 5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGL----ERPD-SGTILFGGEDA-TDVPV--QERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 91 GMVFQKPNPFP-MSIYDNVAYGPRTHGLR---DKKQLDKIVEESLKGAAIwDEVKDRLKSSalgLSGGQQQRICIARAIA 166
Cdd:cd03296 77 GFVFQHYALFRhMTVFDNVAFGLRVKPRSerpPEAEIRAKVHELLKLVQL-DWLADRYPAQ---LSGGQRQRVALARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 167 MRPEVILMDEPTSALDPistlKV-EELIEDLKK-----DYTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTP 240
Cdd:cd03296 153 VEPKVLLLDEPFGALDA----KVrKELRRWLRRlhdelHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHP 228
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
10-228 |
1.25e-37 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 131.79 E-value: 1.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIrtlnrmnDLIEDVTI--KGNISVDGEDIyTSDDViNLR 87
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLF-------NLISGFLRptSGSVLFDGEDI-TGLPP-HEI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 88 TKVGMV--FQKPNPFP-MSIYDNVAYGPRTHG---------LRDKKQLDKIVEESLKGAAIWDevkdRLKSSALGLSGGQ 155
Cdd:cd03219 73 ARLGIGrtFQIPRLFPeLTVLENVMVAAQARTgsglllaraRREEREARERAEELLERVGLAD----LADRPAGELSYGQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489527602 156 QQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLK-KDYTIVIVTHNMQQAARISDETAFFLNGEVI 228
Cdd:cd03219 149 QRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELReRGITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-228 |
2.45e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 132.84 E-value: 2.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 21 KQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNrmnDLIEDVtiKGNISVdGEDIYTSD----DVINLRTKVGMVFQK 96
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLN---GLLQPT--SGTVTI-GERVITAGkknkKLKPLRKKVGIVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 97 PNP--FPMSIYDNVAYGPRTHGLRDKKQLDKiVEESLKGAAIWDEVKDRlksSALGLSGGQQQRICIARAIAMRPEVILM 174
Cdd:PRK13634 94 PEHqlFEETVEKDICFGPMNFGVSEEDAKQK-AREMIELVGLPEELLAR---SPFELSGGQMRRVAIAGVLAMEPEVLVL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489527602 175 DEPTSALDPISTLKVEELIEDL--KKDYTIVIVTHNMQQAARISDETAFFLNGEVI 228
Cdd:PRK13634 170 DEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAARYADQIVVMHKGTVF 225
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
11-236 |
2.50e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 132.12 E-value: 2.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 11 VKDLDLFYGD-KQALKKINMDIKENKVTALIGPSGCGKSTfirTLNRMNDLIEDVtiKGNISVDGEDI-YTSDDVINLRT 88
Cdd:PRK13639 4 TRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKST---LFLHFNGILKPT--SGEVLIKGEPIkYDKKSLLEVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 89 KVGMVFQKPNP--FPMSIYDNVAYGPRTHGLrDKKQLDKIVEESLKGAAIwdevKDRLKSSALGLSGGQQQRICIARAIA 166
Cdd:PRK13639 79 TVGIVFQNPDDqlFAPTVEEDVAFGPLNLGL-SKEEVEKRVKEALKAVGM----EGFENKPPHHLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489527602 167 MRPEVILMDEPTSALDPISTLKVEELIEDL-KKDYTIVIVTHNMQQAARISDETAFFLNGEVIE-------FSDTKTM 236
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKegtpkevFSDIETI 231
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
10-230 |
3.60e-37 |
|
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: 130.01 E-value: 3.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQALKKINMDIkENKVTALIGPSGCGKSTFIRTLNrmnDLIEDVtiKGNISVDGEDIytSDDVINLRTK 89
Cdd:cd03264 2 QLENLTKRYGKKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILA---TLTPPS--SGTIRIDGQDV--LKQPQKLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 90 VGMVFQKPNPFP-MSIYDNVAYGPRTHGLRDKKQlDKIVEESLKGAAIWDEVKDRLKSsalgLSGGQQQRICIARAIAMR 168
Cdd:cd03264 74 IGYLPQEFGVYPnFTVREFLDYIAWLKGIPSKEV-KARVDEVLELVNLGDRAKKKIGS----LSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489527602 169 PEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHNMQQAARISDETAFFLNGEVIEF 230
Cdd:cd03264 149 PSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
10-228 |
2.31e-36 |
|
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: 128.56 E-value: 2.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndliedVTIK-GNISVDGEDIytsddvINLRT 88
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGL------LPPRsGSIRFDGEDI------TGLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 89 K------VGMVFQKPNPFP-MSIYDNVAYGPRTHglRDKKQLDKIVEEslkgaaIWD---EVKDRLKSSALGLSGGQQQR 158
Cdd:COG0410 73 HriarlgIGYVPEGRRIFPsLTVEENLLLGAYAR--RDRAEVRADLER------VYElfpRLKERRRQRAGTLSGGEQQM 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489527602 159 ICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKD-YTIVIVTHNMQQAARISDeTAFFL-NGEVI 228
Cdd:COG0410 145 LAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREgVTILLVEQNARFALEIAD-RAYVLeRGRIV 215
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
9-237 |
5.55e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 129.20 E-value: 5.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGD-KQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEDVTIKGNISVDgediYTSDDVINLR 87
Cdd:PRK13636 6 LKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID----YSRKGLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 88 TKVGMVFQKPNP--FPMSIYDNVAYGPRTHGLrDKKQLDKIVEESLKGAAIwDEVKDRLKSSalgLSGGQQQRICIARAI 165
Cdd:PRK13636 82 ESVGMVFQDPDNqlFSASVYQDVSFGAVNLKL-PEDEVRKRVDNALKRTGI-EHLKDKPTHC---LSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489527602 166 AMRPEVILMDEPTSALDPISTLKVEELIEDLKK--DYTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMF 237
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
9-228 |
6.03e-36 |
|
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: 127.24 E-value: 6.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGDKQ--ALKKINMDIKENKVTALIGPSGCGKSTFIRTLN---RMNdliedvtiKGNISVDGEDIYTSDDV 83
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTgelRPT--------SGTAYINGYSIRTDRKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 84 InlRTKVGMVFQKPNPFP-MSIYDNVAYGPRTHGLRdKKQLDKIVEESLKGAAIwDEVKDRLKSSalgLSGGQQQRICIA 162
Cdd:cd03263 73 A--RQSLGYCPQFDALFDeLTVREHLRFYARLKGLP-KSEIKEEVELLLRVLGL-TDKANKRART---LSGGMKRKLSLA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489527602 163 RAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHNMQQAARISDETAFFLNGEVI 228
Cdd:cd03263 146 IALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
9-229 |
9.62e-36 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 130.16 E-value: 9.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndlieDVTIKGNISVDGEDIytSDDVINLRt 88
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGL-----ERQTAGTIYQGGRDI--TRLPPQKR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 89 KVGMVFQKPNPFP-MSIYDNVAYGPRTHGLrDKKQLDKIVEESLKGAAIwDEVKDRLKSSalgLSGGQQQRICIARAIAM 167
Cdd:TIGR03265 77 DYGIVFQSYALFPnLTVADNIAYGLKNRGM-GRAEVAERVAELLDLVGL-PGSERKYPGQ---LSGGQQQRVALARALAT 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489527602 168 RPEVILMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARISDETAfFLNGEVIE 229
Cdd:TIGR03265 152 SPGLLLLDEPLSALDARVREHLRTEIRQLQRRLgvTTIMVTHDQEEALSMADRIV-VMNHGVIE 214
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
23-237 |
1.34e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 127.94 E-value: 1.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 23 ALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNdliedVTIKGNISVDGEDIyTSD----DVINLRTKVGMVFQKPN 98
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLH-----VPTQGSVRVDDTLI-TSTsknkDIKQIRKKVGLVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 99 P--FPMSIYDNVAYGPRTHGLrDKKQLDKIVEESLKGAAIWDEVKDRlksSALGLSGGQQQRICIARAIAMRPEVILMDE 176
Cdd:PRK13649 96 SqlFEETVLKDVAFGPQNFGV-SQEEAEALAREKLALVGISESLFEK---NPFELSGGQMRRVAIAGILAMEPKILVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489527602 177 PTSALDPISTLKVEELIEDLKKD-YTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMF 237
Cdd:PRK13649 172 PTAGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
21-236 |
1.50e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 127.90 E-value: 1.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 21 KQALKKINMDIKENKVTALIGPSGCGKSTFIRtlnRMNDLIedVTIKGNISVDGEDIYTSDDVINLRTKVGMVFQKP-NP 99
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAK---HMNALL--IPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQNPdNQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 100 FPMSIYD-NVAYGPRTHGLrDKKQLDKIVEESLKGAAIWdEVKdrlKSSALGLSGGQQQRICIARAIAMRPEVILMDEPT 178
Cdd:PRK13633 98 IVATIVEeDVAFGPENLGI-PPEEIRERVDESLKKVGMY-EYR---RHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489527602 179 SALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARiSDETAFFLNGEVIE-------FSDTKTM 236
Cdd:PRK13633 173 AMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVE-ADRIIVMDSGKVVMegtpkeiFKEVEMM 238
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
11-228 |
2.06e-35 |
|
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: 125.95 E-value: 2.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 11 VKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDliedvTIKGNISVDGEDIytSDDVINLRTKV 90
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLK-----PTSGRATVAGHDV--VREPREVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 91 GMVFQKPNPFP-MSIYDNVAYGPRTHGLRDKKqLDKIVEESLKGAAIWdEVKDRLKSSalgLSGGQQQRICIARAIAMRP 169
Cdd:cd03265 76 GIVFQDLSVDDeLTGWENLYIHARLYGVPGAE-RRERIDELLDFVGLL-EAADRLVKT---YSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527602 170 EVILMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARISDETAFFLNGEVI 228
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
10-229 |
6.75e-35 |
|
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: 131.04 E-value: 6.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFY--GDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndliEDVTiKGNISVDGEDI--YTSDDvin 85
Cdd:COG4987 335 ELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRF----LDPQ-SGSITLGGVDLrdLDEDD--- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 86 LRTKVGMVFQKPNPFPMSIYDNvaygprthgLR---------------DKKQLDKIVEESLKGaaiWDevkDRLKSSALG 150
Cdd:COG4987 407 LRRRIAVVPQRPHLFDTTLREN---------LRlarpdatdeelwaalERVGLGDWLAALPDG---LD---TWLGEGGRR 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489527602 151 LSGGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHNMQQAARIsDETAFFLNGEVIE 229
Cdd:COG4987 472 LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERM-DRILVLEDGRIVE 549
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
18-240 |
1.09e-34 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 127.14 E-value: 1.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 18 YGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndliEDVTiKGNISVDGEDIytSDDVINLRtKVGMVFQKP 97
Cdd:PRK11432 16 FGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGL----EKPT-EGQIFIDGEDV--THRSIQQR-DICMVFQSY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 98 NPFP-MSIYDNVAYGPRTHGlRDKKQLDKIVEESLKG---AAIWDEVKDRLkssalglSGGQQQRICIARAIAMRPEVIL 173
Cdd:PRK11432 88 ALFPhMSLGENVGYGLKMLG-VPKEERKQRVKEALELvdlAGFEDRYVDQI-------SGGQQQRVALARALILKPKVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489527602 174 MDEPTSALDPISTLKVEELIEDLKKDYTI--VIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTP 240
Cdd:PRK11432 160 FDEPLSNLDANLRRSMREKIRELQQQFNItsLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
27-240 |
2.11e-34 |
|
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: 126.37 E-value: 2.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 27 INMDIKENKVTALIGPSGCGKSTFIRT---LNRMNDliedvtikGNISVDGEDIYTSDDVINLRT---KVGMVFQKPNPF 100
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAiagLERPDS--------GRIRLGGEVLQDSARGIFLPPhrrRIGYVFQEARLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 101 P-MSIYDNVAYG-PRTHGLRDKKQLDKIVE----ESLkgaaiwdevkdrLKSSALGLSGGQQQRICIARAIAMRPEVILM 174
Cdd:COG4148 90 PhLSVRGNLLYGrKRAPRAERRISFDEVVEllgiGHL------------LDRRPATLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 175 DEPTSALDpiSTLKVE--ELIEDLKKDYTI--VIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTP 240
Cdd:COG4148 158 DEPLAALD--LARKAEilPYLERLRDELDIpiLYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
18-230 |
2.58e-34 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 125.20 E-value: 2.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 18 YGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndliedvtIK---GNISVDGEDIYTSDDviNLRTKVGMVF 94
Cdd:TIGR01188 3 YGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTL--------LRptsGTARVAGYDVVREPR--KVRRSIGIVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 95 QKPNPFP-MSIYDNVAYGPRTHGLRdKKQLDKIVEESLKGAAIWDEVKDRLKssalGLSGGQQQRICIARAIAMRPEVIL 173
Cdd:TIGR01188 73 QYASVDEdLTGRENLEMMGRLYGLP-KDEAEERAEELLELFELGEAADRPVG----TYSGGMRRRLDIAASLIHQPDVLF 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489527602 174 MDEPTSALDPISTLKVEELIEDLKK-DYTIVIVTHNMQQAARISDETAFFLNGEVIEF 230
Cdd:TIGR01188 148 LDEPTTGLDPRTRRAIWDYIRALKEeGVTILLTTHYMEEADKLCDRIAIIDHGRIIAE 205
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
20-229 |
6.08e-34 |
|
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: 122.34 E-value: 6.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 20 DKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEdvtikGNISVDGEDI--YTSDdviNLRTKVGMVFQKP 97
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSS-----GSILIDGQDIreVTLD---SLRRAIGVVPQDT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 98 NPFPMSIYDNVAYGprthglrDKKQLDKIVEESLKGAAIWDEVKD-------RLKSSALGLSGGQQQRICIARAIAMRPE 170
Cdd:cd03253 85 VLFNDTIGYNIRYG-------RPDATDEEVIEAAKAAQIHDKIMRfpdgydtIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489527602 171 VILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHNMQQAARiSDETAFFLNGEVIE 229
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVE 215
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
10-229 |
7.88e-34 |
|
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: 121.95 E-value: 7.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQ--ALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEdvtikGNISVDGEDI--YTSDDvin 85
Cdd:cd03251 2 EFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDS-----GRILIDGHDVrdYTLAS--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 86 LRTKVGMVFQKPNPFPMSIYDNVAYGPRTHGLRDkkqldkiVEESLKGAAIWDEVKD-------RLKSSALGLSGGQQQR 158
Cdd:cd03251 74 LRRQIGLVSQDVFLFNDTVAENIAYGRPGATREE-------VEEAARAANAHEFIMElpegydtVIGERGVKLSGGQRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489527602 159 ICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHnmqqaaRIS-----DETAFFLNGEVIE 229
Cdd:cd03251 147 IAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAH------RLStienaDRIVVLEDGKIVE 216
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
10-228 |
9.94e-34 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 122.66 E-value: 9.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYG----DKQALKKINMDIKENKVTALIGPSGCGKSTFirtLNRMNDLIEDVTikGNISVDGEDIYTSDdvin 85
Cdd:COG4525 5 TVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTL---LNLIAGFLAPSS--GEITLDGVPVTGPG---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 86 lrTKVGMVFQKPNPFP-MSIYDNVAYGPRTHGLrDKKQLDKIVEESLK--------GAAIWDevkdrlkssalgLSGGQQ 156
Cdd:COG4525 76 --ADRGVVFQKDALLPwLNVLDNVAFGLRLRGV-PKAERRARAEELLAlvgladfaRRRIWQ------------LSGGMR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489527602 157 QRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHnmqqaariSDETAFFLNGEVI 228
Cdd:COG4525 141 QRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTgkGVFLITH--------SVEEALFLATRLV 206
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
18-229 |
1.16e-33 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 125.06 E-value: 1.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 18 YGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRtlnrmndLI---EDVTiKGNISVDGEDIytsDDVINLRTKVGMVF 94
Cdd:PRK09452 24 FDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLR-------LIagfETPD-SGRIMLDGQDI---THVPAENRHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 95 QKPNPFP-MSIYDNVAYGprthgLRDKK----QLDKIVEESLKGAAIwDEVKDRLKSSalgLSGGQQQRICIARAIAMRP 169
Cdd:PRK09452 93 QSYALFPhMTVFENVAFG-----LRMQKtpaaEITPRVMEALRMVQL-EEFAQRKPHQ---LSGGQQQRVAIARAVVNKP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489527602 170 EVILMDEPTSALDpiSTLKVEELIEdLKK-----DYTIVIVTHNMQQAARISDETAFFLNGeVIE 229
Cdd:PRK09452 164 KVLLLDESLSALD--YKLRKQMQNE-LKAlqrklGITFVFVTHDQEEALTMSDRIVVMRDG-RIE 224
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
39-240 |
1.16e-33 |
|
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: 124.14 E-value: 1.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 39 LIGPSGCGKSTFIRTLNRMNDLIEdvtikGNISVDGEDIytsDDVINLRTKVGMVFQKPNPFP-MSIYDNVAYGPRTHGL 117
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDS-----GSIMLDGEDV---TNVPPHLRHINMVFQSYALFPhMTVEENVAFGLKMRKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 118 rDKKQLDKIVEESLKGAaiwdEVKDRLKSSALGLSGGQQQRICIARAIAMRPEVILMDEPTSALD----PISTLKVEELI 193
Cdd:TIGR01187 73 -PRAEIKPRVLEALRLV----QLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDkklrDQMQLELKTIQ 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489527602 194 EDLkkDYTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTP 240
Cdd:TIGR01187 148 EQL--GITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEP 192
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-240 |
1.88e-33 |
|
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: 126.72 E-value: 1.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 19 GDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRmndLIEDvtiKGNISVDGEDI--YTSDDVINLRTKVGMVFQK 96
Cdd:COG4172 297 GHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR---LIPS---EGEIRFDGQDLdgLSRRALRPLRRRMQVVFQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 97 P----NPfPMSIYDNVAYGPRTHGL-RDKKQLDKIVEESLkgaaiwDEVkdRLKSSALG-----LSGGQQQRICIARAIA 166
Cdd:COG4172 371 PfgslSP-RMTVGQIIAEGLRVHGPgLSAAERRARVAEAL------EEV--GLDPAARHrypheFSGGQRQRIAIARALI 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489527602 167 MRPEVILMDEPTSALDpISTLK-VEELIEDLKKDY--TIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTP 240
Cdd:COG4172 442 LEPKLLVLDEPTSALD-VSVQAqILDLLRDLQREHglAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAP 517
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
10-228 |
3.11e-33 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 120.91 E-value: 3.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndliedvtIK---GNISVDGEDIytsddvINL 86
Cdd:COG0411 6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGF--------YRptsGRILFDGRDI------TGL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 87 ----RTKVGMV--FQKPNPFP-MSIYDNVAYGPRTHG--------------LRDKKQLDKIVEESLKGAAIwDEVKDRLk 145
Cdd:COG0411 72 pphrIARLGIArtFQNPRLFPeLTVLENVLVAAHARLgrgllaallrlpraRREEREARERAEELLERVGL-ADRADEP- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 146 ssALGLSGGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKD--YTIVIVTHNMQQAARISDETAFFL 223
Cdd:COG0411 150 --AGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErgITILLIEHDMDLVMGLADRIVVLD 227
|
....*
gi 489527602 224 NGEVI 228
Cdd:COG0411 228 FGRVI 232
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
8-229 |
6.38e-33 |
|
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: 119.64 E-value: 6.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 8 KMSVKDLDLFY-GDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDliedvTIKGNISVDGEDIyTSDDVINL 86
Cdd:cd03254 2 EIEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYD-----PQKGQILIDGIDI-RDISRKSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 87 RTKVGMVFQKPNPFPMSIYDNVAYGprthglrDKKQLDKIVEESLKGAAIWDEVKDR-------LKSSALGLSGGQQQRI 159
Cdd:cd03254 76 RSMIGVVLQDTFLFSGTIMENIRLG-------RPNATDEEVIEAAKEAGAHDFIMKLpngydtvLGENGGNLSQGERQLL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 160 CIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHNMqQAARISDETAFFLNGEVIE 229
Cdd:cd03254 149 AIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRL-STIKNADKILVLDDGKIIE 217
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-238 |
8.28e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 120.48 E-value: 8.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 4 IDKIKMSVKDLDLFYGD--KQALKKINMDIKENKVTALIGPSGCGKSTFIRTLnrmndliedVTI----KGNISVDGEDI 77
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKIL---------TGLlkpqSGEIKIDGITI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 78 yTSDDVINLRTKVGMVFQKP-NPF-PMSIYDNVAYGPRTHGLrDKKQLDKIVEESLKGAAIwdevKDRLKSSALGLSGGQ 155
Cdd:PRK13632 74 -SKENLKEIRKKIGIIFQNPdNQFiGATVEDDIAFGLENKKV-PPKKMKDIIDDLAKKVGM----EDYLDKEPQNLSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 156 QQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKK--DYTIVIVTHNMQQAArISDETAFFLNGEVIEFSDT 233
Cdd:PRK13632 148 KQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKP 226
|
....*
gi 489527602 234 KTMFT 238
Cdd:PRK13632 227 KEILN 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
11-237 |
9.46e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 120.61 E-value: 9.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 11 VKDLDLFYGDKQ---ALKKINMDIKENKVTALIGPSGCGKSTFIRTLNrmnDLIEDVTikGNISVDGEDIyTSDDVINLR 87
Cdd:PRK13650 7 VKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLID---GLLEAES--GQIIIDGDLL-TEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 88 TKVGMVFQKP-NPF-PMSIYDNVAYGPRTHGLrDKKQLDKIVEESLKGAAIWDeVKDRLKSSalgLSGGQQQRICIARAI 165
Cdd:PRK13650 81 HKIGMVFQNPdNQFvGATVEDDVAFGLENKGI-PHEEMKERVNEALELVGMQD-FKEREPAR---LSGGQKQRVAIAGAV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489527602 166 AMRPEVILMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAArISDETAFFLNGEVIEFSDTKTMF 237
Cdd:PRK13650 156 AMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELF 228
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
20-248 |
1.09e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 120.65 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 20 DKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNrmnDLIEDVTikGNISVDGEDIY--TSDDVIN-LRTKVGMVFQK 96
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNIN---ALLKPTT--GTVTVDDITIThkTKDKYIRpVRKRIGMVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 97 PNP--FPMSIYDNVAYGPRTHGLrdkkQLDKIVEESLKGAAIWDEVKDRLKSSALGLSGGQQQRICIARAIAMRPEVILM 174
Cdd:PRK13646 94 PESqlFEDTVEREIIFGPKNFKM----NLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489527602 175 DEPTSALDPISTLKVEELIEDL--KKDYTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTpvDKRTEDY 248
Cdd:PRK13646 170 DEPTAGLDPQSKRQVMRLLKSLqtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD--KKKLADW 243
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
8-229 |
2.08e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 119.35 E-value: 2.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 8 KMSVKDLDLFYGD--KQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndLIEDvtiKGNISVDGEdIYTSDDVIN 85
Cdd:PRK13635 5 IIRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGL--LLPE---AGTITVGGM-VLSEETVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 86 LRTKVGMVFQKP-NPF-PMSIYDNVAYGPRTHGL-RDkkQLDKIVEESLKGAAIwDEVKDRLKSSalgLSGGQQQRICIA 162
Cdd:PRK13635 79 VRRQVGMVFQNPdNQFvGATVQDDVAFGLENIGVpRE--EMVERVDQALRQVGM-EDFLNREPHR---LSGGQKQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489527602 163 RAIAMRPEVILMDEPTSALDPISTLKVEELIEDLK--KDYTIVIVTHNMQQAARiSDETAFFLNGEVIE 229
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVLETVRQLKeqKGITVLSITHDLDEAAQ-ADRVIVMNKGEILE 220
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
7-233 |
2.67e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 119.81 E-value: 2.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 7 IKMSVKDLDLFYGDK-----QALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNdLIEDVTI-------KGNISVDG 74
Cdd:PRK13651 1 MQIKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALL-LPDTGTIewifkdeKNKKKTKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 75 EDIYTSDDVI------------NLRTKVGMVFQ--KPNPFPMSIYDNVAYGPRTHGLrDKKQLDKIVEESLKGAAIwDEv 140
Cdd:PRK13651 80 KEKVLEKLVIqktrfkkikkikEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGV-SKEEAKKRAAKYIELVGL-DE- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 141 kDRLKSSALGLSGGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDL-KKDYTIVIVTHNMQQAARISDET 219
Cdd:PRK13651 157 -SYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVLEWTKRT 235
|
250
....*....|....
gi 489527602 220 AFFLNGEVIEFSDT 233
Cdd:PRK13651 236 IFFKDGKIIKDGDT 249
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
19-214 |
3.08e-32 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 117.35 E-value: 3.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 19 GDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndlieDVTIKGNISVDGEDI--YTSDDVINLRTKVGMVFQK 96
Cdd:TIGR02673 13 GGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGA-----LTPSRGQVRIAGEDVnrLRGRQLPLLRRRIGVVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 97 PNPFP-MSIYDNVAYGPRTHGlRDKKQLDKIVEESLKgaaiWDEVKDRLKSSALGLSGGQQQRICIARAIAMRPEVILMD 175
Cdd:TIGR02673 88 FRLLPdRTVYENVALPLEVRG-KKEREIQRRVGAALR----QVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLAD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489527602 176 EPTSALDPISTLKVEELIEDL-KKDYTIVIVTHNMQQAAR 214
Cdd:TIGR02673 163 EPTGNLDPDLSERILDLLKRLnKRGTTVIVATHDLSLVDR 202
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
22-238 |
4.07e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 118.96 E-value: 4.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 22 QALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndLIEDV--TIKGNISVDGeDIYTSDDVINLRTKVGMVFQKP-- 97
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGL--IISETgqTIVGDYAIPA-NLKKIKEVKRLRKEIGLVFQFPey 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 98 NPFPMSIYDNVAYGPRTHGlRDKKQLDKIVEESLKGAAIwdeVKDRLKSSALGLSGGQQQRICIARAIAMRPEVILMDEP 177
Cdd:PRK13645 102 QLFQETIEKDIAFGPVNLG-ENKQEAYKKVPELLKLVQL---PEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489527602 178 TSALDPISTLKVEELIEDLKKDYT--IVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFT 238
Cdd:PRK13645 178 TGGLDPKGEEDFINLFERLNKEYKkrIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
22-236 |
4.63e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 122.43 E-value: 4.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 22 QALKKINMDIKENKVTALIGPSGCGKSTFIRTLN---RMNDliedvtikGNISVDGEDIYTSDDVINLRTKVGMVFQKPN 98
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILSgvyQPDS--------GEILLDGEPVRFRSPRDAQAAGIAIIHQELN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 99 PFP-MSIYDNVAYG--PRTHGLRDKKQLDKIVEESLK--GAAI--WDEVKDrlkssalgLSGGQQQRICIARAIAMRPEV 171
Cdd:COG1129 90 LVPnLSVAENIFLGrePRRGGLIDWRAMRRRARELLArlGLDIdpDTPVGD--------LSVAQQQLVEIARALSRDARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489527602 172 ILMDEPTSALDPISTLKVEELIEDLKKD-YTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTM 236
Cdd:COG1129 162 LILDEPTASLTEREVERLFRIIRRLKAQgVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
9-241 |
8.29e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 117.98 E-value: 8.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGD--KQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndLIEDVTIKGNISVDGEDIyTSDDVINL 86
Cdd:PRK13640 6 VEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGL--LLPDDNPNSKITVDGITL-TAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 87 RTKVGMVFQKP-NPF-PMSIYDNVAYGPRTHGLrDKKQLDKIVEESLKGAAIWDEVKdrlkSSALGLSGGQQQRICIARA 164
Cdd:PRK13640 83 REKVGIVFQNPdNQFvGATVGDDVAFGLENRAV-PRPEMIKIVRDVLADVGMLDYID----SEPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489527602 165 IAMRPEVILMDEPTSALDPISTLKVEELIEDLKKD--YTIVIVTHNMQQAArISDETAFFLNGEVIEFSDTKTMFTTPV 241
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnnLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
22-237 |
9.03e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 118.30 E-value: 9.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 22 QALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEDVTIKGNISVDGEDiyTSDDVINLRTKVGMVFQKPNP-- 99
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTS--KQKEIKPVRKKVGVVFQFPESql 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 100 FPMSIYDNVAYGPRTHGLrDKKQLDKIVEESLKGAAIWDEVKDRlksSALGLSGGQQQRICIARAIAMRPEVILMDEPTS 179
Cdd:PRK13643 98 FEETVLKDVAFGPQNFGI-PKEKAEKIAAEKLEMVGLADEFWEK---SPFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489527602 180 ALDPISTLKVEELIEDLKKD-YTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMF 237
Cdd:PRK13643 174 GLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
9-240 |
1.53e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 117.62 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVK--DLDLFYG-----DKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndLIEDvtiKGNISVDGEDI---Y 78
Cdd:PRK13641 1 MSIKfeNVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNAL--LKPS---SGTITIAGYHItpeT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 79 TSDDVINLRTKVGMVFQKPNP--FPMSIYDNVAYGPRTHGLRDKKQLDKIVEeSLKGAAIWDEVKDRlksSALGLSGGQQ 156
Cdd:PRK13641 76 GNKNLKKLRKKVSLVFQFPEAqlFENTVLKDVEFGPKNFGFSEDEAKEKALK-WLKKVGLSEDLISK---SPFELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 157 QRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKD-YTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKT 235
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAgHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKE 231
|
....*
gi 489527602 236 MFTTP 240
Cdd:PRK13641 232 IFSDK 236
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
20-229 |
1.81e-31 |
|
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: 121.73 E-value: 1.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 20 DKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDliedvTIKGNISVDGEDIYTSDDViNLRTKVGMVFQKPNP 99
Cdd:TIGR02204 352 DQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYD-----PQSGRILLDGVDLRQLDPA-ELRARMALVPQDPVL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 100 FPMSIYDNVAYGpRTHGLRDKkqldkiVEESLKgAAIWDEVKDRLKSS--------ALGLSGGQQQRICIARAIAMRPEV 171
Cdd:TIGR02204 426 FAASVMENIRYG-RPDATDEE------VEAAAR-AAHAHEFISALPEGydtylgerGVTLSGGQRQRIAIARAILKDAPI 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527602 172 ILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHNM---QQAARIsdetAFFLNGEVIE 229
Cdd:TIGR02204 498 LLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLatvLKADRI----VVMDQGRIVA 554
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-240 |
2.08e-31 |
|
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: 120.94 E-value: 2.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGD----KQALKKINMDIKENKVTALIGPSGCGKS-TFIRTLNrmndLIED--VTIKGNISVDGEDIYT-S 80
Cdd:COG4172 7 LSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILR----LLPDpaAHPSGSILFDGQDLLGlS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 81 DDVIN-LR-TKVGMVFQKP----NPFpMSIYDNVAYGPRTH-GLRDKKQLDKIVEeSLKGAAIwDEVKDRLKSSALGLSG 153
Cdd:COG4172 83 ERELRrIRgNRIAMIFQEPmtslNPL-HTIGKQIAEVLRLHrGLSGAAARARALE-LLERVGI-PDPERRLDAYPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 154 GQQQRICIARAIAMRPEVILMDEPTSALDPisTLKVE--ELIEDLKKDY--TIVIVTHNMQQAARISDETAFFLNGEVIE 229
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALDV--TVQAQilDLLKDLQRELgmALLLITHDLGVVRRFADRVAVMRQGEIVE 237
|
250
....*....|.
gi 489527602 230 FSDTKTMFTTP 240
Cdd:COG4172 238 QGPTAELFAAP 248
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
20-215 |
2.11e-31 |
|
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: 115.65 E-value: 2.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 20 DKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIedvtiKGNISVDGEDIYTSDDVInLRTKVGMVFQKPNP 99
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQ-----GGQVLLDGKPISQYEHKY-LHSKVSLVGQEPVL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 100 FPMSIYDNVAYGPRThglrdkKQLDKIVEESLKGAA----------IWDEVKDRlksSALgLSGGQQQRICIARAIAMRP 169
Cdd:cd03248 100 FARSLQDNIAYGLQS------CSFECVKEAAQKAHAhsfiselasgYDTEVGEK---GSQ-LSGGQKQRVAIARALIRNP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489527602 170 EVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHNM---QQAARI 215
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLstvERADQI 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
19-227 |
2.18e-31 |
|
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: 115.20 E-value: 2.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 19 GDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndliEDVTiKGNISVDGEDI--YTSDDVINLRTKVGMVFQK 96
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKE----ELPT-SGTIRVNGQDVsdLRGRAIPYLRRKIGVVFQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 97 PNPFP-MSIYDNVAYGPRTHGlRDKKQLDKIVEESLKGAAIwdevKDRLKSSALGLSGGQQQRICIARAIAMRPEVILMD 175
Cdd:cd03292 87 FRLLPdRNVYENVAFALEVTG-VPPREIRKRVPAALELVGL----SHKHRALPAELSGGEQQRVAIARAIVNSPTILIAD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489527602 176 EPTSALDPISTLKVEELIEDL-KKDYTIVIVTHNMQQAARISDETAFFLNGEV 227
Cdd:cd03292 162 EPTGNLDPDTTWEIMNLLKKInKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
22-228 |
2.22e-31 |
|
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: 115.16 E-value: 2.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 22 QALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndLIEDvtiKGNISVDGEDiyTSDDVINLRTKVGMVFQKPNPFP 101
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGL--LEPD---AGFATVDGFD--VVKEPAEARRRLGFVSDSTGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 102 -MSIYDNVAYGPRTHGLRDKKQLDKIveeslkgaaiwDEVKDRLKSSAL------GLSGGQQQRICIARAIAMRPEVILM 174
Cdd:cd03266 92 rLTARENLEYFAGLYGLKGDELTARL-----------EELADRLGMEELldrrvgGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489527602 175 DEPTSALDPISTLKVEELIEDLKKD-YTIVIVTHNMQQAARISDETAFFLNGEVI 228
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-240 |
8.11e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 115.29 E-value: 8.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 1 MELIDkikmsVKDLDLFY-GDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDliedvTIKGNISVDGEDIyT 79
Cdd:PRK13652 1 MHLIE-----TRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILK-----PTSGSVLIRGEPI-T 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 80 SDDVINLRTKVGMVFQKPNP--FPMSIYDNVAYGPRTHGLrDKKQLDKIVEESLKGAAIwDEVKDRLKSSalgLSGGQQQ 157
Cdd:PRK13652 70 KENIREVRKFVGLVFQNPDDqiFSPTVEQDIAFGPINLGL-DEETVAHRVSSALHMLGL-EELRDRVPHH---LSGGEKK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 158 RICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKT 235
Cdd:PRK13652 145 RVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYgmTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEE 224
|
....*
gi 489527602 236 MFTTP 240
Cdd:PRK13652 225 IFLQP 229
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
10-207 |
1.14e-30 |
|
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: 118.93 E-value: 1.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDK-QALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEdvtikGNISVDGEDIyTSDDVINLRT 88
Cdd:TIGR02857 323 EFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTE-----GSIAVNGVPL-ADADADSWRD 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 89 KVGMVFQKPNPFPMSIYDNVAygprthgLRDKKQLDKIVEESLKGAAIWDEVKDR-------LKSSALGLSGGQQQRICI 161
Cdd:TIGR02857 397 QIAWVPQHPFLFAGTIAENIR-------LARPDASDAEIREALERAGLDEFVAALpqgldtpIGEGGAGLSGGQAQRLAL 469
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489527602 162 ARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTH 207
Cdd:TIGR02857 470 ARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTH 515
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
9-213 |
1.29e-30 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 112.96 E-value: 1.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFirtLNRMN-DLIEDVTIKGNISVDGEDIytsDDVINLR 87
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTL---LAAIAgTLSPAFSASGEVLLNGRRL---TALPAEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 88 TKVGMVFQKPNPFP-MSIYDNVAYG-PRTHGLRDKKQLdkiVEESLKGAAIwDEVKDRLKSSalgLSGGQQQRICIARAI 165
Cdd:COG4136 76 RRIGILFQDDLLFPhLSVGENLAFAlPPTIGRAQRRAR---VEQALEEAGL-AGFADRDPAT---LSGGQRARVALLRAL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489527602 166 AMRPEVILMDEPTSALDPISTLKVEELIEDLKKDYTI--VIVTHNMQQAA 213
Cdd:COG4136 149 LAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIpaLLVTHDEEDAP 198
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-240 |
1.47e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 115.72 E-value: 1.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 3 LIDKIKMSVKDLDLFYGDKQ-----ALKKINMDIKENKVTALIGPSGCGKSTFIRTLN-----RMNDL-IEDVTIKGNIS 71
Cdd:PRK13631 16 LSDDIILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNgliksKYGTIqVGDIYIGDKKN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 72 VDGEDIYTSDDVIN----LRTKVGMVFQKP--NPFPMSIYDNVAYGPRTHGLRdKKQLDKIVEESLKGAAIWDEVKDRlk 145
Cdd:PRK13631 96 NHELITNPYSKKIKnfkeLRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVK-KSEAKKLAKFYLNKMGLDDSYLER-- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 146 sSALGLSGGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKD-YTIVIVTHNMQQAARISDETAFFLN 224
Cdd:PRK13631 173 -SPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANnKTVFVITHTMEHVLEVADEVIVMDK 251
|
250
....*....|....*.
gi 489527602 225 GEVIEFSDTKTMFTTP 240
Cdd:PRK13631 252 GKILKTGTPYEIFTDQ 267
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
10-228 |
1.65e-30 |
|
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: 111.37 E-value: 1.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLnrMNDLIEDvtiKGNISVDGEDIYTSDDVINLRTK 89
Cdd:cd03216 2 ELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKIL--SGLYKPD---SGEILVDGKEVSFASPRDARRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 90 VGMVFQkpnpfpmsiydnvaygprthglrdkkqldkiveeslkgaaiwdevkdrlkssalgLSGGQQQRICIARAIAMRP 169
Cdd:cd03216 77 IAMVYQ-------------------------------------------------------LSVGERQMVEIARALARNA 101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 170 EVILMDEPTSALDPISTLKVEELIEDLKKD-YTIVIVTHNMQQAARISDETAFFLNGEVI 228
Cdd:cd03216 102 RLLILDEPTAALTPAEVERLFKVIRRLRAQgVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
10-228 |
1.72e-30 |
|
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: 112.35 E-value: 1.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQ-ALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDliedvTIKGNISVDGEDIYTSDdvinLRT 88
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIK-----ESSGSILLNGKPIKAKE----RRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 89 KVGMVFQKPNP--FPMSIYDNVAYGprthgLRDKKQLDKIVEESLKGAAIWDEvKDRLKSSalgLSGGQQQRICIARAIA 166
Cdd:cd03226 72 SIGYVMQDVDYqlFTDSVREELLLG-----LKELDAGNEQAETVLKDLDLYAL-KERHPLS---LSGGQKQRLAIAAALL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489527602 167 MRPEVILMDEPTSALDPISTLKVEELIEDLKK-DYTIVIVTHNMQQAARISDETAFFLNGEVI 228
Cdd:cd03226 143 SGKDLLIFDEPTSGLDYKNMERVGELIRELAAqGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
11-228 |
2.06e-30 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 113.57 E-value: 2.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 11 VKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNdliedVTIKGNISVDGEDIYTSDDVINLRTKV 90
Cdd:PRK11231 5 TENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLL-----TPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 91 GMVFQKPNPFPMSIYDNVAYGPRTH-----GLRDKKQldKIVEESLKGAAIwDEVKDRLKSSalgLSGGQQQRICIARAI 165
Cdd:PRK11231 80 LLPQHHLTPEGITVRELVAYGRSPWlslwgRLSAEDN--ARVNQAMEQTRI-NHLADRRLTD---LSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489527602 166 AMRPEVILMDEPTSALDPISTLKVEELIEDLK-KDYTIVIVTHNMQQAARISDETAFFLNGEVI 228
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDINHQVELMRLMRELNtQGKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
10-243 |
2.57e-30 |
|
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: 112.62 E-value: 2.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLnrmndlIEDVTIK-GNISVDGEDIYTSDDVINLRT 88
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTL------MGLLPVKsGSIRLDGEDITKLPPHERARA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 89 KVGMVFQKPNPFP-MSIYDNVAYGPRTHGLRDKKqldkIVEESLKGAAIWDEVKDRLkssALGLSGGQQQRICIARAIAM 167
Cdd:TIGR03410 76 GIAYVPQGREIFPrLTVEENLLTGLAALPRRSRK----IPDEIYELFPVLKEMLGRR---GGDLSGGQQQQLAIARALVT 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489527602 168 RPEVILMDEPTSALDPISTLKVEELIEDLKK--DYTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTPVDK 243
Cdd:TIGR03410 149 RPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAegGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKVRR 226
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
20-242 |
4.45e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 113.26 E-value: 4.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 20 DKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEdvtikGNISVDGEDIyTSDDVINLRTKVGMVFQKP-N 98
Cdd:PRK13642 19 DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFE-----GKVKIDGELL-TAENVWNLRRKIGMVFQNPdN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 99 PF-PMSIYDNVAYGPRTHGLrDKKQLDKIVEESLKGAAIWDeVKDRLKSSalgLSGGQQQRICIARAIAMRPEVILMDEP 177
Cdd:PRK13642 93 QFvGATVEDDVAFGMENQGI-PREEMIKRVDEALLAVNMLD-FKTREPAR---LSGGQKQRVAVAGIIALRPEIIILDES 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489527602 178 TSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARiSDETAFFLNGEVIEFSDTKTMFTTPVD 242
Cdd:PRK13642 168 TSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSED 233
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
10-229 |
5.01e-30 |
|
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: 111.54 E-value: 5.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTlnrMNDLIEDVTikGNISVDGEDIytsDDVINLRTK 89
Cdd:cd03268 2 KTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKI---ILGLIKPDS--GEITFDGKSY---QKNIEALRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 90 VGMVFQKPNPFP-MSIYDNVAYGPRTHGLRdkkqlDKIVEESLKGAAIWDEVKDRLKSSALGLsggqQQRICIARAIAMR 168
Cdd:cd03268 74 IGALIEAPGFYPnLTARENLRLLARLLGIR-----KKRIDEVLDVVGLKDSAKKKVKGFSLGM----KQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489527602 169 PEVILMDEPTSALDPISTLKVEELIEDLKKD-YTIVIVTHNMQQAARISDETAFFLNGEVIE 229
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
9-229 |
5.98e-30 |
|
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: 110.48 E-value: 5.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYG--DKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRmnDLIEDvtiKGNISVDGEDIYTSDDviNL 86
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG--DLKPQ---QGEITLDGVPVSDLEK--AL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 87 RTKVGMVFQKPNPFPMSIYDNVaygprthGLRdkkqldkiveeslkgaaiwdevkdrlkssalgLSGGQQQRICIARAIA 166
Cdd:cd03247 74 SSLISVLNQRPYLFDTTLRNNL-------GRR--------------------------------FSGGERQRLALARILL 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489527602 167 MRPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHNMQQAARIsDETAFFLNGEVIE 229
Cdd:cd03247 115 QDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHM-DKILFLENGKIIM 176
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
18-217 |
1.62e-29 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 113.59 E-value: 1.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 18 YGDKQALKKINMDIKENKVTALIGPSGCGKSTfirtLNRMNDLIEDVTiKGNISVDGEDIytsDDVINLRTKVGMVFQKP 97
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKST----LLRMIAGLEDIT-SGDLFIGEKRM---NDVPPAERGVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 98 NPFP-MSIYDNVAYGPRTHGLrDKKQLDKIVE---ESLKGAAIWDEvkdRLKSsalgLSGGQQQRICIARAIAMRPEVIL 173
Cdd:PRK11000 85 ALYPhLSVAENMSFGLKLAGA-KKEEINQRVNqvaEVLQLAHLLDR---KPKA----LSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489527602 174 MDEPTSALDpiSTLKVEELIE--DLKKDY--TIVIVTHNMQQAARISD 217
Cdd:PRK11000 157 LDEPLSNLD--AALRVQMRIEisRLHKRLgrTMIYVTHDQVEAMTLAD 202
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
19-238 |
2.70e-29 |
|
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: 111.05 E-value: 2.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 19 GDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLnrmndLIEDVTIKGNISVDGEDIYTSD--DVINLRTKVGMVFQK 96
Cdd:TIGR02769 22 QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLL-----LGLEKPAQGTVSFRGQDLYQLDrkQRRAFRRDVQLVFQD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 97 P----NPfPMSIYDNVAYgPRTHGLRDKK--QLDKIvEESLKGAAIWDEVKDRLKSSalgLSGGQQQRICIARAIAMRPE 170
Cdd:TIGR02769 97 SpsavNP-RMTVRQIIGE-PLRHLTSLDEseQKARI-AELLDMVGLRSEDADKLPRQ---LSGGQLQRINIARALAVKPK 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 171 VILMDEPTSALDPISTLKVEELIEDLKKDYTI--VIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFT 238
Cdd:TIGR02769 171 LIVLDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLS 240
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
16-240 |
4.92e-29 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 111.59 E-value: 4.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 16 LFYGDK--QALKKINMDIKENKVTALIGPSGCGKSTfirtLNRMNDLIEDVTiKGNISVDGEDIYTSD--DVINLRTKVG 91
Cdd:PRK11308 21 LFKPERlvKALDGVSFTLERGKTLAVVGESGCGKST----LARLLTMIETPT-GGELYYQGQDLLKADpeAQKLLRQKIQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 92 MVFQKPnpfpmsiydnvaYG---PRthglrdkKQLDKIVEESLK-----GAAiwdEVKDRLKS--SALGL---------- 151
Cdd:PRK11308 96 IVFQNP------------YGslnPR-------KKVGQILEEPLLintslSAA---ERREKALAmmAKVGLrpehydryph 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 152 --SGGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDYTI--VIVTHNMQQAARISDETAFFLNGEV 227
Cdd:PRK11308 154 mfSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLsyVFISHDLSVVEHIADEVMVMYLGRC 233
|
250
....*....|...
gi 489527602 228 IEFSDTKTMFTTP 240
Cdd:PRK11308 234 VEKGTKEQIFNNP 246
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
14-244 |
5.03e-29 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 110.46 E-value: 5.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 14 LDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNdliedVTIKGNISVDGEDI--YTSDDVINlrtKVG 91
Cdd:PRK10253 13 LTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLM-----TPAHGHVWLDGEHIqhYASKEVAR---RIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 92 MVFQKP-NPFPMSIYDNVAYGPRTHG---LRDKKQLDKIVEESLKGAAIWDEVKDRLKSsalgLSGGQQQRICIARAIAM 167
Cdd:PRK10253 85 LLAQNAtTPGDITVQELVARGRYPHQplfTRWRKEDEEAVTKAMQATGITHLADQSVDT----LSGGQRQRAWIAMVLAQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489527602 168 RPEVILMDEPTSALDPISTLKVEELIEDL--KKDYTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTPVDKR 244
Cdd:PRK10253 161 ETAIMLLDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIER 239
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-229 |
5.08e-29 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 114.73 E-value: 5.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 4 IDKIK--MSVKDLDLFY--GDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEdvtikGNISVDGEDI-- 77
Cdd:PRK11176 335 IERAKgdIEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDE-----GEILLDGHDLrd 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 78 YTsddVINLRTKVGMVFQKPNPFPMSIYDNVAYGprthglRDKKQLDKIVEESLKGAAIWDEVK--DRLKSSALG----- 150
Cdd:PRK11176 410 YT---LASLRNQVALVSQNVHLFNDTIANNIAYA------RTEQYSREQIEEAARMAYAMDFINkmDNGLDTVIGengvl 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 151 LSGGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHnmqqaaRIS-----DETAFFLNG 225
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAH------RLStiekaDEILVVEDG 554
|
....
gi 489527602 226 EVIE 229
Cdd:PRK11176 555 EIVE 558
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
9-228 |
5.38e-29 |
|
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: 108.91 E-value: 5.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndLIEDvtiKGNISVDGEDIYTSDdvinlRT 88
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGI--ILPD---SGEVLFDGKPLDIAA-----RN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 89 KVGMVFQKPNPFP-MSIYDNVAYGPRTHGLRdKKQLDKIVEESLKGAAIWDEVKDRLKSsalgLSGGQQQRICIARAIAM 167
Cdd:cd03269 71 RIGYLPEERGLYPkMKVIDQLVYLAQLKGLK-KEEARRRIDEWLERLELSEYANKRVEE----LSKGNQQKVQFIAAVIH 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489527602 168 RPEVILMDEPTSALDPISTLKVEELIEDLK-KDYTIVIVTHNMQQAARISDETAFFLNGEVI 228
Cdd:cd03269 146 DPELLILDEPFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
10-228 |
6.25e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 110.58 E-value: 6.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTlnrMNDLIE-DvtiKGNISVDGEDIyTSDDvinlRT 88
Cdd:COG4152 3 ELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRI---ILGILApD---SGEVLWDGEPL-DPED----RR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 89 KVG-M-----VFQKpnpfpMSIYDNVAYGPRTHGLrDKKQLDKIVEESLKGAAIWDEVKDRLKSsalgLSGGQQQRICIA 162
Cdd:COG4152 72 RIGyLpeergLYPK-----MKVGEQLVYLARLKGL-SKAEAKRRADEWLERLGLGDRANKKVEE----LSKGNQQKVQLI 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489527602 163 RAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIV-THNMQQAARISDETAFFLNGEVI 228
Cdd:COG4152 142 AALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFsSHQMELVEELCDRIVIINKGRKV 208
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
23-251 |
1.06e-28 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 112.05 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 23 ALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRmndLIEDVtiKGNISVDGEDIYTSDDVI---NLRTKVGMVFQKPNP 99
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNR---LIEPT--RGQVLIDGVDIAKISDAElreVRRKKIAMVFQSFAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 100 FP-MSIYDNVAYGPRTHGL----RDKKQLDKIVEESLKGAA--IWDEvkdrlkssalgLSGGQQQRICIARAIAMRPEVI 172
Cdd:PRK10070 118 MPhMTVLDNTAFGMELAGInaeeRREKALDALRQVGLENYAhsYPDE-----------LSGGMRQRVGLARALAINPDIL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 173 LMDEPTSALDP-ISTLKVEELIE-DLKKDYTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTPVDKRTEDYIT 250
Cdd:PRK10070 187 LMDEAFSALDPlIRTEMQDELVKlQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFR 266
|
.
gi 489527602 251 G 251
Cdd:PRK10070 267 G 267
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
35-228 |
1.51e-28 |
|
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: 107.58 E-value: 1.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 35 KVTALIGPSGCGKSTFirtLNrmndLIE--DVTIKGNISVDGEDIYTSDDVinlRTKVGMVFQKPNPFP-MSIYDNVAYG 111
Cdd:cd03298 25 EITAIVGPSGSGKSTL---LN----LIAgfETPQSGRVLINGVDVTAAPPA---DRPVSMLFQENNLFAhLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 112 pRTHGLRdkkqLDKIVEESLKGAAIWDEVKDRLKSSALGLSGGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEE 191
Cdd:cd03298 95 -LSPGLK----LTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 489527602 192 LIEDLKKD--YTIVIVTHNMQQAARISDETAFFLNGEVI 228
Cdd:cd03298 170 LVLDLHAEtkMTVLMVTHQPEDAKRLAQRVVFLDNGRIA 208
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
11-214 |
1.98e-28 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 107.32 E-value: 1.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 11 VKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFirtLNRMNdLIEDVTiKGNISVDGED---IYTSDDVINLR 87
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTL---LNIIG-LLEKFD-SGQVYLNGQEtppLNSKKASKFRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 88 TKVGMVFQKpnpFPM----SIYDNVAYGPRTHGLRDKKQLDKIVEeSLKGAAIWDEVKDRLKSsalgLSGGQQQRICIAR 163
Cdd:TIGR03608 76 EKLGYLFQN---FALieneTVEENLDLGLKYKKLSKKEKREKKKE-ALEKVGLNLKLKQKIYE----LSGGEQQRVALAR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489527602 164 AIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKD-YTIVIVTHNMQQAAR 214
Cdd:TIGR03608 148 AILKPPPLILADEPTGSLDPKNRDEVLDLLLELNDEgKTIIIVTHDPEVAKQ 199
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
17-229 |
2.97e-28 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 112.36 E-value: 2.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 17 FYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDliedvTIKGNISVDGEDIyTSDDVINLRTKVGMVFQK 96
Cdd:PRK13657 344 YDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFD-----PQSGRILIDGTDI-RTVTRASLRRNIAVVFQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 97 PNPFPMSIYDNVAYGPRThglrdkkQLDKIVEESLKGAAIWDEVKDRLK--SSALG-----LSGGQQQRICIARAIAMRP 169
Cdd:PRK13657 418 AGLFNRSIEDNIRVGRPD-------ATDEEMRAAAERAQAHDFIERKPDgyDTVVGergrqLSGGERQRLAIARALLKDP 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 170 EVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHNMqQAARISDETAFFLNGEVIE 229
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRL-STVRNADRILVFDNGRVVE 549
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
11-251 |
5.36e-28 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 107.54 E-value: 5.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 11 VKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNrmNDLIEDvtiKGNISVDGEDI--YTSDDVINLRT 88
Cdd:PRK11831 10 MRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIG--GQIAPD---HGEILFDGENIpaMSRSRLYTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 89 KVGMVFQKPNPFP-MSIYDNVAYGPRTHG-----LRDKKQLDKIVEESLKGAAiwdevkdRLKSSALglSGGQQQRICIA 162
Cdd:PRK11831 85 RMSMLFQSGALFTdMNVFDNVAYPLREHTqlpapLLHSTVMMKLEAVGLRGAA-------KLMPSEL--SGGMARRAALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 163 RAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKK--DYTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTP 240
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
250
....*....|.
gi 489527602 241 vDKRTEDYITG 251
Cdd:PRK11831 236 -DPRVRQFLDG 245
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
10-215 |
5.39e-28 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 104.99 E-value: 5.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQA--LKKINMDIKENKVTALIGPSGCGKSTFIRTlnrMNDLIEDVtiKGNISVDGEDIyTSDDVINLR 87
Cdd:cd03246 2 EVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARL---ILGLLRPT--SGRVRLDGADI-SQWDPNELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 88 TKVGMVFQKPNPFPMSIYDNVaygprthglrdkkqldkiveeslkgaaiwdevkdrlkssalgLSGGQQQRICIARAIAM 167
Cdd:cd03246 76 DHVGYLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYG 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489527602 168 RPEVILMDEPTSALDPISTLKVEELIEDLKK-DYTIVIVTHNM---QQAARI 215
Cdd:cd03246 114 NPRILVLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPetlASADRI 165
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-233 |
1.00e-27 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 108.63 E-value: 1.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 4 IDKIKMsvkdldlFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRT---LNRMNdliedvtiKGNISVDGEDI--- 77
Cdd:PRK10851 5 IANIKK-------SFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIiagLEHQT--------SGHIRFHGTDVsrl 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 78 YTSDdvinlrTKVGMVFQKPNPFP-MSIYDNVAYG----PRtHGLRDKKQLDKIVEESLKGAAIwDEVKDRLKSSalgLS 152
Cdd:PRK10851 70 HARD------RKVGFVFQHYALFRhMTVFDNIAFGltvlPR-RERPNAAAIKAKVTQLLEMVQL-AHLADRYPAQ---LS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 153 GGQQQRICIARAIAMRPEVILMDEPTSALDpiSTLKVE------ELIEDLKkdYTIVIVTHNMQQAARISDETAFFLNGe 226
Cdd:PRK10851 139 GGQKQRVALARALAVEPQILLLDEPFGALD--AQVRKElrrwlrQLHEELK--FTSVFVTHDQEEAMEVADRVVVMSQG- 213
|
....*..
gi 489527602 227 VIEFSDT 233
Cdd:PRK10851 214 NIEQAGT 220
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
26-241 |
1.17e-27 |
|
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: 108.66 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 26 KINMDIKENKVTALIGPSGCGKSTFIRtlnrmndLIEDVT--IKGNISVDGEDIYTSDDVINL---RTKVGMVFQKPNPF 100
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIR-------LIAGLTrpDEGEIVLNGRTLFDSRKGIFLppeKRRIGYVFQEARLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 101 P-MSIYDNVAYG-PRTHGLRDKKQLDKIVEesLKGAaiwDEVKDRLKSSalgLSGGQQQRICIARAIAMRPEVILMDEPT 178
Cdd:TIGR02142 88 PhLSVRGNLRYGmKRARPSERRISFERVIE--LLGI---GHLLGRLPGR---LSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489527602 179 SALDPISTLKVEELIEDLKKDYTI--VIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTPV 241
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLHAEFGIpiLYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
23-229 |
1.34e-27 |
|
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: 106.03 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 23 ALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNdliedVTIKGNISVDGEDIYTSDDViNLRTKVGMVFQKPNPFPM 102
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFY-----VPENGRVLVDGHDLALADPA-WLRRQVGVVLQENVLFNR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 103 SIYDNVAYGprthglRDKKQLDKIVE-ESLKGAAI--------WDEVkdrLKSSALGLSGGQQQRICIARAIAMRPEVIL 173
Cdd:cd03252 91 SIRDNIALA------DPGMSMERVIEaAKLAGAHDfiselpegYDTI---VGEQGAGLSGGQRQRIAIARALIHNPRILI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489527602 174 MDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHNMqQAARISDETAFFLNGEVIE 229
Cdd:cd03252 162 FDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVE 216
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
15-233 |
2.58e-27 |
|
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: 104.56 E-value: 2.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 15 DLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFirtLNRMNDLIEDVTikGNISVDGEDIYTSDDVinlRTKVGMVF 94
Cdd:TIGR01277 5 KVRYEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTL---LNLIAGFIEPAS--GSIKVNDQSHTGLAPY---QRPVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 95 QKPNPFP-MSIYDNVAYGprthgLRDKKQLDKIVEESLKGAAIW---DEVKDRLKSSalgLSGGQQQRICIARAIAMRPE 170
Cdd:TIGR01277 77 QENNLFAhLTVRQNIGLG-----LHPGLKLNAEQQEKVVDAAQQvgiADYLDRLPEQ---LSGGQRQRVALARCLVRPNP 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489527602 171 VILMDEPTSALDPISTLKVEELIEDL--KKDYTIVIVTHNMQQAARISDETAFFLNGEVIEFSDT 233
Cdd:TIGR01277 149 ILLLDEPFSALDPLLREEMLALVKQLcsERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
8-230 |
2.87e-27 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 104.50 E-value: 2.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 8 KMSVKDLDLFYGD--KQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEdvtikGNISVDGEDIyTSDDVIN 85
Cdd:cd03244 2 DIEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSS-----GSILIDGVDI-SKIGLHD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 86 LRTKVGMVFQKPNPFPMSIYDNVAygPrtHGLRDkkqlDKIVEESLKGAAIWDEVK-------DRLKSSALGLSGGQQQR 158
Cdd:cd03244 76 LRSRISIIPQDPVLFSGTIRSNLD--P--FGEYS----DEELWQALERVGLKEFVEslpggldTVVEEGGENLSVGQRQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489527602 159 ICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHnmqqaaRI-----SDETAFFLNGEVIEF 230
Cdd:cd03244 148 LCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAH------RLdtiidSDRILVLDKGRVVEF 218
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
8-215 |
5.50e-27 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 109.04 E-value: 5.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 8 KMSVKDLDLFYG--DKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDliedvTIKGNISVDGEDI--YTSDDv 83
Cdd:TIGR02203 330 DVEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYE-----PDSGQILLDGHDLadYTLAS- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 84 inLRTKVGMVFQKPNPFPMSIYDNVAYGPRTHGLRDKkqldkiVEESLKGAAIWDEVkDRLK--------SSALGLSGGQ 155
Cdd:TIGR02203 404 --LRRQVALVSQDVVLFNDTIANNIAYGRTEQADRAE------IERALAAAYAQDFV-DKLPlgldtpigENGVLLSGGQ 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489527602 156 QQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHNM---QQAARI 215
Cdd:TIGR02203 475 RQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLstiEKADRI 537
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
20-240 |
6.91e-27 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 109.04 E-value: 6.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 20 DKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRmndLIEDVTikGNISVDGEDIYTSDDVInLRTKVGMVFQKPNP 99
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQN---LYQPTG--GQVLLDGVPLVQYDHHY-LHRQVALVGQEPVL 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 100 FPMSIYDNVAYGprthglrdkkqLDKIVEESLKGAAIWDEVKDRLKSSALG-----------LSGGQQQRICIARAIAMR 168
Cdd:TIGR00958 567 FSGSVRENIAYG-----------LTDTPDEEIMAAAKAANAHDFIMEFPNGydtevgekgsqLSGGQKQRIAIARALVRK 635
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489527602 169 PEVILMDEPTSALDpistLKVEELIEDLK--KDYTIVIVTHNMQQAARiSDETAFFLNGEVIEFSDTKTMFTTP 240
Cdd:TIGR00958 636 PRVLILDEATSALD----AECEQLLQESRsrASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-240 |
1.58e-26 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 107.63 E-value: 1.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 23 ALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRmndLIEdvTIKGNISVDGEDIYTSDD--VINLRTKVGMVFQKP--- 97
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLR---LVE--SQGGEIIFNGQRIDTLSPgkLQALRRDIQFIFQDPyas 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 98 -NPfPMSIYDNVAYGPRTHGLRDKKQLDKIVEESLKGAAIWDEVKDRLKSSalgLSGGQQQRICIARAIAMRPEVILMDE 176
Cdd:PRK10261 414 lDP-RQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHE---FSGGQRQRICIARALALNPKVIIADE 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489527602 177 PTSALDPISTLKVEELIEDLKKDYTI--VIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTP 240
Cdd:PRK10261 490 AVSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
15-207 |
1.71e-26 |
|
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: 101.86 E-value: 1.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 15 DLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLN--RMNdliedVTIKGNISVDGEDIYTSddviNLRTKVGM 92
Cdd:cd03213 16 SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTG-----LGVSGEVLINGRPLDKR----SFRKIIGY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 93 VFQkpnpfpmsiyDNVAYGPRThglrdkkqldkiVEESLKGAAiwdevkdRLKssalGLSGGQQQRICIARAIAMRPEVI 172
Cdd:cd03213 87 VPQ----------DDILHPTLT------------VRETLMFAA-------KLR----GLSGGERKRVSIALELVSNPSLL 133
|
170 180 190
....*....|....*....|....*....|....*.
gi 489527602 173 LMDEPTSALDPISTLKVEELIEDLKKD-YTIVIVTH 207
Cdd:cd03213 134 FLDEPTSGLDSSSALQVMSLLRRLADTgRTIICSIH 169
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
23-209 |
4.07e-26 |
|
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: 101.51 E-value: 4.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 23 ALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEdvtikGNISVDGEDIyTSDDVINLRTKVGMVFQKPNPFPM 102
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTS-----GSVLLDGTDI-RQLDPADLRRNIGYVPQDVTLFYG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 103 SIYDNVAYGPRTHGlrdkkqlDKIVEESLKGAAIWDEVKDRLKSSAL-------GLSGGQQQRICIARAIAMRPEVILMD 175
Cdd:cd03245 93 TLRDNITLGAPLAD-------DERILRAAELAGVTDFVNKHPNGLDLqigergrGLSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190
....*....|....*....|....*....|....
gi 489527602 176 EPTSALDPISTLKVEELIEDLKKDYTIVIVTHNM 209
Cdd:cd03245 166 EPTSAMDMNSEERLKERLRQLLGDKTLIIITHRP 199
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
9-249 |
4.30e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 104.53 E-value: 4.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndlieDVTIKGNISVDGEDIytsDDVINLRT 88
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGF-----EQPTAGQIMLDGVDL---SHVPPYQR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 89 KVGMVFQKPNPFP-MSIYDNVAYGPRTHGLrDKKQLDKIVEESLKGAAIWDEVKDRLKSsalgLSGGQQQRICIARAIAM 167
Cdd:PRK11607 92 PINMMFQSYALFPhMTVEQNIAFGLKQDKL-PKAEIASRVNEMLGLVHMQEFAKRKPHQ----LSGGQRQRVALARSLAK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 168 RPEVILMDEPTSALDPI----STLKVEELIEdlKKDYTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTPVDK 243
Cdd:PRK11607 167 RPKLLLLDEPMGALDKKlrdrMQLEVVDILE--RVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTR 244
|
....*.
gi 489527602 244 RTEDYI 249
Cdd:PRK11607 245 YSAEFI 250
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
8-230 |
1.20e-25 |
|
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: 99.79 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 8 KMSVKDLDLFYGDK--QALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEdvtikGNISVDGEDIyTSDDVIN 85
Cdd:cd03369 6 EIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEE-----GKIEIDGIDI-STIPLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 86 LRTKVGMVFQKPNPFPMSIYDNVaygprthglrdkKQLDKIVEESLKGAAiwdevkdRLKSSALGLSGGQQQRICIARAI 165
Cdd:cd03369 80 LRSSLTIIPQDPTLFSGTIRSNL------------DPFDEYSDEEIYGAL-------RVSEGGLNLSQGQRQLLCLARAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489527602 166 AMRPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHNMQQAARIsDETAFFLNGEVIEF 230
Cdd:cd03369 141 LKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEY 204
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
22-234 |
1.47e-25 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 99.79 E-value: 1.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 22 QALKKINMDIKENKVTALIGPSGCGKSTFIRTLNrMNDLIEdvtiKGNISVDGEDIYT---SDDVINLRTKVGMVFQKPN 98
Cdd:NF038007 19 KVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIG-MFDSLD----SGSLTLAGKEVTNlsySQKIILRRELIGYIFQSFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 99 PFP-MSIYDNVAYGPRTHGLRDKKQLDKiVEESLKGAAIwdevKDRLKSSALGLSGGQQQRICIARAIAMRPEVILMDEP 177
Cdd:NF038007 94 LIPhLSIFDNVALPLKYRGVAKKERIER-VNQVLNLFGI----DNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489527602 178 TSALDPISTLKVEELIEDL-KKDYTIVIVTHnmqqaariSDETAFFLNgEVIEFSDTK 234
Cdd:NF038007 169 TGNLDSKNARAVLQQLKYInQKGTTIIMVTH--------SDEASTYGN-RIINMKDGK 217
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
19-254 |
1.77e-25 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 100.68 E-value: 1.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 19 GDKQALKKINMDIKENKVTALIGPSGCGKSTfirtLNRMNDLIEDVTiKGNISVDGEDIYTSDdvINLRTK-VGMVFQKP 97
Cdd:COG4167 24 QQFEAVKPVSFTLEAGQTLAIIGENGSGKST----LAKMLAGIIEPT-SGEILINGHKLEYGD--YKYRCKhIRMIFQDP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 98 NpfpmsiydnVAYGPRThglrdkkQLDKIVEESLKGAAIWDE------VKDRLKSSAL----------GLSGGQQQRICI 161
Cdd:COG4167 97 N---------TSLNPRL-------NIGQILEEPLRLNTDLTAeereerIFATLRLVGLlpehanfyphMLSSGQKQRVAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 162 ARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDYTI--VIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTT 239
Cdd:COG4167 161 ARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGIsyIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFAN 240
|
250
....*....|....*
gi 489527602 240 PVDKRTEDYITGRFG 254
Cdd:COG4167 241 PQHEVTKRLIESHFG 255
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
9-244 |
2.08e-25 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 100.04 E-value: 2.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTfirTLNRMNDLIE-DvtiKGNISVDGEDIytSDDVINLR 87
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTT---SFYMIVGLVRpD---AGKILIDGQDI--THLPMHER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 88 TKVGMVF--QKPNPF-PMSIYDNVAYGPRTHGLRDKKQLDKIVEESLKGAAIwdevKDRLKSSALGLSGGQQQRICIARA 164
Cdd:TIGR04406 74 ARLGIGYlpQEASIFrKLTVEENIMAVLEIRKDLDRAEREERLEALLEEFQI----SHLRDNKAMSLSGGERRRVEIARA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 165 IAMRPEVILMDEPTSALDPISTLKVEELIEDLK-KDYTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTPVDK 243
Cdd:TIGR04406 150 LATNPKFILLDEPFAGVDPIAVGDIKKIIKHLKeRGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVR 229
|
.
gi 489527602 244 R 244
Cdd:TIGR04406 230 R 230
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
12-210 |
2.22e-25 |
|
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: 104.56 E-value: 2.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 12 KDLDLFY-GDKQ-ALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEdvtikGNISVDGEDIyTSDDVINLRTK 89
Cdd:TIGR03375 467 RNVSFAYpGQETpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTE-----GSVLLDGVDI-RQIDPADLRRN 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 90 VGMVFQKPNPFPMSIYDNVAYGP------------RTHGL-----RDKKQLDKIVEEslKGAaiwdevkdrlkssalGLS 152
Cdd:TIGR03375 541 IGYVPQDPRLFYGTLRDNIALGApyaddeeilraaELAGVtefvrRHPDGLDMQIGE--RGR---------------SLS 603
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489527602 153 GGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHNMQ 210
Cdd:TIGR03375 604 GGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHRTS 661
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
5-208 |
2.36e-25 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 103.98 E-value: 2.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 5 DKIKMSVKDLDLFY-GDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDliedvTIKGNISVDGEDIyTSDDV 83
Cdd:TIGR02868 331 GKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD-----PLQGEVTLDGVPV-SSLDQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 84 INLRTKVGMVFQKPNPFPMSIYDNVAYGprthglrDKKQLDKIVEESLKGA--AIW-----DEVKDRLKSSALGLSGGQQ 156
Cdd:TIGR02868 405 DEVRRRVSVCAQDAHLFDTTVRENLRLA-------RPDATDEELWAALERVglADWlralpDGLDTVLGEGGARLSGGER 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489527602 157 QRICIARAIAMRPEVILMDEPTSALDPISTlkvEELIEDLKK---DYTIVIVTHN 208
Cdd:TIGR02868 478 QRLALARALLADAPILLLDEPTEHLDAETA---DELLEDLLAalsGRTVVLITHH 529
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
9-241 |
2.56e-25 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 100.16 E-value: 2.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFirtLNRMNDLIE-DvtiKGNISVDGEDI--YTSDDvin 85
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTL---LSMISRLLPpD---SGEVLVDGLDVatTPSRE--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 86 LRTKVGMVFQKpNPFPM--SIYDNVAYG--PRTHGlRDKKQLDKIVEESLKGAAIwDEVKDR-LKSsalgLSGGQQQRIC 160
Cdd:COG4604 73 LAKRLAILRQE-NHINSrlTVRELVAFGrfPYSKG-RLTAEDREIIDEAIAYLDL-EDLADRyLDE----LSGGQRQRAF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 161 IARAIAMRPEVILMDEPTSALDP------ISTLKveELIEDLKKdyTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTK 234
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPLNNLDMkhsvqmMKLLR--RLADELGK--TVVIVLHDINFASCYADHIVAMKDGRVVAQGTPE 221
|
....*..
gi 489527602 235 TMFTTPV 241
Cdd:COG4604 222 EIITPEV 228
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
18-227 |
2.94e-25 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 100.14 E-value: 2.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 18 YGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDliedvtikgniSVDGEDIYTSDDVINLRTKVGMVFQKP 97
Cdd:PRK11247 22 YGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLET-----------PSAGELLAGTAPLAEAREDTRLMFQDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 98 NPFP-MSIYDNVAYGPRTHgLRDKkqldkiVEESLKGAAIwdevKDRLKSSALGLSGGQQQRICIARAIAMRPEVILMDE 176
Cdd:PRK11247 91 RLLPwKKVIDNVGLGLKGQ-WRDA------ALQALAAVGL----ADRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489527602 177 PTSALDPISTLKVEELIEDL--KKDYTIVIVTHNMQQAARISDETAFFLNGEV 227
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLwqQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
10-239 |
4.31e-25 |
|
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: 99.39 E-value: 4.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEDVTIKgnisVDGEDiYTSDDVINLRTK 89
Cdd:COG1119 5 ELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVR----LFGER-RGGEDVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 90 VGMV---FQKPNPFPMSIYDNV---AYGprTHGLRDK---KQLDKiVEESLK--GAAiwdEVKDRLKSSalgLSGGQQQR 158
Cdd:COG1119 80 IGLVspaLQLRFPRDETVLDVVlsgFFD--SIGLYREptdEQRER-ARELLEllGLA---HLADRPFGT---LSQGEQRR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 159 ICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTM 236
Cdd:COG1119 151 VLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGapTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
...
gi 489527602 237 FTT 239
Cdd:COG1119 231 LTS 233
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
19-229 |
5.20e-25 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 101.46 E-value: 5.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 19 GDKQALKKINMDIKENKVTALIGPSGCGKSTfirtLNRMNDLIEDVTiKGNISVDGEDiytsddVINLRTK---VGMVFQ 95
Cdd:PRK11650 15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKST----LLRMVAGLERIT-SGEIWIGGRV------VNELEPAdrdIAMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 96 KPNPFP-MSIYDNVAYGPRTHGLrDKKQLDKIVEESLKGAAIwDEVKDRlKSSALglSGGQQQRICIARAIAMRPEVILM 174
Cdd:PRK11650 84 NYALYPhMSVRENMAYGLKIRGM-PKAEIEERVAEAARILEL-EPLLDR-KPREL--SGGQRQRVAMGRAIVREPAVFLF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489527602 175 DEPTSALDpiSTLKVEELIEdLKK-----DYTIVIVTHN----MQQAARIsdetaFFLNGEVIE 229
Cdd:PRK11650 159 DEPLSNLD--AKLRVQMRLE-IQRlhrrlKTTSLYVTHDqveaMTLADRV-----VVMNGGVAE 214
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
24-225 |
7.76e-25 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 98.31 E-value: 7.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 24 LKKINMDIKENKVTALIGPSGCGKSTFirtLNRMNDLieDVTIKGNISVDGEDIytsddvinlrTKVG----MVFQKPNP 99
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTL---LNLISGL--AQPTSGGVILEGKQI----------TEPGpdrmVVFQNYSL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 100 FP-MSIYDNVAYG-PRTHGLRDKKQLDKIVEESLKGAAIWDEVKDRLKSsalgLSGGQQQRICIARAIAMRPEVILMDEP 177
Cdd:TIGR01184 66 LPwLTVRENIALAvDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEP 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489527602 178 TSALDPISTlkvEELIEDLKK-----DYTIVIVTHNMQQAARISDETAFFLNG 225
Cdd:TIGR01184 142 FGALDALTR---GNLQEELMQiweehRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
4-228 |
8.73e-25 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 98.41 E-value: 8.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 4 IDKIKMSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRmndliEDVTIKGNISVDGEDIYTSDDV 83
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG-----DPRATSGRIVFDGKDITDWQTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 84 INLRTKVGMVFQKPNPFP-MSIYDNVAYGPRthgLRDKKQLDKIVEESLkgaAIWDEVKDRLKSSALGLSGGQQQRICIA 162
Cdd:PRK11614 76 KIMREAVAIVPEGRRVFSrMTVEENLAMGGF---FAERDQFQERIKWVY---ELFPRLHERRIQRAGTMSGGEQQMLAIG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489527602 163 RAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKD-YTIVIVTHNMQQAARISDETAFFLNGEVI 228
Cdd:PRK11614 150 RALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQgMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
9-251 |
9.54e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.46 E-value: 9.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTlnrMNDLIEDVTikGNISVDGEDIyTSDDVINLRT 88
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRA---INGTLTPTA--GTVLVAGDDV-EALSARAASR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 89 KVGMVFQKPN-PFPMSIYDNVAYGPRTHGLR---DKKQLDKIVEESLKGAAIwDEVKDRLKSSalgLSGGQQQRICIARA 164
Cdd:PRK09536 78 RVASVPQDTSlSFEFDVRQVVEMGRTPHRSRfdtWTETDRAAVERAMERTGV-AQFADRPVTS---LSGGERQRVLLARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 165 IAMRPEVILMDEPTSALD---PISTLK-VEELIEDLKkdyTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTP 240
Cdd:PRK09536 154 LAQATPVLLLDEPTASLDinhQVRTLElVRRLVDDGK---TAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
250
....*....|....*....
gi 489527602 241 V-----DKR---TEDYITG 251
Cdd:PRK09536 231 TlraafDARtavGTDPATG 249
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
10-214 |
9.96e-25 |
|
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: 97.89 E-value: 9.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQA----LKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndlieDVTIKGNISVDGEDIYT--SDDV 83
Cdd:COG4181 10 ELRGLTKTVGTGAGeltiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGL-----DRPTSGTVRLAGQDLFAldEDAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 84 INLR-TKVGMVFQK----PNpfpMSIYDNVAYGPRTHGLRDKKQldkiveeslKGAAIWDEV--KDRLKSSALGLSGGQQ 156
Cdd:COG4181 85 ARLRaRHVGFVFQSfqllPT---LTALENVMLPLELAGRRDARA---------RARALLERVglGHRLDHYPAQLSGGEQ 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 157 QRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAAR 214
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgtTLVLVTHDPALAAR 212
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
9-215 |
1.09e-24 |
|
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: 97.15 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGDKQ-----ALKKINMDIKENKVTALIGPSGCGKSTFIRTLnrmndLIEDVTIKGNISVDGEDIYTSddv 83
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL-----LGELEKLSGSVSVPGSIAYVS--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 84 inlrtkvgmvfQKPNPFPMSIYDNVAYGPRthglRDKKQLDKIVE--------ESLKGAaiwD--EVKDRlkssALGLSG 153
Cdd:cd03250 73 -----------QEPWIQNGTIRENILFGKP----FDEERYEKVIKacalepdlEILPDG---DltEIGEK----GINLSG 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489527602 154 GQQQRICIARAIAMRPEVILMDEPTSALDP-ISTLKVEELI-EDLKKDYTIVIVTHNMQ---QAARI 215
Cdd:cd03250 131 GQKQRISLARAVYSDADIYLLDDPLSAVDAhVGRHIFENCIlGLLLNNKTRILVTHQLQllpHADQI 197
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
10-217 |
1.86e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 97.92 E-value: 1.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNrmNDLIEDvtiKGNISVDGEDI--YTSDDVINLR 87
Cdd:PRK13548 4 EARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALS--GELSPD---SGEVRLNGRPLadWSPAELARRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 88 tkvGMVFQKPN-PFPMSIYDNVAYGpRTHGLRDKKQLDKIVEESLKGAAIWDeVKDRLKSSalgLSGGQQQRICIARAIA 166
Cdd:PRK13548 79 ---AVLPQHSSlSFPFTVEEVVAMG-RAPHGLSRAEDDALVAAALAQVDLAH-LAGRDYPQ---LSGGEQQRVQLARVLA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489527602 167 ------MRPEVILMDEPTSALDPISTLKVEELIEDLKKD--YTIVIVTHNMQQAARISD 217
Cdd:PRK13548 151 qlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErgLAVIVVLHDLNLAARYAD 209
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
19-229 |
2.29e-24 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 101.44 E-value: 2.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 19 GDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndliEDVTiKGNISVDGEDI--YTSDDvinLRTKVGMVFQK 96
Cdd:COG5265 369 PERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRF----YDVT-SGRILIDGQDIrdVTQAS---LRAAIGIVPQD 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 97 PNPFPMSIYDNVAYGpRTHGLRDKkqldkiVEESLKGAAIWD-----------EVKDR-LKssalgLSGGQQQRICIARA 164
Cdd:COG5265 441 TVLFNDTIAYNIAYG-RPDASEEE------VEAAARAAQIHDfieslpdgydtRVGERgLK-----LSGGEKQRVAIART 508
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 165 IAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHnmqqaaRIS-----DETAFFLNGEVIE 229
Cdd:COG5265 509 LLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAH------RLStivdaDEILVLEAGRIVE 572
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
23-237 |
3.43e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 97.51 E-value: 3.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 23 ALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRmndlIEDVTiKGNISVDGEDIyTSDDVINLRTKVGMVFQKP-NPFP 101
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIG----IEKVK-SGEIFYNNQAI-TDDNFEKLRKHIGIVFQNPdNQFV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 102 MSI--YDnVAYGPRTHGLRDKKqLDKIVEESLKGAAIWDEVKDRLKSsalgLSGGQQQRICIARAIAMRPEVILMDEPTS 179
Cdd:PRK13648 98 GSIvkYD-VAFGLENHAVPYDE-MHRRVSEALKQVDMLERADYEPNA----LSGGQKQRVAIAGVLALNPSVIILDEATS 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 180 ALDPISTLKVEELIEDLK--KDYTIVIVTHNMQQAARiSDETAFFLNGEVIEFSDTKTMF 237
Cdd:PRK13648 172 MLDPDARQNLLDLVRKVKseHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
6-240 |
6.56e-24 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 97.85 E-value: 6.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 6 KIKMSVKDL----------DLFYGDKQALKK---INMDIKENKVTALIGPSGCGKSTFIRTLNRmndLIEdvTIKGNISV 72
Cdd:PRK15079 6 KVLLEVADLkvhfdikdgkQWFWQPPKTLKAvdgVTLRLYEGETLGVVGESGCGKSTFARAIIG---LVK--ATDGEVAW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 73 DGEDIYTSDDV--INLRTKVGMVFQKP----NPfPMSIYDNVAYGPRTHglrdKKQLDKiveeslkgaaiwDEVKDRLKS 146
Cdd:PRK15079 81 LGKDLLGMKDDewRAVRSDIQMIFQDPlaslNP-RMTIGEIIAEPLRTY----HPKLSR------------QEVKDRVKA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 147 SAL--GL------------SGGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQ 210
Cdd:PRK15079 144 MMLkvGLlpnlinryphefSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLA 223
|
250 260 270
....*....|....*....|....*....|
gi 489527602 211 QAARISDETAFFLNGEVIEFSDTKTMFTTP 240
Cdd:PRK15079 224 VVKHISDRVLVMYLGHAVELGTYDEVYHNP 253
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
9-237 |
7.80e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 96.61 E-value: 7.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLnrmNDLIEDVtiKGNISVDGEDI-YTSDDVINLR 87
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNL---SGLLRPQ--KGAVLWQGKPLdYSKRGLLALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 88 TKVGMVFQKPNP--FPMSIYDNVAYGPRTHGLRDkKQLDKIVEESLkgaAIWDEVKDRlKSSALGLSGGQQQRICIARAI 165
Cdd:PRK13638 77 QQVATVFQDPEQqiFYTDIDSDIAFSLRNLGVPE-AEITRRVDEAL---TLVDAQHFR-HQPIQCLSHGQKKRVAIAGAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489527602 166 AMRPEVILMDEPTSALDPISTLKVEELIEDL-KKDYTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMF 237
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAGRTQMIAIIRRIvAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
24-215 |
2.61e-23 |
|
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: 98.28 E-value: 2.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 24 LKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNdliedVTIKGNISVDGEDIYTSDDViNLRTKVGMVFQKPNPFPMS 103
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLY-----TPQHGQVLVDGVDLAIADPA-WLRRQMGVVLQENVLFSRS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 104 IYDNVA------------YGPRTHGLRD-----KKQLDKIVEEslKGAaiwdevkdrlkssalGLSGGQQQRICIARAIA 166
Cdd:TIGR01846 547 IRDNIAlcnpgapfehviHAAKLAGAHDfiselPQGYNTEVGE--KGA---------------NLSGGQRQRIAIARALV 609
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489527602 167 MRPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHNM---QQAARI 215
Cdd:TIGR01846 610 GNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLstvRACDRI 661
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
10-228 |
5.96e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 93.56 E-value: 5.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTfirTLNRMNDLIE-DvtiKGNISVDGEDIytSDDVINLRT 88
Cdd:COG1137 5 EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTT---TFYMIVGLVKpD---SGRIFLDGEDI--THLPMHKRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 89 KVGM--------VFQKpnpfpMSIYDNVAYGPRTHGLrDKKQLDKIVEESLkgaaiwDE--VKDRLKSSALGLSGGQQQR 158
Cdd:COG1137 77 RLGIgylpqeasIFRK-----LTVEDNILAVLELRKL-SKKEREERLEELL------EEfgITHLRKSKAYSLSGGERRR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527602 159 ICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLK-KDYTIVIVTHNMQQAARISDETAFFLNGEVI 228
Cdd:COG1137 145 VEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKeRGIGVLITDHNVRETLGICDRAYIISEGKVL 215
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
9-207 |
8.12e-23 |
|
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: 92.16 E-value: 8.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLnrMNdLIEDVtiKGNISVDGEDIYTSDDviNLRT 88
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRIL--AG-LLPPS--AGEVLWNGEPIRDARE--DYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 89 KVGMVFQKPNPFP-MSIYDNVAYGPRTHGLR-DKKQLDKIVEE-SLKGAAiwdevkDRLkssALGLSGGQQQRICIARAI 165
Cdd:COG4133 76 RLAYLGHADGLKPeLTVRENLRFWAALYGLRaDREAIDEALEAvGLAGLA------DLP---VRQLSAGQKRRVALARLL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489527602 166 AMRPEVILMDEPTSALDPISTLKVEELIED-LKKDYTIVIVTH 207
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTH 189
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
10-245 |
8.29e-23 |
|
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: 92.99 E-value: 8.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTfirTLNRMNDLIedVTIKGNISVDGEDIytSDDVINLRTK 89
Cdd:cd03218 2 RAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTT---TFYMIVGLV--KPDSGKILLDGQDI--TKLPMHKRAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 90 VGMVF--QKPNPF-PMSIYDNVAYGPRTHGLrDKKQLDKIVEESLKGAAIwDEVKDRLkssALGLSGGQQQRICIARAIA 166
Cdd:cd03218 75 LGIGYlpQEASIFrKLTVEENILAVLEIRGL-SKKEREEKLEELLEEFHI-THLRKSK---ASSLSGGERRRVEIARALA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 167 MRPEVILMDEPTSALDPISTLKVEELIEDLK-KDYTIVIVTHNMQQAARISDeTAFFLN-GEVIEFSDTKTMFTTPVDKR 244
Cdd:cd03218 150 TNPKFLLLDEPFAGVDPIAVQDIQKIIKILKdRGIGVLITDHNVRETLSITD-RAYIIYeGKVLAEGTPEEIAANELVRK 228
|
.
gi 489527602 245 T 245
Cdd:cd03218 229 V 229
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
9-228 |
2.21e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 92.49 E-value: 2.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRmnDLIEDvtiKGNISVDGEDI--YTSDDvinL 86
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTG--ELTPS---SGEVRLNGRPLaaWSPWE---L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 87 RTKVGMVFQKPN-PFPMSIYDNVAYGpRTHGLRDKKQLDKIVEESLKGAAIWDeVKDRLKSSalgLSGGQQQRICIARAI 165
Cdd:COG4559 74 ARRRAVLPQHSSlAFPFTVEEVVALG-RAPHGSSAAQDRQIVREALALVGLAH-LAGRSYQT---LSGGEQQRVQLARVL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527602 166 A-------MRPEVILMDEPTSALDPISTLKVEELIEDL-KKDYTIVIVTHNMQQAARISDETAFFLNGEVI 228
Cdd:COG4559 149 AqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLaRRGGGVVAVLHDLNLAAQYADRILLLHQGRLV 219
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
10-229 |
2.38e-22 |
|
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: 91.05 E-value: 2.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLnrMNDLIEDVTiKGNISVDGEDIytSDDVINLRTK 89
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTI--MGHPKYEVT-EGEILFKGEDI--TDLPPEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 90 VG--MVFQKPnpfpmsiydnvaygPRTHGLRdkkqldkiveeslkgaaiwdeVKDRLKSSALGLSGGQQQRICIARAIAM 167
Cdd:cd03217 77 LGifLAFQYP--------------PEIPGVK---------------------NADFLRYVNEGFSGGEKKRNEILQLLLL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489527602 168 RPEVILMDEPTSALDpISTLK-VEELIEDLK-KDYTIVIVTHNMQQAARISDETAFFL-NGEVIE 229
Cdd:cd03217 122 EPDLAILDEPDSGLD-IDALRlVAEVINKLReEGKSVLIITHYQRLLDYIKPDRVHVLyDGRIVK 185
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
21-229 |
2.70e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 92.44 E-value: 2.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 21 KQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndliEDVTiKGNISVDGEDIYTSD--DVINLRTKVGMVFQKP- 97
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGL----ESPS-QGNVSWRGEPLAKLNraQRKAFRRDIQMVFQDSi 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 98 ---NPfPMSIYDNVAYgPRTH--GLRDKKQLDKiVEESLKGAAIWDEVKDRLKSSalgLSGGQQQRICIARAIAMRPEVI 172
Cdd:PRK10419 100 savNP-RKTVREIIRE-PLRHllSLDKAERLAR-ASEMLRAVDLDDSVLDKRPPQ---LSGGQLQRVCLARALAVEPKLL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489527602 173 LMDEPTSALDPISTLKVEELIEDLKKDYTI--VIVTHNMQQAARISDETAFFLNGEVIE 229
Cdd:PRK10419 174 ILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
28-229 |
2.80e-22 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 95.40 E-value: 2.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 28 NMDIKENKVTALIGPSGCGKSTFIRTLNRMNDliedvTIKGNISVDG---EDIytSDDVinLRTKVGMVFQKPNPFPMSI 104
Cdd:TIGR03796 499 SLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQ-----PWSGEILFDGiprEEI--PREV--LANSVAMVDQDIFLFEGTV 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 105 YDNVAygprthgLRDKKQLDKIVEESLKGAAIWDEVKDR-------LKSSALGLSGGQQQRICIARAIAMRPEVILMDEP 177
Cdd:TIGR03796 570 RDNLT-------LWDPTIPDADLVRACKDAAIHDVITSRpggydaeLAEGGANLSGGQRQRLEIARALVRNPSILILDEA 642
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489527602 178 TSALDPISTLKVEELIEdlKKDYTIVIVTHNMqQAARISDETAFFLNGEVIE 229
Cdd:TIGR03796 643 TSALDPETEKIIDDNLR--RRGCTCIIVAHRL-STIRDCDEIIVLERGKVVQ 691
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
21-230 |
3.35e-22 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 93.40 E-value: 3.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 21 KQALKKINMDIKE----NKVTALIGPSGCGKSTFIrtlnrmnDLIEDVTI--KGNISVDGEDIYTSDDVINL---RTKVG 91
Cdd:PRK11144 7 KQQLGDLCLTVNLtlpaQGITAIFGRSGAGKTSLI-------NAISGLTRpqKGRIVLNGRVLFDAEKGICLppeKRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 92 MVFQKPNPFP-MSIYDNVAYGPRThglRDKKQLDKIVE----ESLKgaaiwdevkDRLKSSalgLSGGQQQRICIARAIA 166
Cdd:PRK11144 80 YVFQDARLFPhYKVRGNLRYGMAK---SMVAQFDKIVAllgiEPLL---------DRYPGS---LSGGEKQRVAIGRALL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 167 MRPEVILMDEPTSALD-PistlKVEELI---EDLKKDYTIVI--VTHNMQQAARISDETAFFLNGEVIEF 230
Cdd:PRK11144 145 TAPELLLMDEPLASLDlP----RKRELLpylERLAREINIPIlyVSHSLDEILRLADRVVVLEQGKVKAF 210
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
28-227 |
3.71e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 91.18 E-value: 3.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 28 NMDIKENKVTALIGPSGCGKSTFirtLNRMNDLIEdvTIKGNISVDGED-IYTSDDvinlRTKVGMVFQKPNPFP-MSIY 105
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTL---LNLIAGFLT--PASGSLTLNGQDhTTTPPS----RRPVSMLFQENNLFShLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 106 DNVAYG--PrthGLR----DKKQLDKIVEE-SLkgaaiwDEVKDRLKSSalgLSGGQQQRICIARAIAMRPEVILMDEPT 178
Cdd:PRK10771 90 QNIGLGlnP---GLKlnaaQREKLHAIARQmGI------EDLLARLPGQ---LSGGQRQRVALARCLVREQPILLLDEPF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489527602 179 SALDPisTLKVE--ELIEDL--KKDYTIVIVTHNMQQAARISDETAFFLNGEV 227
Cdd:PRK10771 158 SALDP--ALRQEmlTLVSQVcqERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
6-224 |
4.15e-22 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 95.10 E-value: 4.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 6 KIKMSVKDLDLFYGDKQAL---KKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEDVTI---------------- 66
Cdd:PTZ00265 1163 KGKIEIMDVNFRYISRPNVpiyKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIvfknehtndmtneqdy 1242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 67 ---------------------------------KGNISVDGEDI--YTSDDVINLrtkVGMVFQKPNPFPMSIYDNVAYG 111
Cdd:PTZ00265 1243 qgdeeqnvgmknvnefsltkeggsgedstvfknSGKILLDGVDIcdYNLKDLRNL---FSIVSQEPMLFNMSIYENIKFG 1319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 112 PRTHGLRDKKQLDKIveeslkgAAIwDEVKDRLKSS--------ALGLSGGQQQRICIARAIAMRPEVILMDEPTSALDP 183
Cdd:PTZ00265 1320 KEDATREDVKRACKF-------AAI-DEFIESLPNKydtnvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDS 1391
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 489527602 184 ISTLKVEELIEDLKK--DYTIVIVTHNMQQAARiSDETAFFLN 224
Cdd:PTZ00265 1392 NSEKLIEKTIVDIKDkaDKTIITIAHRIASIKR-SDKIVVFNN 1433
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-218 |
5.08e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 94.32 E-value: 5.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 18 YGDKQALKKINMDIKENKVTALIGPSGCGKSTFirtlnrMN--------DliedvtiKGNISVDGE--DIYTSDDVINLr 87
Cdd:COG3845 15 FGGVVANDDVSLTVRPGEIHALLGENGAGKSTL------MKilyglyqpD-------SGEILIDGKpvRIRSPRDAIAL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 88 tKVGMVFQKPNPFP-MSIYDNVAYG--PRTHGLRDKKQLDKIVEE-----SLK---GAAIWDevkdrlkssalgLSGGQQ 156
Cdd:COG3845 81 -GIGMVHQHFMLVPnLTVAENIVLGlePTKGGRLDRKAARARIRElseryGLDvdpDAKVED------------LSVGEQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489527602 157 QRICIARAIAMRPEVILMDEPTSALDPistLKVEELIEDLKK----DYTIVIVTHNMQQAARISDE 218
Cdd:COG3845 148 QRVEILKALYRGARILILDEPTAVLTP---QEADELFEILRRlaaeGKSIIFITHKLREVMAIADR 210
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
27-240 |
6.03e-22 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 91.30 E-value: 6.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 27 INMDIKENKVTALIGPSGCGKStfIRTLNRMNDLIEDVT-IKGNISVDGEDIYTSDdvinLR-TKVGMVFQKPNPfpmsi 104
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRqTAGRVLLDGKPVAPCA----LRgRKIATIMQNPRS----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 105 ydnvAYGP----RTHGLRDKKQLDKIVEESLKGAAI----WDEVKDRLKSSALGLSGGQQQRICIARAIAMRPEVILMDE 176
Cdd:PRK10418 91 ----AFNPlhtmHTHARETCLALGKPADDATLTAALeavgLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489527602 177 PTSALDPISTLKVEELIEDL--KKDYTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTP 240
Cdd:PRK10418 167 PTTDLDVVAQARILDLLESIvqKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAP 232
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
7-211 |
6.30e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 94.14 E-value: 6.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 7 IKMSVKDLDLF-YGDKQALKKINMDIKENKVTALIGPSGCGKSTFIrtlnrmNDLIEDVTIKGNISVDGEDIyTSDDVIN 85
Cdd:PRK11174 348 VTIEAEDLEILsPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLL------NALLGFLPYQGSLKINGIEL-RELDPES 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 86 LRTKVGMVFQKPNPFPMSIYDNVAYG------PRTHGLRDKKQLDKIVEESLKGaaiWD-EVKDRlkssALGLSGGQQQR 158
Cdd:PRK11174 421 WRKHLSWVGQNPQLPHGTLRDNVLLGnpdasdEQLQQALENAWVSEFLPLLPQG---LDtPIGDQ----AAGLSVGQAQR 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489527602 159 ICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHNMQQ 211
Cdd:PRK11174 494 LALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLED 546
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
9-240 |
6.68e-22 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 92.48 E-value: 6.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFY----GDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLnrMNDLIEDVTIKGNISVDGEDIytsddvI 84
Cdd:PRK09473 13 LDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFAL--MGLLAANGRIGGSATFNGREI------L 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 85 NLRTK---------VGMVFQKP----NPFpMSIYDNVAYGPRTHGLRDKKQldkIVEESLK--GAAIWDEVKDRLKSSAL 149
Cdd:PRK09473 85 NLPEKelnklraeqISMIFQDPmtslNPY-MRVGEQLMEVLMLHKGMSKAE---AFEESVRmlDAVKMPEARKRMKMYPH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 150 GLSGGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARISDETAFFLNGEV 227
Cdd:PRK09473 161 EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKVLVMYAGRT 240
|
250
....*....|...
gi 489527602 228 IEFSDTKTMFTTP 240
Cdd:PRK09473 241 MEYGNARDVFYQP 253
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
18-219 |
1.59e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 88.44 E-value: 1.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 18 YGDKQALKKINMDIKENKVTALIGPSGCGKSTfirtlnrmndLIEdvTIKGNISVDGEDIYTSDDVinlrtKVGMVFQK- 96
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKST----------LLK--VLAGVLRPTSGTVRRAGGA-----RVAYVPQRs 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 97 --PNPFPMSIYDNVAYG--PRTHGLRDKKQLDK-IVEESLKGAAIWDEVKDRLKSsalgLSGGQQQRICIARAIAMRPEV 171
Cdd:NF040873 65 evPDSLPLTVRDLVAMGrwARRGLWRRLTRDDRaAVDDALERVGLADLAGRQLGE----LSGGQRQRALLAQGLAQEADL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489527602 172 ILMDEPTSALDPISTLKVEELIEDLKKD-YTIVIVTHNMQQAARISDET 219
Cdd:NF040873 141 LLLDEPTTGLDAESRERIIALLAEEHARgATVVVVTHDLELVRRADPCV 189
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
17-214 |
1.95e-21 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 89.16 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 17 FYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRmndlIEDVTiKGNISVDGEDI--YTSDDVINLRTKVGMVF 94
Cdd:PRK10908 11 YLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICG----IERPS-AGKIWFSGHDItrLKNREVPFLRRQIGMIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 95 QKPNPF-PMSIYDNVAY-----GPRTHGLRDK--KQLDKIveeslkgaaiwdEVKDRLKSSALGLSGGQQQRICIARAIA 166
Cdd:PRK10908 86 QDHHLLmDRTVYDNVAIpliiaGASGDDIRRRvsAALDKV------------GLLDKAKNFPIQLSGGEQQRVGIARAVV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489527602 167 MRPEVILMDEPTSALDPISTLKVEELIEDLKK-DYTIVIVTHNMQQAAR 214
Cdd:PRK10908 154 NKPAVLLADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHDIGLISR 202
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
18-212 |
2.42e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 89.76 E-value: 2.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 18 YGDKQALKKINMDIKENKVTALIGPSGCGKSTFirtLNRMNDLIEDVTikGNISVDGEDiytsddVINLRTKVGMVFQKP 97
Cdd:PRK11248 11 YGGKPALEDINLTLESGELLVVLGPSGCGKTTL---LNLIAGFVPYQH--GSITLDGKP------VEGPGAERGVVFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 98 NPFP-MSIYDNVAYGPRTHGLrDKKQLDKIVEESLK-----GAA---IWDevkdrlkssalgLSGGQQQRICIARAIAMR 168
Cdd:PRK11248 80 GLLPwRNVQDNVAFGLQLAGV-EKMQRLEIAHQMLKkvgleGAEkryIWQ------------LSGGQRQRVGIARALAAN 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489527602 169 PEVILMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQA 212
Cdd:PRK11248 147 PQLLLLDEPFGALDAFTREQMQTLLLKLWQETgkQVLLITHDIEEA 192
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
10-208 |
2.78e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 88.97 E-value: 2.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLnrMNDLIEDVTiKGNISVDGEDIytSDDVINLRTK 89
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVL--MGHPKYEVT-SGSILLDGEDI--LELSPDERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 90 VG--MVFQKPNPFP-MSIYD--NVAYGPRTHGLRDKKQLDKIVEESLKgaaiwdEVKdrLKSSAL------GLSGGQQQR 158
Cdd:COG0396 77 AGifLAFQYPVEIPgVSVSNflRTALNARRGEELSAREFLKLLKEKMK------ELG--LDEDFLdryvneGFSGGEKKR 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489527602 159 ICIARAIAMRPEVILMDEPTSALDpISTLK-VEELIEDLK-KDYTIVIVTHN 208
Cdd:COG0396 149 NEILQMLLLEPKLAILDETDSGLD-IDALRiVAEGVNKLRsPDRGILIITHY 199
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-240 |
3.49e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.08 E-value: 3.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 19 GDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndliedVTIKGNISVDGEDIYTSD--DVINLRTKVGMVFQK 96
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRL------INSQGEIWFDGQPLHNLNrrQLLPVRHRIQVVFQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 97 P----NPfPMSIYDNVAYGPRTH-GLRDKKQLDKIVEESLKGAAIWDEVKDRLKSSalgLSGGQQQRICIARAIAMRPEV 171
Cdd:PRK15134 371 PnsslNP-RLNVLQIIEEGLRVHqPTLSAAQREQQVIAVMEEVGLDPETRHRYPAE---FSGGQRQRIAIARALILKPSL 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527602 172 ILMDEPTSALDPISTLKVEELIEDLKKDYTI--VIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTP 240
Cdd:PRK15134 447 IILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAP 517
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-228 |
3.81e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 89.37 E-value: 3.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 21 KQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNrmNDLIEDvtiKGNISVDGEDI-YTSDDVinlRTK-VGMVFQkpN 98
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIA--GSLPPD---SGSILIDGKDVtKLPEYK---RAKyIGRVFQ--D 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 99 PF----P-MSIYDN--VAYG---PRTHGLRDKKQLDKIVEESLKGAAIWDEvkDRLKSSALGLSGGQQQRICIARAIAMR 168
Cdd:COG1101 89 PMmgtaPsMTIEENlaLAYRrgkRRGLRRGLTKKRRELFRELLATLGLGLE--NRLDTKVGLLSGGQRQALSLLMATLTK 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489527602 169 PEVILMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARISDETAFFLNGEVI 228
Cdd:COG1101 167 PKLLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
11-227 |
5.78e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 88.92 E-value: 5.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 11 VKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndLIEDVTIKGNISVDGEDIYT----SDDVINL 86
Cdd:PRK09984 7 VEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL--ITGDKSAGSHIELLGRTVQRegrlARDIRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 87 RTKVGMVFQKPNPFP-MSIYDNVAYGP-------RTHGLRDKKQLDKIVEESLKGAAIWDEVKDRLKSsalgLSGGQQQR 158
Cdd:PRK09984 85 RANTGYIFQQFNLVNrLSVLENVLIGAlgstpfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVST----LSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527602 159 ICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKD--YTIVIVTHNMQQAARISDETAFFLNGEV 227
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
24-214 |
5.80e-21 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 87.91 E-value: 5.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 24 LKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEdvtikGNISVDGEDIYTSDDV--INLRTK-VGMVFQKPNPF 100
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSS-----GEVSLVGQPLHQMDEEarAKLRAKhVGFVFQSFMLI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 101 P-MSIYDNVAYGPRTHGLRDKKQLDKIVE--ESLKgaaiwdeVKDRLKSSALGLSGGQQQRICIARAIAMRPEVILMDEP 177
Cdd:PRK10584 101 PtLNALENVELPALLRGESSRQSRNGAKAllEQLG-------LGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 489527602 178 TSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAAR 214
Cdd:PRK10584 174 TGNLDRQTGDKIADLLFSLNREHgtTLILVTHDLQLAAR 212
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
23-226 |
6.28e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 88.89 E-value: 6.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 23 ALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDliedvTIKGNISVDGEDIYTSDDVINLRTKVGMVFQKPNP--F 100
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLR-----PQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNPETqfV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 101 PMSIYDNVAYGPRTHGL---RDKKQLDKIVEESLKGaaiwdevKDRLKSSAlGLSGGQQQRICIARAIAMRPEVILMDEP 177
Cdd:PRK13644 92 GRTVEEDLAFGPENLCLppiEIRKRVDRALAEIGLE-------KYRHRSPK-TLSGGQGQCVALAGILTMEPECLIFDEV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489527602 178 TSALDPISTLKVEELIEDL-KKDYTIVIVTHNMQQ---AARI--SDETAFFLNGE 226
Cdd:PRK13644 164 TSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEElhdADRIivMDRGKIVLEGE 218
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
19-230 |
6.43e-21 |
|
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: 91.35 E-value: 6.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 19 GDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLnrmndliedV----TIKGNISVDGEDIYTSDDViNLRTKVGMVF 94
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLL---------VgvwpPTAGSVRLDGADLSQWDRE-ELGRHIGYLP 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 95 QKPNPFPMSIYDNVAygpRTHGLRDkkqlDKIVEeslkgAAIWDEVKD-----------RLKSSALGLSGGQQQRICIAR 163
Cdd:COG4618 413 QDVELFDGTIAENIA---RFGDADP----EKVVA-----AAKLAGVHEmilrlpdgydtRIGEGGARLSGGQRQRIGLAR 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489527602 164 AIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKD-YTIVIVTHNMqQAARISDETAFFLNGEVIEF 230
Cdd:COG4618 481 ALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHRP-SLLAAVDKLLVLRDGRVQAF 547
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-229 |
9.32e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 91.04 E-value: 9.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 4 IDKIKMSVKDLDLFYGDKQ--ALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEdvtikGNISVDGEDI--YT 79
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQ-----GEILLNGQPIadYS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 80 SDDvinLRTKVGMVFQKPNPFPMSIYDNVAYGprTHGLRDKK--------QLDKIVEESlKGAAIWdevkdrlkssaLG- 150
Cdd:PRK11160 409 EAA---LRQAISVVSQRVHLFSATLRDNLLLA--APNASDEAlievlqqvGLEKLLEDD-KGLNAW-----------LGe 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 151 ----LSGGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHN---MQQAARIsdetAFFL 223
Cdd:PRK11160 472 ggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRltgLEQFDRI----CVMD 547
|
....*.
gi 489527602 224 NGEVIE 229
Cdd:PRK11160 548 NGQIIE 553
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
19-215 |
1.14e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 90.55 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 19 GDKQ--ALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndlieDVTIKGNISVDGEDIYT--SDDVINLRTK-VGMV 93
Cdd:PRK10535 17 GEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCL-----DKPTSGTYRVAGQDVATldADALAQLRREhFGFI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 94 FQKPNPFP-MSIYDNVAYGPRTHGLRDKKQLDKIVEESLKGAaiwdeVKDRLKSSALGLSGGQQQRICIARAIAMRPEVI 172
Cdd:PRK10535 92 FQRYHLLShLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLG-----LEDRVEYQPSQLSGGQQQRVSIARALMNGGQVI 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489527602 173 LMDEPTSALDPISTLKVEELIEDLK-KDYTIVIVTHNMQ---QAARI 215
Cdd:PRK10535 167 LADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQvaaQAERV 213
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
18-229 |
2.20e-20 |
|
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: 89.80 E-value: 2.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 18 YGDKqALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDliedvTIKGNISVDGEDIYTSDDVInLRTKVGMVFQKP 97
Cdd:TIGR01193 485 YGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQ-----ARSGEILLNGFSLKDIDRHT-LRQFINYLPQEP 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 98 NPFPMSIYDNVAYGPRTHGLRDKkqldkiVEESLKGAAIWDEVKD-------RLKSSALGLSGGQQQRICIARAIAMRPE 170
Cdd:TIGR01193 558 YIFSGSILENLLLGAKENVSQDE------IWAACEIAEIKDDIENmplgyqtELSEEGSSISGGQKQRIALARALLTDSK 631
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489527602 171 VILMDEPTSALDPISTLKVEELIEDLkKDYTIVIVTHNMQQAARiSDETAFFLNGEVIE 229
Cdd:TIGR01193 632 VLILDESTSNLDTITEKKIVNNLLNL-QDKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIE 688
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-229 |
2.48e-20 |
|
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: 89.48 E-value: 2.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMND-------------LIEDVTIKGNISVDGE 75
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyeptsgriiyhvaLCEKCGYVERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 76 --------------DIYTSDDVI--NLRTKVGMVFQKPnpFPM----SIYDNVAYGPRTHGLRDKKQLDKIVEeslkgaa 135
Cdd:TIGR03269 81 pcpvcggtlepeevDFWNLSDKLrrRIRKRIAIMLQRT--FALygddTVLDNVLEALEEIGYEGKEAVGRAVD------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 136 IWDEVK--DRLKSSALGLSGGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQ 211
Cdd:TIGR03269 152 LIEMVQlsHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEV 231
|
250
....*....|....*...
gi 489527602 212 AARISDETAFFLNGEVIE 229
Cdd:TIGR03269 232 IEDLSDKAIWLENGEIKE 249
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
9-228 |
3.08e-20 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 85.91 E-value: 3.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndLIEDvtiKGNISVDGEDIYTSDdvinLRt 88
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGI--LRPT---SGEIIFDGHPWTRKD----LH- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 89 KVGMVFQKPNPFP-MSIYDNVAYGPRTHGLRDKKqldkiVEESLKGAAIWDEVKDRLKSSALGLsggqQQRICIARAIAM 167
Cdd:TIGR03740 71 KIGSLIESPPLYEnLTARENLKVHTTLLGLPDSR-----IDEVLNIVDLTNTGKKKAKQFSLGM----KQRLGIAIALLN 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489527602 168 RPEVILMDEPTSALDPISTLKVEELIEDLKKD-YTIVIVTHNMQQAARISDETAFFLNGEVI 228
Cdd:TIGR03740 142 HPKLLILDEPTNGLDPIGIQELRELIRSFPEQgITVILSSHILSEVQQLADHIGIISEGVLG 203
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
9-229 |
4.84e-20 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 86.04 E-value: 4.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNrmNDLIEDVTIKGNISVDGE--DIYT---SDDV 83
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLA--GRLAPDHGTATYIMRSGAelELYQlseAERR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 84 INLRTKVGMVFQKPNP---FPMSIYDNVAYGPRTHGLRDKKQLDKIVEESLKGAAIwdeVKDRLKSSALGLSGGQQQRIC 160
Cdd:TIGR02323 82 RLMRTEWGFVHQNPRDglrMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEI---DPTRIDDLPRAFSGGMQQRLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527602 161 IARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDYTI--VIVTHNMQQAARISDETAFFLNGEVIE 229
Cdd:TIGR02323 159 IARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLavIIVTHDLGVARLLAQRLLVMQQGRVVE 229
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
20-206 |
6.42e-20 |
|
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: 85.02 E-value: 6.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 20 DKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDliEDVTIKGNISVDGE--DIYTSDDvinlrtKVGMVFQKP 97
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVE--GGGTTSGQILFNGQprKPDQFQK------CVAYVRQDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 98 NPFP-MSIYDNVAYGP--RTHGLRDKKQLDKIVE-ESLKGAAIWDEVKDRLKssalGLSGGQQQRICIARAIAMRPEVIL 173
Cdd:cd03234 91 ILLPgLTVRETLTYTAilRLPRKSSDAIRKKRVEdVLLRDLALTRIGGNLVK----GISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190
....*....|....*....|....*....|...
gi 489527602 174 MDEPTSALDPISTLKVEELIEDLKKDYTIVIVT 206
Cdd:cd03234 167 LDEPTSGLDSFTALNLVSTLSQLARRNRIVILT 199
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
22-217 |
6.72e-20 |
|
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: 85.18 E-value: 6.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 22 QALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRmNDLIEdvtiKGNISVDGE----DIYTSDD--VINLR-TKVGMVF 94
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG-NYLPD----SGSILVRHDggwvDLAQASPreILALRrRTIGYVS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 95 QkpnpFPMSIydnvaygPRThglrdkKQLDkIVEESL--KGAAIwDEVKDRLKS--SALGL------------SGGQQQR 158
Cdd:COG4778 100 Q----FLRVI-------PRV------SALD-VVAEPLleRGVDR-EEARARAREllARLNLperlwdlppatfSGGEQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 159 ICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDYT-IVIVTHNMQQAARISD 217
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTaIIGIFHDEEVREAVAD 220
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
12-208 |
1.24e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 84.38 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 12 KDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNrmnDLIEDVTikGNISVDGEDIYTSDDVInLRTKVG 91
Cdd:PRK10247 11 QNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVA---SLISPTS--GTLLFEGEDISTLKPEI-YRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 92 MVFQKPNPFPMSIYDNVAYgprTHGLRDKKQLDKIVEESLKGAAIWDEVkdrLKSSALGLSGGQQQRICIARAIAMRPEV 171
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIF---PWQIRNQQPDPAIFLDDLERFALPDTI---LTKNIAELSGGEKQRISLIRNLQFMPKV 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 489527602 172 ILMDEPTSALDPISTLKVEELIEDLKKDYTIVI--VTHN 208
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRYVREQNIAVlwVTHD 197
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
9-217 |
1.68e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 84.66 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKST-------FIRTLNrmndliedvtikGNISVDGEDI--YT 79
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTvfncltgFYKPTG------------GTILLRGQHIegLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 80 SDDVINLrtkvGMV--FQKPNPF-PMSIYDNVAYGPRTH-------GLRDKKQLDKIVEESLKGAAIWDEV---KDRLKS 146
Cdd:PRK11300 74 GHQIARM----GVVrtFQHVRLFrEMTVIENLLVAQHQQlktglfsGLLKTPAFRRAESEALDRAATWLERvglLEHANR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489527602 147 SALGLSGGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARISD 217
Cdd:PRK11300 150 QAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGISD 222
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-217 |
2.25e-19 |
|
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: 83.92 E-value: 2.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 18 YGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNrmnDLIedVTIKGNISVDGEDIYtsDDVINLRTKVGMVFQKP 97
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILS---GLL--QPTSGEVRVAGLVPW--KRRKKFLRRIGVVFGQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 98 NP--FPMSIYDNVAYGPRTHGLRD---KKQLDKIVEESlkgaaiwdEVKDRLKSSALGLSGGQQQRICIARAIAMRPEVI 172
Cdd:cd03267 104 TQlwWDLPVIDSFYLLAAIYDLPParfKKRLDELSELL--------DLEELLDTPVRQLSLGQRMRAEIAAALLHEPEIL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489527602 173 LMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARISD 217
Cdd:cd03267 176 FLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALAR 222
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-209 |
2.38e-19 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 87.01 E-value: 2.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 2 ELIDKIKMSVKDLDLFYG---DKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEdvtikGNISVDgeDIY 78
Cdd:PTZ00265 376 KLKDIKKIQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTE-----GDIIIN--DSH 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 79 TSDDvINL---RTKVGMVFQKPNPFPMSIYDNVAYGprTHGLRDKKQLDKIVEESLKG---------------------- 133
Cdd:PTZ00265 449 NLKD-INLkwwRSKIGVVSQDPLLFSNSIKNNIKYS--LYSLKDLEALSNYYNEDGNDsqenknkrnscrakcagdlndm 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 134 -------------------------------------AAIWDEVKDRLKSSALGLSGGQQQRICIARAIAMRPEVILMDE 176
Cdd:PTZ00265 526 snttdsneliemrknyqtikdsevvdvskkvlihdfvSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDE 605
|
250 260 270
....*....|....*....|....*....|....*
gi 489527602 177 PTSALDPISTLKVEELIEDLK--KDYTIVIVTHNM 209
Cdd:PTZ00265 606 ATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRL 640
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
18-230 |
2.91e-19 |
|
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: 83.35 E-value: 2.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 18 YGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRmndlIEDVTiKGNISVDGEDIYtsddVINLrtkvGMVFQkP 97
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAG----IYPPD-SGTVTVRGRVSS----LLGL----GGGFN-P 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 98 NpfpMSIYDNVAYGPRTHGLrDKKQLDKIVEEslkgaaIWD--EVKDRLKSSALGLSGGQQQRICIARAIAMRPEVILMD 175
Cdd:cd03220 98 E---LTGRENIYLNGRLLGL-SRKEIDEKIDE------IIEfsELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLID 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489527602 176 EPTSALDPISTLKVEELIEDLKKDYTIVI-VTHNMQQAARISDETAFFLNGEVIEF 230
Cdd:cd03220 168 EVLAVGDAAFQEKCQRRLRELLKQGKTVIlVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-240 |
7.42e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 85.14 E-value: 7.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 20 DKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEDVTIKGNISVDGEDIYTSDDViNLR----TKVGMVFQ 95
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGESLLHASEQ-TLRgvrgNKIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 96 KP----NPFpmsiydnvaygprtHGLrdKKQLDKIV-------EESLKGAAI--WDEV-----KDRLKSSALGLSGGQQQ 157
Cdd:PRK15134 100 EPmvslNPL--------------HTL--EKQLYEVLslhrgmrREAARGEILncLDRVgirqaAKRLTDYPHQLSGGERQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 158 RICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKK--DYTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKT 235
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAAT 243
|
....*
gi 489527602 236 MFTTP 240
Cdd:PRK15134 244 LFSAP 248
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
21-227 |
9.12e-19 |
|
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: 85.45 E-value: 9.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 21 KQALKKINMDIKENKVTALIGPSGCGKSTfirTLNRMNDLIEDVTikGNISVDGEDIYTSDDVInlRTKVGMVFQKPNPF 100
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTT---TLSILTGLLPPTS--GTVLVGGKDIETNLDAV--RQSLGMCPQHNILF 1015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 101 P-MSIYDNVAYGPRTHGLR-DKKQLDkiVEESLKGAAIwdevKDRLKSSALGLSGGQQQRICIARAIAMRPEVILMDEPT 178
Cdd:TIGR01257 1016 HhLTVAEHILFYAQLKGRSwEEAQLE--MEAMLEDTGL----HHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489527602 179 SALDPISTLKVEELIEDLKKDYTIVIVTHNMQQAARISDETAFFLNGEV 227
Cdd:TIGR01257 1090 SGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
18-228 |
1.06e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 82.25 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 18 YGDKQALKKINMDIKENKVTALIGPSGCGKSTfirTLNRMNDLIEDVTikGNISVDGEDIYTSDDVINLRTKVGMVFQKP 97
Cdd:PRK10895 13 YKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTT---TFYMVVGIVPRDA--GNIIIDDEDISLLPLHARARRGIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 98 NPFP-MSIYDNV-AYGPRTHGLRDKKQLDKiVEESLKGAAIwDEVKDRLKSSalgLSGGQQQRICIARAIAMRPEVILMD 175
Cdd:PRK10895 88 SIFRrLSVYDNLmAVLQIRDDLSAEQREDR-ANELMEEFHI-EHLRDSMGQS---LSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489527602 176 EPTSALDPISTLKVEELIEDLKKDYTIVIVT-HNMQQAARISDETAFFLNGEVI 228
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVRETLAVCERAYIVSQGHLI 216
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-232 |
1.82e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.19 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 22 QALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEdvtikGNISVDGEDIYTSDDVINLRTKVGMVFQKPNPFP 101
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDA-----GSILIDGQEMRFASTTAALAAGVAIIYQELHLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 102 -MSIYDNVAYG--PRTHGLRDKKQLDKIVEESLKGAAIWDEVKDRLKSsalgLSGGQQQRICIARAIAMRPEVILMDEPT 178
Cdd:PRK11288 93 eMTVAENLYLGqlPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489527602 179 SALDPISTLKVEELIEDLKKDYTIVI-VTHNMQQAARISDETAFFLNGEVIE-FSD 232
Cdd:PRK11288 169 SSLSAREIEQLFRVIRELRAEGRVILyVSHRMEEIFALCDAITVFKDGRYVAtFDD 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-207 |
1.82e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.96 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 11 VKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLnrMNDLIEDvtiKGNISVDGediytsddvinlRTKV 90
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKIL--AGELEPD---SGEVSIPK------------GLRI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 91 GMVFQKPNPFP-MSIYDNV--AYGPRTHGLRDKKQLDKIVEESLKGAAIWDEVKDRLKS--------------SALG--- 150
Cdd:COG0488 64 GYLPQEPPLDDdLTVLDTVldGDAELRALEAELEELEAKLAEPDEDLERLAELQEEFEAlggweaearaeeilSGLGfpe 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489527602 151 ---------LSGGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKdyTIVIVTH 207
Cdd:COG0488 144 edldrpvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPG--TVLVVSH 207
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
9-240 |
1.83e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 84.14 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGDKQ----ALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRmndLIEDVTikGNISVDGEDIYT-SDDV 83
Cdd:PRK10261 13 LAVENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMR---LLEQAG--GLVQCDKMLLRRrSRQV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 84 INLRTK------------VGMVFQKP----NP-FPMSiyDNVAYGPRTH-GLRDkkqldkivEESLKGAA-IWDEVKDRL 144
Cdd:PRK10261 88 IELSEQsaaqmrhvrgadMAMIFQEPmtslNPvFTVG--EQIAESIRLHqGASR--------EEAMVEAKrMLDQVRIPE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 145 KSSALG-----LSGGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDYT--IVIVTHNMQQAARISD 217
Cdd:PRK10261 158 AQTILSryphqLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIAD 237
|
250 260
....*....|....*....|...
gi 489527602 218 ETAFFLNGEVIEFSDTKTMFTTP 240
Cdd:PRK10261 238 RVLVMYQGEAVETGSVEQIFHAP 260
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-228 |
1.84e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 82.55 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNdliedVTIKGNISVDGEDIYTSDDVInlRT 88
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLT-----HPDAGSISLCGEPVPSRARHA--RQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 89 KVGMVFQKPNPFP-MSIYDNVAYGPRTHGLrDKKQLDKIVEESLKGAaiwdevkdRLKSSALG----LSGGQQQRICIAR 163
Cdd:PRK13537 81 RVGVVPQFDNLDPdFTVRENLLVFGRYFGL-SAAAARALVPPLLEFA--------KLENKADAkvgeLSGGMKRRLTLAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489527602 164 AIAMRPEVILMDEPTSALDPIST-LKVEELIEDLKKDYTIVIVTHNMQQAARISDETAFFLNGEVI 228
Cdd:PRK13537 152 ALVNDPDVLVLDEPTTGLDPQARhLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKI 217
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
18-217 |
2.38e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 82.96 E-value: 2.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 18 YGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDliEDVtikGNISVDGEDIytSDDVINLRTKVGMVFQKP 97
Cdd:PRK13536 51 YGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTS--PDA---GKITVLGVPV--PARARLARARIGVVPQFD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 98 NPFP-MSIYDNVAYGPRTHGLRdKKQLDKIVEESLKGAAIWDEVKDRLKSsalgLSGGQQQRICIARAIAMRPEVILMDE 176
Cdd:PRK13536 124 NLDLeFTVRENLLVFGRYFGMS-TREIEAVIPSLLEFARLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489527602 177 PTSALDPIST-LKVEELIEDLKKDYTIVIVTHNMQQAARISD 217
Cdd:PRK13536 199 PTTGLDPHARhLIWERLRSLLARGKTILLTTHFMEEAERLCD 240
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
9-207 |
1.39e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 81.39 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGDKQAL-KKINMDIKENKVTALIGPSGCGKSTFIRTLNRmndliedvtI----KGNISV-DGEDiytsdd 82
Cdd:COG4178 363 LALEDLTLRTPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG---------LwpygSGRIARpAGAR------ 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 83 vinlrtkvgMVF--QKPNpFPM-SIYDNVAYgPRTHGLRDKKQLDKIVE--------ESLKGAAIWDEVkdrlkssalgL 151
Cdd:COG4178 428 ---------VLFlpQRPY-LPLgTLREALLY-PATAEAFSDAELREALEavglghlaERLDEEADWDQV----------L 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489527602 152 SGGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTH 207
Cdd:COG4178 487 SLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGH 542
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
19-207 |
1.53e-17 |
|
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: 81.63 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 19 GDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLnrmndliedVTI----KGNISVDGEDIYTSDDViNLRTKVGMVF 94
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLI---------VGIwpptSGSVRLDGADLKQWDRE-TFGKHIGYLP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 95 QKPNPFPMSIYDNVAYgprthgLRDKKQLDKIVEES-LKGAaiwDEVKDRLKS---SALG-----LSGGQQQRICIARAI 165
Cdd:TIGR01842 399 QDVELFPGTVAENIAR------FGENADPEKIIEAAkLAGV---HELILRLPDgydTVIGpggatLSGGQRQRIALARAL 469
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489527602 166 AMRPEVILMDEPTSALDPISTLKVEELIEDLKK-DYTIVIVTH 207
Cdd:TIGR01842 470 YGDPKLVVLDEPNSNLDEEGEQALANAIKALKArGITVVVITH 512
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
9-254 |
1.65e-17 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 79.49 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLnrMNDLIED-----VTIKGNISVDGEDIyTSDDV 83
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKAL--AGDLTGGgaprgARVTGDVTLNGEPL-AAIDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 84 INLRTKVGMVFQKPNP-FPMSIYDNVAYGPRTHGLRDKkqldkivEESLKGAAIWDEVKDRLKSSALG------LSGGQQ 156
Cdd:PRK13547 79 PRLARLRAVLPQAAQPaFAFSAREIVLLGRYPHARRAG-------ALTHRDGEIAWQALALAGATALVgrdvttLSGGEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 157 QRICIARAIAM---------RPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVT--HNMQQAARISDETAFFLNG 225
Cdd:PRK13547 152 ARVQFARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAivHDPNLAARHADRIAMLADG 231
|
250 260
....*....|....*....|....*....
gi 489527602 226 EVIEFSdtktmftTPVDKRTEDYITGRFG 254
Cdd:PRK13547 232 AIVAHG-------APADVLTPAHIARCYG 253
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
11-230 |
4.45e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.11 E-value: 4.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 11 VKDLDLFYGDKQALKKINMDI-KENKVtALIGPSGCGKSTFIRTLNrmndliedvtikGNISVDGEDIYTSDDVinlrtK 89
Cdd:COG0488 318 LEGLSKSYGDKTLLDDLSLRIdRGDRI-GLIGPNGAGKSTLLKLLA------------GELEPDSGTVKLGETV-----K 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 90 VGMVFQKPNPFP--MSIYDNVAYGprthglRDKKQldkivEESL---------KGAAIWDEVKDrlkssalgLSGGQQQR 158
Cdd:COG0488 380 IGYFDQHQEELDpdKTVLDELRDG------APGGT-----EQEVrgylgrflfSGDDAFKPVGV--------LSGGEKAR 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489527602 159 ICIARAIAMRPEVILMDEPTSALDpISTLkveELIEDLKKDY--TIVIVTHNMQQAARISDETAFFLNGEVIEF 230
Cdd:COG0488 441 LALAKLLLSPPNVLLLDEPTNHLD-IETL---EALEEALDDFpgTVLLVSHDRYFLDRVATRILEFEDGGVREY 510
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
22-254 |
6.02e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 77.91 E-value: 6.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 22 QALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndlIEDVTikGNISVDGEDIYTSDdvINLRT-KVGMVFQKPNpf 100
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGM---IEPTS--GELLIDDHPLHFGD--YSYRSqRIRMIFQDPS-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 101 pmsiydnVAYGPRThglRDKKQLDK--IVEESLKGAAIWDEVKDRLKSSAL----------GLSGGQQQRICIARAIAMR 168
Cdd:PRK15112 98 -------TSLNPRQ---RISQILDFplRLNTDLEPEQREKQIIETLRQVGLlpdhasyyphMLAPGQKQRLGLARALILR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 169 PEVILMDEPTSALDPISTLKVEELIEDLKKDYTI--VIVTHNMQQAARISDETAFFLNGEVIEFSDTKTMFTTPVDKRTE 246
Cdd:PRK15112 168 PKVIIADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTK 247
|
....*...
gi 489527602 247 DYITGRFG 254
Cdd:PRK15112 248 RLIAGHFG 255
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
10-234 |
8.33e-17 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 74.79 E-value: 8.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLnrMNDLIEDvtiKGNISVDGediytsddvinlRTK 89
Cdd:cd03221 2 ELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLI--AGELEPD---EGIVTWGS------------TVK 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 90 VGMVFQkpnpfpmsiydnvaygprthglrdkkqldkiveeslkgaaiwdevkdrlkssalgLSGGQQQRICIARAIAMRP 169
Cdd:cd03221 65 IGYFEQ-------------------------------------------------------LSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489527602 170 EVILMDEPTSALDPIStlkVEELIEDLKKDY-TIVIVTHNmqqaarisdetAFFLNG---EVIEFSDTK 234
Cdd:cd03221 90 NLLLLDEPTNHLDLES---IEALEEALKEYPgTVILVSHD-----------RYFLDQvatKIIELEDGK 144
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
18-235 |
9.03e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 77.04 E-value: 9.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 18 YGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRmndlIEDVTiKGNISVDG------EdiytsddvinlrtkVG 91
Cdd:COG1134 36 REEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAG----ILEPT-SGRVEVNGrvsallE--------------LG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 92 MVFQkPNpfpMSIYDNVAYGPRTHGLRdKKQLDKIVEEslkgaaIWD--EVKDRL----KSsalgLSGGQQQRICIARAI 165
Cdd:COG1134 97 AGFH-PE---LTGRENIYLNGRLLGLS-RKEIDEKFDE------IVEfaELGDFIdqpvKT----YSSGMRARLAFAVAT 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527602 166 AMRPEVILMDEPTSALDPISTLKVEELIEDLKKDY-TIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKT 235
Cdd:COG1134 162 AVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGrTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
24-210 |
2.09e-16 |
|
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: 75.45 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 24 LKKINMDIKENKVTALIGPSGCGKSTFI-RTLNRMNdliedvTIKGNI----SVDGEDIYTSDDVINlRTKVGMVFQKPN 98
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQ------TLEGKVhwsnKNESEPSFEATRSRN-RYSVAYAAQKPW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 99 PFPMSIYDNVAYGPRTHGLRDKKQLDKI-VEESLKGAAIWDEVKdrLKSSALGLSGGQQQRICIARAIAMRPEVILMDEP 177
Cdd:cd03290 90 LLNATVEENITFGSPFNKQRYKAVTDACsLQPDIDLLPFGDQTE--IGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 489527602 178 TSALDPIST--LKVEELIEDLKKD-YTIVIVTHNMQ 210
Cdd:cd03290 168 FSALDIHLSdhLMQEGILKFLQDDkRTLVLVTHKLQ 203
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
24-207 |
2.17e-16 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 74.11 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 24 LKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIedvtiKGNISV-DGEDIYtsddvinlrtkvgMVFQKPnpfpm 102
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWG-----SGRIGMpEGEDLL-------------FLPQRP----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 103 siydnvaYGPRThglrdkkqldkiveeSLKGAAI--WDEVkdrlkssalgLSGGQQQRICIARAIAMRPEVILMDEPTSA 180
Cdd:cd03223 74 -------YLPLG---------------TLREQLIypWDDV----------LSGGEQQRLAFARLLLHKPKFVFLDEATSA 121
|
170 180
....*....|....*....|....*..
gi 489527602 181 LDPISTLKVEELIEDLKkdYTIVIVTH 207
Cdd:cd03223 122 LDEESEDRLYQLLKELG--ITVISVGH 146
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
9-229 |
5.88e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 74.96 E-value: 5.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRmnDLIEDvtiKGNISVDGE-----DIYTSDDV 83
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSA--RLAPD---AGEVHYRMRdgqlrDLYALSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 84 IN---LRTKVGMVFQKP-NPFPMSIY--DNV-----AYGPRTHG-LRDKkqldkiveeslkgAAIW-DEVK---DRLKSS 147
Cdd:PRK11701 82 ERrrlLRTEWGFVHQHPrDGLRMQVSagGNIgerlmAVGARHYGdIRAT-------------AGDWlERVEidaARIDDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 148 ALGLSGGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARISDETAFFLNG 225
Cdd:PRK11701 149 PTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELglAVVIVTHDLAVARLLAHRLLVMKQG 228
|
....
gi 489527602 226 EVIE 229
Cdd:PRK11701 229 RVVE 232
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
24-216 |
7.46e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 74.47 E-value: 7.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 24 LKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndlieDVTIKGNISVDGEDIYT--SDDVINLRT-KVGMVFQKPNPF 100
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL-----DTPTSGDVIFNGQPMSKlsSAAKAELRNqKLGFIYQFHHLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 101 P-MSIYDNVAYgPRTHGLRDKKQLDKIVEESLkgAAIWDEVKDRLKSSALglSGGQQQRICIARAIAMRPEVILMDEPTS 179
Cdd:PRK11629 100 PdFTALENVAM-PLLIGKKKPAEINSRALEML--AAVGLEHRANHRPSEL--SGGERQRVAIARALVNNPRLVLADEPTG 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 489527602 180 ALDPISTLKVEELIEDL--KKDYTIVIVTHNMQQAARIS 216
Cdd:PRK11629 175 NLDARNADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMS 213
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
35-228 |
1.23e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 74.05 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 35 KVTALIGPSGCGKSTFIRTLNRMNDLIEdvtikGNISVDGEDIYTSDDVINLRTKVGMVFQKPNPFPMSIYDNVAYGPRT 114
Cdd:PRK10575 38 KVTGLIGHNGSGKSTLLKMLGRHQPPSE-----GEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVRELVAIGRYP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 115 -HG------LRDKKQLDK-IVEESLKGAAiwdevkDRLKSSalgLSGGQQQRICIARAIAMRPEVILMDEPTSALDPIST 186
Cdd:PRK10575 113 wHGalgrfgAADREKVEEaISLVGLKPLA------HRLVDS---LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQ 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489527602 187 LKVEELIEDL--KKDYTIVIVTHNMQQAARISDETAFFLNGEVI 228
Cdd:PRK10575 184 VDVLALVHRLsqERGLTVIAVLHDINMAARYCDYLVALRGGEMI 227
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
9-240 |
3.13e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 74.01 E-value: 3.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGDK----QALKKINMDIKENKVTALIGPSGCGKStfIRTLNRMNdLIEdvtIKGNISVDGEDiYTSDDVI 84
Cdd:PRK11022 4 LNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKS--VSSLAIMG-LID---YPGRVMAEKLE-FNGQDLQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 85 NLRTK---------VGMVFQKP----NPFPMSIYdNVAYGPRTHGLRDKKQLDKIVEESLKGAAIWDEvKDRLKSSALGL 151
Cdd:PRK11022 77 RISEKerrnlvgaeVAMIFQDPmtslNPCYTVGF-QIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDP-ASRLDVYPHQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 152 SGGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDL--KKDYTIVIVTHNMQQAARISDETAFFLNGEVIE 229
Cdd:PRK11022 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqqKENMALVLITHDLALVAEAAHKIIVMYAGQVVE 234
|
250
....*....|.
gi 489527602 230 FSDTKTMFTTP 240
Cdd:PRK11022 235 TGKAHDIFRAP 245
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
23-239 |
3.68e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.99 E-value: 3.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 23 ALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIedvtiKGNISVDGEDIytsddviNLRTKVGMVFQKPNP--- 99
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLA-----SGKISILGQPT-------RQALQKNLVAYVPQSeev 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 100 ---FPMSIYDNVAYGPRTHG--LRDKKQLDK-IVEESLKGAAIWDevkdrLKSSALG-LSGGQQQRICIARAIAMRPEVI 172
Cdd:PRK15056 90 dwsFPVLVEDVVMMGRYGHMgwLRRAKKRDRqIVTAALARVDMVE-----FRHRQIGeLSGGQKKRVFLARAIAQQGQVI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489527602 173 LMDEPTSALDPISTLKVEELIEDLKKD-YTIVIVTHNMQQAARISDETAfFLNGEVIEFSDTKTMFTT 239
Cdd:PRK15056 165 LLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASGPTETTFTA 231
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
10-208 |
1.16e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 70.29 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRmndLIEDVtiKGNISVDGEDIyTSDDVINLRTK 89
Cdd:PRK13539 4 EGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAG---LLPPA--AGTIKLDGGDI-DDPDVAEACHY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 90 VG----MvfqKPNpfpMSIYDNVAYGPRTHGlrdkkQLDKIVEESLKGAAIwDEVKDRlksSALGLSGGQQQRICIAR-A 164
Cdd:PRK13539 78 LGhrnaM---KPA---LTVAENLEFWAAFLG-----GEELDIAAALEAVGL-APLAHL---PFGYLSAGQKRRVALARlL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489527602 165 IAMRPeVILMDEPTSALDPISTLKVEELIED-LKKDYTIVIVTHN 208
Cdd:PRK13539 143 VSNRP-IWILDEPTAALDAAAVALFAELIRAhLAQGGIVIAATHI 186
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
22-234 |
1.79e-14 |
|
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: 72.53 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 22 QALKKINMDIKENKVTALIGPSGCGKSTFIRTLNrmnDLIEDVTIKGNISVDGEDIYTSDDVINLRTKV----GMVFQKP 97
Cdd:TIGR03269 298 KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIA---GVLEPTSGEVNVRVGDEWVDMTKPGPDGRGRAkryiGILHQEY 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 98 NPFP-MSIYDNV--AYG---PRTHGLRDKKQLDKIVEESLKGAaiwDEVKDRLKSSalgLSGGQQQRICIARAIAMRPEV 171
Cdd:TIGR03269 375 DLYPhRTVLDNLteAIGlelPDELARMKAVITLKMVGFDEEKA---EEILDKYPDE---LSEGERHRVALAQVLIKEPRI 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489527602 172 ILMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQQAARISDETAFFLNGEVIEFSDTK 234
Cdd:TIGR03269 449 VILDEPTGTMDPITKVDVTHSILKAREEMeqTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPE 513
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-196 |
2.14e-14 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 69.58 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 19 GDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTL-NRMndliEDVTIKGNISVDGEDIytsddVINLRTKVGMVFQKP 97
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRK----TAGVITGEILINGRPL-----DKNFQRSTGYVEQQD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 98 NPFPMSiydnvaygprthglrdkkqldkIVEESLkgaaiwdevkdrLKSSAL-GLSGGQQQRICIARAIAMRPEVILMDE 176
Cdd:cd03232 89 VHSPNL----------------------TVREAL------------RFSALLrGLSVEQRKRLTIGVELAAKPSILFLDE 134
|
170 180
....*....|....*....|
gi 489527602 177 PTSALDPISTLKVEELIEDL 196
Cdd:cd03232 135 PTSGLDSQAAYNIVRFLKKL 154
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
9-233 |
5.33e-14 |
|
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: 68.23 E-value: 5.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLfygdKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndlieDVTIKGNISVDGEDI--YTSDDVINL 86
Cdd:cd03215 5 LEVRGLSV----KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGL-----RPPASGEITLDGKPVtrRSPRDAIRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 87 --------RTKVGMVFQkpnpfpMSIYDNVAYGPRthglrdkkqldkiveeslkgaaiwdevkdrlkssalgLSGGQQQR 158
Cdd:cd03215 76 giayvpedRKREGLVLD------LSVAENIALSSL-------------------------------------LSGGNQQK 112
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489527602 159 ICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVthnmqqaarISDETAfflngEVIEFSDT 233
Cdd:cd03215 113 VVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLL---------ISSELD-----ELLGLCDR 173
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
8-210 |
5.47e-14 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 69.88 E-value: 5.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 8 KMSVKDLDLFY--GDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndliedVTIKGNISVDGediyTSDDVIN 85
Cdd:cd03289 2 QMTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL------LNTEGDIQIDG----VSWNSVP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 86 L---RTKVGMVFQKPNPFPMSIYDNVaygpRTHGLRDKKQLDKIVEE-SLKgaAIWDEVKDRLKSSALG----LSGGQQQ 157
Cdd:cd03289 72 LqkwRKAFGVIPQKVFIFSGTFRKNL----DPYGKWSDEEIWKVAEEvGLK--SVIEQFPGQLDFVLVDggcvLSHGHKQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489527602 158 RICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHNMQ 210
Cdd:cd03289 146 LMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIE 198
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
16-217 |
1.13e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.98 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 16 LFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRmnDLIEDvtikgnisvDGEDIYTSDDVinlrtkVGMVFQ 95
Cdd:PRK11147 11 LSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNG--EVLLD---------DGRIIYEQDLI------VARLQQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 96 KPnpfPM----SIYDNVAYG--------PRTHGLRDK----------KQLDKiVEESLKGAAIW---DEVKDRLKSSAL- 149
Cdd:PRK11147 74 DP---PRnvegTVYDFVAEGieeqaeylKRYHDISHLvetdpseknlNELAK-LQEQLDHHNLWqleNRINEVLAQLGLd 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 150 ------GLSGGQQQRICIARAIAMRPEVILMDEPTSALDpISTLkveELIEDLKKDY--TIVIVTH------NMqqAARI 215
Cdd:PRK11147 150 pdaalsSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD-IETI---EWLEGFLKTFqgSIIFISHdrsfirNM--ATRI 223
|
..
gi 489527602 216 SD 217
Cdd:PRK11147 224 VD 225
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-240 |
2.78e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 68.97 E-value: 2.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 20 DKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEdvtikGNISVDGEDIYTS--DDvinLRTKVGMVFQKP 97
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSE-----GDIRFHDIPLTKLqlDS---WRSRLAVVSQTP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 98 NPFPMSIYDNVAYG-PrthglrDKKQLDkiVEESLKGAAIWD-----------EVKDRlkssALGLSGGQQQRICIARAI 165
Cdd:PRK10789 399 FLFSDTVANNIALGrP------DATQQE--IEHVARLASVHDdilrlpqgydtEVGER----GVMLSGGQKQRISIARAL 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489527602 166 AMRPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHNMqQAARISDETAFFLNGEVIEFSDTKTMFTTP 240
Cdd:PRK10789 467 LLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRL-SALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
8-237 |
6.80e-13 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 66.47 E-value: 6.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 8 KMSVKDLDLFYGD--KQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEdvtikGNISVDGEDIyTSDDVIN 85
Cdd:cd03288 19 EIKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFD-----GKIVIDGIDI-SKLPLHT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 86 LRTKVGMVFQKPNPFPMSIYDNVayGPrthglrDKKQLDKIVEESLKGAaiwdEVKDRLKSSALGL-----------SGG 154
Cdd:cd03288 93 LRSRLSIILQDPILFSGSIRFNL--DP------ECKCTDDRLWEALEIA----QLKNMVKSLPGGLdavvteggenfSVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 155 QQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHNMQQAARiSDETAFFLNGEVIEFSDTK 234
Cdd:cd03288 161 QRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPE 239
|
...
gi 489527602 235 TMF 237
Cdd:cd03288 240 NLL 242
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
9-217 |
1.02e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.12 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDliedvTIKGNISVDGEDIYTSDDVINLRT 88
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHE-----PTKGTITINNINYNKLDHKLAAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 89 KVGMVFQKPNPF-PMSIYDNVAYG----PRTHGLR--DKKQLDKIVEESLKGAAIwdevKDRLKSSALGLSGGQQQRICI 161
Cdd:PRK09700 81 GIGIIYQELSVIdELTVLENLYIGrhltKKVCGVNiiDWREMRVRAAMMLLRVGL----KVDLDEKVANLSISHKQMLEI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489527602 162 ARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDYT-IVIVTHNMQQAARISD 217
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTaIVYISHKLAEIRRICD 213
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
8-207 |
1.13e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 67.05 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 8 KMSVKDLDLFY-GDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLnrMNDLIEDvtiKGNISVDGEDIYT-SDDVin 85
Cdd:PRK10790 340 RIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLL--MGYYPLT---EGEIRLDGRPLSSlSHSV-- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 86 LRTKVGMVFQKPNPFPMSIYDNVAYGprthglRDkkqldkIVEESLKGA-----------AIWDEVKDRLKSSALGLSGG 154
Cdd:PRK10790 413 LRQGVAMVQQDPVVLADTFLANVTLG------RD------ISEEQVWQAletvqlaelarSLPDGLYTPLGEQGNNLSVG 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489527602 155 QQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTH 207
Cdd:PRK10790 481 QKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAH 533
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-251 |
1.21e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.06 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 22 QALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEdvtikGNISVDGEDIYTSDDVINLRTKVGMVFQKPNPF- 100
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDS-----GSILFQGKEIDFKSSKEALENGISMVHQELNLVl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 101 PMSIYDNVAYG--PRTHGLRDKkqlDKIVEESlkgAAIWDE----VKDRLKSSALGLSggQQQRICIARAIAMRPEVILM 174
Cdd:PRK10982 87 QRSVMDNMWLGryPTKGMFVDQ---DKMYRDT---KAIFDEldidIDPRAKVATLSVS--QMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 175 DEPTSALdpiSTLKVEEL---IEDLK-KDYTIVIVTHNMQQAARISDETAFFLNGEVIEfsdtktmfTTPVDKRTEDYIT 250
Cdd:PRK10982 159 DEPTSSL---TEKEVNHLftiIRKLKeRGCGIVYISHKMEEIFQLCDEITILRDGQWIA--------TQPLAGLTMDKII 227
|
.
gi 489527602 251 G 251
Cdd:PRK10982 228 A 228
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
9-207 |
1.55e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 65.20 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLieDVTiKGNISVDGEDIYTSDDVINLRT 88
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDY--EVT-GGTVEFKGKDLLELSPEDRAGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 89 KVGMVFQKP-------NPFPMSIYDNVAYGPRTHGLRDKKQLDKIVEESLKGAAIWDEVKDRlkSSALGLSGGQQQRICI 161
Cdd:PRK09580 79 GIFMAFQYPveipgvsNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTR--SVNVGFSGGEKKRNDI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489527602 162 ARAIAMRPEVILMDEPTSALDpISTLK-VEELIEDLKK-DYTIVIVTH 207
Cdd:PRK09580 157 LQMAVLEPELCILDESDSGLD-IDALKiVADGVNSLRDgKRSFIIVTH 203
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-240 |
1.69e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 66.08 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 1 MELIDkIKMSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIR------------TLNRMN----DLIEdV 64
Cdd:COG4170 1 MPLLD-IRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKaicgitkdnwhvTADRFRwngiDLLK-L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 65 TIKGNISVDGEDIytsddvinlrtkvGMVFQKPNPF--PM---------SIYDNVAYGPRTHGLRDKKqldKIVEESLKG 133
Cdd:COG4170 79 SPRERRKIIGREI-------------AMIFQEPSSCldPSakigdqlieAIPSWTFKGKWWQRFKWRK---KRAIELLHR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 134 AAIWDEvKDRLKSSALGLSGGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKK--DYTIVIVTHNMQQ 211
Cdd:COG4170 143 VGIKDH-KDIMNSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlqGTSILLISHDLES 221
|
250 260
....*....|....*....|....*....
gi 489527602 212 AARISDETAFFLNGEVIEFSDTKTMFTTP 240
Cdd:COG4170 222 ISQWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-209 |
2.82e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 66.12 E-value: 2.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 19 GDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTL-NRMNDLIEDVTIKGNISVDGEDIYTSDDvinlrtkvgmvfqkp 97
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALlAEMDKVEGHVHMKGSVAYVPQQAWIQND--------------- 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 98 npfpmSIYDNVAYGprtHGLRDKKqldkiVEESLKGAAIWDEVK-----DR--LKSSALGLSGGQQQRICIARAIAMRPE 170
Cdd:TIGR00957 714 -----SLRENILFG---KALNEKY-----YQQVLEACALLPDLEilpsgDRteIGEKGVNLSGGQKQRVSLARAVYSNAD 780
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489527602 171 VILMDEPTSALDP-ISTLKVEELI--EDLKKDYTIVIVTHNM 209
Cdd:TIGR00957 781 IYLFDDPLSAVDAhVGKHIFEHVIgpEGVLKNKTRILVTHGI 822
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-236 |
2.96e-12 |
|
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: 65.62 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 18 YGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNrmnDLIEDVTIKGNISVDGEDIYTSDDVINLRTKVGMVFQKP 97
Cdd:TIGR02633 11 FGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILS---GVYPHGTWDGEIYWSGSPLKASNIRDTERAGIVIIHQEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 98 NPFP-MSIYDNVAYGPR-TH--GLRDKKQLDKIVEESLKGAAIwDEVKDRLKSSALGlsGGQQQRICIARAIAMRPEVIL 173
Cdd:TIGR02633 88 TLVPeLSVAENIFLGNEiTLpgGRMAYNAMYLRAKNLLRELQL-DADNVTRPVGDYG--GGQQQLVEIAKALNKQARLLI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489527602 174 MDEPTSALDPISTLKVEELIEDLK-KDYTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTM 236
Cdd:TIGR02633 165 LDEPSSSLTEKETEILLDIIRDLKaHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM 228
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-210 |
3.80e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 64.72 E-value: 3.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 7 IKMSVKDLdlF---YGDKQALKKINMDIKENKVTALIGPSGCGKSTfirtlnrmndliedvTIK----------GNISVD 73
Cdd:COG4586 20 LKGALKGL--FrreYREVEAVDDISFTIEPGEIVGFIGPNGAGKST---------------TIKmltgilvptsGEVRVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 74 GEDIYtsDDVINLRTKVGMVFqkpnpfpmsiydnvayGPRThglrdkkQL--DKIVEESLK-GAAIWD----EVKDRLK- 145
Cdd:COG4586 83 GYVPF--KRRKEFARRIGVVF----------------GQRS-------QLwwDLPAIDSFRlLKAIYRipdaEYKKRLDe 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489527602 146 -SSALGLSG-----------GQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDY--TIVIVTHNMQ 210
Cdd:COG4586 138 lVELLDLGElldtpvrqlslGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMD 216
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
21-242 |
5.84e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 65.07 E-value: 5.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 21 KQALKKINMDIKENKVTALIGPSGCGKSTFIRTLnrMNDLIEDVTIKGNISVDGEDIytsdDVINLRTKVGMVFQKPNPF 100
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNAL--AFRSPKGVKGSGSVLLNGMPI----DAKEMRAISAYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 101 PM-SIYDNVAYG-----PRTHGLRDKKQ-LDKIVEE-SLKGAA---IWDEvkDRLKssalGLSGGQQQRICIARAIAMRP 169
Cdd:TIGR00955 112 PTlTVREHLMFQahlrmPRRVTKKEKRErVDEVLQAlGLRKCAntrIGVP--GRVK----GLSGGERKRLAFASELLTDP 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489527602 170 EVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVT-HnmQQAARIsdetaFFLNGEVIEFSDTKTMFTTPVD 242
Cdd:TIGR00955 186 PLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTiH--QPSSEL-----FELFDKIILMAEGRVAYLGSPD 252
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
9-218 |
6.85e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.59 E-value: 6.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 9 MSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTlnrmndliedvtIKGNISVDGEDIYTSDdvinlRT 88
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRV------------VLGLVAPDEGVIKRNG-----KL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 89 KVGMVFQKPN---PFPMSIYDNVAYGPrthGLRDKKQLDKIveESLKGAAIWDEVKDRLkssalglSGGQQQRICIARAI 165
Cdd:PRK09544 68 RIGYVPQKLYldtTLPLTVNRFLRLRP---GTKKEDILPAL--KRVQAGHLIDAPMQKL-------SGGETQRVLLARAL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489527602 166 AMRPEVILMDEPTSALDPISTLKVEELIEDLKK--DYTIVIVTHNMQQAARISDE 218
Cdd:PRK09544 136 LNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVMAKTDE 190
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-207 |
7.87e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.05 E-value: 7.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 21 KQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRmndLIEDVTIKGNISVDGEDIYTSDDVInlrtkvgmvfqkpnpf 100
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG---ALKGTPVAGCVDVPDNQFGREASLI---------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 101 pmsiyDNVAygprthglRDKKQLDKIveESLKGAAIWDEVKDRLKSSALglSGGQQQRICIARAIAMRPEVILMDEPTSA 180
Cdd:COG2401 104 -----DAIG--------RKGDFKDAV--ELLNAVGLSDAVLWLRRFKEL--STGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170 180 190
....*....|....*....|....*....|.
gi 489527602 181 LDP----ISTLKVEELIEDLKKdyTIVIVTH 207
Cdd:COG2401 167 LDRqtakRVARNLQKLARRAGI--TLVVATH 195
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
8-210 |
8.17e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 64.93 E-value: 8.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 8 KMSVKDLDLFY--GDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndliedVTIKGNISVDGediyTSDDVIN 85
Cdd:TIGR01271 1217 QMDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL------LSTEGEIQIDG----VSWNSVT 1286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 86 L---RTKVGMVFQKPNPFPMSIYDNVaygpRTHGLRDKKQLDKIVEE-SLKgaAIWDEVKDRLK----SSALGLSGGQQQ 157
Cdd:TIGR01271 1287 LqtwRKAFGVIPQKVFIFSGTFRKNL----DPYEQWSDEEIWKVAEEvGLK--SVIEQFPDKLDfvlvDGGYVLSNGHKQ 1360
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489527602 158 RICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHNMQ 210
Cdd:TIGR01271 1361 LMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVE 1413
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
19-240 |
8.65e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 64.05 E-value: 8.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 19 GDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTlnrmndlIEDVTiKGNISVDGeDIYTSDDVINLRT---------- 88
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKA-------ICGVT-KDNWRVTA-DRMRFDDIDLLRLsprerrklvg 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 89 -KVGMVFQKP----NP-----------FPMSIYDNVAYgpRTHGLRDKKQLdkiveESLKGAAIWDEvKDRLKSSALGLS 152
Cdd:PRK15093 89 hNVSMIFQEPqsclDPservgrqlmqnIPGWTYKGRWW--QRFGWRKRRAI-----ELLHRVGIKDH-KDAMRSFPYELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 153 GGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKD--YTIVIVTHNMQQAARISDETAFFLNGEVIEF 230
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnnTTILLISHDLQMLSQWADKINVLYCGQTVET 240
|
250
....*....|
gi 489527602 231 SDTKTMFTTP 240
Cdd:PRK15093 241 APSKELVTTP 250
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-232 |
1.35e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 63.88 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 4 IDKIKMSVKDLdlfyGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndlieDVTIKGNISVDGE--DIYTSD 81
Cdd:COG1129 252 PGEVVLEVEGL----SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGA-----DPADSGEIRLDGKpvRIRSPR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 82 DVINL--------RTKVGMVFqkpnpfPMSIYDNVAYGP----RTHGLRDKKQLDKIVEE-----SLKGAAIWDEVKDrl 144
Cdd:COG1129 323 DAIRAgiayvpedRKGEGLVL------DLSIRENITLASldrlSRGGLLDRRRERALAEEyikrlRIKTPSPEQPVGN-- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 145 kssalgLSGGQQQRICIARAIAMRPEVILMDEPTSALDpISTlKVE--ELIEDLKKDYTIVIVthnmqqaarISDETAff 222
Cdd:COG1129 395 ------LSGGNQQKVVLAKWLATDPKVLILDEPTRGID-VGA-KAEiyRLIRELAAEGKAVIV---------ISSELP-- 455
|
250
....*....|
gi 489527602 223 lngEVIEFSD 232
Cdd:COG1129 456 ---ELLGLSD 462
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-209 |
1.73e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.67 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 31 IKENKVTALIGPSGCGKSTFIRTLNRmndliedvTIKGNISvDGEDIYTSDDVINL--RTKVGMVFQKpnpfpmsIYDN- 107
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSG--------ELIPNLG-DYEEEPSWDEVLKRfrGTELQNYFKK-------LYNGe 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 108 --VAYGPRthgLRDK--KQLDKIVEESLKGA---AIWDEVKDRLKSSAL------GLSGGQQQRICIARAIAMRPEVILM 174
Cdd:PRK13409 160 ikVVHKPQ---YVDLipKVFKGKVRELLKKVderGKLDEVVERLGLENIldrdisELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190
....*....|....*....|....*....|....*
gi 489527602 175 DEPTSALDPISTLKVEELIEDLKKDYTIVIVTHNM 209
Cdd:PRK13409 237 DEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
13-230 |
8.27e-11 |
|
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: 61.89 E-value: 8.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 13 DLDLfygdkqALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDliedvTIKGNISVDGEDIyTSDDVINLRTKVGM 92
Cdd:TIGR00957 1297 DLDL------VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINE-----SAEGEIIIDGLNI-AKIGLHDLRFKITI 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 93 VFQKPNPFPMSIYDNV-AYGPRThglrDKKQLDKIVEESLKG--AAIWDEVKDRLKSSALGLSGGQQQRICIARAIAMRP 169
Cdd:TIGR00957 1365 IPQDPVLFSGSLRMNLdPFSQYS----DEEVWWALELAHLKTfvSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKT 1440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489527602 170 EVILMDEPTSALDpistLKVEELIEDLKK----DYTIVIVTHNMQQaarISDETAFFL--NGEVIEF 230
Cdd:TIGR00957 1441 KILVLDEATAAVD----LETDNLIQSTIRtqfeDCTVLTIAHRLNT---IMDYTRVIVldKGEVAEF 1500
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
11-207 |
1.55e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.66 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 11 VKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLiedVTIKGNISVDGEDIYTSDDviNLRTKV 90
Cdd:CHL00131 10 IKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAY---KILEGDILFKGESILDLEP--EERAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 91 G--MVFQKPNPFP-MSIYD--NVAYGPRtHGLRDKKQLD-----KIVEESLKgaaiwdevKDRLKSSAL------GLSGG 154
Cdd:CHL00131 85 GifLAFQYPIEIPgVSNADflRLAYNSK-RKFQGLPELDpleflEIINEKLK--------LVGMDPSFLsrnvneGFSGG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489527602 155 QQQRICIARAIAMRPEVILMDEPTSALDpISTLK-VEELIEDLK-KDYTIVIVTH 207
Cdd:CHL00131 156 EKKRNEILQMALLDSELAILDETDSGLD-IDALKiIAEGINKLMtSENSIILITH 209
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
19-215 |
1.85e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 60.91 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 19 GDKQALKKINMDIKENKVTALIGPSGCGKSTFIRtlnrmndliedvtikgniSVDGEDIYTSDDVINLRTKVGMVFQKPN 98
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLIS------------------AMLGELPPRSDASVVIRGTVAYVPQVSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 99 PFPMSIYDNVAYGPRTHGLRDKKQLDKIVE----ESLKGAAIwDEVKDRlkssALGLSGGQQQRICIARAIAMRPEVILM 174
Cdd:PLN03130 690 IFNATVRDNILFGSPFDPERYERAIDVTALqhdlDLLPGGDL-TEIGER----GVNISGGQKQRVSMARAVYSNSDVYIF 764
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489527602 175 DEPTSALDPISTLKV-EELIEDLKKDYTIVIVT---HNMQQAARI 215
Cdd:PLN03130 765 DDPLSALDAHVGRQVfDKCIKDELRGKTRVLVTnqlHFLSQVDRI 809
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
18-249 |
1.90e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.33 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 18 YGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNrmndlieDV----TIKGNISVDGEDIYTSDDVINLRTKVGMV 93
Cdd:PRK13549 15 FGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLS-------GVyphgTYEGEIIFEGEELQASNIRDTERAGIAII 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 94 FQKPNPFP-MSIYDNVAYG--PRTHGLRDKKQLDKIVEESLKGAAIwdEVKDRLKSSALGlsGGQQQRICIARAIAMRPE 170
Cdd:PRK13549 88 HQELALVKeLSVLENIFLGneITPGGIMDYDAMYLRAQKLLAQLKL--DINPATPVGNLG--LGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 171 VILMDEPTSALDPISTLKVEELIEDLK-KDYTIVIVTHNMQQAARISDETAfflngeVIEfsDTKTMFTTPVDKRTEDYI 249
Cdd:PRK13549 164 LLILDEPTASLTESETAVLLDIIRDLKaHGIACIYISHKLNEVKAISDTIC------VIR--DGRHIGTRPAAGMTEDDI 235
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-237 |
4.26e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.60 E-value: 4.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 20 DKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNrmndliedvtikgnisvdGEDIYTSDDVINLRTKVGMVFQKPNP 99
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAML------------------GELSHAETSSVVIRGSVAYVPQVSWI 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 100 FPMSIYDNVAYGPRTHGLRDKKQLD-KIVEESLKGAAIWD--EVKDRlkssALGLSGGQQQRICIARAIAMRPEVILMDE 176
Cdd:PLN03232 691 FNATVRENILFGSDFESERYWRAIDvTALQHDLDLLPGRDltEIGER----GVNISGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489527602 177 PTSALDPISTLKV-EELIEDLKKDYTIVIVT---HNMQQAARI--SDETAFFLNGEVIEFSDTKTMF 237
Cdd:PLN03232 767 PLSALDAHVAHQVfDSCMKDELKGKTRVLVTnqlHFLPLMDRIilVSEGMIKEEGTFAELSKSGSLF 833
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-228 |
4.38e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.25 E-value: 4.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 22 QALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLieDVtikGNISVDGEDIYTSDDVINLRTKVGMVFQKPNPFP 101
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTR--DA---GSILYLGKEVTFNGPKSSQEAGIGIIHQELNLIP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 102 -MSIYDNVAYGPRTHGLRDKKQLDKIVEESlkgaaiwDEVKDRLK---SS--ALG-LSGGQQQRICIARAIAMRPEVILM 174
Cdd:PRK10762 93 qLTIAENIFLGREFVNRFGRIDWKKMYAEA-------DKLLARLNlrfSSdkLVGeLSIGEQQMVEIAKVLSFESKVIIM 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489527602 175 DEPTSALDPISTLKVEELIEDLK-KDYTIVIVTHNMQQAARISDETAFFLNGEVI 228
Cdd:PRK10762 166 DEPTDALTDTETESLFRVIRELKsQGRGIVYISHRLKEIFEICDDVTVFRDGQFI 220
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-209 |
8.42e-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: 58.64 E-value: 8.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 32 KENKVTALIGPSGCGKSTFIRTLNrmNDLIEDVtikGNISVDGEdiytSDDVINL--RTKVGMVFQKpnpfpmsIYDN-- 107
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILS--GELKPNL---GDYDEEPS----WDEVLKRfrGTELQDYFKK-------LANGei 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 108 -VAYGPrthglrdkKQLDKI-------VEESLKGA---AIWDEVKDRLKSSAL------GLSGGQQQRICIARAIAMRPE 170
Cdd:COG1245 161 kVAHKP--------QYVDLIpkvfkgtVRELLEKVderGKLDELAEKLGLENIldrdisELSGGELQRVAIAAALLRDAD 232
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489527602 171 VILMDEPTSALDPISTLKVEELIEDL-KKDYTIVIVTHNM 209
Cdd:COG1245 233 FYFFDEPSSYLDIYQRLNVARLIRELaEEGKYVLVVEHDL 272
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
151-235 |
1.62e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.43 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 151 LSGGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDL-KKDYTIVIVTHNMQQAARISDETAFFLNGEVIE 229
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEMPELLGITDRILVMSNGLVAG 471
|
....*.
gi 489527602 230 FSDTKT 235
Cdd:PRK10982 472 IVDTKT 477
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
26-206 |
1.91e-09 |
|
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: 57.45 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 26 KINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIEDVTIK---GNISVDGEDIYTSddVINLRTKVgmvfqkpnPFPM 102
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKpakGKLFYVPQRPYMT--LGTLRDQI--------IYPD 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 103 SIYDNvaygpRTHGLRDKK--------QLDKIVEESLKGAAI--WDEVkdrlkssalgLSGGQQQRICIARAIAMRPEVI 172
Cdd:TIGR00954 540 SSEDM-----KRRGLSDKDleqildnvQLTHILEREGGWSAVqdWMDV----------LSGGEKQRIAMARLFYHKPQFA 604
|
170 180 190
....*....|....*....|....*....|....
gi 489527602 173 LMDEPTSALDPistlKVEELIEDLKKDYTIVIVT 206
Cdd:TIGR00954 605 ILDECTSAVSV----DVEGYMYRLCREFGITLFS 634
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
39-238 |
2.39e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.29 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 39 LIGPSGCGKSTFIRTLNRMNDLIedvtiKGNISVDGEDIyTSDDVINLRTKVGMVFQKPNPFPMSIYDNvaygprthglr 118
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELE-----KGRIMIDDCDV-AKFGLTDLRRVLSIIPQSPVLFSGTVRFN----------- 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 119 dkkqLDKIVEESlkGAAIWD-----EVKDRLKSSALGL-----------SGGQQQRICIARAIAMRPEVILMDEPTSALD 182
Cdd:PLN03232 1330 ----IDPFSEHN--DADLWEaleraHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489527602 183 PISTLKVEELIEDLKKDYTIVIVTHNMQQAARiSDETAFFLNGEVIEFSDTKTMFT 238
Cdd:PLN03232 1404 VRTDSLIQRTIREEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLS 1458
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-214 |
3.04e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.10 E-value: 3.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 24 LKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDliedvTIKGNISVDGEDIyTSDDVINLRTKVGMVFQKPNPFPMS 103
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVE-----VCGGEIRVNGREI-GAYGLRELRRQFSMIPQDPVLFDGT 1399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 104 IYDNVaygprthglrdkkqlDKIVEESlkGAAIWDEV-----KDRLKSSALGL-----------SGGQQQRICIARAIAM 167
Cdd:PTZ00243 1400 VRQNV---------------DPFLEAS--SAEVWAALelvglRERVASESEGIdsrvleggsnySVGQRQLMCMARALLK 1462
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489527602 168 RPE-VILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTHNMQQAAR 214
Cdd:PTZ00243 1463 KGSgFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQ 1510
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-222 |
4.09e-09 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 55.49 E-value: 4.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 30 DIKENKVTALIGPSGCGKSTFIRTLnrmndliedvtiKGNISVDGEDIYTSDDVINLRTkvgmvfQKPNP-FPMSIYDNV 108
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKML------------AGVLKPDEGDIEIELDTVSYKP------QYIKAdYEGTVRDLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 109 AYGPRTHG--------LRDKKQLDKIVEEslkgaaiwdEVKDrlkssalgLSGGQQQRICIARAIAMRPEVILMDEPTSA 180
Cdd:cd03237 83 SSITKDFYthpyfkteIAKPLQIEQILDR---------EVPE--------LSGGELQRVAIAACLSKDADIYLLDEPSAY 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489527602 181 LDPISTLKVEELIED--LKKDYTIVIVTHNMQQAARISDETAFF 222
Cdd:cd03237 146 LDVEQRLMASKVIRRfaENNEKTAFVVEHDIIMIDYLADRLIVF 189
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
24-187 |
6.96e-09 |
|
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: 54.19 E-value: 6.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 24 LKKINMDIKENKVTALIGPSGCGKSTFIRTLNrmNDLIEDVTIKGNISVDGEDIYtsddvinlrtkvgmvfQKPNPFPMS 103
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALA--NRTEGNVSVEGDIHYNGIPYK----------------EFAEKYPGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 104 IYDNVAygprthglRDKKQLDKIVEESLKGAAiwdevkdRLKSSAL--GLSGGQQQRICIARAIAMRPEVILMDEPTSAL 181
Cdd:cd03233 85 IIYVSE--------EDVHFPTLTVRETLDFAL-------RCKGNEFvrGISGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
....*.
gi 489527602 182 DPISTL 187
Cdd:cd03233 150 DSSTAL 155
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-210 |
7.30e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.73 E-value: 7.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 6 KIKMSVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLnrMNDLIEDvtiKGNISVDgediytsddvin 85
Cdd:PRK11147 317 KIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLM--LGQLQAD---SGRIHCG------------ 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 86 lrTKVgmvfqkpnpfpmsiydNVAYGPRThglRDKKQLDKIVEESLKGAAIWDEVKDRlKSSALG--------------- 150
Cdd:PRK11147 380 --TKL----------------EVAYFDQH---RAELDPEKTVMDNLAEGKQEVMVNGR-PRHVLGylqdflfhpkramtp 437
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489527602 151 ---LSGGQQQRICIARaIAMRP-EVILMDEPTSALDpISTLkveELIEDLKKDY--TIVIVTHNMQ 210
Cdd:PRK11147 438 vkaLSGGERNRLLLAR-LFLKPsNLLILDEPTNDLD-VETL---ELLEELLDSYqgTVLLVSHDRQ 498
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-236 |
9.41e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.18 E-value: 9.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 20 DKQALKKINMDIKENKVTALIGPSGCGKSTFirtlnrMNDLI-EDVTIKGNISVDGEDIYTSDDVINLrtKVGMVFQKPN 98
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTEL------MNCLFgVDKRAGGEIRLNGKDISPRSPLDAV--KKGMAYITES 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 99 P-----FP-MSIYDNVAYGPR--------THGLRDKKQLDKIVEE-----SLKGAAIWDEVKDrlkssalgLSGGQQQRI 159
Cdd:PRK09700 347 RrdngfFPnFSIAQNMAISRSlkdggykgAMGLFHEVDEQRTAENqrellALKCHSVNQNITE--------LSGGNQQKV 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489527602 160 CIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKD-YTIVIVTHNMQQAARISDETAFFLNGEVIE-FSDTKTM 236
Cdd:PRK09700 419 LISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVFCEGRLTQiLTNRDDM 497
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
35-215 |
1.74e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 54.50 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 35 KVTALIGPSGCGKSTFirtLNRMNDLIEDVTIKGNISVDGEDIYTSddvinLRTKVGMVFQKPNPFP-MSIYDNVAYgpr 113
Cdd:PLN03211 95 EILAVLGPSGSGKSTL---LNALAGRIQGNNFTGTILANNRKPTKQ-----ILKRTGFVTQDDILYPhLTVRETLVF--- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 114 THGLRDKKQLDKIVEESLKGAAIWDEVKDRLKSSAL------GLSGGQQQRICIARAIAMRPEVILMDEPTSALDPISTL 187
Cdd:PLN03211 164 CSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIgnsfirGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAY 243
|
170 180
....*....|....*....|....*....
gi 489527602 188 K-VEELIEDLKKDYTIVIVTHnmQQAARI 215
Cdd:PLN03211 244 RlVLTLGSLAQKGKTIVTSMH--QPSSRV 270
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-207 |
2.34e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 54.36 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 24 LKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIedvtiKGNISVDGEDIyTSDDVINLRTKVGMVFQKPNPFPMS 103
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELE-----RGRILIDGCDI-SKFGLMDLRKVLGIIPQAPVLFSGT 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 104 IYDNvaygprthglrdkkqLDKIVEESlkGAAIWD-----EVKDRLKSSALGL-----------SGGQQQRICIARAIAM 167
Cdd:PLN03130 1329 VRFN---------------LDPFNEHN--DADLWEsleraHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLR 1391
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489527602 168 RPEVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIVTH 207
Cdd:PLN03130 1392 RSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAH 1431
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
10-182 |
2.92e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.88 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLF-YGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMndlieDVTIKGNISVDGEDI--YTSDDVINL 86
Cdd:COG3845 259 EVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGL-----RPPASGSIRLDGEDItgLSPRERRRL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 87 --------RTKVGMVfqkPNpfpMSIYDNVA----YGPR--THGLRDKKQL----DKIVEE-SLKGAAIWDEVKdrlkss 147
Cdd:COG3845 334 gvayipedRLGRGLV---PD---MSVAENLIlgryRRPPfsRGGFLDRKAIrafaEELIEEfDVRTPGPDTPAR------ 401
|
170 180 190
....*....|....*....|....*....|....*
gi 489527602 148 alGLSGGQQQRICIARAIAMRPEVILMDEPTSALD 182
Cdd:COG3845 402 --SLSGGNQQKVILARELSRDPKLLIAAQPTRGLD 434
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
2-226 |
3.31e-08 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 52.94 E-value: 3.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 2 ELIDKIKMSVKDLDLFYGDKQA------------LKKINMDIKENKVTALIGPSGCGKSTFIRTLnrmndLIEDVTIKGN 69
Cdd:cd03291 19 ELLEKAKQENNDRKHSSDDNNLffsnlclvgapvLKNINLKIEKGEMLAITGSTGSGKTSLLMLI-----LGELEPSEGK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 70 ISVDGEDIYTSddvinlrtkvgmvfQKPNPFPMSIYDNVAYGPRTHGLRDKKQLDKI-VEESLkgAAIWDEVKDRLKSSA 148
Cdd:cd03291 94 IKHSGRISFSS--------------QFSWIMPGTIKENIIFGVSYDEYRYKSVVKACqLEEDI--TKFPEKDNTVLGEGG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489527602 149 LGLSGGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKV-EELIEDLKKDYTIVIVTHNMQQaARISDETAFFLNGE 226
Cdd:cd03291 158 ITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEH-LKKADKILILHEGS 235
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-225 |
4.10e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 53.76 E-value: 4.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 2 ELIDKIK-------MSVKDLDLFYGD-----KQALKKINMDIKENKVTALIGPSGCGKSTFIrtlnrMNDLIEDVTIKGN 69
Cdd:TIGR01271 408 ELFEKIKqnnkarkQPNGDDGLFFSNfslyvTPVLKNISFKLEKGQLLAVAGSTGSGKSSLL-----MMIMGELEPSEGK 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 70 ISVDGEDIYTSddvinlrtkvgmvfQKPNPFPMSIYDNVAYGPRTHGLRDKKQLDKI-VEESLkgAAIWDEVKDRLKSSA 148
Cdd:TIGR01271 483 IKHSGRISFSP--------------QTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACqLEEDI--ALFPEKDKTVLGEGG 546
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489527602 149 LGLSGGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKV-EELIEDLKKDYTIVIVTHNMQQAARiSDETAFFLNG 225
Cdd:TIGR01271 547 ITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-205 |
5.61e-08 |
|
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: 52.37 E-value: 5.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 32 KENKVTALIGPSGCGKSTFIRTLNRmndliedvTIKGNI-SVDGEDIYtsDDVIN-------------LR-------TKV 90
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAG--------KLKPNLgKFDDPPDW--DEILDefrgselqnyftkLLegdvkviVKP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 91 GMVFQKPNPFPMSIYDNVAygpRTHglrDKKQLDKIVEE-SLKGaaiwdeVKDRLKSSalgLSGGQQQRICIARAIAMRP 169
Cdd:cd03236 94 QYVDLIPKAVKGKVGELLK---KKD---ERGKLDELVDQlELRH------VLDRNIDQ---LSGGELQRVAIAAALARDA 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 489527602 170 EVILMDEPTSALDPISTLKVEELIEDLKKDYTIVIV 205
Cdd:cd03236 159 DFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLV 194
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-233 |
9.97e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 52.36 E-value: 9.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 24 LKKINMDIKENKVTALIGPSGCGKSTFIRtlnrmndLIEDVTI--KGNISVDGEDIYTSDDVINLRTKVGMVFQKPNPFP 101
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMK-------IIAGIVPpdSGTLEIGGNPCARLTPAKAHQLGIYLVPQEPLLFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 102 -MSIYDNVAYG-PRTHGLRDK-KQLDKIVEESLKgaaiwdevkdrLKSSALGLSGGQQQRICIARAIAMRPEVILMDEPT 178
Cdd:PRK15439 100 nLSVKENILFGlPKRQASMQKmKQLLAALGCQLD-----------LDSSAGSLEVADRQIVEILRGLMRDSRILILDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489527602 179 SALDPIST----LKVEELiedLKKDYTIVIVTHNM----QQAARIS--DETAFFLNGEVIEFSDT 233
Cdd:PRK15439 169 ASLTPAETerlfSRIREL---LAQGVGIVFISHKLpeirQLADRISvmRDGTIALSGKTADLSTD 230
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
151-217 |
1.15e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.93 E-value: 1.15e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489527602 151 LSGGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKD-YTIVIVTHNMQQAARISD 217
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEgLSIILVSSEMPEVLGMSD 463
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
147-228 |
1.28e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 51.66 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 147 SALGLSGGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKD-YTIVIVTHNMQQAARISDETAFFLNG 225
Cdd:NF000106 141 AAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEEAEQLAHELTVIDRG 220
|
...
gi 489527602 226 EVI 228
Cdd:NF000106 221 RVI 223
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
11-233 |
1.85e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.43 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 11 VKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLnrMNDLIEDV-TIK-------GNISVDGEDIYTSDd 82
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL--VGELEPDSgTVKwsenaniGYYAQDHAYDFEND- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 83 vinlrtkvgmvfqkpnpfpMSIYDNVAYgprthgLRDKKQLDKIVEESLkGAAIWDEvkDRLKSSALGLSGGQQQRICIA 162
Cdd:PRK15064 399 -------------------LTLFDWMSQ------WRQEGDDEQAVRGTL-GRLLFSQ--DDIKKSVKVLSGGEKGRMLFG 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 163 RAIAMRPEVILMDEPTSALDpistlkvEELIEDLK---KDY--TIVIVTHNMQ----QAARISDETAfflnGEVIEFSDT 233
Cdd:PRK15064 451 KLMMQKPNVLVMDEPTNHMD-------MESIESLNmalEKYegTLIFVSHDREfvssLATRIIEITP----DGVVDFSGT 519
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
10-214 |
1.92e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.66 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 10 SVKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIrtlnrmnDLIEDVTI--KGNISVDGEDIYTSDDvinlR 87
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLL-------SLIAGARKiqQGRVEVLGGDMADARH----R 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 88 TKVG-----MvfqkP-----NPFP-MSIYDNVAYGPRTHGLrDKKQLDKIVEESLKGAAIwDEVKDRLkssALGLSGGQQ 156
Cdd:NF033858 72 RAVCpriayM----PqglgkNLYPtLSVFENLDFFGRLFGQ-DAAERRRRIDELLRATGL-APFADRP---AGKLSGGMK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527602 157 QRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKD---YTIVIVTHNMQQAAR 214
Cdd:NF033858 143 QKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpgMSVLVATAYMEEAER 203
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-243 |
2.44e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 51.32 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 21 KQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDL-------------------IEDVTIKGNI-SVDGEDIYTS 80
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEIsegrvwaersiayvpqqawIMNATVRGNIlFFDEEDAARL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 81 DDVInlrtkvgmvfqkpnpfpmsiydnvaygpRTHGLR-DKKQLdkiveeslkGAAIWDEVKDRlkssALGLSGGQQQRI 159
Cdd:PTZ00243 753 ADAV----------------------------RVSQLEaDLAQL---------GGGLETEIGEK----GVNLSGGQKARV 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 160 CIARAIAMRPEVILMDEPTSALDP-ISTLKVEELIEDLKKDYTIVIVTHNMQQAARISDETAffLNGEVIEFS-DTKTMF 237
Cdd:PTZ00243 792 SLARAVYANRDVYLLDDPLSALDAhVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVA--LGDGRVEFSgSSADFM 869
|
....*.
gi 489527602 238 TTPVDK 243
Cdd:PTZ00243 870 RTSLYA 875
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
23-217 |
4.08e-07 |
|
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: 48.86 E-value: 4.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 23 ALKKINMDIKENKVTALIGPSGCGKSTFIrtlnrmNDLIEDVtikgnisvdGEDIYTSDDVINLRTKVGMVfqkpnpfpm 102
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLV------NEGLYAS---------GKARLISFLPKFSRNKLIFI--------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 103 siydnvaygprthglrdkKQLDKIVEESLKGAaiwdevkdRLKSSALGLSGGQQQRICIARAIAMRPE--VILMDEPTSA 180
Cdd:cd03238 66 ------------------DQLQFLIDVGLGYL--------TLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTG 119
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489527602 181 LDPISTLKVEELIEDL-KKDYTIVIVTHN---MQQAARISD 217
Cdd:cd03238 120 LHQQDINQLLEVIKGLiDLGNTVILIEHNldvLSSADWIID 160
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
36-228 |
4.63e-07 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 49.45 E-value: 4.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 36 VTALIGPSGCGKSTFirtLNRMNDLIEDvtiKGNISVDGEDI--YTSDDVINLRTKVGMvfQKPNPFPMSIYDNVA-YGP 112
Cdd:COG4138 24 LIHLIGPNGAGKSTL---LARMAGLLPG---QGEILLNGRPLsdWSAAELARHRAYLSQ--QQSPPFAMPVFQYLAlHQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 113 rtHGLRDKKQLDKIVE--ESLKgaaiwdeVKDRLKSSALGLSGGQQQRICIARAI-----AMRPE--VILMDEPTSALDP 183
Cdd:COG4138 96 --AGASSEAVEQLLAQlaEALG-------LEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPMNSLDV 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489527602 184 ISTLKVEELIEDLK-KDYTIVIVTHNMQQAARISDETAFFLNGEVI 228
Cdd:COG4138 167 AQQAALDRLLRELCqQGITVVMSSHDLNHTLRHADRVWLLKQGKLV 212
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
139-216 |
6.11e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.12 E-value: 6.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 139 EVKDRLkSSALGLsgGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDL--KKDYTIVIVTHNMQQAA--- 213
Cdd:NF033858 389 DVADAL-PDSLPL--GIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELsrEDGVTIFISTHFMNEAErcd 465
|
...
gi 489527602 214 RIS 216
Cdd:NF033858 466 RIS 468
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
38-207 |
8.25e-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: 48.12 E-value: 8.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 38 ALIGPSGCGKSTFIRTLNRMndLIEDvtiKGNISVDGEDIYTSDDvinLRTKV--------GMvfqKPNpfpMSIYDNVA 109
Cdd:TIGR01189 30 QVTGPNGIGKTTLLRILAGL--LRPD---SGEVRWNGTPLAEQRD---EPHENilylghlpGL---KPE---LSALENLH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 110 YGPRTHGLRDKKQLDKIVEESLKGAAiwdevkDRLkssALGLSGGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKV 189
Cdd:TIGR01189 96 FWAAIHGGAQRTIEDALAAVGLTGFE------DLP---AAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALL 166
|
170
....*....|....*....
gi 489527602 190 EELIED-LKKDYTIVIVTH 207
Cdd:TIGR01189 167 AGLLRAhLARGGIVLLTTH 185
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-249 |
1.03e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.02 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 17 FYGDKqALKKINMDIKENKVTALIGPSGCGKSTFIRTLNrmndlieDV----TIKGNISVDGEDIYTSDdvINLRTKVGM 92
Cdd:NF040905 11 FPGVK-ALDDVNLSVREGEIHALCGENGAGKSTLMKVLS-------GVyphgSYEGEILFDGEVCRFKD--IRDSEALGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 93 VF--QKPNPFP-MSIYDNVAYG--PRTHGLRDKKQLDKIVEESLKGAAIwDEVKDRLKSSaLGLsgGQQQRICIARAIAM 167
Cdd:NF040905 81 VIihQELALIPyLSIAENIFLGneRAKRGVIDWNETNRRARELLAKVGL-DESPDTLVTD-IGV--GKQQLVEIAKALSK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 168 RPEVILMDEPTSALDPISTLKVEELIEDLK-KDYTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTKTmfttpvDKRTE 246
Cdd:NF040905 157 DVKLLILDEPTAALNEEDSAALLDLLLELKaQGITSIIISHKLNEIRRVADSITVLRDGRTIETLDCRA------DEVTE 230
|
...
gi 489527602 247 DYI 249
Cdd:NF040905 231 DRI 233
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
19-207 |
2.05e-06 |
|
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: 48.39 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 19 GDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLnrmndliedvtikgnISVDGEdiYTSDDVINLRTKVGMVFQKPN 98
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM---------------AGVDKD--FNGEARPQPGIKVGYLPQEPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 99 PFP-MSIYDNVAygprtHGLRDKKQL------------------DKIVEESLKGAAI------WD-EVKDRLKSSAL--- 149
Cdd:TIGR03719 79 LDPtKTVRENVE-----EGVAEIKDAldrfneisakyaepdadfDKLAAEQAELQEIidaadaWDlDSQLEIAMDALrcp 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489527602 150 -------GLSGGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKKdyTIVIVTH 207
Cdd:TIGR03719 154 pwdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG--TVVAVTH 216
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
34-209 |
2.35e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 46.21 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 34 NKVTALIGPSGCGKSTFIRTLNRmndlIEDVTIKGNISVDGEDIYTSDDVINLRTKVGmvfqkpnpfpmsiydnvaygpr 113
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALAR----ELGPPGGGVIYIDGEDILEEVLDQLLLIIVG---------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 114 thglrdkkqldkiveeslkgaaiwdevkdrlkSSALGLSGGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELI 193
Cdd:smart00382 56 --------------------------------GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLE 103
|
170 180
....*....|....*....|..
gi 489527602 194 ED------LKKDYTIVIVTHNM 209
Cdd:smart00382 104 ELrlllllKSEKNLTVILTTND 125
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
39-182 |
2.64e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 47.23 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 39 LIGPSGCGKSTFirtLNRMNDLIEDvtiKGNISVDGEDIYTSDDVINLRTKVGMVFQKPNPFPMSIYDNVA-YGP-RTHG 116
Cdd:PRK03695 27 LVGPNGAGKSTL---LARMAGLLPG---SGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYLTlHQPdKTRT 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489527602 117 LRDKKQLDKIVeESLKgaaiwdeVKDRLKSSALGLSGGQQQRICIARAI-----AMRPE--VILMDEPTSALD 182
Cdd:PRK03695 101 EAVASALNEVA-EALG-------LDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLLDEPMNSLD 165
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
25-227 |
2.77e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 47.74 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 25 KKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDliedvTIKGNISVDGEDIytSDDVINLRTKVGMVF-----QKPNP 99
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRP-----ARGGRIMLNGKEI--NALSTAQRLARGLVYlpedrQSSGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 100 F-PMSIYDNV---AYGPRTHGLRDKKQlDKIVEESLKGAAIWDEVKDRlksSALGLSGGQQQRICIARAIAMRPEVILMD 175
Cdd:PRK15439 353 YlDAPLAWNVcalTHNRRGFWIKPARE-NAVLERYRRALNIKFNHAEQ---AARTLSGGNQQKVLIAKCLEASPQLLIVD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489527602 176 EPTSALDPISTLKVEELIEDLKKDYTIVI-VTHNMQQAARISDETAFFLNGEV 227
Cdd:PRK15439 429 EPTRGVDVSARNDIYQLIRSIAAQNVAVLfISSDLEEIEQMADRVLVMHQGEI 481
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
23-225 |
3.63e-06 |
|
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: 47.70 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 23 ALKKINMDIKENKVTALIGPSGCGKSTFIRTLNrmndliEDVTI-KGNISVDGEDIYTSddVINLRTKVGMVFQkpnpfp 101
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLT------GDTTVtSGDATVAGKSILTN--ISDVHQNMGYCPQ------ 2019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 102 MSIYDNVAYGpRTH-----GLRD--KKQLDKIVEESLK--GAAIWdevKDRLKSSalgLSGGQQQRICIARAIAMRPEVI 172
Cdd:TIGR01257 2020 FDAIDDLLTG-REHlylyaRLRGvpAEEIEKVANWSIQslGLSLY---ADRLAGT---YSGGNKRKLSTAIALIGCPPLV 2092
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489527602 173 LMDEPTSALDPISTLKV-EELIEDLKKDYTIVIVTHNMQQAARISDETAFFLNG 225
Cdd:TIGR01257 2093 LLDEPTTGMDPQARRMLwNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
21-221 |
6.00e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.03 E-value: 6.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 21 KQALKKINMDIKENKVTALIGPSGCGKSTFIRTLNRMNDLIeDVTIKGNISVDG---EDI---YTSDDVINLRTKV---- 90
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGF-HIGVEGVITYDGitpEEIkkhYRGDVVYNAETDVhfph 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 91 -----GMVF----QKPNPFPMSI----YDN--VAYGPRTHGL---RDKKQLDKIVEeslkgaaiwdevkdrlkssalGLS 152
Cdd:TIGR00956 153 ltvgeTLDFaarcKTPQNRPDGVsreeYAKhiADVYMATYGLshtRNTKVGNDFVR---------------------GVS 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489527602 153 GGQQQRICIARAIAMRPEVILMDEPTSALDPISTLkveELIEDLKkdytivivthnmqQAARISDETAF 221
Cdd:TIGR00956 212 GGERKRVSIAEASLGGAKIQCWDNATRGLDSATAL---EFIRALK-------------TSANILDTTPL 264
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
120-227 |
6.57e-06 |
|
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: 46.74 E-value: 6.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 120 KKQLDKIVEESLKGAAIwDEVKDRLKSSAL---GLSGGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDL 196
Cdd:TIGR02633 371 KMRIDAAAELQIIGSAI-QRLKVKTASPFLpigRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQL 449
|
90 100 110
....*....|....*....|....*....|..
gi 489527602 197 -KKDYTIVIVTHNMQQAARISDETAFFLNGEV 227
Cdd:TIGR02633 450 aQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
8-183 |
6.74e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 46.89 E-value: 6.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 8 KMSVKDLDLFYGDKQ-ALKKINMDIKENKVTALIGPSGCGKSTFIRTLnrmNDLIEDVtiKGNISVDGEDIyTSDDVINL 86
Cdd:PRK10522 322 TLELRNVTFAYQDNGfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLL---TGLYQPQ--SGEILLDGKPV-TAEQPEDY 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 87 RTKVGMVFQKPNPFpmsiydnvaygprTHGLRDKKQ--LDKIVEESLKGAAIWDEVK-DRLKSSALGLSGGQQQRICIAR 163
Cdd:PRK10522 396 RKLFSAVFTDFHLF-------------DQLLGPEGKpaNPALVEKWLERLKMAHKLElEDGRISNLKLSKGQKKRLALLL 462
|
170 180
....*....|....*....|
gi 489527602 164 AIAMRPEVILMDEPTSALDP 183
Cdd:PRK10522 463 ALAEERDILLLDEWAADQDP 482
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
152-207 |
7.62e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 7.62e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 489527602 152 SGGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIedLKKDYTIVIVTH 207
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSH 399
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
137-222 |
7.66e-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: 45.26 E-value: 7.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 137 WDEVKDRLKSSALGLSGGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDL--KKDYTIVIVTHNMQQAAR 214
Cdd:cd03222 58 WDGITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseEGKKTALVVEHDLAVLDY 137
|
....*...
gi 489527602 215 ISDETAFF 222
Cdd:cd03222 138 LSDRIHVF 145
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
24-217 |
7.94e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 45.71 E-value: 7.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 24 LKKINMDIKENKVTALIGPSGCGKST--------------------FIRT-LNRMN----DLIEDVTIKgnISVDGEDIY 78
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSlafdtiyaegqrryveslsaYARQfLGQMDkpdvDSIEGLSPA--IAIDQKTTS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 79 TsddviNLRTKVGMVfqkpnpfpMSIYDNVAYGPRTHGLRDK-KQLDKIVEESLkgaaiwdevkdRLKSSALGLSGGQQQ 157
Cdd:cd03270 89 R-----NPRSTVGTV--------TEIYDYLRLLFARVGIRERlGFLVDVGLGYL-----------TLSRSAPTLSGGEAQ 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489527602 158 RICIARAIAMRPEVIL--MDEPTSALDPISTLKVEELIEDLK-KDYTIVIVTHN---MQQAARISD 217
Cdd:cd03270 145 RIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRdLGNTVLVVEHDedtIRAADHVID 210
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
11-207 |
1.76e-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: 45.31 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 11 VKDLDLFYGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTlnrmndliedvtIKGNISVDGEDIYTSDDVinlrtKV 90
Cdd:TIGR03719 325 AENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRM------------ITGQEQPDSGTIEIGETV-----KL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 91 GMVFQK-----PNPfpmSIYDNVAYGprthglRDKKQLDKIVEES--------LKGAAIWDEVKDrlkssalgLSGGQQQ 157
Cdd:TIGR03719 388 AYVDQSrdaldPNK---TVWEEISGG------LDIIKLGKREIPSrayvgrfnFKGSDQQKKVGQ--------LSGGERN 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489527602 158 RICIARAIAMRPEVILMDEPTSALDpISTLK-VEELIEDLKKdyTIVIVTH 207
Cdd:TIGR03719 451 RVHLAKTLKSGGNVLLLDEPTNDLD-VETLRaLEEALLNFAG--CAVVISH 498
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
23-232 |
1.90e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.81 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 23 ALKKINMDIKENKVTALIGPSGCGKStfirTLNRMndliedvtIKGNISVDGEDIYTSDDVINLRTKVGMVFQkpnpfpM 102
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKS----TLSNI--------IGGSLSPTVGKVDRNGEVSVIAISAGLSGQ------L 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 103 SIYDNVAYGPRTHGLRD---KKQLDKIVEESLKGAAIWDEVKDrlkssalgLSGGQQQRICIARAIAMRPEVILMDEPTS 179
Cdd:PRK13546 101 TGIENIEFKMLCMGFKRkeiKAMTPKIIEFSELGEFIYQPVKK--------YSSGMRAKLGFSINITVNPDILVIDEALS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489527602 180 ALDPISTLKVEELIEDLK-KDYTIVIVTHNMQQAARISDETAFFLNGEVIEFSD 232
Cdd:PRK13546 173 VGDQTFAQKCLDKIYEFKeQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGE 226
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
31-217 |
2.77e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.80 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 31 IKENKVTALIGPSGCGKSTFIRTLnrmndliedvtiKGNISVDGEDIYTSDDVI----NLRTKVGMVFQKpnpFPMSIYD 106
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLL------------AGVLKPDEGEVDPELKISykpqYIKPDYDGTVED---LLRSITD 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 107 NVAYGPRTHGLRDKKQLDKIVEESLKGaaiwdevkdrlkssalgLSGGQQQRICIARAIAMRPEVILMDEPTSALDpist 186
Cdd:PRK13409 427 DLGSSYYKSEIIKPLQLERLLDKNVKD-----------------LSGGELQRVAIAACLSRDADLYLLDEPSAHLD---- 485
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489527602 187 lkVEE----------LIEdlKKDYTIVIVTHNMQQAARISD 217
Cdd:PRK13409 486 --VEQrlavakairrIAE--EREATALVVDHDIYMIDYISD 522
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
150-226 |
3.58e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 44.62 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 150 GLSGGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDL--KKDYTIVIVTHNMQQAAR-ISDETAFFLNGE 226
Cdd:PRK10938 401 SLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLisEGETQLLFVSHHAEDAPAcITHRLEFVPDGD 480
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
39-207 |
3.78e-05 |
|
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: 43.25 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 39 LIGPSGCGKSTFIRTLNRMNDLIEdvtikGNISVDGEdiytsddvinlrtkvGMVFQKPnpfpmSIYDNVAYGPRTHGLr 118
Cdd:cd03231 31 VTGPNGSGKTTLLRILAGLSPPLA-----GRVLLNGG---------------PLDFQRD-----SIARGLLYLGHAPGI- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 119 dKKQLDkiVEESLK-------GAAIWDEVkDRLKSSALG------LSGGQQQRICIARAIAMRPEVILMDEPTSALDPIS 185
Cdd:cd03231 85 -KTTLS--VLENLRfwhadhsDEQVEEAL-ARVGLNGFEdrpvaqLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
170 180
....*....|....*....|...
gi 489527602 186 TLKVEELI-EDLKKDYTIVIVTH 207
Cdd:cd03231 161 VARFAEAMaGHCARGGMVVLTTH 183
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
4-234 |
3.97e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.50 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 4 IDKIKmsvkdlDLFYGDKQ-----ALKKINMDIKENKVTALIGPSGCGKSTfirtlnrMNDLIEDVTI--KGNIsvdgeD 76
Cdd:PRK13545 21 FDKLK------DLFFRSKDgeyhyALNNISFEVPEGEIVGIIGLNGSGKST-------LSNLIAGVTMpnKGTV-----D 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 77 IYTSDDVINLRTkvGMVFQkpnpfpMSIYDNVAYGPRTHGLRdKKQLDKIVEESLKGAAIWDEVKDRLKSsalgLSGGQQ 156
Cdd:PRK13545 83 IKGSAALIAISS--GLNGQ------LTGIENIELKGLMMGLT-KEKIKEIIPEIIEFADIGKFIYQPVKT----YSSGMK 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489527602 157 QRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLK-KDYTIVIVTHNMQQAARISDETAFFLNGEVIEFSDTK 234
Cdd:PRK13545 150 SRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKeQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIK 228
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
103-182 |
4.10e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.13 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 103 SIYDNVAYGPRTHGLRDKKQLDKIVEESLKGAAIWD-EVKDRLKSSALG-LSGGQQQRICIARAIAMRPEVILMDEPTSA 180
Cdd:PRK11288 347 SVADNINISARRHHLRAGCLINNRWEAENADRFIRSlNIKTPSREQLIMnLSGGNQQKAILGRWLSEDMKVILLDEPTRG 426
|
..
gi 489527602 181 LD 182
Cdd:PRK11288 427 ID 428
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
24-209 |
1.07e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 42.60 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 24 LKKINMDIKENKVTALIGPSGCGKSTFI-----RTLNRMNDLiEDVTIKGNISVDG-EDIytsDDVINL------RTkvg 91
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlyPALARRLHL-KKEQPGNHDRIEGlEHI---DKVIVIdqspigRT--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 92 mvfQKPNPFP-MSIYDNV--AYGPRTHGLRDKKQ--------------LDKIVEESLKGAAIWDEVKDRLKS-------- 146
Cdd:cd03271 84 ---PRSNPATyTGVFDEIreLFCEVCKGKRYNREtlevrykgksiadvLDMTVEEALEFFENIPKIARKLQTlcdvglgy 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489527602 147 -----SALGLSGGQQQRICIARAIAMR---PEVILMDEPTSALdpiSTLKVEELIEDL----KKDYTIVIVTHNM 209
Cdd:cd03271 161 iklgqPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGL---HFHDVKKLLEVLqrlvDKGNTVVVIEHNL 232
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
149-214 |
1.49e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.19 E-value: 1.49e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489527602 149 LGLSGGQQQRICIARAIAM-----RPEVILmDEPTSALDPISTLKVEELIED-LKKDYTIVIVTHNMQQAAR 214
Cdd:cd03227 76 LQLSGGEKELSALALILALaslkpRPLYIL-DEIDRGLDPRDGQALAEAILEhLVKGAQVIVITHLPELAEL 146
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
151-207 |
1.58e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.41 E-value: 1.58e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 489527602 151 LSGGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIedlkKDY--TIVIVTH 207
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFL----HDYpgTVVAVTH 218
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
18-248 |
1.71e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.46 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 18 YGDKQALKKINMDIKENKVTALIGPSGCGKSTFIRTLnrmndliedvtiKGNISVDGEDIYTSDDVinlrtKVG------ 91
Cdd:PRK10636 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLL------------AGELAPVSGEIGLAKGI-----KLGyfaqhq 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 92 MVFQKPNPFPMSIYDNVAYGPRTHGLRDKK-----QLDKIVEESLKgaaiwdevkdrlkssalgLSGGQQQRICIARAIA 166
Cdd:PRK10636 385 LEFLRADESPLQHLARLAPQELEQKLRDYLggfgfQGDKVTEETRR------------------FSGGEKARLVLALIVW 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 167 MRPEVILMDEPTSALD-PISTLKVEELIEdlkKDYTIVIVTHNMQQAARISDETAFFLNGEViefsdtktmftTPVDKRT 245
Cdd:PRK10636 447 QRPNLLLLDEPTNHLDlDMRQALTEALID---FEGALVVVSHDRHLLRSTTDDLYLVHDGKV-----------EPFDGDL 512
|
...
gi 489527602 246 EDY 248
Cdd:PRK10636 513 EDY 515
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
22-182 |
1.85e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.53 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 22 QALKKINMDIKENKVTALIGPSGCGKSTFIRTL--NRMNDLIE-DVTIKG---------NIS--VDGEDIYTSddviNLR 87
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEgDIRISGfpkkqetfaRISgyCEQNDIHSP----QVT 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 88 TKVGMVFQkpnpfpmsiydnvAYgprthgLRDKKQLDKivEESLKgaaIWDEVK-----DRLKSSALGLSG------GQQ 156
Cdd:PLN03140 970 VRESLIYS-------------AF------LRLPKEVSK--EEKMM---FVDEVMelvelDNLKDAIVGLPGvtglstEQR 1025
|
170 180
....*....|....*....|....*.
gi 489527602 157 QRICIARAIAMRPEVILMDEPTSALD 182
Cdd:PLN03140 1026 KRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-217 |
2.17e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 42.08 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 30 DIKENKVTALIGPSGCGKSTFIRTLNRM-----NDLIEDVTI--KGN-ISVDGEDiyTSDDVinLRTKVGmvfqkpNPFP 101
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVlkpdeGEVDEDLKIsyKPQyISPDYDG--TVEEF--LRSANT------DDFG 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 102 MSIYdnvaygprTHGLRDKKQLDKIVEESLKGaaiwdevkdrlkssalgLSGGQQQRICIARAIAMRPEVILMDEPTSAL 181
Cdd:COG1245 432 SSYY--------KTEIIKPLGLEKLLDKNVKD-----------------LSGGELQRVAIAACLSRDADLYLLDEPSAHL 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489527602 182 DpistlkVEELIEDLK--------KDYTIVIVTHNMQQAARISD 217
Cdd:COG1245 487 D------VEQRLAVAKairrfaenRGKTAMVVDHDIYLIDYISD 524
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
24-207 |
2.50e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 41.53 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 24 LKKINMDIKENkVTALIGPSGCGKSTFIRTLNRMNDLiedvtiKGNISVDGEDIYTSDDVINLRTKVGMVFQKPnpfPMS 103
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGP------SSSRKFDEEDFYLGDDPDLPEIEIELTFGSL---LSR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 104 IYDNVAYGPRTHGLRDK----------------KQLDKIVEESLKGAAI-----WDEVKDRLKSSALGLSG--------- 153
Cdd:COG3593 84 LLRLLLKEEDKEELEEAleelneelkealkalnELLSEYLKELLDGLDLelelsLDELEDLLKSLSLRIEDgkelpldrl 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489527602 154 --GQQQRICIARAIAM-------RPEVILMDEPTSALDPISTLKVEELIEDL-KKDYTIVIVTH 207
Cdd:COG3593 164 gsGFQRLILLALLSALaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELsEKPNQVIITTH 227
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
151-249 |
2.64e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 2.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 151 LSGGQQQRICIARAIAMRPEVI--LMDEPTSALDPISTLKVEELIEDLK-KDYTIVIVTHNMQQ---AARISD--ETAFF 222
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRdQGNTVLLVEHDEQMislADRIIDigPGAGI 556
|
90 100
....*....|....*....|....*..
gi 489527602 223 LNGEVIeFSDTKTMFTTPVDKRTEDYI 249
Cdd:PRK00635 557 FGGEVL-FNGSPREFLAKSDSLTAKYL 582
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
36-207 |
3.73e-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: 40.28 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 36 VTALIGPSGCGKSTFIRTLNrmndliedVTIKGNISVDGEDIYTSDDVIN---LRTKVGMVFQKPNPFPM------SIYD 106
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALK--------YALTGELPPNSKGGAHDPKLIRegeVRAQVKLAFENANGKKYtitrslAILE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 107 NVAYGPrthglrdKKQLDKIVEESLKGaaiwdevkdrlkssalgLSGGQQQ------RICIARAIAMRPEVILMDEPTSA 180
Cdd:cd03240 96 NVIFCH-------QGESNWPLLDMRGR-----------------CSGGEKVlasliiRLALAETFGSNCGILALDEPTTN 151
|
170 180 190
....*....|....*....|....*....|
gi 489527602 181 LDPIS-TLKVEELIEDLKKDYT--IVIVTH 207
Cdd:cd03240 152 LDEENiEESLAEIIEERKSQKNfqLIVITH 181
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
143-209 |
4.06e-04 |
|
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: 41.54 E-value: 4.06e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527602 143 RLKSSALGLSGGQQQRICIARAIAMR---PEVILMDEPTSALDPISTLKVEELIEDL-KKDYTIVIVTHNM 209
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLvDKGNTVVVIEHNL 892
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
126-205 |
5.22e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 40.68 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 126 IVEESLKGAAIWDEVKdRLK----SSAL---GLSGGQQQRICIARAIAMRPEVILMDEPTSALDPISTLKVEELIEDLKK 198
Cdd:PRK13549 375 RIDDAAELKTILESIQ-RLKvktaSPELaiaRLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQ 453
|
....*..
gi 489527602 199 DYTIVIV 205
Cdd:PRK13549 454 QGVAIIV 460
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
151-233 |
6.35e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 6.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 151 LSGGQQQRICIARAIAMRPEVILMDEPTSALDPIStlkVEELIEDLKK-DYTIVIVTHNMQQAARISDETAFFLNGEVIE 229
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA---VEALIQGLVLfQGGVLMVSHDEHLISGSVDELWVVSEGKVTP 704
|
....
gi 489527602 230 FSDT 233
Cdd:PLN03073 705 FHGT 708
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
151-218 |
8.18e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 39.40 E-value: 8.18e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 151 LSGGQQQRICIAR-AIAMRPEVILmDEPTSALDPISTLKVEELIED-LKKDYTIVIVTHnmQQAARISDE 218
Cdd:PRK13538 130 LSAGQQRRVALARlWLTRAPLWIL-DEPFTAIDKQGVARLEALLAQhAEQGGMVILTTH--QDLPVASDK 196
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
36-149 |
1.10e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 38.09 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 36 VTALIGPSGCGKSTFIRTLNRMNDLIEDVTIKGNISVDGEdiytsddvinlrtkvgmvfqkpnpfPMSIYDNV--AYGPR 113
Cdd:pfam13401 7 ILVLTGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTS-------------------------PKDLLRALlrALGLP 61
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 489527602 114 THGLRDKKQLDKIVEESLKGAA-----IWDEVkDRLKSSAL 149
Cdd:pfam13401 62 LSGRLSKEELLAALQQLLLALAvavvlIIDEA-QHLSLEAL 101
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
35-56 |
1.16e-03 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 38.27 E-value: 1.16e-03
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
125-253 |
1.62e-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: 39.61 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 125 KIVEESLKgaaiwdEVKDRLK-------------SSALGLSGGQQQRICIARAIAMRPEVIL--MDEPTSALDPISTLKv 189
Cdd:TIGR00630 456 KIAEEVLK------EIRERLGflidvgldylslsRAAGTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHQRDNRR- 528
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489527602 190 eeLIEDLK--KDY--TIVIVTHN---MQQAARISD--ETAFFLNGEVIeFSDTKTMFTTPVDKRTEDYITGRF 253
Cdd:TIGR00630 529 --LINTLKrlRDLgnTLIVVEHDedtIRAADYVIDigPGAGEHGGEVV-ASGTPEEILANPDSLTGQYLSGRK 598
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
151-217 |
1.88e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.43 E-value: 1.88e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489527602 151 LSGGQQQRICIAR---AIAMRPEVILMDEPTSALdpiSTLKVEELIEDLK----KDYTIVIVTHNMqQAARISD 217
Cdd:PRK00635 810 LSGGEIQRLKLAYellAPSKKPTLYVLDEPTTGL---HTHDIKALIYVLQslthQGHTVVIIEHNM-HVVKVAD 879
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
39-208 |
3.97e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 38.23 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 39 LIGPSGCGKSTFIRTLnrmndliedvtiKGNISVDGEDIYTSDDvinlrTKVGMVFQKPNPFPMSIYDNVAYGPRTHglR 118
Cdd:PRK10636 32 LVGKNGCGKSTLLALL------------KNEISADGGSYTFPGN-----WQLAWVNQETPALPQPALEYVIDGDREY--R 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527602 119 DKKQLDKIVEESLKGAAI------------WdEVKDRLKSSALGL--------------SGGQQQRICIARAIAMRPEVI 172
Cdd:PRK10636 93 QLEAQLHDANERNDGHAIatihgkldaidaW-TIRSRAASLLHGLgfsneqlerpvsdfSGGWRMRLNLAQALICRSDLL 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 489527602 173 LMDEPTSALDPISTLKVEELIedlkKDY--TIVIVTHN 208
Cdd:PRK10636 172 LLDEPTNHLDLDAVIWLEKWL----KSYqgTLILISHD 205
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
33-54 |
4.07e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 37.38 E-value: 4.07e-03
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
33-54 |
6.34e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 36.37 E-value: 6.34e-03
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
29-51 |
7.17e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.11 E-value: 7.17e-03
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
33-71 |
7.50e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 37.11 E-value: 7.50e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 489527602 33 ENKVTALIGPSGCGKSTFIrtlnrmNDLIEDVTIK-GNIS 71
Cdd:PRK00098 163 AGKVTVLAGQSGVGKSTLL------NALAPDLELKtGEIS 196
|
|
| |
