|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-252 |
0e+00 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 549.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 1 MTDAILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDLNPEVTTTGSVVYNGHNIYSPRTD 80
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 81 TVELRKEIGMVFQQPNPFPMTIYENVVYGLRINGIKDKQVLDEAVEKALQGASIWDEVKDRLYDSAIGLSGGQQQRVCVA 160
Cdd:PRK14239 81 TVDLRKEIGMVFQQPNPFPMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 161 RVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQMFLDPQH 240
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKH 240
|
250
....*....|..
gi 2038545162 241 KETEDYITGKFG 252
Cdd:PRK14239 241 KETEDYISGKFG 252
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-252 |
2.62e-176 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 484.93 E-value: 2.62e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 2 TDAILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDLNPEVTTTGSVVYNGHNIYSPRTDT 81
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGARVEGEILLDGEDIYDPDVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 82 VELRKEIGMVFQQPNPFPMTIYENVVYGLRINGIKDKQVLDEAVEKALQGASIWDEVKDRLYDSAIGLSGGQQQRVCVAR 161
Cdd:COG1117 88 VELRRRVGMVFQKPNPFPKSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDEVKDRLKKSALGLSGGQQQRLCIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 162 VLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQMFLDPQHK 241
Cdd:COG1117 168 ALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDK 247
|
250
....*....|.
gi 2038545162 242 ETEDYITGKFG 252
Cdd:COG1117 248 RTEDYITGRFG 258
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
5-251 |
2.77e-157 |
|
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: 436.34 E-value: 2.77e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDLNPEVTTTGSVVYNGHNIYSPRTDTVEL 84
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPGVRIEGKVLFDGQDIYDKKIDVVEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 85 RKEIGMVFQQPNPFPMTIYENVVYGLRINGIKDKQVLDEAVEKALQGASIWDEVKDRLYDSAIGLSGGQQQRVCVARVLA 164
Cdd:TIGR00972 81 RRRVGMVFQKPNPFPMSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALWDEVKDRLHDSALGLSGGQQQRLCIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 165 TSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQMFLDPQHKETE 244
Cdd:TIGR00972 161 VEPEVLLLDEPTSALDPIATGKIEELIQELKKKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKRTE 240
|
....*..
gi 2038545162 245 DYITGKF 251
Cdd:TIGR00972 241 DYISGRF 247
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-233 |
1.16e-126 |
|
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: 358.03 E-value: 1.16e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDLNPEVTTTGSVVYNGHNIYSPRTDTVELR 85
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 86 KEIGMVFQQPNPFPMTIYENVVYGLRINGIKDKQVLDEAVEKALQGASIWDEVKDRLydSAIGLSGGQQQRVCVARVLAT 165
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRL--HALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038545162 166 SPKIILLDEPTSALDPISAGKIEETLYGLKDKYTMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQ 233
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQ 226
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-252 |
2.06e-112 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 323.66 E-value: 2.06e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 2 TDAILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDLNPEVTTTGSVVYNGHNIYSPRTDT 81
Cdd:PRK14243 7 TETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFHGKNLYAPDVDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 82 VELRKEIGMVFQQPNPFPMTIYENVVYGLRINGIKDKqvLDEAVEKALQGASIWDEVKDRLYDSAIGLSGGQQQRVCVAR 161
Cdd:PRK14243 87 VEVRRRIGMVFQKPNPFPKSIYDNIAYGARINGYKGD--MDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 162 VLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTMLLVTRSMQQASRISDKTGFF---------LDGDLIEFNDTK 232
Cdd:PRK14243 165 AIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTE 244
|
250 260
....*....|....*....|
gi 2038545162 233 QMFLDPQHKETEDYITGKFG 252
Cdd:PRK14243 245 KIFNSPQQQATRDYVSGRFG 264
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-252 |
1.12e-94 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 278.26 E-value: 1.12e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDLNPEVTTTGSVVYNGHNIYSPRTDTVELR 85
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 86 KEIGMVFQQPNPFP-MTIYENVVYGLRING-IKDKQVLDEAVEKALQGASIWDEVKDRLYDSAIGLSGGQQQRVCVARVL 163
Cdd:PRK14267 85 REVGMVFQYPNPFPhLTIYDNVAIGVKLNGlVKSKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 164 ATSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQMFLDPQHKET 243
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELT 244
|
....*....
gi 2038545162 244 EDYITGKFG 252
Cdd:PRK14267 245 EKYVTGALG 253
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-252 |
4.36e-87 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 259.20 E-value: 4.36e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDLNPEVTTTGSVVYNGHNIYSPRTDTVELR 85
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 86 KEIGMVFQQPNPFPMTIYENVVYGLRINGIKDKQVLDEAVEKALQGASIWDEVKDRLYDSAIGLSGGQQQRVCVARVLAT 165
Cdd:PRK14258 88 RQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 166 SPKIILLDEPTSALDPISAGKIEETLYG--LKDKYTMLLVTRSMQQASRISDKTGFFLD-----GDLIEFNDTKQMFLDP 238
Cdd:PRK14258 168 KPKVLLMDEPCFGLDPIASMKVESLIQSlrLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSP 247
|
250
....*....|....
gi 2038545162 239 QHKETEDYITGKFG 252
Cdd:PRK14258 248 HDSRTREYVLSRLG 261
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-250 |
9.94e-84 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 250.22 E-value: 9.94e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 4 AILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDLNPEVTTTGSVVYNGHNIYspRTDTVE 83
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIF--KMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 84 LRKEIGMVFQQPNPFP-MTIYENVVYGLRINGI-KDKQVLDEAVEKALQGASIWDEVKDRLYDSAIGLSGGQQQRVCVAR 161
Cdd:PRK14247 80 LRRRVQMVFQIPNPIPnLSIFENVALGLKLNRLvKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 162 VLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQMFLDPQHK 241
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHE 239
|
....*....
gi 2038545162 242 ETEDYITGK 250
Cdd:PRK14247 240 LTEKYVTGR 248
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-252 |
1.06e-75 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 230.75 E-value: 1.06e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 10 DLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDLNPEVTTTGSVVYNGHNIYSPRtDTVELRKEIG 89
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYR-DVLEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 90 MVFQQPNPFPMTIYENVVYGLRINGIKDKQVLDEAVEKALQGASIWDEVKDRLYDSAIGLSGGQQQRVCVARVLATSPKI 169
Cdd:PRK14271 105 MLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 170 ILLDEPTSALDPISAGKIEETLYGLKDKYTMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQMFLDPQHKETEDYITG 249
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAG 264
|
...
gi 2038545162 250 KFG 252
Cdd:PRK14271 265 LSG 267
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
5-247 |
3.50e-73 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 222.95 E-value: 3.50e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdlnpEVTTTGSVVYNGHNIYSPRTDTVEL 84
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLL-----EEPDSGTITVDGEDLTDSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 85 RKEIGMVFQQPNPFP-MTIYENVVYGLRINGIKDKqvlDEAVEKALqgasiwdEVKDR--LYDSA----IGLSGGQQQRV 157
Cdd:COG1126 76 RRKVGMVFQQFNLFPhLTVLENVTLAPIKVKKMSK---AEAEERAM-------ELLERvgLADKAdaypAQLSGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 158 CVARVLATSPKIILLDEPTSALDPISAGKIEETLYGL-KDKYTMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQMFL 236
Cdd:COG1126 146 AIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLaKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFE 225
|
250
....*....|.
gi 2038545162 237 DPQHKETEDYI 247
Cdd:COG1126 226 NPQHERTRAFL 236
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-250 |
1.20e-69 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 214.91 E-value: 1.20e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDL-NPEVTTTGSVVYNGHNIYspRTDTVE 83
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIyDSKIKVDGKVLYFGKDIF--QIDAIK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 84 LRKEIGMVFQQPNPFP-MTIYENVVYGLRINGIKDKQVLDEAVEKALQGASIWDEVKDRLYDSAIGLSGGQQQRVCVARV 162
Cdd:PRK14246 88 LRKEVGMVFQQPNPFPhLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 163 LATSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQMFLDPQHKE 242
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNEL 247
|
....*...
gi 2038545162 243 TEDYITGK 250
Cdd:PRK14246 248 TEKYVIGR 255
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-240 |
2.76e-63 |
|
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: 205.91 E-value: 2.76e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 1 MTDAILQVSDLSVYY-----NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdLNPevtTTGSVVYNGHNIY 75
Cdd:COG1123 256 AAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGL--LRP---TSGSILFDGKDLT 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 76 S-PRTDTVELRKEIGMVFQQP----NPFpMTIYENVVYGLRINGIKDKQVLDEAVEKALQGASIWDEVKDRlYDSAigLS 150
Cdd:COG1123 331 KlSRRSLRELRRRVQMVFQDPysslNPR-MTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADR-YPHE--LS 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 151 GGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRISDKTGFFLDGDLIEF 228
Cdd:COG1123 407 GGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYLFISHDLAVVRYIADRVAVMYDGRIVED 486
|
250
....*....|..
gi 2038545162 229 NDTKQMFLDPQH 240
Cdd:COG1123 487 GPTEEVFANPQH 498
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-223 |
2.23e-61 |
|
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: 191.97 E-value: 2.23e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdlnpEVTTTGSVVYNGHNIYSPRTDTVELR 85
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLL-----EEPDSGTIIIDGLKLTDDKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 86 KEIGMVFQQPNPFP-MTIYENVVYGLRINGIKDKqvlDEAVEKALQgasIWDEV--KDRLYDSAIGLSGGQQQRVCVARV 162
Cdd:cd03262 76 QKVGMVFQQFNLFPhLTVLENITLAPIKVKGMSK---AEAEERALE---LLEKVglADKADAYPAQLSGGQQQRVAIARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2038545162 163 LATSPKIILLDEPTSALDPISAGKIEETLYGL-KDKYTMLLVTRSMQQASRISDKTGFFLDG 223
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDPELVGEVLDVMKDLaEEGMTMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-229 |
1.39e-59 |
|
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: 188.10 E-value: 1.39e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYY----NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNIYSPRTD 80
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAI--LGLLKP---TSGSIIFDGKDLLKLSRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 81 TVELR-KEIGMVFQQP----NPFpMTIYENVVYGLRINGIKDKQV-LDEAVEKALQGASIWDEVKDRLydsAIGLSGGQQ 154
Cdd:cd03257 76 LRKIRrKEIQMVFQDPmsslNPR-MTIGEQIAEPLRIHGKLSKKEaRKEAVLLLLVGVGLPEEVLNRY---PHELSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038545162 155 QRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRISDKTGFFLDGDLIEFN 229
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-247 |
3.93e-58 |
|
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: 184.80 E-value: 3.93e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 1 MTDAILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNIYS-PRT 79
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLI--IGLLRP---DSGEILVDGQDITGlSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 80 DTVELRKEIGMVFQQPNPF-PMTIYENVVYGLRINGIKDKQVLDEAVEKALQGASIwDEVKDrLYDSAigLSGGQQQRVC 158
Cdd:COG1127 76 ELYELRRRIGMLFQGGALFdSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGL-PGAAD-KMPSE--LSGGMRKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 159 VARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRISDKTGFFLDGDLIeFNDTKQMFL 236
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAIADRVAVLADGKII-AEGTPEELL 230
|
250
....*....|.
gi 2038545162 237 DPQHKETEDYI 247
Cdd:COG1127 231 ASDDPWVRQFL 241
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-223 |
6.15e-58 |
|
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: 182.00 E-value: 6.15e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdlnpEVTTTGSVVYNGHNIYSPRTDTVELR 85
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGL-----EEPDSGSILIDGEDLTDLEDELPPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 86 KEIGMVFQQPNPFP-MTIYENVVYglringikdkqvldeavekalqgasiwdevkdrlydsaiGLSGGQQQRVCVARVLA 164
Cdd:cd03229 76 RRIGMVFQDFALFPhLTVLENIAL---------------------------------------GLSGGQQQRVALARALA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038545162 165 TSPKIILLDEPTSALDPISAGKIEETLYGLKDK--YTMLLVTRSMQQASRISDKTGFFLDG 223
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-216 |
1.96e-56 |
|
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: 179.84 E-value: 1.96e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYY-NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPevtTTGSVVYNGHNIYspRTDTVEL 84
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLN--GLLKP---TSGEVLVDGKDIT--KKNLREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 85 RKEIGMVFQqpNP----FPMTIYENVVYGLRINGIKDKQVlDEAVEKALQ--GASiwdEVKDRlydSAIGLSGGQQQRVC 158
Cdd:COG1122 74 RRKVGLVFQ--NPddqlFAPTVEEDVAFGPENLGLPREEI-RERVEEALElvGLE---HLADR---PPHELSGGQKQRVA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2038545162 159 VARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDK-YTMLLVTRSMQQASRISDK 216
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEgKTVIIVTHDLDLVAELADR 203
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-240 |
3.64e-56 |
|
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: 180.00 E-value: 3.64e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYY----NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGdLNPEvtTTGSVVYNGHNIYSPRTdt 81
Cdd:COG1124 2 LEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRAL--AG-LERP--WSGEVTFDGRPVTRRRR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 82 VELRKEIGMVFQQP----NPFpMTIYENVVYGLRINGIKDKqvlDEAVEKALQGASIWDEVKDRLYDSaigLSGGQQQRV 157
Cdd:COG1124 75 KAFRRRVQMVFQDPyaslHPR-HTVDRILAEPLRIHGLPDR---EERIAELLEQVGLPPSFLDRYPHQ---LSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 158 CVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQMF 235
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
....*
gi 2038545162 236 LDPQH 240
Cdd:COG1124 228 AGPKH 232
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-223 |
9.68e-56 |
|
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: 177.68 E-value: 9.68e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYY----NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPevtTTGSVVYNGHNIY--SPRT 79
Cdd:cd03255 1 IELKNLSKTYggggEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILG--GLDRP---TSGEVRVDGTDISklSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 80 DTVELRKEIGMVFQQPNPFP-MTIYENVVYGLRINGIKDKQVLDEAvEKALQGASIwdevKDRLYDSAIGLSGGQQQRVC 158
Cdd:cd03255 76 LAAFRRRHIGFVFQSFNLLPdLTALENVELPLLLAGVPKKERRERA-EELLERVGL----GDRLNHYPSELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038545162 159 VARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRiSDKTGFFLDG 223
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDPELAEY-ADRIIELRDG 216
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-240 |
3.29e-54 |
|
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: 174.61 E-value: 3.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNIYS-PRTDTVEL 84
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLI--VGLLRP---DSGEVLIDGEDISGlSEAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 85 RKEIGMVFQQPNPF-PMTIYENVVYGLRINGIKDKQVLDEAVEKALQGASIwdEVKDRLYDSAigLSGGQQQRVCVARVL 163
Cdd:cd03261 76 RRRMGMLFQSGALFdSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGL--RGAEDLYPAE--LSGGMKKRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038545162 164 ATSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRISDKTGFFLDGdLIEFNDTKQMFLDPQH 240
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELglTSIMVTHDLDTAFAIADRIAVLYDG-KIVAEGTPEELRASDD 229
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-227 |
5.70e-54 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 173.69 E-value: 5.70e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 3 DAILQVSDLSVYY----NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLkslNRMGDLnpEVTTTGSVVYNGHNIYS-P 77
Cdd:COG1136 2 SPLLELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLL---NILGGL--DRPTSGEVLIDGQDISSlS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 78 RTDTVELR-KEIGMVFQQPNPFP-MTIYENVVYGLRINGIKDKQVLDEAVEkALqgasiwDEV--KDRLYDSAIGLSGGQ 153
Cdd:COG1136 77 ERELARLRrRHIGFVFQFFNLLPeLTALENVALPLLLAGVSRKERRERARE-LL------ERVglGDRLDHRPSQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038545162 154 QQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRiSDKTGFFLDGDLIE 227
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgtTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-226 |
1.12e-53 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 172.94 E-value: 1.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNIyspRTDTVELR 85
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRML--LGLLRP---TSGEVRVLGEDV---ARDPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 86 KEIGMVFQQPNPFP-MTIYENVVYGLRINGIkDKQVLDEAVEKALQGASIWDeVKDRLYDSaigLSGGQQQRVCVARVLA 164
Cdd:COG1131 73 RRIGYVPQEPALYPdLTVRENLRFFARLYGL-PRKEARERIDELLELFGLTD-AADRKVGT---LSGGMKQRLGLALALL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038545162 165 TSPKIILLDEPTSALDPISAGKIEETLYGLKDK-YTMLLVTRSMQQASRISDKTGFFLDGDLI 226
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLCDRVAIIDKGRIV 210
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-216 |
2.39e-53 |
|
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: 172.92 E-value: 2.39e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdLNPevtTTGSVVYNGHNI--YSPRtdtv 82
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGL--LKP---SSGEVLLDGRDLasLSRR---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 83 ELRKEIGMVFQQPN-PFPMTIYENVVYG-------LRINGIKDkqvlDEAVEKALQGASIWDeVKDRLYDSaigLSGGQQ 154
Cdd:COG1120 72 ELARRIAYVPQEPPaPFGLTVRELVALGryphlglFGRPSAED----REAVEEALERTGLEH-LADRPVDE---LSGGER 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038545162 155 QRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRISDK 216
Cdd:COG1120 144 QRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERgrTVVMVLHDLNLAARYADR 207
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-228 |
2.66e-53 |
|
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: 171.55 E-value: 2.66e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdlnpEVTTTGSVVYNGHNIysprTDTVELR 85
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGL-----ERPDSGEILIDGRDV----TGVPPER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 86 KEIGMVFQQPNPFP-MTIYENVVYGLRINGIKDKQVlDEAVEKALQGASIwDEVKDRLYDSaigLSGGQQQRVCVARVLA 164
Cdd:cd03259 72 RNIGMVFQDYALFPhLTVAENIAFGLKLRGVPKAEI-RARVRELLELVGL-EGLLNRYPHE---LSGGQQQRVALARALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038545162 165 TSPKIILLDEPTSALDPISAGKIEETLYGLKD--KYTMLLVTRSMQQASRISDKTGFFLDGDLIEF 228
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEEALALADRIAVMNEGRIVQV 212
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-240 |
3.73e-53 |
|
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: 174.47 E-value: 3.73e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYYNKK----KALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEVTTTGSVVYNGHNI--YSPR 78
Cdd:COG0444 1 LLEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAI--LGLLPPPGITSGEILFDGEDLlkLSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 79 tdtvELR----KEIGMVFQQP----NPFpMTIYENVVYGLRINGIKDKQVLDEAVEKALQGASIwDEVKDRLYDSAIGLS 150
Cdd:COG0444 79 ----ELRkirgREIQMIFQDPmtslNPV-MTVGDQIAEPLRIHGGLSKAEARERAIELLERVGL-PDPERRLDRYPHELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 151 GGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRISDKTGFFLDGDLIEF 228
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELglAILFITHDLGVVAEIADRVAVMYAGRIVEE 232
|
250
....*....|..
gi 2038545162 229 NDTKQMFLDPQH 240
Cdd:COG0444 233 GPVEELFENPRH 244
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-191 |
1.92e-52 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 170.24 E-value: 1.92e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 4 AILQVSDLSV-YYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdLNPevtTTGSVVYNGHNIYSPRTDTV 82
Cdd:COG3638 1 PMLELRNLSKrYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGL--VEP---TSGEILVDGQDVTALRGRAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 83 -ELRKEIGMVFQQPNPFP-MTIYENVVYGL--RINGIK------DKQVLDEAVEkALqgasiwDEV--KDRLYDSAIGLS 150
Cdd:COG3638 76 rRLRRRIGMIFQQFNLVPrLSVLTNVLAGRlgRTSTWRsllglfPPEDRERALE-AL------ERVglADKAYQRADQLS 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2038545162 151 GGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETL 191
Cdd:COG3638 149 GGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLL 189
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-235 |
5.54e-52 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 169.11 E-value: 5.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 1 MTDAILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNIysprtd 80
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAI--LGLLPP---TSGTVRLFGKPP------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 81 tVELRKEIGMVFQQPN---PFPMTIYENVVYGL-------RINGIKDKQVLDEAVEKAlqGASiwdEVKDRLydsaIG-L 149
Cdd:COG1121 71 -RRARRRIGYVPQRAEvdwDFPITVRDVVLMGRygrrglfRRPSRADREAVDEALERV--GLE---DLADRP----IGeL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 150 SGGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDK-YTMLLVTRSMQQASRISDKTgFFLDGDLIEF 228
Cdd:COG1121 141 SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHDLGAVREYFDRV-LLLNRGLVAH 219
|
....*..
gi 2038545162 229 NDTKQMF 235
Cdd:COG1121 220 GPPEEVL 226
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-223 |
5.95e-52 |
|
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: 168.03 E-value: 5.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 7 QVSDLSVYYNK--KKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPevtTTGSVVYNGHNIYSprTDTVEL 84
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLN--GLLGP---TSGEVLVDGKDLTK--LSLKEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 85 RKEIGMVFQQPNP--FPMTIYENVVYGLRINGIKDKQVlDEAVEKALQGASIWDEVKDRLYDsaigLSGGQQQRVCVARV 162
Cdd:cd03225 74 RRKVGLVFQNPDDqfFGPTVEEEVAFGLENLGLPEEEI-EERVEEALELVGLEGLRDRSPFT----LSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2038545162 163 LATSPKIILLDEPTSALDPISAGKIEETLYGLKDK-YTMLLVTRSMQQASRISDKTGFFLDG 223
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-217 |
2.76e-51 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 166.14 E-value: 2.76e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmgDLNPevTTTGSVVYNGHNI--YSPRtdtvE 83
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALA---DLDP--PTSGEIYLDGKPLsaMPPP----E 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 84 LRKEIGMVFQQPNPFPMTIYENVVYGLRIngiKDKQVLDEAVEKALQGASIWDEVKDRlydSAIGLSGGQQQRVCVARVL 163
Cdd:COG4619 72 WRRQVAYVPQEPALWGGTVRDNLPFPFQL---RERKFDRERALELLERLGLPPDILDK---PVERLSGGERQRLALIRAL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2038545162 164 ATSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRISDKT 217
Cdd:COG4619 146 LLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEgrAVLWVSHDPEQIERVADRV 201
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-247 |
4.47e-51 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 169.49 E-value: 4.47e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYYNKKK----ALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdlnpEVTTTGSVVYNGHNI--YSPR 78
Cdd:COG1135 1 MIELENLSKTFPTKGgpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLL-----ERPTSGSVLVDGVDLtaLSER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 79 tDTVELRKEIGMVFQQPNPFP-MTIYENVVYGLRINGIkDKQVLDEAVEKALqgasiwDEV--KDRL--YDSAigLSGGQ 153
Cdd:COG1135 76 -ELRAARRKIGMIFQHFNLLSsRTVAENVALPLEIAGV-PKAEIRKRVAELL------ELVglSDKAdaYPSQ--LSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 154 QQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRISDKTGFFLDGDLIEFNDT 231
Cdd:COG1135 146 KQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELglTIVLITHEMDVVRRICDRVAVLENGRIVEQGPV 225
|
250
....*....|....*.
gi 2038545162 232 KQMFLDPQHKETEDYI 247
Cdd:COG1135 226 LDVFANPQSELTRRFL 241
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-216 |
9.67e-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: 164.95 E-value: 9.67e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYY----NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLkslnRM--GDLNPevtTTGSVVYNGHNIYSPRT 79
Cdd:cd03293 1 LEVRNVSKTYggggGAVTALEDISLSVEEGEFVALVGPSGCGKSTLL----RIiaGLERP---TSGEVLVDGEPVTGPGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 80 DtvelrkeIGMVFQQPNPFP-MTIYENVVYGLRINGIKDKQVLDEAVE--KA--LQGASiwdevkdRLYDSAigLSGGQQ 154
Cdd:cd03293 74 D-------RGYVFQQDALLPwLTVLDNVALGLELQGVPKAEARERAEEllELvgLSGFE-------NAYPHQ--LSGGMR 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038545162 155 QRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGL--KDKYTMLLVTRSMQQASRISDK 216
Cdd:cd03293 138 QRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIwrETGKTVLLVTHDIDEAVFLADR 201
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-216 |
3.04e-50 |
|
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: 165.70 E-value: 3.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNK-----KKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPevtTTGSVVYNGHNIYS-PRT 79
Cdd:TIGR04521 1 IKLKNVSYIYQPgtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLN--GLLKP---TSGTVTIDGRDITAkKKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 80 DTVELRKEIGMVFQQPNP--FPMTIYENVVYGLRINGIKDKQVlDEAVEKALQGASIWDEVKDRlydSAIGLSGGQQQRV 157
Cdd:TIGR04521 76 KLKDLRKKVGLVFQFPEHqlFEETVYKDIAFGPKNLGLSEEEA-EERVKEALELVGLDEEYLER---SPFELSGGQMRRV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038545162 158 CVARVLATSPKIILLDEPTSALDPisAGKIE--ETLYGLKDKY--TMLLVTRSMQQASRISDK 216
Cdd:TIGR04521 152 AIAGVLAMEPEVLILDEPTAGLDP--KGRKEilDLFKRLHKEKglTVILVTHSMEDVAEYADR 212
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-216 |
3.10e-50 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 165.26 E-value: 3.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 1 MTDAILQVSDLSVYYNKKK----ALNSVSLSFQPKEITALIGPSGSGKSTLLkslnRM--GDLNPevtTTGSVVYNGHNI 74
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGggvtALDDVSLTVAAGEFVALVGPSGCGKSTLL----RLiaGLEKP---TSGEVLVDGKPV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 75 YSPRTDtvelrkeIGMVFQQPNPFP-MTIYENVVYGLRINGIKDKQVlDEAVEKALqgasiwDEV-----KDRlYDSAig 148
Cdd:COG1116 76 TGPGPD-------RGVVFQEPALLPwLTVLDNVALGLELRGVPKAER-RERARELL------ELVglagfEDA-YPHQ-- 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 149 LSGGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGL--KDKYTMLLVTRSMQQASRISDK 216
Cdd:COG1116 139 LSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHDVDEAVFLADR 208
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-177 |
2.46e-49 |
|
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: 159.35 E-value: 2.46e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 21 LNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNIYSPRTDtvELRKEIGMVFQQPNPFP- 99
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLI--AGLLSP---TEGTILLDGQDLTDDERK--SLRKEIGYVFQDPQLFPr 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038545162 100 MTIYENVVYGLRINGIKDKQVLDEAvEKALQGASIWDEVKDRLYDSAIGLSGGQQQRVCVARVLATSPKIILLDEPTS 177
Cdd:pfam00005 74 LTVRENLRLGLLLKGLSKREKDARA-EEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-239 |
3.59e-49 |
|
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: 168.93 E-value: 3.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 1 MTdAILQVSDLSVYY--NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEVTTTGSVVYNGHNIyspR 78
Cdd:COG1123 1 MT-PLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALAL--MGLLPHGGRISGEVLLDGRDL---L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 79 TDTVELR-KEIGMVFQQP--NPFPMTIYENVVYGLRINGIkDKQVLDEAVEKALQGASIwdevkDRLYDSAIG-LSGGQQ 154
Cdd:COG1123 75 ELSEALRgRRIGMVFQDPmtQLNPVTVGDQIAEALENLGL-SRAEARARVLELLEAVGL-----ERRLDRYPHqLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 155 QRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTK 232
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE 228
|
....*..
gi 2038545162 233 QMFLDPQ 239
Cdd:COG1123 229 EILAAPQ 235
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-239 |
4.21e-49 |
|
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: 161.21 E-value: 4.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYY----NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdlnpEVTTTGSVVYNGHNIYS-PRT 79
Cdd:cd03258 1 MIELKNVSKVFgdtgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGL-----ERPTSGSVLVDGTDLTLlSGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 80 DTVELRKEIGMVFQQPNPF-PMTIYENVVYGLRINGIKDKQVlDEAVEKALQGASIWDevKDRLYDSAigLSGGQQQRVC 158
Cdd:cd03258 76 ELRKARRRIGMIFQHFNLLsSRTVFENVALPLEIAGVPKAEI-EERVLELLELVGLED--KADAYPAQ--LSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 159 VARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQMFL 236
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFA 230
|
...
gi 2038545162 237 DPQ 239
Cdd:cd03258 231 NPQ 233
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-213 |
5.45e-49 |
|
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: 171.17 E-value: 5.45e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYY--NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNI--YSPRtdt 81
Cdd:COG2274 474 IELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLL--LGLYEP---TSGRILIDGIDLrqIDPA--- 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 82 vELRKEIGMVFQQPNPFPMTIYENVVYGlringikDKQVLDEAVEKALQGASIWDEVKdRL---YDSAIG-----LSGGQ 153
Cdd:COG2274 546 -SLRRQIGVVLQDVFLFSGTIRENITLG-------DPDATDEEIIEAARLAGLHDFIE-ALpmgYDTVVGeggsnLSGGQ 616
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038545162 154 QQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTMLLVT---RSMQQASRI 213
Cdd:COG2274 617 RQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAhrlSTIRLADRI 679
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-223 |
9.88e-49 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 163.73 E-value: 9.88e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 1 MTDAILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLkslnRM--GDLNPevtTTGSVVYNGHNIyspr 78
Cdd:COG3842 1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLL----RMiaGFETP---DSGRILLDGRDV---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 79 TDT-VELRkEIGMVFQQPNPFP-MTIYENVVYGLRINGIkDKQVLDEAVEKALqgasiwDEVK-DRLYDSAIG-LSGGQQ 154
Cdd:COG3842 70 TGLpPEKR-NVGMVFQDYALFPhLTVAENVAFGLRMRGV-PKAEIRARVAELL------ELVGlEGLADRYPHqLSGGQQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038545162 155 QRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRISDKTGFFLDG 223
Cdd:COG3842 142 QRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELgiTFIYVTHDQEEALALADRIAVMNDG 212
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
13-247 |
1.91e-48 |
|
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: 160.16 E-value: 1.91e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 13 VYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdLNPevtTTGSVVYNGHNIYspRTDTVELRKEIGMVF 92
Cdd:cd03295 9 RYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRL--IEP---TSGEIFIDGEDIR--EQDPVELRRKIGYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 93 QQPNPFP-MTIYENVVYGLRINGIKDKQVLDEAVEK-ALQGASIwDEVKDRlYDSAigLSGGQQQRVCVARVLATSPKII 170
Cdd:cd03295 82 QQIGLFPhMTVEENIALVPKLLKWPKEKIRERADELlALVGLDP-AEFADR-YPHE--LSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038545162 171 LLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQMFLDPQHKETEDYI 247
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQELgkTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFV 236
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-213 |
2.99e-47 |
|
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: 154.46 E-value: 2.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYY--NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdLNPevtTTGSVVYNGHNIYSPrtDTVE 83
Cdd:cd03228 1 IEFKNVSFSYpgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRL--YDP---TSGEILIDGVDLRDL--DLES 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 84 LRKEIGMVFQQPNPFPMTIYENVvyglringikdkqvldeavekalqgasiwdevkdrlydsaigLSGGQQQRVCVARVL 163
Cdd:cd03228 74 LRKNIAYVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARAL 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2038545162 164 ATSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTMLLVTR---SMQQASRI 213
Cdd:cd03228 112 LRDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHrlsTIRDADRI 164
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-191 |
1.20e-46 |
|
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: 155.42 E-value: 1.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYY-NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdLNPevtTTGSVVYNGHNIYS-PRTDTVE 83
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGL--VEP---TSGSVLIDGTDINKlKGKALRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 84 LRKEIGMVFQQPNPFP-MTIYENVVYGL--RINGIKD--KQVLDEAVEKALQgasIWDEV--KDRLYDSAIGLSGGQQQR 156
Cdd:cd03256 76 LRRQIGMIFQQFNLIErLSVLENVLSGRlgRRSTWRSlfGLFPKEEKQRALA---ALERVglLDKAYQRADQLSGGQQQR 152
|
170 180 190
....*....|....*....|....*....|....*
gi 2038545162 157 VCVARVLATSPKIILLDEPTSALDPISAGKIEETL 191
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASSRQVMDLL 187
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-214 |
1.70e-46 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 162.64 E-value: 1.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 14 YYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDlnpevTTTGSVVYNGHNI--YSPRtdtvELRKEIGMV 91
Cdd:COG1132 349 YPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD-----PTSGRILIDGVDIrdLTLE----SLRRQIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 92 FQQPNPFPMTIYENVVYGlringikDKQVLDEAVEKALQGASIWDEVkDRL---YDSAIG-----LSGGQQQRVCVARVL 163
Cdd:COG1132 420 PQDTFLFSGTIRENIRYG-------RPDATDEEVEEAAKAAQAHEFI-EALpdgYDTVVGergvnLSGGQRQRIAIARAL 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2038545162 164 ATSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTMLLVtrsmqqASRIS 214
Cdd:COG1132 492 LKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVI------AHRLS 536
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-242 |
1.90e-46 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 155.02 E-value: 1.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNiysPRTDTVELR 85
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRML--AGLLKP---DSGSILIDGED---VRKEPREAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 86 KEIGMVFQQPNPFP-MTIYENVVYGLRINGIKDKQvLDEAVEKALQGASIwDEVKDRLYDsaiGLSGGQQQRVCVARVLA 164
Cdd:COG4555 74 RQIGVLPDERGLYDrLTVRENIRYFAELYGLFDEE-LKKRIEELIELLGL-EEFLDRRVG---ELSTGMKKKVALARALV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038545162 165 TSPKIILLDEPTSALDPISAGKIEETLYGLKD-KYTMLLVTRSMQQASRISDKTGFFLDGDLIeFNDTKQMFLDPQHKE 242
Cdd:COG4555 149 HDPKVLLLDEPTNGLDVMARRLLREILRALKKeGKTVLFSSHIMQEVEALCDRVVILHKGKVV-AQGSLDELREEIGEE 226
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
5-187 |
2.29e-46 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 154.05 E-value: 2.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYY-NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNIYS-PRTDTV 82
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLL--YGEERP---TSGQVLVNGQDLSRlKRREIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 83 ELRKEIGMVFQQ----PNpfpMTIYENVVYGLRINGIKDKQVlDEAVEKALqgasiwDEV--KDRLYDSAIGLSGGQQQR 156
Cdd:COG2884 76 YLRRRIGVVFQDfrllPD---RTVYENVALPLRVTGKSRKEI-RRRVREVL------DLVglSDKAKALPHELSGGEQQR 145
|
170 180 190
....*....|....*....|....*....|.
gi 2038545162 157 VCVARVLATSPKIILLDEPTSALDPISAGKI 187
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPETSWEI 176
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
4-251 |
4.80e-46 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 154.14 E-value: 4.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 4 AILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDLNPEVTTTGSVVYNGHNIYSPRTDTV- 82
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQQKGLIr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 83 ELRKEIGMVFQQPNPFP-MTIYENVVYGLRIngIKdKQVLDEAVEKALQG-ASIWDEVKDRLYDSAigLSGGQQQRVCVA 160
Cdd:PRK11264 82 QLRQHVGFVFQNFNLFPhRTVLENIIEGPVI--VK-GEPKEEATARARELlAKVGLAGKETSYPRR--LSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 161 RVLATSPKIILLDEPTSALDPISAGKIEETLYGL-KDKYTMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQMFLDPQ 239
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQ 236
|
250
....*....|..
gi 2038545162 240 HKETEDYItGKF 251
Cdd:PRK11264 237 QPRTRQFL-EKF 247
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-227 |
7.51e-46 |
|
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: 160.69 E-value: 7.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYY-NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNIYSPRTDTveL 84
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLL--LGFLPP---YSGSILINGVDLSDLDPAS--W 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 85 RKEIGMVFQQPNPFPMTIYENVvyglrinGIKDKQVLDEAVEKALQGASIWDEVkDRL---YDSAIG-----LSGGQQQR 156
Cdd:COG4988 410 RRQIAWVPQNPYLFAGTIRENL-------RLGRPDASDEELEAALEAAGLDEFV-AALpdgLDTPLGeggrgLSGGQAQR 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2038545162 157 VCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTMLLVT---RSMQQASRIsdktgFFLD-GDLIE 227
Cdd:COG4988 482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILIThrlALLAQADRI-----LVLDdGRIVE 551
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-226 |
1.08e-45 |
|
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: 152.27 E-value: 1.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNK--KKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNIyspRTDTVE 83
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKML--TGELRP---TSGTAYINGYSI---RTDRKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 84 LRKEIGMVFQQPNPFP-MTIYENVVYGLRINGIKDKQVlDEAVEKALQGASIwDEVKDRLydsAIGLSGGQQQRVCVARV 162
Cdd:cd03263 73 ARQSLGYCPQFDALFDeLTVREHLRFYARLKGLPKSEI-KEEVELLLRVLGL-TDKANKR---ARTLSGGMKRKLSLAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038545162 163 LATSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTMLLVTRSMQQASRISDKTGFFLDGDLI 226
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
5-238 |
1.30e-45 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 152.55 E-value: 1.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdlnpEVTTTGSVVYNGHNIYSPRTDTVEL 84
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKL-----EEITSGDLIVDGLKVNDPKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 85 RKEIGMVFQQPNPFP-MTIYENVVYG-LRINGIKDKQVldEAVEKALQGASIWDEVKDRlYDSAigLSGGQQQRVCVARV 162
Cdd:PRK09493 76 RQEAGMVFQQFYLFPhLTALENVMFGpLRVRGASKEEA--EKQARELLAKVGLAERAHH-YPSE--LSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 163 LATSPKIILLDEPTSALDPisagkiE---ETLYGLKD----KYTMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQMF 235
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDP------ElrhEVLKVMQDlaeeGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLI 224
|
...
gi 2038545162 236 LDP 238
Cdd:PRK09493 225 KNP 227
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-223 |
2.70e-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: 2.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNIyspRTDTVELR 85
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKII--LGLLKP---DSGEIKVLGKDI---KKEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 86 KEIGMVFQQPNPFP-MTIYENVVYglringikdkqvldeavekalqgasiwdevkdrlydsaiglSGGQQQRVCVARVLA 164
Cdd:cd03230 73 RRIGYLPEEPSLYEnLTVRENLKL-----------------------------------------SGGMKQRLALAQALL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 165 TSPKIILLDEPTSALDPISAGKIEETLYGLKDKY-TMLLVTRSMQQASRISDKTGFFLDG 223
Cdd:cd03230 112 HDPELLILDEPTSGLDPESRREFWELLRELKKEGkTILLSSHILEEAERLCDRVAILNNG 171
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-226 |
1.00e-44 |
|
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: 149.61 E-value: 1.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 7 QVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNIysprtdtVELRK 86
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAI--LGLLKP---TSGSIRVFGKPL-------EKERK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 87 EIGMVFQQPN---PFPMTIYENVVYGL-------RINGIKDKQVLDEAVEKAlqGASiwdEVKDRLYDSaigLSGGQQQR 156
Cdd:cd03235 69 RIGYVPQRRSidrDFPISVRDVVLMGLyghkglfRRLSKADKAKVDEALERV--GLS---ELADRQIGE---LSGGQQQR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038545162 157 VCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDK-YTMLLVTRSMQQASRISDKTgFFLDGDLI 226
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEYFDRV-LLLNRTVV 210
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
3-249 |
2.19e-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: 150.49 E-value: 2.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 3 DAILQVSDLSVyynkkkALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdLNPevtTTGSVVYNGHNIYS-PRTDT 81
Cdd:cd03294 28 EEILKKTGQTV------GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRL--IEP---TSGKVLIDGQDIAAmSRKEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 82 VELR-KEIGMVFQQPNPFP-MTIYENVVYGLRINGIkDKQVLDEAVEKALQ--GASIWdevKDRLYDSaigLSGGQQQRV 157
Cdd:cd03294 97 RELRrKKISMVFQSFALLPhRTVLENVAFGLEVQGV-PRAEREERAAEALElvGLEGW---EHKYPDE---LSGGMQQRV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 158 CVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQMF 235
Cdd:cd03294 170 GLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELqkTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
250
....*....|....
gi 2038545162 236 LDPQHKETEDYITG 249
Cdd:cd03294 250 TNPANDYVREFFRG 263
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
13-236 |
2.39e-44 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 151.40 E-value: 2.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 13 VYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDLnpevtTTGSVVYNGHNIYSprTDTVELRKEIGMVF 92
Cdd:COG1125 10 RYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEP-----TSGRILIDGEDIRD--LDPVELRRRIGYVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 93 QQPNPFP-MTIYENVVYGLRINGiKDKQVLDEAVEKALQGASIW-DEVKDRlYDSAigLSGGQQQRVCVARVLATSPKII 170
Cdd:COG1125 83 QQIGLFPhMTVAENIATVPRLLG-WDKERIRARVDELLELVGLDpEEYRDR-YPHE--LSGGQQQRVGVARALAADPPIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038545162 171 LLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRISDKTGFFLDGDLIEFnDTKQMFL 236
Cdd:COG1125 159 LMDEPFGALDPITREQLQDELLRLQRELgkTIVFVTHDIDEALKLGDRIAVMREGRIVQY-DTPEEIL 225
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-215 |
4.31e-44 |
|
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: 147.97 E-value: 4.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNIYSPRTDTVeLR 85
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTI--MGLLPP---RSGSIRFDGRDITGLPPHER-AR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 86 KEIGMVFQQPNPFP-MTIYENVVYGLRINGIKD-KQVLDEAVEkalqgasIWDEVKDRLYDSAIGLSGGQQQRVCVARVL 163
Cdd:cd03224 75 AGIGYVPEGRRIFPeLTVEENLLLGAYARRRAKrKARLERVYE-------LFPRLKERRKQLAGTLSGGEQQMLAIARAL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2038545162 164 ATSPKIILLDEPTSALDPISAGKIEETLYGLKDK-YTMLLVTRSMQQASRISD 215
Cdd:cd03224 148 MSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEgVTILLVEQNARFALEIAD 200
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-216 |
5.65e-44 |
|
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: 148.35 E-value: 5.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPevtTTGSVVYNGHNI--YSPRtdtvE 83
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLIS--GFLRP---TSGSVLFDGEDItgLPPH----E 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 84 L-RKEIGMVFQQPNPFP-MTIYENVV------YGLRINGIKDKQVLDEAVEKALQgasIWDEVK--DRLYDSAIGLSGGQ 153
Cdd:cd03219 72 IaRLGIGRTFQIPRLFPeLTVLENVMvaaqarTGSGLLLARARREEREARERAEE---LLERVGlaDLADRPAGELSYGQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038545162 154 QQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDK-YTMLLVTRSMQQASRISDK 216
Cdd:cd03219 149 QRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERgITVLLVEHDMDVVMSLADR 212
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-223 |
3.13e-43 |
|
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: 143.92 E-value: 3.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 7 QVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdLNPevtTTGSVVYNGHNIysPRTDTVELRK 86
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGL--LKP---TSGEILIDGKDI--AKLPLEELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 87 EIGMVFQqpnpfpmtiyenvvyglringikdkqvldeavekalqgasiwdevkdrlydsaigLSGGQQQRVCVARVLATS 166
Cdd:cd00267 74 RIGYVPQ-------------------------------------------------------LSGGQRQRVALARALLLN 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2038545162 167 PKIILLDEPTSALDPISAGKIEETLYGLKDK-YTMLLVTRSMQQASRISDKTGFFLDG 223
Cdd:cd00267 99 PDLLLLDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-191 |
1.92e-42 |
|
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: 144.36 E-value: 1.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLS-VYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDLnpevtTTGSVVYNGHNIYSPR-TDTV 82
Cdd:TIGR02315 1 MLEVENLSkVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEP-----SSGSILLEGTDITKLRgKKLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 83 ELRKEIGMVFQQPNPFP-MTIYENVVYGlRINGIKDKQVL-----DEAVEKALQgasIWDEV--KDRLYDSAIGLSGGQQ 154
Cdd:TIGR02315 76 KLRRRIGMIFQHYNLIErLTVLENVLHG-RLGYKPTWRSLlgrfsEEDKERALS---ALERVglADKAYQRADQLSGGQQ 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 2038545162 155 QRVCVARVLATSPKIILLDEPTSALDPISAGKIEETL 191
Cdd:TIGR02315 152 QRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYL 188
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-213 |
3.96e-42 |
|
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: 150.69 E-value: 3.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 2 TDAILQVSDLSVYY--NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNIYSPRT 79
Cdd:COG4987 330 GGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALL--LRFLDP---QSGSITLGGVDLRDLDE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 80 DTveLRKEIGMVFQQPNPFPMTIYENvvygLRIngiKDKQVLDEAVEKALQGASIWDEVKD-------RLYDSAIGLSGG 152
Cdd:COG4987 405 DD--LRRRIAVVPQRPHLFDTTLREN----LRL---ARPDATDEELWAALERVGLGDWLAAlpdgldtWLGEGGRRLSGG 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2038545162 153 QQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYG-LKDKyTMLLVT---RSMQQASRI 213
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEaLAGR-TVLLIThrlAGLERMDRI 539
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
6-216 |
7.72e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 144.42 E-value: 7.72e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNK-----KKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPevtTTGSVVYNGHNIYSPRTD 80
Cdd:PRK13637 3 IKIENLTHIYMEgtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLN--GLLKP---TSGKIIIDGVDITDKKVK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 81 TVELRKEIGMVFQQP--NPFPMTIYENVVYGLRINGIKDKQVLDEaVEKALQGASI-WDEVKDRlydSAIGLSGGQQQRV 157
Cdd:PRK13637 78 LSDIRKKVGLVFQYPeyQLFEETIEKDIAFGPINLGLSEEEIENR-VKRAMNIVGLdYEDYKDK---SPFELSGGQKRRV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038545162 158 CVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTM--LLVTRSMQQASRISDK 216
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMtiILVSHSMEDVAKLADR 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
6-216 |
1.81e-41 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 144.90 E-value: 1.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNIY---SPRTdtv 82
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRII--AGLETP---DSGRIVLNGRDLFtnlPPRE--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 83 elRKeIGMVFQQPNPFP-MTIYENVVYGLRINGiKDKQVLDEAVEKALqgasiwDEVK-----DRlYDSAigLSGGQQQR 156
Cdd:COG1118 75 --RR-VGFVFQHYALFPhMTVAENIAFGLRVRP-PSKAEIRARVEELL------ELVQleglaDR-YPSQ--LSGGQRQR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2038545162 157 VCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRISDK 216
Cdd:COG1118 142 VALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELggTTVFVTHDQEEALELADR 203
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-226 |
2.25e-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: 2.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 7 QVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdLNPEvttTGSVVYNGHNI--YSPRtdtvEL 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGL--LKPS---SGEILLDGKDLasLSPK----EL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 85 RKEIGMVFQQpnpfpmtiyenvvygLRINGIKDKqvldeavekalqgasiwdevKDRLYDSaigLSGGQQQRVCVARVLA 164
Cdd:cd03214 72 ARKIAYVPQA---------------LELLGLAHL--------------------ADRPFNE---LSGGERQRVLLARALA 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038545162 165 TSPKIILLDEPTSALDPisAGKIE--ETLYGLKDKY--TMLLVTRSMQQASRISDKTGFFLDGDLI 226
Cdd:cd03214 114 QEPPILLLDEPTSHLDI--AHQIEllELLRRLARERgkTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
4-181 |
2.60e-41 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 144.45 E-value: 2.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 4 AILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLkslnRM--GdLnpEVTTTGSVVYNGHNIysprTDT 81
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLL----RMiaG-L--EDPTSGEILIGGRDV----TDL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 82 VELRKEIGMVFQQPNPFP-MTIYENVVYGLRINGIkDKQVLDEAVEKALQGASIwDEVKDRLydsAIGLSGGQQQRVCVA 160
Cdd:COG3839 71 PPKDRNIAMVFQSYALYPhMTVYENIAFPLKLRKV-PKAEIDRRVREAAELLGL-EDLLDRK---PKQLSGGQRQRVALG 145
|
170 180
....*....|....*....|.
gi 2038545162 161 RVLATSPKIILLDEPTSALDP 181
Cdd:COG3839 146 RALVREPKVFLLDEPLSNLDA 166
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-181 |
4.56e-41 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 141.45 E-value: 4.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 4 AILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPevtTTGSVVYNGHNI--YSPRtdt 81
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALS--GELSP---DSGEVRLNGRPLadWSPA--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 82 vELRKEIGMVFQQPN-PFPMTIYENVVYGLRINGIKDKQVlDEAVEKALQGASIWDeVKDRLYDSaigLSGGQQQRVCVA 160
Cdd:PRK13548 73 -ELARRRAVLPQHSSlSFPFTVEEVVAMGRAPHGLSRAED-DALVAAALAQVDLAH-LAGRDYPQ---LSGGEQQRVQLA 146
|
170 180
....*....|....*....|....*..
gi 2038545162 161 RVLA------TSPKIILLDEPTSALDP 181
Cdd:PRK13548 147 RVLAqlwepdGPPRWLLLDEPTSALDL 173
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
18-249 |
1.50e-40 |
|
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: 143.07 E-value: 1.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 18 KKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdLNPevtTTGSVVYNGHNIYspRTDTVEL----RKEIGMVFQ 93
Cdd:TIGR01186 6 KKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRL--IEP---TAGQIFIDGENIM--KQSPVELrevrRKKIGMVFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 94 QPNPFP-MTIYENVVYGLRINGIkDKQvldEAVEKALQGASIWD--EVKDRLYDSaigLSGGQQQRVCVARVLATSPKII 170
Cdd:TIGR01186 79 QFALFPhMTILQNTSLGPELLGW-PEQ---ERKEKALELLKLVGleEYEHRYPDE---LSGGMQQRVGLARALAAEPDIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 171 LLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQMFLDPQHKETEDYIT 248
Cdd:TIGR01186 152 LMDEAFSALDPLIRDSMQDELKKLQATLqkTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIG 231
|
.
gi 2038545162 249 G 249
Cdd:TIGR01186 232 K 232
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
3-215 |
5.79e-40 |
|
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: 137.81 E-value: 5.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 3 DAILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNIYSPRTDTV 82
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAI--SGLLPP---RSGSIRFDGEDITGLPPHRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 83 eLRKEIGMVFQQPNPFP-MTIYENVVYGLRINgiKDKQVLDEAVEKALQgasIWDEVKDRLYDSAIGLSGGQQQRVCVAR 161
Cdd:COG0410 76 -ARLGIGYVPEGRRIFPsLTVEENLLLGAYAR--RDRAEVRADLERVYE---LFPRLKERRRQRAGTLSGGEQQMLAIGR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2038545162 162 VLATSPKIILLDEPTSALDPISAGKIEETLYGLKDK-YTMLLVTRSMQQASRISD 215
Cdd:COG0410 150 ALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREgVTILLVEQNARFALEIAD 204
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-239 |
7.73e-40 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 138.39 E-value: 7.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 1 MTDAI---LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdlnpEVTTTGSVVYNGHNIYSP 77
Cdd:COG4598 1 MTDTAppaLEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLL-----ETPDSGEIRVGGEEIRLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 78 RT----------DTVE-LRKEIGMVFQQPNPFP-MTIYENVVYG-LRINGIKDKQVLDEAvEKALQGASIWDeVKDRlYD 144
Cdd:COG4598 76 PDrdgelvpadrRQLQrIRTRLGMVFQSFNLWShMTVLENVIEApVHVLGRPKAEAIERA-EALLAKVGLAD-KRDA-YP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 145 SAigLSGGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDK-YTMLLVTRSMQQASRISDKTGFFLDG 223
Cdd:COG4598 153 AH--LSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEgRTMLVVTHEMGFARDVSSHVVFLHQG 230
|
250
....*....|....*.
gi 2038545162 224 DLIEFNDTKQMFLDPQ 239
Cdd:COG4598 231 RIEEQGPPAEVFGNPK 246
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
6-247 |
1.00e-39 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 137.45 E-value: 1.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdlnpEVTTTGSVVYNGHNIYSPRT----DT 81
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLL-----ETPDSGQLNIAGHQFDFSQKpsekAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 82 VELRKEIGMVFQQPNPFP-MTIYENVVYG-LRINGIKDKQVLDEAVE--KALQgasiWDEVKDRLydsAIGLSGGQQQRV 157
Cdd:COG4161 78 RLLRQKVGMVFQQYNLWPhLTVMENLIEApCKVLGLSKEQAREKAMKllARLR----LTDKADRF---PLHLSGGQQQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 158 CVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDK-YTMLLVTRSMQQASRISDKTGFFLDGDLIEFNDtKQMFL 236
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTgITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFT 229
|
250
....*....|.
gi 2038545162 237 DPQHKETEDYI 247
Cdd:COG4161 230 QPQTEAFAHYL 240
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
6-181 |
1.44e-39 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 137.55 E-value: 1.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPevtTTGSVVYNGHNI--YSPRtdtvE 83
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLT--GELTP---SSGEVRLNGRPLaaWSPW----E 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 84 LRKEIGMVFQQPN-PFPMTIYENVVYGlRINGIKDKQVLDEAVEKALQGASIWDeVKDRLYDSaigLSGGQQQRVCVARV 162
Cdd:COG4559 73 LARRRAVLPQHSSlAFPFTVEEVVALG-RAPHGSSAAQDRQIVREALALVGLAH-LAGRSYQT---LSGGEQQRVQLARV 147
|
170 180
....*....|....*....|....*.
gi 2038545162 163 LA-------TSPKIILLDEPTSALDP 181
Cdd:COG4559 148 LAqlwepvdGGPRWLFLDEPTSALDL 173
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
13-247 |
3.65e-39 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 138.78 E-value: 3.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 13 VYYNKKK---ALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdlnpEVTTTGSVVYNGHNIYS-PRTDTVELRKEI 88
Cdd:PRK11153 10 VFPQGGRtihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLL-----ERPTSGRVLVDGQDLTAlSEKELRKARRQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 89 GMVFQQpnpFPM----TIYENVVYGLRINGiKDKQVLDEAVEKALQGASIWDEvKDRlYDSAigLSGGQQQRVCVARVLA 164
Cdd:PRK11153 85 GMIFQH---FNLlssrTVFDNVALPLELAG-TPKAEIKARVTELLELVGLSDK-ADR-YPAQ--LSGGQKQRVAIARALA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 165 TSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQMFLDPQHKE 242
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILELLKDINRELglTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPL 236
|
....*
gi 2038545162 243 TEDYI 247
Cdd:PRK11153 237 TREFI 241
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-247 |
3.68e-39 |
|
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: 135.93 E-value: 3.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKaLNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEvttTGSVVYNGHNIysprTDTVELR 85
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETI--AGFIKPD---SGKILLNGKDI----TNLPPEK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 86 KEIGMVFQQPNPFP-MTIYENVVYGLRINGIKDKQVlDEAVEKALQGASIwDEVKDRlydSAIGLSGGQQQRVCVARVLA 164
Cdd:cd03299 71 RDISYVPQNYALFPhMTVYKNIAYGLKKRKVDKKEI-ERKVLEIAEMLGI-DHLLNR---KPETLSGGEQQRVAIARALV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 165 TSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQMFLDPQHKE 242
Cdd:cd03299 146 VNPKILLLDEPFSALDVRTKEKLREELKKIRKEFgvTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEF 225
|
....*
gi 2038545162 243 TEDYI 247
Cdd:cd03299 226 VAEFL 230
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-180 |
7.50e-39 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 137.56 E-value: 7.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 1 MTDAILQVSDLSVYYNKK-----------KALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdlnpEVTTTGSVVY 69
Cdd:COG4608 3 MAEPLLEVRDLKKHFPVRgglfgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRL-----EEPTSGEILF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 70 NGHNIYS-PRTDTVELRKEIGMVFQQP----NPfPMTIYENVVYGLRINGIKDKQVLDEAVEKALQgasiwdevkdrlyd 144
Cdd:COG4608 78 DGQDITGlSGRELRPLRRRMQMVFQDPyaslNP-RMTVGDIIAEPLRIHGLASKAERRERVAELLE-------------- 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2038545162 145 sAIGL------------SGGQQQRVCVARVLATSPKIILLDEPTSALD 180
Cdd:COG4608 143 -LVGLrpehadryphefSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
19-191 |
1.08e-38 |
|
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: 134.59 E-value: 1.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 19 KALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDLnpevtTTGSVVYNGHNI--YSPRtdtvELRKEIGMVFQQPN 96
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDP-----TSGEILLDGVDIrdLNLR----WLRSQIGLVSQEPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 97 PFPMTIYENVVYGlringikDKQVLDEAVEKALQGASIWDEVKDrL---YDSAIG-----LSGGQQQRVCVARVLATSPK 168
Cdd:cd03249 88 LFDGTIAENIRYG-------KPDATDEEVEEAAKKANIHDFIMS-LpdgYDTLVGergsqLSGGQKQRIAIARALLRNPK 159
|
170 180
....*....|....*....|...
gi 2038545162 169 IILLDEPTSALDPISAGKIEETL 191
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEAL 182
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
6-248 |
4.33e-38 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 133.22 E-value: 4.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdlnpEVTTTGSVVYNGHNI-YSPRTDT--- 81
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLL-----EMPRSGTLNIAGNHFdFSKTPSDkai 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 82 VELRKEIGMVFQQPNPFP-MTIYENVVYG-LRINGIkDKQvldEAVEKALQgasIWDEVkdRLYDSA----IGLSGGQQQ 155
Cdd:PRK11124 78 RELRRNVGMVFQQYNLWPhLTVQQNLIEApCRVLGL-SKD---QALARAEK---LLERL--RLKPYAdrfpLHLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 156 RVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKD-KYTMLLVTRSMQQASRISDKTGFFLDGDLIEFNDtKQM 234
Cdd:PRK11124 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASC 227
|
250
....*....|....
gi 2038545162 235 FLDPQHKETEDYIT 248
Cdd:PRK11124 228 FTQPQTEAFKNYLS 241
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-240 |
7.72e-38 |
|
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: 138.66 E-value: 7.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYYNKK-----------KALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdlnpeVTTTGSVVYNGHN 73
Cdd:COG4172 275 LLEARDLKVWFPIKrglfrrtvghvKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL------IPSEGEIRFDGQD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 74 IYS-PRTDTVELRKEIGMVFQQP----NPfPMTIYENVVYGLRINGIK-DKQVLDEAVEKALQGASIWDEVKDRlYDSAi 147
Cdd:COG4172 349 LDGlSRRALRPLRRRMQVVFQDPfgslSP-RMTVGQIIAEGLRVHGPGlSAAERRARVAEALEEVGLDPAARHR-YPHE- 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 148 gLSGGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVT------RSMqqasriSDKTGF 219
Cdd:COG4172 426 -FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHglAYLFIShdlavvRAL------AHRVMV 498
|
250 260
....*....|....*....|.
gi 2038545162 220 FLDGDLIEFNDTKQMFLDPQH 240
Cdd:COG4172 499 MKDGKVVEQGPTEQVFDAPQH 519
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-204 |
2.63e-37 |
|
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: 137.03 E-value: 2.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYY-NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDlnpevTTTGSVVYNGHNIYSPRTDTveL 84
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVD-----PTEGSIAVNGVPLADADADS--W 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 85 RKEIGMVFQQPNPFPMTIYENVVYGlringikDKQVLDEAVEKALQGASIWDEVKDR-------LYDSAIGLSGGQQQRV 157
Cdd:TIGR02857 395 RDQIAWVPQHPFLFAGTIAENIRLA-------RPDASDAEIREALERAGLDEFVAALpqgldtpIGEGGAGLSGGQAQRL 467
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2038545162 158 CVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTMLLVT 204
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVT 514
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-240 |
3.47e-37 |
|
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: 136.74 E-value: 3.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 1 MTDAILQVSDLSVYY----NKKKALNSVSLSFQPKEITALIGPSGSGKS-TLLkSLnrMGdLNPE--VTTTGSVVYNGHN 73
Cdd:COG4172 2 MSMPLLSVEDLSVAFgqggGTVEAVKGVSFDIAAGETLALVGESGSGKSvTAL-SI--LR-LLPDpaAHPSGSILFDGQD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 74 I--YSPRtdtvELRK----EIGMVFQQP----NPFpMTIYENVVYGLRI-NGIKDKQVLDEAVEkALQGASIwDEVKDRL 142
Cdd:COG4172 78 LlgLSER----ELRRirgnRIAMIFQEPmtslNPL-HTIGKQIAEVLRLhRGLSGAAARARALE-LLERVGI-PDPERRL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 143 YDSAIGLSGGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTM--LLVTRSMQQASRISDKTGFF 220
Cdd:COG4172 151 DAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMalLLITHDLGVVRRFADRVAVM 230
|
250 260
....*....|....*....|
gi 2038545162 221 LDGDLIEFNDTKQMFLDPQH 240
Cdd:COG4172 231 RQGEIVEQGPTAELFAAPQH 250
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-235 |
5.90e-37 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 131.29 E-value: 5.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 1 MTDAILQVSDLSVYY--NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPEvttTGSVVYNGHNIyspR 78
Cdd:PRK13635 1 MKEEIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLN--GLLLPE---AGTITVGGMVL---S 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 79 TDTV-ELRKEIGMVFQQP-NPF-PMTIYENVVYGLRINGIKDKQVLdEAVEKALQGASIwdevKDRLYDSAIGLSGGQQQ 155
Cdd:PRK13635 73 EETVwDVRRQVGMVFQNPdNQFvGATVQDDVAFGLENIGVPREEMV-ERVDQALRQVGM----EDFLNREPHRLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 156 RVCVARVLATSPKIILLDEPTSALDPIsaGKIE--ETLYGLKDK--YTMLLVTRSMQQASRiSDKTGFFLDGDLIEFNDT 231
Cdd:PRK13635 148 RVAIAGVLALQPDIIILDEATSMLDPR--GRREvlETVRQLKEQkgITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTP 224
|
....
gi 2038545162 232 KQMF 235
Cdd:PRK13635 225 EEIF 228
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-216 |
7.26e-37 |
|
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: 130.54 E-value: 7.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 2 TDAILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPevtTTGSVVYNGHNI--YSPRt 79
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLIT--GFYRP---TSGRILFDGRDItgLPPH- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 80 dtvelrkEI---GMV--FQQPNPFP-MTIYENVVYGLR-----------INGIKDKQVLDEAVEKALQgasIWDEVK--D 140
Cdd:COG0411 75 -------RIarlGIArtFQNPRLFPeLTVLENVLVAAHarlgrgllaalLRLPRARREEREARERAEE---LLERVGlaD 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038545162 141 RLYDSAIGLSGGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKD--KYTMLLVTRSMQQASRISDK 216
Cdd:COG0411 145 RADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDerGITILLIEHDMDLVMGLADR 222
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-216 |
1.48e-36 |
|
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: 129.38 E-value: 1.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdlnpEVTTTGSVVYNGHNIysprTDTVELR 85
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGL-----ERPDSGTILFGGEDA----TDVPVQE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 86 KEIGMVFQQPNPFP-MTIYENVVYGLRINGIK---DKQVLDEAVEKALQGASIwDEVKDRlYDSAigLSGGQQQRVCVAR 161
Cdd:cd03296 74 RNVGFVFQHYALFRhMTVFDNVAFGLRVKPRSerpPEAEIRAKVHELLKLVQL-DWLADR-YPAQ--LSGGQRQRVALAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038545162 162 VLATSPKIILLDEPTSALDpisaGKIEETLYG----LKDK--YTMLLVTRSMQQASRISDK 216
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALD----AKVRKELRRwlrrLHDElhVTTVFVTHDQEEALEVADR 206
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-226 |
2.81e-36 |
|
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: 127.87 E-value: 2.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdLNPevtTTGSVVYNGHNIyspRTDTVELR 85
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTL--LKP---TSGRATVAGHDV---VREPREVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 86 KEIGMVFQQPNPFP-MTIYENVVYGLRINGIKdKQVLDEAVEKALQGASIWdEVKDRLYDSaigLSGGQQQRVCVARVLA 164
Cdd:cd03265 73 RRIGIVFQDLSVDDeLTGWENLYIHARLYGVP-GAERRERIDELLDFVGLL-EAADRLVKT---YSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038545162 165 TSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRISDKTGFFLDGDLI 226
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-204 |
3.87e-36 |
|
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: 128.12 E-value: 3.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 14 YYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDlnpevTTTGSVVYNGHNIyspRTDTVE-LRKEIGMVF 92
Cdd:cd03253 10 YDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYD-----VSSGSILIDGQDI---REVTLDsLRRAIGVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 93 QQPNPFPMTIYENVVYGlRINgikdkqVLDEAVEKALQGASIWDEVKdRL---YDSAIG-----LSGGQQQRVCVARVLA 164
Cdd:cd03253 82 QDTVLFNDTIGYNIRYG-RPD------ATDEEVIEAAKAAQIHDKIM-RFpdgYDTIVGerglkLSGGEKQRVAIARAIL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2038545162 165 TSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTMLLVT 204
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIA 193
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-249 |
4.32e-36 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 128.55 E-value: 4.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 1 MTDAILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdlnpEVTTTGSVVYNGHNIYSPRTD 80
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFL-----EKPSEGSIVVNGQTINLVRDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 81 TVEL-----------RKEIGMVFQQPNPFP-MTIYENVVYG-LRINGIKdKQVLDEAVEKALQGASIWDEVKDRLydsAI 147
Cdd:PRK10619 76 DGQLkvadknqlrllRTRLTMVFQHFNLWShMTVLENVMEApIQVLGLS-KQEARERAVKYLAKVGIDERAQGKY---PV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 148 GLSGGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDK-YTMLLVTRSMQQASRISDKTGFFLDGDLI 226
Cdd:PRK10619 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
|
250 260
....*....|....*....|...
gi 2038545162 227 EFNDTKQMFLDPQHKETEDYITG 249
Cdd:PRK10619 232 EEGAPEQLFGNPQSPRLQQFLKG 254
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
3-216 |
6.03e-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: 130.54 E-value: 6.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 3 DAILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdlnpEVTTTGSVVYNGHNIysprTDTV 82
Cdd:TIGR03265 2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGL-----ERQTAGTIYQGGRDI----TRLP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 83 ELRKEIGMVFQQPNPFP-MTIYENVVYGLRINGIKDKQVlDEAVEKALQGASIwDEVKDRlYDSAigLSGGQQQRVCVAR 161
Cdd:TIGR03265 73 PQKRDYGIVFQSYALFPnLTVADNIAYGLKNRGMGRAEV-AERVAELLDLVGL-PGSERK-YPGQ--LSGGQQQRVALAR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038545162 162 VLATSPKIILLDEPTSALDpisaGKIEETLYG-LKD-----KYTMLLVTRSMQQASRISDK 216
Cdd:TIGR03265 148 ALATSPGLLLLDEPLSALD----ARVREHLRTeIRQlqrrlGVTTIMVTHDQEEALSMADR 204
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-213 |
7.21e-36 |
|
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: 128.32 E-value: 7.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYY--NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPevtTTGSVVYNGHNIYSPRTdTVE 83
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLN--GLLLP---TSGKVTVDGLDTLDEEN-LWE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 84 LRKEIGMVFQQP-NPF-PMTIYENVVYGLRINGIKDKQVLdEAVEKALQGASIWDeVKDRlydSAIGLSGGQQQRVCVAR 161
Cdd:TIGR04520 75 IRKKVGMVFQNPdNQFvGATVEDDVAFGLENLGVPREEMR-KRVDEALKLVGMED-FRDR---EPHLLSGGQKQRVAIAG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2038545162 162 VLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQ---QASRI 213
Cdd:TIGR04520 150 VLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEeavLADRV 206
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
10-226 |
9.40e-36 |
|
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: 126.26 E-value: 9.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 10 DLSVYYNKKKALNSVSLSFQ-PKEITALIGPSGSGKSTLLKSLNrmGDLNPEVtttGSVVYNG-------HNIYSPRTDt 81
Cdd:cd03297 1 MLCVDIEKRLPDFTLKIDFDlNEEVTGIFGASGAGKSTLLRCIA--GLEKPDG---GTIVLNGtvlfdsrKKINLPPQQ- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 82 velRKeIGMVFQQPNPFP-MTIYENVVYGLRINGIKDKQVLDEAVEKALQgasiWDEVKDRlydSAIGLSGGQQQRVCVA 160
Cdd:cd03297 75 ---RK-IGLVFQQYALFPhLNVRENLAFGLKRKRNREDRISVDELLDLLG----LDHLLNR---YPAQLSGGEKQRVALA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038545162 161 RVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRISDKTGFFLDGDLI 226
Cdd:cd03297 144 RALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLniPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-247 |
1.08e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 126.79 E-value: 1.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKAlnSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPEvttTGSVVYNGHNIysprTDTVELR 85
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIA--GFLPPD---SGRILWNGQDL----TALPPAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 86 KEIGMVFQQPNPFP-MTIYENVVYGLRIN---GIKDKQVLDEAVEK-ALQGasiwdeVKDRLYDSaigLSGGQQQRVCVA 160
Cdd:COG3840 71 RPVSMLFQENNLFPhLTVAQNIGLGLRPGlklTAEQRAQVEQALERvGLAG------LLDRLPGQ---LSGGQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 161 RVLATSPKIILLDEPTSALDPisaGKIEETLYGLKD-----KYTMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQMF 235
Cdd:COG3840 142 RCLVRKRPILLLDEPFSALDP---ALRQEMLDLVDElcrerGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALL 218
|
250
....*....|..
gi 2038545162 236 LDPQHKETEDYI 247
Cdd:COG3840 219 DGEPPPALAAYL 230
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
20-181 |
1.64e-35 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 130.22 E-value: 1.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 20 ALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRmgdLNPevTTTGSVVYNGHNIYspRTDTVEL----RKEIGMVFQQ- 94
Cdd:COG4175 42 GVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNR---LIE--PTAGEVLIDGEDIT--KLSKKELrelrRKKMSMVFQHf 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 95 ---PNpfpMTIYENVVYGLRINGIkDKQVLDEAVEKALQ--GASIWdevKDRLYDSaigLSGGQQQRVCVARVLATSPKI 169
Cdd:COG4175 115 allPH---RTVLENVAFGLEIQGV-PKAERRERAREALElvGLAGW---EDSYPDE---LSGGMQQRVGLARALATDPDI 184
|
170
....*....|..
gi 2038545162 170 ILLDEPTSALDP 181
Cdd:COG4175 185 LLMDEAFSALDP 196
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-181 |
2.87e-35 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 124.90 E-value: 2.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPEVTTTGSVVYNGHNIYS-PrtdtVEL 84
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIA--GTLSPAFSASGEVLLNGRRLTAlP----AEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 85 RKeIGMVFQQPNPFP-MTIYENVVYGLRiNGIKdKQVLDEAVEKALQGASIwDEVKDRlyDSAIgLSGGQQQRVCVARVL 163
Cdd:COG4136 76 RR-IGILFQDDLLFPhLSVGENLAFALP-PTIG-RAQRRARVEQALEEAGL-AGFADR--DPAT-LSGGQRARVALLRAL 148
|
170
....*....|....*...
gi 2038545162 164 ATSPKIILLDEPTSALDP 181
Cdd:COG4136 149 LAEPRALLLDEPFSKLDA 166
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
10-213 |
2.98e-35 |
|
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: 125.81 E-value: 2.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 10 DLSVYYNKKK--ALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDLnpevtTTGSVVYNGHNIyspRTDTV-ELRK 86
Cdd:cd03251 5 NVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDV-----DSGRILIDGHDV---RDYTLaSLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 87 EIGMVFQQPNPFPMTIYENVVYGLRingikdkQVLDEAVEKALQGASIwDEVKDRL---YDSAIG-----LSGGQQQRVC 158
Cdd:cd03251 77 QIGLVSQDVFLFNDTVAENIAYGRP-------GATREEVEEAARAANA-HEFIMELpegYDTVIGergvkLSGGQRQRIA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2038545162 159 VARVLATSPKIILLDEPTSALDPISAGKIEETLYGL-KDKYTMLLVTR--SMQQASRI 213
Cdd:cd03251 149 IARALLKDPPILILDEATSALDTESERLVQAALERLmKNRTTFVIAHRlsTIENADRI 206
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-210 |
5.02e-35 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 125.74 E-value: 5.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 4 AILQVSDLSVYYNKKK----ALNSVSLSFQPKEITALIGPSGSGKSTLLkslNRM-GDLNPevtTTGSVVYNGHNIYSPR 78
Cdd:COG4525 2 SMLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLL---NLIaGFLAP---SSGEITLDGVPVTGPG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 79 TDtvelRkeiGMVFQQPNPFP-MTIYENVVYGLRINGIKDKQVLDEAVEK----ALQG---ASIWDevkdrlydsaigLS 150
Cdd:COG4525 76 AD----R---GVVFQKDALLPwLNVLDNVAFGLRLRGVPKAERRARAEELlalvGLADfarRRIWQ------------LS 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2038545162 151 GGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQA 210
Cdd:COG4525 137 GGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTgkGVFLITHSVEEA 198
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
13-217 |
1.08e-34 |
|
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: 123.67 E-value: 1.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 13 VYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdlnpEVTTTGSVVYNGHNIYS-PRTDTVELRKEIGMV 91
Cdd:cd03292 9 TYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKE-----ELPTSGTIRVNGQDVSDlRGRAIPYLRRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 92 FQQPNPFP-MTIYENVVYGLRINGIKDKQVlDEAVEKALQGASIwdevKDRLYDSAIGLSGGQQQRVCVARVLATSPKII 170
Cdd:cd03292 84 FQDFRLLPdRNVYENVAFALEVTGVPPREI-RKRVPAALELVGL----SHKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2038545162 171 LLDEPTSALDPISAGKIEETLYGLKDKYTMLLVTrsmQQASRISDKT 217
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA---THAKELVDTT 202
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-181 |
2.03e-34 |
|
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: 122.69 E-value: 2.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKeITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHniySPRTDTVELR 85
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRIL--ATLTPP---SSGTIRIDGQ---DVLKQPQKLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 86 KEIGMVFQQPNPFP-MTIYENVVYGLRINGIKDKQVlDEAVEKALQGASIWDEVKDRLYdsaiGLSGGQQQRVCVARVLA 164
Cdd:cd03264 72 RRIGYLPQEFGVYPnFTVREFLDYIAWLKGIPSKEV-KARVDEVLELVNLGDRAKKKIG----SLSGGMRRRVGIAQALV 146
|
170
....*....|....*..
gi 2038545162 165 TSPKIILLDEPTSALDP 181
Cdd:cd03264 147 GDPSILIVDEPTAGLDP 163
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-204 |
3.66e-34 |
|
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: 122.31 E-value: 3.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYN--KKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNIYspRTDTVE 83
Cdd:cd03245 3 IEFRNVSFSYPnqEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLL--AGLYKP---TSGSVLLDGTDIR--QLDPAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 84 LRKEIGMVFQQPNPFPMTIYENVVYGLRIngikdkqVLDEAVEKALQGASIWDEVKD--RLYDSAIG-----LSGGQQQR 156
Cdd:cd03245 76 LRRNIGYVPQDVTLFYGTLRDNITLGAPL-------ADDERILRAAELAGVTDFVNKhpNGLDLQIGergrgLSGGQRQA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2038545162 157 VCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTMLLVT 204
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIIT 196
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
14-204 |
5.16e-34 |
|
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: 120.99 E-value: 5.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 14 YYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPevtTTGSVVYNGHNIYSPRTDTVELRKEIGMVFQ 93
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLN--GLLRP---QSGAVLIDGEPLDYSRKGLLERRQRVGLVFQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 94 QPNP--FPMTIYENVVYGLRINGIKDKQVlDEAVEKALQGASIwDEVKDRLYDSaigLSGGQQQRVCVARVLATSPKIIL 171
Cdd:TIGR01166 76 DPDDqlFAADVDQDVAFGPLNLGLSEAEV-ERRVREALTAVGA-SGLRERPTHC---LSGGEKKRVAIAGAVAMRPDVLL 150
|
170 180 190
....*....|....*....|....*....|...
gi 2038545162 172 LDEPTSALDPISAGKIEETLYGLKDKYTMLLVT 204
Cdd:TIGR01166 151 LDEPTAGLDPAGREQMLAILRRLRAEGMTVVIS 183
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-223 |
1.32e-33 |
|
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: 121.19 E-value: 1.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdlnpEVTTTGSVVYNGHNIysprTDTVELR 85
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGF-----ETPTSGEILLDGKDI----TNLPPHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 86 KEIGMVFQQPNPFP-MTIYENVVYGLRINGIkDKQVLDEAVEKALQGASIwDEVKDRLYDSaigLSGGQQQRVCVARVLA 164
Cdd:cd03300 72 RPVNTVFQNYALFPhLTVFENIAFGLRLKKL-PKAEIKERVAEALDLVQL-EGYANRKPSQ---LSGGQQQRVAIARALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038545162 165 TSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRISDKTGFFLDG 223
Cdd:cd03300 147 NEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELgiTFVFVTHDQEEALTMSDRIAVMNKG 207
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
20-204 |
2.05e-33 |
|
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: 120.43 E-value: 2.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 20 ALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNIYS-PRTDTVELRKEIGMVFQQPNPF 98
Cdd:TIGR02673 17 ALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLL--YGALTP---SRGQVRIAGEDVNRlRGRQLPLLRRRIGVVFQDFRLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 99 P-MTIYENVVYGLRINGIKdKQVLDEAVEKALQgasiWDEVKDRLYDSAIGLSGGQQQRVCVARVLATSPKIILLDEPTS 177
Cdd:TIGR02673 92 PdRTVYENVALPLEVRGKK-EREIQRRVGAALR----QVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTG 166
|
170 180
....*....|....*....|....*..
gi 2038545162 178 ALDPISAGKIEETLYGLKDKYTMLLVT 204
Cdd:TIGR02673 167 NLDPDLSERILDLLKRLNKRGTTVIVA 193
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-223 |
2.41e-33 |
|
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: 120.05 E-value: 2.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdlnpEVTTTGSVVYNGHNIysprTDTVELR 85
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGL-----EEPTSGRIYIGGRDV----TDLPPKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 86 KEIGMVFQQPNPFP-MTIYENVVYGLRINGIkDKQVLDEAVEKALQGASIwDEVKDRLYDSaigLSGGQQQRVCVARVLA 164
Cdd:cd03301 72 RDIAMVFQNYALYPhMTVYDNIAFGLKLRKV-PKDEIDERVREVAELLQI-EHLLDRKPKQ---LSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038545162 165 TSPKIILLDEPTSALDpisAGKIEETLYGLKD-----KYTMLLVTRSMQQASRISDKTGFFLDG 223
Cdd:cd03301 147 REPKVFLMDEPLSNLD---AKLRVQMRAELKRlqqrlGTTTIYVTHDQVEAMTMADRIAVMNDG 207
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
5-226 |
3.10e-33 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 120.89 E-value: 3.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdLNPEvttTGSVVYNGHNI--YSPRtdtv 82
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARL--LTPQ---SGTVFLGDKPIsmLSSR---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 83 ELRKEIGMVFQQ-PNPFPMTIYENVVYGL--------RINGiKDKQVldeaVEKALQGASIwDEVKDRLYDSaigLSGGQ 153
Cdd:PRK11231 73 QLARRLALLPQHhLTPEGITVRELVAYGRspwlslwgRLSA-EDNAR----VNQAMEQTRI-NHLADRRLTD---LSGGQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038545162 154 QQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDK-YTMLLVTRSMQQASRISDKTGFFLDGDLI 226
Cdd:PRK11231 144 RQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQgKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-191 |
3.26e-33 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 119.51 E-value: 3.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 4 AILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNIyspRTDTVE 83
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRIL--AGLLPP---SAGEVLWNGEPI---RDARED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 84 LRKEIGMVFQQPNPFP-MTIYENVVYGLRINGIkdkQVLDEAVEKALQGASIwdevkDRLYDSAIG-LSGGQQQRVCVAR 161
Cdd:COG4133 73 YRRRLAYLGHADGLKPeLTVRENLRFWAALYGL---RADREAIDEALEAVGL-----AGLADLPVRqLSAGQKRRVALAR 144
|
170 180 190
....*....|....*....|....*....|
gi 2038545162 162 VLATSPKIILLDEPTSALDPISAGKIEETL 191
Cdd:COG4133 145 LLLSPAPLWLLDEPFTALDAAGVALLAELI 174
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-239 |
4.86e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 120.95 E-value: 4.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYYNK-KKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPevtTTGSVVYNGHNIYSPRTDTVE 83
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFN--GILKP---TSGEVLIKGEPIKYDKKSLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 84 LRKEIGMVFQQPNP--FPMTIYENVVYGLRINGIKDKQVlDEAVEKALQGASIWDEVKDRLYDsaigLSGGQQQRVCVAR 161
Cdd:PRK13639 76 VRKTVGIVFQNPDDqlFAPTVEEDVAFGPLNLGLSKEEV-EKRVKEALKAVGMEGFENKPPHH----LSGGQKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038545162 162 VLATSPKIILLDEPTSALDPISAGKIEETLYGLKDK-YTMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQMFLDPQ 239
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEgITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-239 |
8.88e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 120.23 E-value: 8.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 3 DAILQVSDLSVYY-NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPE---VTTTGSVVyNGHNIYspr 78
Cdd:PRK13647 2 DNIIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLN--GIYLPQrgrVKVMGREV-NAENEK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 79 tdtvELRKEIGMVFQQPNP--FPMTIYENVVYGLRINGIKDKQVlDEAVEKALQGASIWDeVKDRlydSAIGLSGGQQQR 156
Cdd:PRK13647 76 ----WVRSKVGLVFQDPDDqvFSSTVWDDVAFGPVNMGLDKDEV-ERRVEEALKAVRMWD-FRDK---PPYHLSYGQKKR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 157 VCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGL-KDKYTMLLVTRSMQQASRISDKTGFFLDGDLIEFNDtKQMF 235
Cdd:PRK13647 147 VAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGD-KSLL 225
|
....
gi 2038545162 236 LDPQ 239
Cdd:PRK13647 226 TDED 229
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
6-231 |
1.52e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 120.58 E-value: 1.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKK-----KALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdLNPEvttTGSVVYNGHN------- 73
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNAL--LLPD---TGTIEWIFKDeknkkkt 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 74 -----------IYSPRTDTV----ELRKEIGMVFQ--QPNPFPMTIYENVVYGLRINGIKDKqvldEAVEKALQGASIWD 136
Cdd:PRK13651 78 kekekvleklvIQKTRFKKIkkikEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKE----EAKKRAAKYIELVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 137 EVKDRLYDSAIGLSGGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDK-YTMLLVTRSMQQASRISD 215
Cdd:PRK13651 154 LDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVLEWTK 233
|
250
....*....|....*.
gi 2038545162 216 KTGFFLDGDLIEFNDT 231
Cdd:PRK13651 234 RTIFFKDGKIIKDGDT 249
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-212 |
1.68e-32 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 118.31 E-value: 1.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 1 MTDAILQVSDLSVYYNKKKA----LNSVSLSFQPKEITALIGPSGSGKSTLLkSLnrMGDLnpEVTTTGSVVYNGHNIYS 76
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGeltiLKGISLEVEAGESVAIVGASGSGKSTLL-GL--LAGL--DRPTSGTVRLAGQDLFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 77 ----PRTdtvELRKE-IGMVFQQ----PNpfpMTIYENVVYGLRINGIKDkqvldeavekALQGASIW-DEV--KDRLYD 144
Cdd:COG4181 79 ldedARA---RLRARhVGFVFQSfqllPT---LTALENVMLPLELAGRRD----------ARARARALlERVglGHRLDH 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 145 SAIGLSGGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASR 212
Cdd:COG4181 143 YPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgtTLVLVTHDPALAAR 212
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
18-239 |
4.94e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 118.58 E-value: 4.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 18 KKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPevtTTGSVVYNGHNIySPRTDTVEL---RKEIGMVFQQ 94
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLN--GLLQP---TSGTVTIGERVI-TAGKKNKKLkplRKKVGIVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 95 PNP--FPMTIYENVVYGLRINGIKDKQVLDEAvEKALQGASIWDEVKDRlydSAIGLSGGQQQRVCVARVLATSPKIILL 172
Cdd:PRK13634 94 PEHqlFEETVEKDICFGPMNFGVSEEDAKQKA-REMIELVGLPEELLAR---SPFELSGGQMRRVAIAGVLAMEPEVLVL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038545162 173 DEPTSALDPISAGKIEETLYGL-KDK-YTMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQMFLDPQ 239
Cdd:PRK13634 170 DEPTAGLDPKGRKEMMEMFYKLhKEKgLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-237 |
1.05e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 117.64 E-value: 1.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 1 MTDAILQVSDLSVYY-NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPevtTTGSVVYNGHNIYSPRT 79
Cdd:PRK13636 1 MEDYILKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLN--GILKP---SSGRILFDGKPIDYSRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 80 DTVELRKEIGMVFQQPNP--FPMTIYENVVYGLRINGIKDKQVlDEAVEKALQGASIwDEVKDRlydSAIGLSGGQQQRV 157
Cdd:PRK13636 76 GLMKLRESVGMVFQDPDNqlFSASVYQDVSFGAVNLKLPEDEV-RKRVDNALKRTGI-EHLKDK---PTHCLSFGQKKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 158 CVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQMF 235
Cdd:PRK13636 151 AIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
..
gi 2038545162 236 LD 237
Cdd:PRK13636 231 AE 232
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
17-211 |
1.31e-31 |
|
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: 114.96 E-value: 1.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 17 KKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEvTTTGSVVYNGHNIYSPrtdtvELRKEIGMVFQQPN 96
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNAL--AGRRTGL-GVSGEVLINGRPLDKR-----SFRKIIGYVPQDDI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 97 PFP-MTIYENVVYGLRINGIkdkqvldeavekalqgasiwdevkdrlydsaiglSGGQQQRVCVARVLATSPKIILLDEP 175
Cdd:cd03213 93 LHPtLTVRETLMFAAKLRGL----------------------------------SGGERKRVSIALELVSNPSLLFLDEP 138
|
170 180 190
....*....|....*....|....*....|....*.
gi 2038545162 176 TSALDPISAGKIEETLYGLKDKYTMLLVTrsMQQAS 211
Cdd:cd03213 139 TSGLDSSSALQVMSLLRRLADTGRTIICS--IHQPS 172
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-213 |
1.50e-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: 116.03 E-value: 1.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 3 DAILQVSDLSVYYNKKKA---LNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDLnpevtTTGSVVYNGHNIysPRT 79
Cdd:cd03248 9 KGIVKFQNVTFAYPTRPDtlvLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQP-----QGGQVLLDGKPI--SQY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 80 DTVELRKEIGMVFQQPNPFPMTIYENVVYGLringikdKQVLDEAVEKALQGASIWDEVKD--RLYDSAIG-----LSGG 152
Cdd:cd03248 82 EHKYLHSKVSLVGQEPVLFARSLQDNIAYGL-------QSCSFECVKEAAQKAHAHSFISElaSGYDTEVGekgsqLSGG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038545162 153 QQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTMLLVT---RSMQQASRI 213
Cdd:cd03248 155 QKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAhrlSTVERADQI 218
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
14-234 |
2.16e-31 |
|
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: 117.49 E-value: 2.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 14 YYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdLNPevtTTGSVVYNGHNIYS-PRtdtvELRKEIGMVF 92
Cdd:TIGR01188 2 VYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTL--LRP---TSGTARVAGYDVVRePR----KVRRSIGIVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 93 QQPNPFP-MTIYENVVYGLRINGIKdKQVLDEAVEKALQGASIWDEVKDRLYdsaiGLSGGQQQRVCVARVLATSPKIIL 171
Cdd:TIGR01188 73 QYASVDEdLTGRENLEMMGRLYGLP-KDEAEERAEELLELFELGEAADRPVG----TYSGGMRRRLDIAASLIHQPDVLF 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038545162 172 LDEPTSALDPISAGKIEETLYGLKD-KYTMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQM 234
Cdd:TIGR01188 148 LDEPTTGLDPRTRRAIWDYIRALKEeGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-206 |
3.09e-31 |
|
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: 120.54 E-value: 3.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYY-NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEvttTGSVVYNGHNIYSPRTDtvEL 84
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATL--AGLLDPL---QGEVTLDGVPVSSLDQD--EV 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 85 RKEIGMVFQQPNPFPMTIYENvvygLRInGIKDkqVLDEAVEKALQGASIWDEVKDRL--YDSAIG-----LSGGQQQRV 157
Cdd:TIGR02868 408 RRRVSVCAQDAHLFDTTVREN----LRL-ARPD--ATDEELWAALERVGLADWLRALPdgLDTVLGeggarLSGGERQRL 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2038545162 158 CVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTMLLVTRS 206
Cdd:TIGR02868 481 ALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-238 |
3.66e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 117.26 E-value: 3.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 3 DAILQVSDLSVYYNKK-----KALNSVSLSFQPKEITALIGPSGSGKSTLLKSLN-----RMGDLNPEVTTTGSVVYNGH 72
Cdd:PRK13631 19 DIILRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNgliksKYGTIQVGDIYIGDKKNNHE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 73 NIYSPRTDTV----ELRKEIGMVFQQP--NPFPMTIYENVVYGLRINGIKDkqvlDEAVEKA---LQGASIWDEVKDRly 143
Cdd:PRK13631 99 LITNPYSKKIknfkELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKK----SEAKKLAkfyLNKMGLDDSYLER-- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 144 dSAIGLSGGQQQRVCVARVLATSPKIILLDEPTSALDPisAGK---IEETLYGLKDKYTMLLVTRSMQQASRISDKTGFF 220
Cdd:PRK13631 173 -SPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDP--KGEhemMQLILDAKANNKTVFVITHTMEHVLEVADEVIVM 249
|
250
....*....|....*...
gi 2038545162 221 LDGDLIEFNDTKQMFLDP 238
Cdd:PRK13631 250 DKGKILKTGTPYEIFTDQ 267
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
6-208 |
4.22e-31 |
|
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: 120.74 E-value: 4.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYY--NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNIyspRT-DTV 82
Cdd:TIGR03375 464 IEFRNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLL--LGLYQP---TEGSVLLDGVDI---RQiDPA 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 83 ELRKEIGMVFQQPNPFPMTIYENVVYGlringikDKQVLDEAVEKALQGASIwDEVKDRL---YDSAIG-----LSGGQQ 154
Cdd:TIGR03375 536 DLRRNIGYVPQDPRLFYGTLRDNIALG-------APYADDEEILRAAELAGV-TEFVRRHpdgLDMQIGergrsLSGGQR 607
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2038545162 155 QRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTMLLVTRSMQ 208
Cdd:TIGR03375 608 QAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHRTS 661
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
6-215 |
4.81e-31 |
|
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: 114.54 E-value: 4.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNIySPRTDTVELR 85
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTL--MGLLPV---KSGSIRLDGEDI-TKLPPHERAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 86 KEIGMVFQQPNPFP-MTIYENVVYGLRINGIKDKQVLDEAVE--KALQgasiwdEVKDRLydsAIGLSGGQQQRVCVARV 162
Cdd:TIGR03410 75 AGIAYVPQGREIFPrLTVEENLLTGLAALPRRSRKIPDEIYElfPVLK------EMLGRR---GGDLSGGQQQQLAIARA 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2038545162 163 LATSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTM--LLVTRSMQQASRISD 215
Cdd:TIGR03410 146 LVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMaiLLVEQYLDFARELAD 200
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-223 |
6.88e-31 |
|
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: 113.74 E-value: 6.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 25 SLSFQPKEITALIGPSGSGKSTLLkslNRMGDLnpEVTTTGSVVYNGHNI-YSPRTDtvelrKEIGMVFQQPNPFP-MTI 102
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLL---NLIAGF--ETPQSGRVLINGVDVtAAPPAD-----RPVSMLFQENNLFAhLTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 103 YENVVYGlRINGIKDKQVLDEAVEKALQGASIwDEVKDRLYDSaigLSGGQQQRVCVARVLATSPKIILLDEPTSALDPI 182
Cdd:cd03298 88 EQNVGLG-LSPGLKLTAEDRQAIEVALARVGL-AGLEKRLPGE---LSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2038545162 183 SAGKIEETLYGL--KDKYTMLLVTRSMQQASRISDKTGFFLDG 223
Cdd:cd03298 163 LRAEMLDLVLDLhaETKMTVLMVTHQPEDAKRLAQRVVFLDNG 205
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-204 |
1.58e-30 |
|
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: 113.64 E-value: 1.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 3 DAILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPevtTTGSVVY-----NGhniysp 77
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLIT--GDLPP---TYGNDVRlfgerRG------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 78 RTDTVELRKEIGMV---FQQPNPFPMTIyENVVyglrINGIKD-----KQVLDEAVEKALQGASIW--DEVKDRLYDSai 147
Cdd:COG1119 70 GEDVWELRKRIGLVspaLQLRFPRDETV-LDVV----LSGFFDsiglyREPTDEQRERARELLELLglAHLADRPFGT-- 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2038545162 148 gLSGGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGL--KDKYTMLLVT 204
Cdd:COG1119 143 -LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaaEGAPTLVLVT 200
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
36-238 |
1.95e-30 |
|
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: 115.28 E-value: 1.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 36 LIGPSGSGKSTLLKSLNRMgdlnpEVTTTGSVVYNGHNIysprTDTVELRKEIGMVFQQPNPFP-MTIYENVVYGLRING 114
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGF-----EQPDSGSIMLDGEDV----TNVPPHLRHINMVFQSYALFPhMTVEENVAFGLKMRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 115 IkDKQVLDEAVEKALQGASIWDEVKDRlydsAIGLSGGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGL 194
Cdd:TIGR01187 72 V-PRAEIKPRVLEALRLVQLEEFADRK----PHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTI 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2038545162 195 KDKY--TMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQMFLDP 238
Cdd:TIGR01187 147 QEQLgiTFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEP 192
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
17-225 |
2.82e-30 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 112.12 E-value: 2.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 17 KKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDLNpevttTGSVVYNGHNI----YSPRtdtVELRKE-IGMV 91
Cdd:NF038007 17 KTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLD-----SGSLTLAGKEVtnlsYSQK---IILRRElIGYI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 92 FQQPNPFP-MTIYENVVYGLRINGIKDKqvldEAVEKALQGASIWDeVKDRLYDSAIGLSGGQQQRVCVARVLATSPKII 170
Cdd:NF038007 89 FQSFNLIPhLSIFDNVALPLKYRGVAKK----ERIERVNQVLNLFG-IDNRRNHKPMQLSGGQQQRVAIARAMVSNPALL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2038545162 171 LLDEPTSALDPISAGKIEETLYGLKDK-YTMLLVTRSmQQASRISDKTGFFLDGDL 225
Cdd:NF038007 164 LADEPTGNLDSKNARAVLQQLKYINQKgTTIIMVTHS-DEASTYGNRIINMKDGKL 218
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-227 |
5.32e-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: 5.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYY--NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEvttTGSVVYNGHNIYSPRTdtvE 83
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLL--TGDLKPQ---QGEITLDGVPVSDLEK---A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 84 LRKEIGMVFQQPNPFPMTIYENVvyGLRingikdkqvldeavekalqgasiwdevkdrlydsaigLSGGQQQRVCVARVL 163
Cdd:cd03247 73 LSSLISVLNQRPYLFDTTLRNNL--GRR-------------------------------------FSGGERQRLALARIL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2038545162 164 ATSPKIILLDEPTSALDPISAGKIEETLYG-LKDKyTMLLVTRSMQQASRIsDKTGFFLDGDLIE 227
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDPITERQLLSLIFEvLKDK-TLIWITHHLTGIEHM-DKILFLENGKIIM 176
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-227 |
5.47e-30 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 111.93 E-value: 5.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 14 YYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdLNPEvttTGSVVYNGHNIYSprTDTVELRKEIGMVFQ 93
Cdd:cd03254 12 YDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRF--YDPQ---KGQILIDGIDIRD--ISRKSLRSMIGVVLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 94 QPNPFPMTIYENVVYGLRINGikdkqvlDEAVEKALQGASIWDEVKDRL--YDSAIG-----LSGGQQQRVCVARVLATS 166
Cdd:cd03254 85 DTFLFSGTIMENIRLGRPNAT-------DEEVIEAAKEAGAHDFIMKLPngYDTVLGenggnLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038545162 167 PKIILLDEPTSALDPISAGKIEETLYGLKDKYTMLLVtrsmqqASRIS-----DKTGFFLDGDLIE 227
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKGRTSIII------AHRLStiknaDKILVLDDGKIIE 217
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
8-213 |
8.57e-30 |
|
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: 110.78 E-value: 8.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 8 VSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLkslNRMGDLnpEVTTTGSVVYNGHNIYSPRTDTVE--LR 85
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLL---NIIGLL--EKFDSGQVYLNGQETPPLNSKKASkfRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 86 KEIGMVFQQpnpFPM----TIYENVVYGLrINGIKDKQVLDEAVEKALQGASIWDEVKDRLYDsaigLSGGQQQRVCVAR 161
Cdd:TIGR03608 76 EKLGYLFQN---FALieneTVEENLDLGL-KYKKLSKKEKREKKKEALEKVGLNLKLKQKIYE----LSGGEQQRVALAR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2038545162 162 VLATSPKIILLDEPTSALDPISAGKIEETLYGLKDK-YTMLLVTRSM---QQASRI 213
Cdd:TIGR03608 148 AILKPPPLILADEPTGSLDPKNRDEVLDLLLELNDEgKTIIIVTHDPevaKQADRV 203
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
6-237 |
1.59e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 112.18 E-value: 1.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNK-----KKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPevtTTGSVVYNGHNIYSPRTD 80
Cdd:PRK13646 3 IRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNIN--ALLKP---TTGTVTVDDITITHKTKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 81 TV--ELRKEIGMVFQQPNP--FPMTIYENVVYGLRINGIKDKQVLDEAVEKALQ-GASiwdevKDRLYDSAIGLSGGQQQ 155
Cdd:PRK13646 78 KYirPVRKRIGMVFQFPESqlFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDlGFS-----RDVMSQSPFQMSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 156 RVCVARVLATSPKIILLDEPTSALDPISAGKIEETL--YGLKDKYTMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQ 233
Cdd:PRK13646 153 KIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLksLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKE 232
|
....
gi 2038545162 234 MFLD 237
Cdd:PRK13646 233 LFKD 236
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-181 |
1.97e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 115.12 E-value: 1.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 2 TDAILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNiYSPRTDT 81
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKIL--SGVYQP---DSGEILLDGEP-VRFRSPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 82 VELRKEIGMVFQQPNPFP-MTIYENVVYG--LRINGIKDKQVLDEAVEKALQ--GASI--WDEVKDrlydsaigLSGGQQ 154
Cdd:COG1129 75 DAQAAGIAIIHQELNLVPnLSVAENIFLGrePRRGGLIDWRAMRRRARELLArlGLDIdpDTPVGD--------LSVAQQ 146
|
170 180
....*....|....*....|....*..
gi 2038545162 155 QRVCVARVLATSPKIILLDEPTSALDP 181
Cdd:COG1129 147 QLVEIARALSRDARVLILDEPTASLTE 173
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-192 |
4.72e-29 |
|
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: 109.12 E-value: 4.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYY--NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDLnpevtTTGSVVYNGHNIYS-PRTDtv 82
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVEL-----SSGSILIDGVDISKiGLHD-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 83 eLRKEIGMVFQQPNPFPMTIYENvvygLRINGIKDkqvlDEAVEKALQGASIWDEVK-------DRLYDSAIGLSGGQQQ 155
Cdd:cd03244 76 -LRSRISIIPQDPVLFSGTIRSN----LDPFGEYS----DEELWQALERVGLKEFVEslpggldTVVEEGGENLSVGQRQ 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 2038545162 156 RVCVARVLATSPKIILLDEPTSALDPISAGKIEETLY 192
Cdd:cd03244 147 LLCLARALLRKSKILVLDEATASVDPETDALIQKTIR 183
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-239 |
5.62e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 110.69 E-value: 5.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 17 KKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPevtTTGSVVYNGHNIySPRTDTV---ELRKEIGMVFQ 93
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFN--ALLKP---SSGTITIAGYHI-TPETGNKnlkKLRKKVSLVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 94 QPNP--FPMTIYENVVYGLRINGIKDkqvlDEAVEKALQ---GASIWDEVKDRlydSAIGLSGGQQQRVCVARVLATSPK 168
Cdd:PRK13641 93 FPEAqlFENTVLKDVEFGPKNFGFSE----DEAKEKALKwlkKVGLSEDLISK---SPFELSGGQMRRVAIAGVMAYEPE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2038545162 169 IILLDEPTSALDPISAGKIEETLYGL-KDKYTMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQMFLDPQ 239
Cdd:PRK13641 166 ILCLDEPAAGLDPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
14-227 |
9.47e-29 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 113.90 E-value: 9.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 14 YYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDlnPevtTTGSVVYNGHNIyspRTDTVE-LRKEIGMVF 92
Cdd:PRK13657 344 YDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFD--P---QSGRILIDGTDI---RTVTRAsLRRNIAVVF 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 93 QQPNPFPMTIYENvvygLRInGIKDKQvlDEAVEKALQGASIWD--EVKDRLYDSAIG-----LSGGQQQRVCVARVLAT 165
Cdd:PRK13657 416 QDAGLFNRSIEDN----IRV-GRPDAT--DEEMRAAAERAQAHDfiERKPDGYDTVVGergrqLSGGERQRLAIARALLK 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038545162 166 SPKIILLDEPTSALDPISAGKIEETLYGL-KDKYTMLLVTR--SMQQASRIsdktgFFLD-GDLIE 227
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVKAALDELmKGRTTFIIAHRlsTVRNADRI-----LVFDnGRVVE 549
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
7-226 |
1.09e-28 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 107.73 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 7 QVSDLSVYYNKK-KALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNIySPRtdtvELR 85
Cdd:cd03226 1 RIENISFSYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKIL--AGLIKE---SSGSILLNGKPI-KAK----ERR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 86 KEIGMVFQQPNP--FPMTIYENVVYGLringiKDKQVLDEAVEKALQGASIWDEvKDRLYDSaigLSGGQQQRVCVARVL 163
Cdd:cd03226 71 KSIGYVMQDVDYqlFTDSVREELLLGL-----KELDAGNEQAETVLKDLDLYAL-KERHPLS---LSGGQKQRLAIAAAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038545162 164 ATSPKIILLDEPTSALDPISAGKIEETLYGL-KDKYTMLLVTRSMQQASRISDKTGFFLDGDLI 226
Cdd:cd03226 142 LSGKDLLIFDEPTSGLDYKNMERVGELIRELaAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
19-213 |
1.15e-28 |
|
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: 113.66 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 19 KALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDlnpevTTTGSVVYNGHNIYSPRTDtvELRKEIGMVFQQPNPF 98
Cdd:TIGR02203 346 PALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYE-----PDSGQILLDGHDLADYTLA--SLRRQVALVSQDVVLF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 99 PMTIYENVVYGLRingikdKQVLDEAVEKALQGASIWDEVkDRL---YDSAIG-----LSGGQQQRVCVARVLATSPKII 170
Cdd:TIGR02203 419 NDTIANNIAYGRT------EQADRAEIERALAAAYAQDFV-DKLplgLDTPIGengvlLSGGQRQRLAIARALLKDAPIL 491
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2038545162 171 LLDEPTSALDPISAGKIEETLYGLKDKYTMLLVTR---SMQQASRI 213
Cdd:TIGR02203 492 ILDEATSALDNESERLVQAALERLMQGRTTLVIAHrlsTIEKADRI 537
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-215 |
1.19e-28 |
|
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: 110.96 E-value: 1.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 24 VSLSFQPKEITALIGPSGSGKSTLLkslnRM--GDLNPEvttTGSVVYNGHNIYSPRTDT---VELRKeIGMVFQQPNPF 98
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLL----RAiaGLERPD---SGRIRLGGEVLQDSARGIflpPHRRR-IGYVFQEARLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 99 P-MTIYENVVYGL-RINGIKDKQVLDEAVEkaLQGasIwdevkDRLYDSAIG-LSGGQQQRVCVARVLATSPKIILLDEP 175
Cdd:COG4148 90 PhLSVRGNLLYGRkRAPRAERRISFDEVVE--LLG--I-----GHLLDRRPAtLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2038545162 176 TSALDPISAGKIEETLYGLKDKYT--MLLVTRSMQQASRISD 215
Cdd:COG4148 161 LAALDLARKAEILPYLERLRDELDipILYVSHSLDEVARLAD 202
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-236 |
2.10e-28 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 108.04 E-value: 2.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 1 MTDAILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDlnPEvTTTGSVVYNGHNIYSPRTD 80
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTL--CGD--PR-ATSGRIVFDGKDITDWQTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 81 TVeLRKEIGMVFQQPNPFP-MTIYENVVYGlriNGIKDKQVLDEAVEKALQgasIWDEVKDRLYDSAIGLSGGQQQRVCV 159
Cdd:PRK11614 76 KI-MREAVAIVPEGRRVFSrMTVEENLAMG---GFFAERDQFQERIKWVYE---LFPRLHERRIQRAGTMSGGEQQMLAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038545162 160 ARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDK-YTMLLVTRSMQQASRISDKtGFFLDGDLIEFNDTKQMFL 236
Cdd:PRK11614 149 GRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQgMTIFLVEQNANQALKLADR-GYVLENGHVVLEDTGDALL 225
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-180 |
3.56e-28 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 110.04 E-value: 3.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 1 MTDAILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdlnpEVTTTGSVVYNGHNIysprTD 80
Cdd:PRK09452 10 SLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGF-----ETPDSGRIMLDGQDI----TH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 81 TVELRKEIGMVFQQPNPFP-MTIYENVVYGLRINGIKDKQVlDEAVEKALQGASIwDEVKDRlydSAIGLSGGQQQRVCV 159
Cdd:PRK09452 81 VPAENRHVNTVFQSYALFPhMTVFENVAFGLRMQKTPAAEI-TPRVMEALRMVQL-EEFAQR---KPHQLSGGQQQRVAI 155
|
170 180
....*....|....*....|.
gi 2038545162 160 ARVLATSPKIILLDEPTSALD 180
Cdd:PRK09452 156 ARAVVNKPKVLLLDESLSALD 176
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
5-214 |
4.01e-28 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 107.21 E-value: 4.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYYNKKK----ALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrmGDLnpEVTTTGSVVYNGHNIYS-PRT 79
Cdd:PRK11629 5 LLQCDNLCKRYQEGSvqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLL---GGL--DTPTSGDVIFNGQPMSKlSSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 80 DTVELR-KEIGMVFQQPNPFP-MTIYENVVYGLRINGIKDKQVLDEAVEkALQGASIWDEVKDRLYDsaigLSGGQQQRV 157
Cdd:PRK11629 80 AKAELRnQKLGFIYQFHHLLPdFTALENVAMPLLIGKKKPAEINSRALE-MLAAVGLEHRANHRPSE----LSGGERQRV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2038545162 158 CVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRIS 214
Cdd:PRK11629 155 AIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQgtAFLVVTHDLQLAKRMS 213
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-204 |
5.97e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 111.48 E-value: 5.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVY-YNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEvtttGSVVYNGhniysprtdtVEL 84
Cdd:PRK11174 350 IEAEDLEILsPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNAL--LGFLPYQ----GSLKING----------IEL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 85 --------RKEIGMVFQQPNPFPMTIYENVVYGlringikDKQVLDEAVEKALQGASIWDEVkDRLY--------DSAIG 148
Cdd:PRK11174 414 reldpeswRKHLSWVGQNPQLPHGTLRDNVLLG-------NPDASDEQLQQALENAWVSEFL-PLLPqgldtpigDQAAG 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2038545162 149 LSGGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTMLLVT 204
Cdd:PRK11174 486 LSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVT 541
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-244 |
6.06e-28 |
|
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: 107.22 E-value: 6.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 4 AILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPEvttTGSVVY-----NGHNIYS-P 77
Cdd:TIGR02323 2 PLLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLA--GRLAPD---HGTATYimrsgAELELYQlS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 78 RTDTVEL-RKEIGMVFQQP-NPFPMTIYENVVYGLRINGIKDKQV--LDEAVEKALQGASIwdeVKDRLYDSAIGLSGGQ 153
Cdd:TIGR02323 77 EAERRRLmRTEWGFVHQNPrDGLRMRVSAGANIGERLMAIGARHYgnIRATAQDWLEEVEI---DPTRIDDLPRAFSGGM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 154 QQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRISDKTGFFLDGDLIEFNDT 231
Cdd:TIGR02323 154 QQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLglAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLT 233
|
250
....*....|...
gi 2038545162 232 KQMFLDPQHKETE 244
Cdd:TIGR02323 234 DQVLDDPQHPYTQ 246
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-216 |
6.22e-28 |
|
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: 104.43 E-value: 6.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGH--NIYSPRtDTVE 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKIL--SGLYKP---DSGEILVDGKevSFASPR-DARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 84 LRkeIGMVFQqpnpfpmtiyenvvyglringikdkqvldeavekalqgasiwdevkdrlydsaigLSGGQQQRVCVARVL 163
Cdd:cd03216 75 AG--IAMVYQ-------------------------------------------------------LSVGERQMVEIARAL 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2038545162 164 ATSPKIILLDEPTSALDPISAGKIEETLYGLKDK-YTMLLVTRSMQQASRISDK 216
Cdd:cd03216 98 ARNARLLILDEPTAALTPAEVERLFKVIRRLRAQgVAVIFISHRLDEVFEIADR 151
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
13-231 |
6.70e-28 |
|
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: 106.10 E-value: 6.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 13 VYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNIysprTDTVELRKEIGMVF 92
Cdd:TIGR01277 6 VRYEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLI--AGFIEP---ASGSIKVNDQSH----TGLAPYQRPVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 93 QQPNPFP-MTIYENVVYGLRiNGIKDKQVLDEAVEKALQGASIwDEVKDRLYDSaigLSGGQQQRVCVARVLATSPKIIL 171
Cdd:TIGR01277 77 QENNLFAhLTVRQNIGLGLH-PGLKLNAEQQEKVVDAAQQVGI-ADYLDRLPEQ---LSGGQRQRVALARCLVRPNPILL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038545162 172 LDEPTSALDPisagKIEETLYGL------KDKYTMLLVTRSMQQASRISDKTGFFLDGDLIEFNDT 231
Cdd:TIGR01277 152 LDEPFSALDP----LLREEMLALvkqlcsERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
16-234 |
6.78e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 107.48 E-value: 6.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 16 NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdLNPevtTTGSVVYNGHNIySPRTDTVELRKEIGMVFQQP 95
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNAL--LIP---SEGKVYVDGLDT-SDEENLWDIRNKAGMVFQNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 96 -NPFPMTIYE-NVVYGLRINGIKDKQVlDEAVEKALQGASIWDEvkdRLYDSAIgLSGGQQQRVCVARVLATSPKIILLD 173
Cdd:PRK13633 95 dNQIVATIVEeDVAFGPENLGIPPEEI-RERVDESLKKVGMYEY---RRHAPHL-LSGGQKQRVAIAGILAMRPECIIFD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038545162 174 EPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQ---QASRI--SDKTGFFLDGDLIE-FNDTKQM 234
Cdd:PRK13633 170 EPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEeavEADRIivMDSGKVVMEGTPKEiFKEVEMM 238
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-216 |
8.15e-28 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 109.02 E-value: 8.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdlnpEVTTTGSVVYNGHNIysprtDTVELR 85
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGL-----EHQTSGHIRFHGTDV-----SRLHAR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 86 -KEIGMVFQQPNPFP-MTIYENVVYGLRI---NGIKDKQVLDEAVEKALQGASIwDEVKDRlYDSAigLSGGQQQRVCVA 160
Cdd:PRK10851 73 dRKVGFVFQHYALFRhMTVFDNIAFGLTVlprRERPNAAAIKAKVTQLLEMVQL-AHLADR-YPAQ--LSGGQKQRVALA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2038545162 161 RVLATSPKIILLDEPTSALDPISAGKIEETLYGLKD--KYTMLLVTRSMQQASRISDK 216
Cdd:PRK10851 149 RALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEelKFTSVFVTHDQEEAMEVADR 206
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-239 |
9.20e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 107.00 E-value: 9.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 3 DAILQVSDLSVYYN--KKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNP---EVTTTGsVVYNGHNIYsp 77
Cdd:PRK13632 5 SVMIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKIL--TGLLKPqsgEIKIDG-ITISKENLK-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 78 rtdtvELRKEIGMVFQQP-NPF-PMTIYENVVYGL---RINGIKDKQVLDEAVEKAlqgasiwdEVKDRLYDSAIGLSGG 152
Cdd:PRK13632 80 -----EIRKKIGIIFQNPdNQFiGATVEDDIAFGLenkKVPPKKMKDIIDDLAKKV--------GMEDYLDKEPQNLSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 153 QQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDK--YTMLLVTRSMQQASrISDKTGFFLDGDLIEFND 230
Cdd:PRK13632 147 QKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTrkKTLISITHDMDEAI-LADKVIVFSEGKLIAQGK 225
|
....*....
gi 2038545162 231 TKQMFLDPQ 239
Cdd:PRK13632 226 PKEILNNKE 234
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-242 |
1.78e-27 |
|
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: 105.43 E-value: 1.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTllkSLNRMGDLNPevTTTGSVVYNGHNIYS-PrtdtVE 83
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTT---SFYMIVGLVR--PDAGKILIDGQDITHlP----MH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 84 LRKEIGMVF--QQPNPF-PMTIYENVVYGLRINGIKDKQVLDEAVEKALQGASIwdevkDRLYDS-AIGLSGGQQQRVCV 159
Cdd:TIGR04406 72 ERARLGIGYlpQEASIFrKLTVEENIMAVLEIRKDLDRAEREERLEALLEEFQI-----SHLRDNkAMSLSGGERRRVEI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 160 ARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTMLLVT-RSMQQASRISDKTGFFLDGDLIEFNDTKQMFLDP 238
Cdd:TIGR04406 147 ARALATNPKFILLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITdHNVRETLDICDRAYIISDGKVLAEGTPAEIVANE 226
|
....
gi 2038545162 239 QHKE 242
Cdd:TIGR04406 227 KVRR 230
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
21-191 |
2.20e-27 |
|
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: 109.91 E-value: 2.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 21 LNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDLnpevtTTGSVVYNGHNIyspRTDTVE-LRKEIGMVFQQPNPFP 99
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDV-----TSGRILIDGQDI---RDVTQAsLRAAIGIVPQDTVLFN 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 100 MTIYENVVYGlRINgikdkqVLDEAVEKALQGASIWDEVkDRL---YDSAIG-----LSGGQQQRVCVARVLATSPKIIL 171
Cdd:COG5265 446 DTIAYNIAYG-RPD------ASEEEVEAAARAAQIHDFI-ESLpdgYDTRVGerglkLSGGEKQRVAIARTLLKNPPILI 517
|
170 180
....*....|....*....|
gi 2038545162 172 LDEPTSALDPISAGKIEETL 191
Cdd:COG5265 518 FDEATSALDSRTERAIQAAL 537
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-215 |
2.25e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 106.35 E-value: 2.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNIysprtdTVEL 84
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRII--LGILAP---DSGEVLWDGEPL------DPED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 85 RKEIG-MvfqqpnpfP--------MTIYENVVYGLRINGIKDKqvldEAVEKALQgasiWDE---VKDRLYDSAIGLSGG 152
Cdd:COG4152 70 RRRIGyL--------PeerglypkMKVGEQLVYLARLKGLSKA----EAKRRADE----WLErlgLGDRANKKVEELSKG 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038545162 153 QQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDK-YTMLLVTRSMQQASRISD 215
Cdd:COG4152 134 NQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKgTTVIFSSHQMELVEELCD 197
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-227 |
2.50e-27 |
|
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: 104.22 E-value: 2.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNIysprTDTVELR 85
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKII--LGLIKP---DSGEITFDGKSY----QKNIEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 86 KEIGMVFQQPNPFP-MTIYENVVYGLRINGIKDKQVlDEAVEKALQGASIWDEVKdrlydsaiGLSGGQQQRVCVARVLA 164
Cdd:cd03268 72 RRIGALIEAPGFYPnLTARENLRLLARLLGIRKKRI-DEVLDVVGLKDSAKKKVK--------GFSLGMKQRLGIALALL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038545162 165 TSPKIILLDEPTSALDPISAGKIEETLYGLKDK-YTMLLVTRSMQQASRISDKTGFFLDGDLIE 227
Cdd:cd03268 143 GNPDLLILDEPTNGLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-213 |
2.53e-27 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 103.06 E-value: 2.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYY--NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNIYSprTDTVE 83
Cdd:cd03246 1 LEVENVSFRYpgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLI--LGLLRP---TSGRVRLDGADISQ--WDPNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 84 LRKEIGMVFQQPNPFPMTIYENVvyglringikdkqvldeavekalqgasiwdevkdrlydsaigLSGGQQQRVCVARVL 163
Cdd:cd03246 74 LGDHVGYLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARAL 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2038545162 164 ATSPKIILLDEPTSALDPISAGKIEETLYGLK-DKYTMLLVT---RSMQQASRI 213
Cdd:cd03246 112 YGNPRILVLDEPNSHLDVEGERALNQAIAALKaAGATRIVIAhrpETLASADRI 165
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
6-213 |
3.46e-27 |
|
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: 103.70 E-value: 3.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKK-----ALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHniysprtd 80
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL--LGELEK---LSGSVSVPGS-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 81 tvelrkeIGMVFQQPNPFPMTIYENVVYGLRINGIKDKQVLDE-AVEKALQgasIWD-----EVKDRlydsAIGLSGGQQ 154
Cdd:cd03250 68 -------IAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKAcALEPDLE---ILPdgdltEIGEK----GINLSGGQK 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038545162 155 QRVCVARVLATSPKIILLDEPTSALDPISAGKI-EETLYG-LKDKYTMLLVTRSMQ---QASRI 213
Cdd:cd03250 134 QRISLARAVYSDADIYLLDDPLSAVDAHVGRHIfENCILGlLLNNKTRILVTHQLQllpHADQI 197
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
6-227 |
4.32e-27 |
|
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: 109.44 E-value: 4.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYN-KKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEvttTGSVVYNGHNIysPRTDTVEL 84
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLL--VGFFQAR---SGEILLNGFSL--KDIDRHTL 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 85 RKEIGMVFQQPNPFPMTIYENVVYGLRINgikdkqVLDEAVEKALQGASIWDEVKD-------RLYDSAIGLSGGQQQRV 157
Cdd:TIGR01193 547 RQFINYLPQEPYIFSGSILENLLLGAKEN------VSQDEIWAACEIAEIKDDIENmplgyqtELSEEGSSISGGQKQRI 620
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 158 CVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKyTMLLVTRSMQQASRiSDKTGFFLDGDLIE 227
Cdd:TIGR01193 621 ALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK-TIIFVAHRLSVAKQ-SDKIIVLDHGKIIE 688
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
3-235 |
4.64e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 105.48 E-value: 4.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 3 DAILqvSDLSVYYNKK-----KALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdlnpEVTTTGSVVYNGHNIYSP 77
Cdd:PRK13645 6 DIIL--DNVSYTYAKKtpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGL-----IISETGQTIVGDYAIPAN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 78 RTDTVE---LRKEIGMVFQQP--NPFPMTIYENVVYGlRINGIKDKQVLDEAVEKALQGASIWDEVKDRlydSAIGLSGG 152
Cdd:PRK13645 79 LKKIKEvkrLRKEIGLVFQFPeyQLFQETIEKDIAFG-PVNLGENKQEAYKKVPELLKLVQLPEDYVKR---SPFELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 153 QQQRVCVARVLATSPKIILLDEPTSALDPisagKIEETLYGL------KDKYTMLLVTRSMQQASRISDKTGFFLDGDLI 226
Cdd:PRK13645 155 QKRRVALAGIIAMDGNTLVLDEPTGGLDP----KGEEDFINLferlnkEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
|
....*....
gi 2038545162 227 EFNDTKQMF 235
Cdd:PRK13645 231 SIGSPFEIF 239
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-226 |
6.05e-27 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 103.60 E-value: 6.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYYNKKK----ALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEvttTGSVVYNGhniYSPRTD 80
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRML--AGLLEPD---AGFATVDG---FDVVKE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 81 TVELRKEIGMVFQQPNPFP-MTIYENVVYGLRINGIKDKQVLDeAVEKALQGASIwDEVKDRlydSAIGLSGGQQQRVCV 159
Cdd:cd03266 73 PAEARRRLGFVSDSTGLYDrLTARENLEYFAGLYGLKGDELTA-RLEELADRLGM-EELLDR---RVGGFSTGMRQKVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038545162 160 ARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDK-YTMLLVTRSMQQASRISDKTGFFLDGDLI 226
Cdd:cd03266 148 ARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-223 |
6.84e-27 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 103.89 E-value: 6.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 25 SLSFQPKEITALIGPSGSGKSTLLkslNRM-GDLNPEvttTGSVVYNGHNiyspRTDTVELRKEIGMVFQQPNPFP-MTI 102
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLL---NLIaGFLTPA---SGSLTLNGQD----HTTTPPSRRPVSMLFQENNLFShLTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 103 YENVVYG----LRINGIKDKQVLDEAVEKALqgasiwDEVKDRLYDSaigLSGGQQQRVCVARVLATSPKIILLDEPTSA 178
Cdd:PRK10771 89 AQNIGLGlnpgLKLNAAQREKLHAIARQMGI------EDLLARLPGQ---LSGGQRQRVALARCLVREQPILLLDEPFSA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2038545162 179 LDPisAGKiEETLYGLKD-----KYTMLLVTRSMQQASRISDKTGFFLDG 223
Cdd:PRK10771 160 LDP--ALR-QEMLTLVSQvcqerQLTLLMVSHSLEDAARIAPRSLVVADG 206
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
2-204 |
7.35e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 104.81 E-value: 7.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 2 TDAILQVSDLSVYYNK---KKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPEvttTGSVVYNGHNIyspR 78
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLID--GLLEAE---SGQIIIDGDLL---T 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 79 TDTV-ELRKEIGMVFQQP-NPF-PMTIYENVVYGLRINGIkDKQVLDEAVEKALQGASIWDeVKDRlydSAIGLSGGQQQ 155
Cdd:PRK13650 73 EENVwDIRHKIGMVFQNPdNQFvGATVEDDVAFGLENKGI-PHEEMKERVNEALELVGMQD-FKER---EPARLSGGQKQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2038545162 156 RVCVARVLATSPKIILLDEPTSALDPisAGKIE--ETLYGLKDKYTMLLVT 204
Cdd:PRK13650 148 RVAIAGAVAMRPKIIILDEATSMLDP--EGRLEliKTIKGIRDDYQMTVIS 196
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-216 |
8.11e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 107.81 E-value: 8.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 1 MTDAILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGH--NIYSPR 78
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKIL--YGLYQP---DSGEILIDGKpvRIRSPR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 79 tDTVELRkeIGMVFQQPNPFP-MTIYENVVYGL--RINGIKDKQVLDEAVEKALQ--------GASIWDevkdrlydsai 147
Cdd:COG3845 76 -DAIALG--IGMVHQHFMLVPnLTVAENIVLGLepTKGGRLDRKAARARIRELSErygldvdpDAKVED----------- 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 148 gLSGGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDK-YTMLLVTRSMQQASRISDK 216
Cdd:COG3845 142 -LSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEgKSIIFITHKLREVMAIADR 210
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-237 |
8.86e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 104.83 E-value: 8.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 19 KALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPevtTTGSVVYNGHNI--YSPRTDTVELRKEIGMVFQQPN 96
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLN--GLHVP---TQGSVRVDDTLItsTSKNKDIKQIRKKVGLVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 97 P--FPMTIYENVVYGLRINGIKDKQVLDEAVEK-ALQGASiwDEVKDRlydSAIGLSGGQQQRVCVARVLATSPKIILLD 173
Cdd:PRK13649 96 SqlFEETVLKDVAFGPQNFGVSQEEAEALAREKlALVGIS--ESLFEK---NPFELSGGQMRRVAIAGILAMEPKILVLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2038545162 174 EPTSALDPISAGKIEETLYGL-KDKYTMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQMFLD 237
Cdd:PRK13649 171 EPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
20-213 |
1.19e-26 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 103.33 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 20 ALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdlnpEVTTTGSVVYNGHNIYSprTDTVELRKEIGMVFQQPNPFP 99
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRF-----YVPENGRVLVDGHDLAL--ADPAWLRRQVGVVLQENVLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 100 MTIYENVVYGlringiKDKQVLDEAVEKA-LQGASIWDEVKDRLYDSAIG-----LSGGQQQRVCVARVLATSPKIILLD 173
Cdd:cd03252 90 RSIRDNIALA------DPGMSMERVIEAAkLAGAHDFISELPEGYDTIVGeqgagLSGGQRQRIAIARALIHNPRILIFD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2038545162 174 EPTSALDPISAGKIEETLYGLKDKYTMLLVTR---SMQQASRI 213
Cdd:cd03252 164 EATSALDYESEHAIMRNMHDICAGRTVIIIAHrlsTVKNADRI 206
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-210 |
1.27e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 103.63 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYYNK-----KKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPevtTTGSVVYNGHNIysprT 79
Cdd:COG1101 1 MLELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIA--GSLPP---DSGSILIDGKDV----T 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 80 DTVELR--KEIGMVFQqpNPF----P-MTIYENVV--------YGLRInGI--KDKQVLDEAVEKALQGasiwdeVKDRL 142
Cdd:COG1101 72 KLPEYKraKYIGRVFQ--DPMmgtaPsMTIEENLAlayrrgkrRGLRR-GLtkKRRELFRELLATLGLG------LENRL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038545162 143 yDSAIG-LSGGQQQrvCVARVLAT--SPKIILLDEPTSALDPISAGKIEEtlygL------KDKYTMLLVTRSMQQA 210
Cdd:COG1101 143 -DTKVGlLSGGQRQ--ALSLLMATltKPKLLLLDEHTAALDPKTAALVLE----LtekiveENNLTTLMVTHNMEQA 212
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-210 |
1.29e-26 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 103.63 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEvttTGSVVYNGHNIYSPRTdtvel 84
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLI--AGFVPYQ---HGSITLDGKPVEGPGA----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 85 rkEIGMVFQQPNPFP-MTIYENVVYGLRINGIKDKQVLDEAVEK----ALQGAS---IWDevkdrlydsaigLSGGQQQR 156
Cdd:PRK11248 71 --ERGVVFQNEGLLPwRNVQDNVAFGLQLAGVEKMQRLEIAHQMlkkvGLEGAEkryIWQ------------LSGGQRQR 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2038545162 157 VCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGL--KDKYTMLLVTRSMQQA 210
Cdd:PRK11248 137 VGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLwqETGKQVLLITHDIEEA 192
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
4-197 |
1.41e-26 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 103.19 E-value: 1.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 4 AILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNIysprTDtve 83
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMI--VGLVKP---DSGRIFLDGEDI----TH--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 84 L------RKEIGMVFQQPNPF-PMTIYENVVYGLRINGiKDKQVLDEAVEKALQGASIwDEVKDRLydsAIGLSGGQQQR 156
Cdd:COG1137 70 LpmhkraRLGIGYLPQEASIFrKLTVEDNILAVLELRK-LSKKEREERLEELLEEFGI-THLRKSK---AYSLSGGERRR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2038545162 157 VCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDK 197
Cdd:COG1137 145 VEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKER 185
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-247 |
1.48e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 105.69 E-value: 1.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdlnpEVTTTGSVVYNGHNIysprTDTVEL 84
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGF-----EQPTAGQIMLDGVDL----SHVPPY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 85 RKEIGMVFQQPNPFP-MTIYENVVYGLRINGIKDKQVLDEaVEKALQGASIWDEVKDRLYDsaigLSGGQQQRVCVARVL 163
Cdd:PRK11607 90 QRPINMMFQSYALFPhMTVEQNIAFGLKQDKLPKAEIASR-VNEMLGLVHMQEFAKRKPHQ----LSGGQRQRVALARSL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 164 ATSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQMFLDPQHK 241
Cdd:PRK11607 165 AKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVgvTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTR 244
|
....*.
gi 2038545162 242 ETEDYI 247
Cdd:PRK11607 245 YSAEFI 250
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
15-238 |
1.94e-26 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 105.19 E-value: 1.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 15 YNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNIysprTDTVELRKEIGMVFQQ 94
Cdd:PRK11432 16 FGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLV--AGLEKP---TEGQIFIDGEDV----THRSIQQRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 95 PNPFP-MTIYENVVYGLRINGIKD---KQVLDEAVEKA-LQGasiwdeVKDRLYDSaigLSGGQQQRVCVARVLATSPKI 169
Cdd:PRK11432 87 YALFPhMSLGENVGYGLKMLGVPKeerKQRVKEALELVdLAG------FEDRYVDQ---ISGGQQQRVALARALILKPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038545162 170 ILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQMFLDP 238
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIRELQQQFniTSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
21-238 |
2.02e-26 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 107.50 E-value: 2.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 21 LNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdLNPevtTTGSVVYNGHNIysPRTDTVELRKEIGMVFQQPNPFPM 100
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNL--YQP---TGGQVLLDGVPL--VQYDHHYLHRQVALVGQEPVLFSG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 101 TIYENVVYGLRingikdkQVLDEAVEKALQGASIWDEVKD--RLYDSAIG-----LSGGQQQRVCVARVLATSPKIILLD 173
Cdd:TIGR00958 570 SVRENIAYGLT-------DTPDEEIMAAAKAANAHDFIMEfpNGYDTEVGekgsqLSGGQKQRIAIARALVRKPRVLILD 642
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038545162 174 EPTSALDpisaGKIEETLYGLKDKY--TMLLVTRSMQQASRiSDKTGFFLDGDLIEFNDTKQMFLDP 238
Cdd:TIGR00958 643 EATSALD----AECEQLLQESRSRAsrTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
5-232 |
2.32e-26 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 103.17 E-value: 2.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRM--GDLNPE--VTTTGSVVYNGHNIYSprtD 80
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitGDKSAGshIELLGRTVQREGRLAR---D 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 81 TVELRKEIGMVFQQPNPFP-MTIYENVVYG-----------LRINGIKDKQVLDEAVEKALQGASIWDEVKDrlydsaig 148
Cdd:PRK09984 81 IRKSRANTGYIFQQFNLVNrLSVLENVLIGalgstpfwrtcFSWFTREQKQRALQALTRVGMVHFAHQRVST-------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 149 LSGGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLK--DKYTMLLVTRSMQQASRISDKT------GFF 220
Cdd:PRK09984 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINqnDGITVVVTLHQVDYALRYCERIvalrqgHVF 232
|
250
....*....|..
gi 2038545162 221 LDGDLIEFNDTK 232
Cdd:PRK09984 233 YDGSSQQFDNER 244
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
24-247 |
2.57e-26 |
|
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: 104.81 E-value: 2.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 24 VSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPEVtttGSVVYNGHNIYSPR--TDTVELRKEIGMVFQQPNPFP-M 100
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIA--GLTRPDE---GEIVLNGRTLFDSRkgIFLPPEKRRIGYVFQEARLFPhL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 101 TIYENVVYGLRINGIKDKQVLDEAVEKALQgasiWDEVKDRLYDSaigLSGGQQQRVCVARVLATSPKIILLDEPTSALD 180
Cdd:TIGR02142 91 SVRGNLRYGMKRARPSERRISFERVIELLG----IGHLLGRLPGR---LSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038545162 181 PISAGKIEETLYGLKD--KYTMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQMFLDP----QHKETEDYI 247
Cdd:TIGR02142 164 DPRKYEILPYLERLHAefGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPdlpwLAREDQGSL 236
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-244 |
3.28e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 106.33 E-value: 3.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 1 MTDAILQVSDLSVYYNK----KKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDLNPEVTTTGSVVYNGHNIYs 76
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQqqtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGESLL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 77 pRTDTVELRK----EIGMVFQQP----NPFpMTI----YEnvVYGLRiNGIKDKQVLDEAVEkALQGASIwDEVKDRLYD 144
Cdd:PRK15134 80 -HASEQTLRGvrgnKIAMIFQEPmvslNPL-HTLekqlYE--VLSLH-RGMRREAARGEILN-CLDRVGI-RQAAKRLTD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 145 SAIGLSGGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTM--LLVTRSMQQASRISDKTGFFLD 222
Cdd:PRK15134 153 YPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMglLFITHNLSIVRKLADRVAVMQN 232
|
250 260
....*....|....*....|..
gi 2038545162 223 GDLIEFNDTKQMFLDPQHKETE 244
Cdd:PRK15134 233 GRCVEQNRAATLFSAPTHPYTQ 254
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-235 |
3.59e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 102.86 E-value: 3.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 3 DAILQVSDLSVYYNKK---KALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDLNPEVTTTGSVVYNGHNIYSprt 79
Cdd:PRK13642 2 NKILEVENLVFKYEKEsdvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWN--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 80 dtveLRKEIGMVFQQP-NPF-PMTIYENVVYGLRINGIKDKQVLdEAVEKALQGASIWDeVKDRlydSAIGLSGGQQQRV 157
Cdd:PRK13642 79 ----LRRKIGMVFQNPdNQFvGATVEDDVAFGMENQGIPREEMI-KRVDEALLAVNMLD-FKTR---EPARLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 158 CVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRiSDKTGFFLDGDLIEFNDTKQMF 235
Cdd:PRK13642 150 AVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-239 |
3.97e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 102.96 E-value: 3.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 1 MTDAILQVSDLSVYY--NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPEVTTTGSVVYNGHNIYSpr 78
Cdd:PRK13640 1 MKDNIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLIN--GLLLPDDNPNSKITVDGITLTA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 79 tDTV-ELRKEIGMVFQQP-NPF-PMTIYENVVYGLRINGIKDKQVLdEAVEKALQGASIWDEVKDRlydsAIGLSGGQQQ 155
Cdd:PRK13640 77 -KTVwDIREKVGIVFQNPdNQFvGATVGDDVAFGLENRAVPRPEMI-KIVRDVLADVGMLDYIDSE----PANLSGGQKQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 156 RVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDK--YTMLLVTRSMQQASrISDKTGFFLDGDLIEFNDTKQ 233
Cdd:PRK13640 151 RVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnnLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVE 229
|
....*.
gi 2038545162 234 MFLDPQ 239
Cdd:PRK13640 230 IFSKVE 235
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
6-180 |
3.99e-26 |
|
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: 106.37 E-value: 3.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYY--NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNIYS-PRTdtv 82
Cdd:COG4618 331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLL--VGVWPP---TAGSVRLDGADLSQwDRE--- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 83 ELRKEIGMVFQQPNPFPMTIYENVVyglRINGIKDkqvldEAVEKALQGASIwDEVKDRL---YDSAIG-----LSGGQQ 154
Cdd:COG4618 403 ELGRHIGYLPQDVELFDGTIAENIA---RFGDADP-----EKVVAAAKLAGV-HEMILRLpdgYDTRIGeggarLSGGQR 473
|
170 180
....*....|....*....|....*.
gi 2038545162 155 QRVCVARVLATSPKIILLDEPTSALD 180
Cdd:COG4618 474 QRIGLARALYGDPRLVVLDEPNSNLD 499
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-181 |
4.76e-26 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 102.08 E-value: 4.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 7 QVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLkSLnrMGDLNPevTTTGSVVYNGHNIYspRTDTVELRK 86
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLL-SM--ISRLLP--PDSGEVLVDGLDVA--TTPSRELAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 87 EIGmVFQQPNPFPM--TIYENVVYGL------RINGiKDKQVLDEAVEkALQgasiWDEVKDRLYDSaigLSGGQQQRVC 158
Cdd:COG4604 76 RLA-ILRQENHINSrlTVRELVAFGRfpyskgRLTA-EDREIIDEAIA-YLD----LEDLADRYLDE---LSGGQRQRAF 145
|
170 180
....*....|....*....|...
gi 2038545162 159 VARVLATSPKIILLDEPTSALDP 181
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPLNNLDM 168
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-197 |
6.01e-26 |
|
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: 101.08 E-value: 6.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNIyspRTDTVELR 85
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMI--VGLVKP---DSGKILLDGQDI---TKLPMHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 86 KEIGMVF--QQPNPF-PMTIYENVVYGLRINGiKDKQVLDEAVEKALQGASIwDEVKDRLydsAIGLSGGQQQRVCVARV 162
Cdd:cd03218 73 ARLGIGYlpQEASIFrKLTVEENILAVLEIRG-LSKKEREEKLEELLEEFHI-THLRKSK---ASSLSGGERRRVEIARA 147
|
170 180 190
....*....|....*....|....*....|....*
gi 2038545162 163 LATSPKIILLDEPTSALDPISAGKIEETLYGLKDK 197
Cdd:cd03218 148 LATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDR 182
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-238 |
8.72e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 101.80 E-value: 8.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLS-VYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPevtTTGSVVYNGHNIysPRTDTVE 83
Cdd:PRK13652 3 LIETRDLCySYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFN--GILKP---TSGSVLIRGEPI--TKENIRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 84 LRKEIGMVFQQPNP--FPMTIYENVVYGlRINGIKDKQVLDEAVEKALQGASIwDEVKDRLYDSaigLSGGQQQRVCVAR 161
Cdd:PRK13652 76 VRKFVGLVFQNPDDqiFSPTVEQDIAFG-PINLGLDEETVAHRVSSALHMLGL-EELRDRVPHH---LSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038545162 162 VLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTMLLV--TRSMQQASRISDKTGFFLDGDLIEFNDTKQMFLDP 238
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIfsTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
4-235 |
9.25e-26 |
|
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: 101.42 E-value: 9.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 4 AILQVSDLSVYY-----NKKKA----LNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrmgdLNPEVTTTGSVVYNGHNI 74
Cdd:TIGR02769 1 SLLEVRDVTHTYrtgglFGAKQrapvLTNVSLSIEEGETVGLLGRSGCGKSTLARLL-----LGLEKPAQGTVSFRGQDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 75 YS-PRTDTVELRKEIGMVFQQP----NPfPMTIYENVVYGLRingikDKQVLDEAVEKA-----LQGASIWDEVKDRLYD 144
Cdd:TIGR02769 76 YQlDRKQRRAFRRDVQLVFQDSpsavNP-RMTVRQIIGEPLR-----HLTSLDESEQKAriaelLDMVGLRSEDADKLPR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 145 SaigLSGGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRISDKTGFFLD 222
Cdd:TIGR02769 150 Q---LSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFgtAYLFITHDLRLVQSFCQRVAVMDK 226
|
250
....*....|...
gi 2038545162 223 GDLIEFNDTKQMF 235
Cdd:TIGR02769 227 GQIVEECDVAQLL 239
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-243 |
1.49e-25 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 104.94 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 3 DAILQVSDL-------SVYYNKKK----ALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDlnpevTTTGSVVYNG 71
Cdd:PRK10261 311 EPILQVRNLvtrfplrSGLLNRVTrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVE-----SQGGEIIFNG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 72 HNIYS-PRTDTVELRKEIGMVFQQP----NPfPMTIYENVVYGLRINGIKDKQVLDEAVEKALQGASIWDEVKDRlYDSA 146
Cdd:PRK10261 386 QRIDTlSPGKLQALRRDIQFIFQDPyaslDP-RQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWR-YPHE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 147 igLSGGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRISDKTGFFLDGD 224
Cdd:PRK10261 464 --FSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFgiAYLFISHDMAVVERISHRVAVMYLGQ 541
|
250
....*....|....*....
gi 2038545162 225 LIEFNDTKQMFLDPQHKET 243
Cdd:PRK10261 542 IVEIGPRRAVFENPQHPYT 560
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
7-212 |
1.64e-25 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 99.95 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 7 QVSdlSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdlnpEVTTTGSVVYNGHNIYSPRTDTVE-LR 85
Cdd:PRK10908 6 HVS--KAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGI-----ERPSAGKIWFSGHDITRLKNREVPfLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 86 KEIGMVFQQPNPF-PMTIYENVVYGLRINGIKDKQVlDEAVEKALQGASIWDEVKDrlydSAIGLSGGQQQRVCVARVLA 164
Cdd:PRK10908 79 RQIGMIFQDHHLLmDRTVYDNVAIPLIIAGASGDDI-RRRVSAALDKVGLLDKAKN----FPIQLSGGEQQRVGIARAVV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2038545162 165 TSPKIILLDEPTSALDpisaGKIEETLYGLKDKY-----TMLLVTRSMQQASR 212
Cdd:PRK10908 154 NKPAVLLADEPTGNLD----DALSEGILRLFEEFnrvgvTVLMATHDIGLISR 202
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
21-227 |
1.66e-25 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 99.85 E-value: 1.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 21 LNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDlnpevTTTGSVVYNGHNIYSPRTDT-VELR-KEIGMVFQQPNPF 98
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDD-----GSSGEVSLVGQPLHQMDEEArAKLRaKHVGFVFQSFMLI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 99 P-MTIYENVVYGLRINGIKDKQVLDEAVEKALQGAsiwdeVKDRLYDSAIGLSGGQQQRVCVARVLATSPKIILLDEPTS 177
Cdd:PRK10584 101 PtLNALENVELPALLRGESSRQSRNGAKALLEQLG-----LGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2038545162 178 ALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRiSDKTGFFLDGDLIE 227
Cdd:PRK10584 176 NLDRQTGDKIADLLFSLNREHgtTLILVTHDLQLAAR-CDRRLRLVNGQLQE 226
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
6-214 |
2.17e-25 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 104.33 E-value: 2.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKK--ALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDLNpevttTGSVVYNGHNI--YSPRTdt 81
Cdd:PRK11176 342 IEFRNVTFTYPGKEvpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDID-----EGEILLDGHDLrdYTLAS-- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 82 veLRKEIGMVFQQPNPFPMTIYENVVYGlringiKDKQVLDEAVEKALQGASIWDEVK--DRLYDSAIG-----LSGGQQ 154
Cdd:PRK11176 415 --LRNQVALVSQNVHLFNDTIANNIAYA------RTEQYSREQIEEAARMAYAMDFINkmDNGLDTVIGengvlLSGGQR 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 155 QRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTMLLVtrsmqqASRIS 214
Cdd:PRK11176 487 QRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVI------AHRLS 540
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
15-191 |
3.09e-25 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 98.46 E-value: 3.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 15 YNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHniysprtdtvelrKEIGMVFQQ 94
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVL--AGVLRP---TSGTVRRAGG-------------ARVAYVPQR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 95 ---PNPFPMTIYENVVYG-------LRINGIKDKQVLDEAVEkALQGAsiwdevkdRLYDSAIG-LSGGQQQRVCVARVL 163
Cdd:NF040873 64 sevPDSLPLTVRDLVAMGrwarrglWRRLTRDDRAAVDDALE-RVGLA--------DLAGRQLGeLSGGQRQRALLAQGL 134
|
170 180
....*....|....*....|....*...
gi 2038545162 164 ATSPKIILLDEPTSALDPISAGKIEETL 191
Cdd:NF040873 135 AQEADLLLLDEPTTGLDAESRERIIALL 162
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-249 |
4.44e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 102.03 E-value: 4.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 20 ALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdLNPevtTTGSVVYNGHNIysPRTDTVELR----KEIGMVFQQP 95
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRL--IEP---TRGQVLIDGVDI--AKISDAELRevrrKKIAMVFQSF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 96 NPFP-MTIYENVVYGLRINGIKDKQVLDEAVEKALQGAsiwdeVKDRLYDSAIGLSGGQQQRVCVARVLATSPKIILLDE 174
Cdd:PRK10070 116 ALMPhMTVLDNTAFGMELAGINAEERREKALDALRQVG-----LENYAHSYPDELSGGMRQRVGLARALAINPDILLMDE 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038545162 175 PTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQMFLDPQHKETEDYITG 249
Cdd:PRK10070 191 AFSALDPLIRTEMQDELVKLQAKHqrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRG 267
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-191 |
5.91e-25 |
|
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: 98.50 E-value: 5.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 16 NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDLNPevTTTGSVVYNGhniySPRtDTVELRKEIGMVFQQP 95
Cdd:cd03234 18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGG--TTSGQILFNG----QPR-KPDQFQKCVAYVRQDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 96 NPFP-MTIYENVVYG--LRINGIKDKQVLDEAVEkalqgasiwDEVKDRLYDSAI------GLSGGQQQRVCVARVLATS 166
Cdd:cd03234 91 ILLPgLTVRETLTYTaiLRLPRKSSDAIRKKRVE---------DVLLRDLALTRIggnlvkGISGGERRRVSIAVQLLWD 161
|
170 180
....*....|....*....|....*
gi 2038545162 167 PKIILLDEPTSALDPISAGKIEETL 191
Cdd:cd03234 162 PKVLILDEPTSGLDSFTALNLVSTL 186
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-204 |
1.32e-24 |
|
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: 96.83 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEVTTtGSVVYNGHNIysprTD-TVEL 84
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTI--MGHPKYEVTE-GEILFKGEDI----TDlPPEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 85 R--KEIGMVFQQPnpfpmtiyenvvygLRINGIKdkqvldeavekalqgasiwdeVKDRLYDSAIGLSGGQQQRVCVARV 162
Cdd:cd03217 74 RarLGIFLAFQYP--------------PEIPGVK---------------------NADFLRYVNEGFSGGEKKRNEILQL 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2038545162 163 LATSPKIILLDEPTSALDpISAGK-IEETLYGLKD-KYTMLLVT 204
Cdd:cd03217 119 LLLEPDLAILDEPDSGLD-IDALRlVAEVINKLREeGKSVLIIT 161
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-215 |
1.33e-24 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 96.97 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNI-YSPRTDTVEL 84
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMI--LGIILP---DSGEVLFDGKPLdIAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 85 RKEIGMvfqqpnpFP-MTIYENVVYGLRINGIKDKQVL---DEAVEKAlqgasiwdEVKDRLYDSAIGLSGGQQQRVCVA 160
Cdd:cd03269 76 PEERGL-------YPkMKVIDQLVYLAQLKGLKKEEARrriDEWLERL--------ELSEYANKRVEELSKGNQQKVQFI 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2038545162 161 RVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDK-YTMLLVTRSMQQASRISD 215
Cdd:cd03269 141 AAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEELCD 196
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
3-180 |
2.33e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 97.09 E-value: 2.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 3 DAILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLK---SLnrmgdLNPevtTTGSVVYNGHNI--YSP 77
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKivaSL-----ISP---TSGTLLFEGEDIstLKP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 78 RTdtveLRKEIGMVFQQPNPFPMTIYENVVYGLRINGIKDKqvldeavEKALQGASIWDEVKDRLYDSAIG-LSGGQQQR 156
Cdd:PRK10247 77 EI----YRQQVSYCAQTPTLFGDTVYDNLIFPWQIRNQQPD-------PAIFLDDLERFALPDTILTKNIAeLSGGEKQR 145
|
170 180
....*....|....*....|....
gi 2038545162 157 VCVARVLATSPKIILLDEPTSALD 180
Cdd:PRK10247 146 ISLIRNLQFMPKVLLLDEITSALD 169
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-240 |
4.96e-24 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 98.26 E-value: 4.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 1 MTDAILQVSDLSVYYNKKK----ALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEVTTTGSVVYNGHNIYS 76
Cdd:PRK09473 8 QADALLDVKDLRVTFSTPDgdvtAVNDLNFSLRAGETLGIVGESGSGKSQTAFAL--MGLLAANGRIGGSATFNGREILN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 77 -PRTDTVELR-KEIGMVFQQP----NPFpMTIYENVVYGLRIN-GIKDKQVLDEAVeKALQGASIwDEVKDRLYDSAIGL 149
Cdd:PRK09473 86 lPEKELNKLRaEQISMIFQDPmtslNPY-MRVGEQLMEVLMLHkGMSKAEAFEESV-RMLDAVKM-PEARKRMKMYPHEF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 150 SGGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRISDKTGFFLDGDLIE 227
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKVLVMYAGRTME 242
|
250
....*....|...
gi 2038545162 228 FNDTKQMFLDPQH 240
Cdd:PRK09473 243 YGNARDVFYQPSH 255
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-180 |
5.42e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 98.11 E-value: 5.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 1 MTDAILQVSDLSVYYNKK----------KALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdlnpEVTTTGSVVYN 70
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPVKrglfkperlvKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMI-----ETPTGGELYYQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 71 GHNIYSPRTDTV-ELRKEIGMVFQQP----NPfPMTIYENVVYGLRINGIKDKQvldEAVEKALQgasIWDEVkdrlyds 145
Cdd:PRK11308 76 GQDLLKADPEAQkLLRQKIQIVFQNPygslNP-RKKVGQILEEPLLINTSLSAA---ERREKALA---MMAKV------- 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2038545162 146 aiGL------------SGGQQQRVCVARVLATSPKIILLDEPTSALD 180
Cdd:PRK11308 142 --GLrpehydryphmfSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-181 |
8.35e-24 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 95.58 E-value: 8.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 1 MTdAILQVSDLS---VYYN----KKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRmgdlNpEVTTTGSVVYN--G 71
Cdd:COG4778 1 MT-TLLEVENLSktfTLHLqggkRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG----N-YLPDSGSILVRhdG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 72 HNI----YSPRtDTVELRK-EIGMVFQQPNPFPMTIYENVVYG-LRINGIKDKQVLDEAVE--KALQgasiwdeVKDRLY 143
Cdd:COG4778 75 GWVdlaqASPR-EILALRRrTIGYVSQFLRVIPRVSALDVVAEpLLERGVDREEARARAREllARLN-------LPERLW 146
|
170 180 190
....*....|....*....|....*....|....*....
gi 2038545162 144 D-SAIGLSGGQQQRVCVARVLATSPKIILLDEPTSALDP 181
Cdd:COG4778 147 DlPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDA 185
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-216 |
1.12e-23 |
|
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: 95.23 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 21 LNSVSLSFQPKEITALIGPSGSGKSTLLkslNRMGDLNPevTTTGSVVYNGHNIYSPRTDTVelrkeigMVFQQPNPFP- 99
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLL---NLISGLAQ--PTSGGVILEGKQITEPGPDRM-------VVFQNYSLLPw 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 100 MTIYENVVYGL-RINGIKDKQVLDEAVEKALQGASIWDEVKDRLYDsaigLSGGQQQRVCVARVLATSPKIILLDEPTSA 178
Cdd:TIGR01184 69 LTVRENIALAVdRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2038545162 179 LDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRISDK 216
Cdd:TIGR01184 145 LDALTRGNLQEELMQIWEEHrvTVLMVTHDVDEALLLSDR 184
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-181 |
1.86e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 95.59 E-value: 1.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 1 MTDAILQVSDLSVYYNKKKA--LNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdlnpEVTTTGSVVYNGHNIYSpr 78
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGI-----EKVKSGEIFYNNQAITD-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 79 TDTVELRKEIGMVFQQP-NPFPMTIYE-NVVYGLRINGIKDKQvLDEAVEKALQGAsiwdEVKDRLYDSAIGLSGGQQQR 156
Cdd:PRK13648 76 DNFEKLRKHIGIVFQNPdNQFVGSIVKyDVAFGLENHAVPYDE-MHRRVSEALKQV----DMLERADYEPNALSGGQKQR 150
|
170 180
....*....|....*....|....*
gi 2038545162 157 VCVARVLATSPKIILLDEPTSALDP 181
Cdd:PRK13648 151 VAIAGVLALNPSVIILDEATSMLDP 175
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
5-243 |
1.96e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 98.62 E-value: 1.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYYNKKK-----------ALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdlnpeVTTTGSVVYNGHN 73
Cdd:PRK15134 275 LLDVEQLQVAFPIRKgilkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRL------INSQGEIWFDGQP 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 74 IYS-PRTDTVELRKEIGMVFQQP----NPfPMTIYENVVYGLRIN--GIKDKQVlDEAVEKALQGASIWDEVKDRlYDSA 146
Cdd:PRK15134 349 LHNlNRRQLLPVRHRIQVVFQDPnsslNP-RLNVLQIIEEGLRVHqpTLSAAQR-EQQVIAVMEEVGLDPETRHR-YPAE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 147 igLSGGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTM--LLVTRSMQQASRISDKTGFFLDGD 224
Cdd:PRK15134 426 --FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRALCHQVIVLRQGE 503
|
250
....*....|....*....
gi 2038545162 225 LIEFNDTKQMFLDPQHKET 243
Cdd:PRK15134 504 VVEQGDCERVFAAPQQEYT 522
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
6-180 |
2.12e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 97.60 E-value: 2.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPevtTTGSVVYNGHNIYSprTDTVELR 85
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAIN--GTLTP---TAGTVLVAGDDVEA--LSARAAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 86 KEIGMVFQQPN-PFPMTIYENVVYGL-----RINGIKDKQvlDEAVEKALQGASIwDEVKDRLYDSaigLSGGQQQRVCV 159
Cdd:PRK09536 77 RRVASVPQDTSlSFEFDVRQVVEMGRtphrsRFDTWTETD--RAAVERAMERTGV-AQFADRPVTS---LSGGERQRVLL 150
|
170 180
....*....|....*....|.
gi 2038545162 160 ARVLATSPKIILLDEPTSALD 180
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLD 171
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-235 |
2.18e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 95.96 E-value: 2.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 19 KALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPEVTTT--GSVVYNGhniYSPRTDTVELRKEIGMVFQQPN 96
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLN--GLLQPTEGKVtvGDIVVSS---TSKQKEIKPVRKKVGVVFQFPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 97 P--FPMTIYENVVYGLRINGIKDKQVLDEAVEKaLQGASIWDEVKDRlydSAIGLSGGQQQRVCVARVLATSPKIILLDE 174
Cdd:PRK13643 95 SqlFEETVLKDVAFGPQNFGIPKEKAEKIAAEK-LEMVGLADEFWEK---SPFELSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038545162 175 PTSALDP---ISAGKIEETLYglKDKYTMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQMF 235
Cdd:PRK13643 171 PTAGLDPkarIEMMQLFESIH--QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-216 |
3.80e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 94.29 E-value: 3.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 1 MTDAILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPevtTTGSVVYNGHNIYSPRTD 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLT--GFYKP---TGGTILLRGQHIEGLPGH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 81 TVElRKEIGMVFQQPNPF-PMTIYEN--VVYGLRIN-----GIKDKQVLDEAVEKALQGASIW------DEVKDRlydSA 146
Cdd:PRK11300 76 QIA-RMGVVRTFQHVRLFrEMTVIENllVAQHQQLKtglfsGLLKTPAFRRAESEALDRAATWlervglLEHANR---QA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2038545162 147 IGLSGGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRISDK 216
Cdd:PRK11300 152 GNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGISDR 223
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-244 |
4.61e-23 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 94.22 E-value: 4.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 1 MTDAILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPevtTTGSVVYNGHNiySPRTD 80
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALS--ARLAP---DAGEVHYRMRD--GQLRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 81 TVEL---------RKEIGMVFQQP-NPFPMTIYE--NVvyGLRINGIKDK---QVLDEAVEkalqgasiW-DEVK---DR 141
Cdd:PRK11701 75 LYALseaerrrllRTEWGFVHQHPrDGLRMQVSAggNI--GERLMAVGARhygDIRATAGD--------WlERVEidaAR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 142 LYDSAIGLSGGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTM--LLVTRSMQQASRISDKTGF 219
Cdd:PRK11701 145 IDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLavVIVTHDLAVARLLAHRLLV 224
|
250 260
....*....|....*....|....*
gi 2038545162 220 FLDGDLIEFNDTKQMFLDPQHKETE 244
Cdd:PRK11701 225 MKQGRVVESGLTDQVLDDPQHPYTQ 249
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
24-247 |
8.38e-23 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 97.02 E-value: 8.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 24 VSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDLNPE------------------------------------------- 60
Cdd:PTZ00265 1187 LTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggs 1266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 61 ------VTTTGSVVYNGHNI--YSPRtdtvELRKEIGMVFQQPNPFPMTIYENVVYGlringiKDKQVLdEAVEKALQGA 132
Cdd:PTZ00265 1267 gedstvFKNSGKILLDGVDIcdYNLK----DLRNLFSIVSQEPMLFNMSIYENIKFG------KEDATR-EDVKRACKFA 1335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 133 SIwDEVKDRL---YDSAIG-----LSGGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTMLLVT 204
Cdd:PTZ00265 1336 AI-DEFIESLpnkYDTNVGpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIIT 1414
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2038545162 205 RSMQQAS-RISDKTGFFLD----GDLIEFNDTKQMFLDPQHKETEDYI 247
Cdd:PTZ00265 1415 IAHRIASiKRSDKIVVFNNpdrtGSFVQAHGTHEELLSVQDGVYKKYV 1462
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-180 |
8.45e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 93.21 E-value: 8.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEVTTtGSVVYNGHNIysprTD-TVEL 84
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVL--MGHPKYEVTS-GSILLDGEDI----LElSPDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 85 R--KEIGMVFQQPNPFP--------MTIYENVvyglRINGIKDKQVLDEAVEKAlqgasiwDEVK------DRlyDSAIG 148
Cdd:COG0396 74 RarAGIFLAFQYPVEIPgvsvsnflRTALNAR----RGEELSAREFLKLLKEKM-------KELGldedflDR--YVNEG 140
|
170 180 190
....*....|....*....|....*....|..
gi 2038545162 149 LSGGQQQRVCVARVLATSPKIILLDEPTSALD 180
Cdd:COG0396 141 FSGGEKKRNEILQMLLLEPKLAILDETDSGLD 172
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
4-180 |
9.13e-23 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 95.30 E-value: 9.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 4 AILQVSDLS-VYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLkslnRM--GdLnpEVTTTGSVVYNGHniyspRTD 80
Cdd:PRK11650 2 AGLKLQAVRkSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLL----RMvaG-L--ERITSGEIWIGGR-----VVN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 81 TVELR-KEIGMVFQQPNPFP-MTIYENVVYGLRINGIkDKQVLDEAVEKAlqgASIWD-----EVKDRlydsaiGLSGGQ 153
Cdd:PRK11650 70 ELEPAdRDIAMVFQNYALYPhMSVRENMAYGLKIRGM-PKAEIEERVAEA---ARILElepllDRKPR------ELSGGQ 139
|
170 180
....*....|....*....|....*..
gi 2038545162 154 QQRVCVARVLATSPKIILLDEPTSALD 180
Cdd:PRK11650 140 RQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
17-180 |
1.55e-22 |
|
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: 95.88 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 17 KKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNIYspRTDTVELRKEIGMVFQQPN 96
Cdd:TIGR01842 330 KKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLI--VGIWPP---TSGSVRLDGADLK--QWDRETFGKHIGYLPQDVE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 97 PFPMTIYENVVyglRIngikDKQVLDEAVEKALQGASIwDEVKDRL---YDSAIG-----LSGGQQQRVCVARVLATSPK 168
Cdd:TIGR01842 403 LFPGTVAENIA---RF----GENADPEKIIEAAKLAGV-HELILRLpdgYDTVIGpggatLSGGQRQRIALARALYGDPK 474
|
170
....*....|..
gi 2038545162 169 IILLDEPTSALD 180
Cdd:TIGR01842 475 LVVLDEPNSNLD 486
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-180 |
3.17e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 92.06 E-value: 3.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYYN---------KKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrmgdLNPEVTTTGSVVYNGHNIY 75
Cdd:PRK10419 3 LLNVSGLSHHYAhgglsgkhqHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLL-----VGLESPSQGNVSWRGEPLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 76 S-PRTDTVELRKEIGMVFQQP----NPfPMTIYENVVYGLRingikDKQVLDEA-----VEKALQGASIWDEVKDRLYDS 145
Cdd:PRK10419 78 KlNRAQRKAFRRDIQMVFQDSisavNP-RKTVREIIREPLR-----HLLSLDKAerlarASEMLRAVDLDDSVLDKRPPQ 151
|
170 180 190
....*....|....*....|....*....|....*
gi 2038545162 146 aigLSGGQQQRVCVARVLATSPKIILLDEPTSALD 180
Cdd:PRK10419 152 ---LSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
24-216 |
3.93e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 93.56 E-value: 3.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 24 VSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDLnpevtTTGSVVYNGHniyspRTDTVELRK-EIGMVFQQPNPFP-MT 101
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDI-----TSGDLFIGEK-----RMNDVPPAErGVGMVFQSYALYPhLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 102 IYENVVYGLRINGIKdKQVLDEAVEKA---LQGASIWD-EVKDrlydsaigLSGGQQQRVCVARVLATSPKIILLDEPTS 177
Cdd:PRK11000 92 VAENMSFGLKLAGAK-KEEINQRVNQVaevLQLAHLLDrKPKA--------LSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2038545162 178 ALDpisAG-----KIEETLYGLKDKYTMLLVTRSMQQASRISDK 216
Cdd:PRK11000 163 NLD---AAlrvqmRIEISRLHKRLGRTMIYVTHDQVEAMTLADK 203
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
19-252 |
7.80e-22 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 91.00 E-value: 7.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 19 KALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdLNPevtTTGSVVYNGHNI----YSPRTdtvelrKEIGMVFQQ 94
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGM--IEP---TSGELLIDDHPLhfgdYSYRS------QRIRMIFQD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 95 P----NPfPMTIYENVVYGLRINGIKDKQVLDEAVEKALQGASIwdeVKDRLYDSAIGLSGGQQQRVCVARVLATSPKII 170
Cdd:PRK15112 96 PstslNP-RQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGL---LPDHASYYPHMLAPGQKQRLGLARALILRPKVI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 171 LLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQMFLDPQHKETEDYIT 248
Cdd:PRK15112 172 IADEALASLDMSMRSQLINLMLELQEKQgiSYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLIA 251
|
....
gi 2038545162 249 GKFG 252
Cdd:PRK15112 252 GHFG 255
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-213 |
9.55e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 93.74 E-value: 9.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYY--NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDLNpevttTGSVVYNGHNI--YSPRTdt 81
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQ-----QGEILLNGQPIadYSEAA-- 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 82 veLRKEIGMVFQQPNPFPMTIYENVVyglringIKDKQVLDEAVEKALQ--GASIWDEVKDRLyDSAIG-----LSGGQQ 154
Cdd:PRK11160 412 --LRQAISVVSQRVHLFSATLRDNLL-------LAAPNASDEALIEVLQqvGLEKLLEDDKGL-NAWLGeggrqLSGGEQ 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038545162 155 QRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGL-KDKyTMLLVT---RSMQQASRI 213
Cdd:PRK11160 482 RRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHaQNK-TVLMIThrlTGLEQFDRI 543
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
2-185 |
1.32e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 90.59 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 2 TDAILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPEvttTGSVVYNGHNIYS-PRTD 80
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIG--GQIAPD---HGEILFDGENIPAmSRSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 81 TVELRKEIGMVFQQPNPFP-MTIYENVVYGLRINGIKDKQVLD-------EAVekALQGASiwdevkdRLYDSAigLSGG 152
Cdd:PRK11831 79 LYTVRKRMSMLFQSGALFTdMNVFDNVAYPLREHTQLPAPLLHstvmmklEAV--GLRGAA-------KLMPSE--LSGG 147
|
170 180 190
....*....|....*....|....*....|...
gi 2038545162 153 QQQRVCVARVLATSPKIILLDEPTSALDPISAG 185
Cdd:PRK11831 148 MARRAALARAIALEPDLIMFDEPFVGQDPITMG 180
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-216 |
1.33e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 91.82 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 1 MTDAILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEvttTGSVVYNGhniySPRTD 80
Cdd:PRK13536 37 MSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMI--LGMTSPD---AGKITVLG----VPVPA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 81 TVEL-RKEIGMVFQQPNPFP-MTIYEN-VVYGlRINGIKDKQVlDEAVEKALQGASIWDEVKDRLYDsaigLSGGQQQRV 157
Cdd:PRK13536 108 RARLaRARIGVVPQFDNLDLeFTVRENlLVFG-RYFGMSTREI-EAVIPSLLEFARLESKADARVSD----LSGGMKRRL 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 158 CVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDK-YTMLLVTRSMQQASRISDK 216
Cdd:PRK13536 182 TLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARgKTILLTTHFMEEAERLCDR 241
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-226 |
1.45e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 90.43 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 1 MTDAI--LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdLNPevtTTGSVVYNGHNIysPR 78
Cdd:PRK10253 1 MTESVarLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRL--MTP---AHGHVWLDGEHI--QH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 79 TDTVELRKEIGMVFQQPN-PFPMTIYENVVYGLRING---IKDKQVLDEAVEKALQGASIwDEVKDRLYDSaigLSGGQQ 154
Cdd:PRK10253 74 YASKEVARRIGLLAQNATtPGDITVQELVARGRYPHQplfTRWRKEDEEAVTKAMQATGI-THLADQSVDT---LSGGQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038545162 155 QRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDK--YTMLLVTRSMQQASRISDKTGFFLDGDLI 226
Cdd:PRK10253 150 QRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREkgYTLAAVLHDLNQACRYASHLIALREGKIV 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-180 |
2.49e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.44 E-value: 2.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 8 VSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHniysprtdtvelrKE 87
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKIL--AGELEP---DSGEVSIPKG-------------LR 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 88 IGMVFQQPNPFP-MTIYENVVYGL-RINGIKDK----------------------QVLDEA--------VEKALQGASIW 135
Cdd:COG0488 63 IGYLPQEPPLDDdLTVLDTVLDGDaELRALEAEleeleaklaepdedlerlaelqEEFEALggweaearAEEILSGLGFP 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2038545162 136 DEVKDRLYDSaigLSGGQQQRVCVARVLATSPKIILLDEPTSALD 180
Cdd:COG0488 143 EEDLDRPVSE---LSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-213 |
2.84e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 92.48 E-value: 2.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 1 MTdAILQVSDLSVYY----NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLkslNRMGDLNPevTTTGSVVYNGHNIYS 76
Cdd:PRK10535 1 MT-ALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLM---NILGCLDK--PTSGTYRVAGQDVAT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 77 PRTDTV-ELRKE-IGMVFQQPNPFP-MTIYENV----VYGlrinGIKDKQVLDEAVEkALQGASIwdevKDRLYDSAIGL 149
Cdd:PRK10535 75 LDADALaQLRREhFGFIFQRYHLLShLTAAQNVevpaVYA----GLERKQRLLRAQE-LLQRLGL----EDRVEYQPSQL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038545162 150 SGGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDK-YTMLLVTRSMQ---QASRI 213
Cdd:PRK10535 146 SGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQvaaQAERV 213
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-227 |
3.08e-21 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 92.17 E-value: 3.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDLNPevtTTGSVVYngHNIYSPRTDTVE-- 83
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEP---TSGRIIY--HVALCEKCGYVErp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 84 -------------------------------LRKEIGMVFQQPnpFPM----TIYENVVYGLRINGIKDKQVLDEAVEka 128
Cdd:TIGR03269 76 skvgepcpvcggtlepeevdfwnlsdklrrrIRKRIAIMLQRT--FALygddTVLDNVLEALEEIGYEGKEAVGRAVD-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 129 lqgasIWDEVK--DRLYDSAIGLSGGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLY-GLKDK-YTMLLVT 204
Cdd:TIGR03269 152 -----LIEMVQlsHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEeAVKASgISMVLTS 226
|
250 260
....*....|....*....|...
gi 2038545162 205 RSMQQASRISDKTGFFLDGDLIE 227
Cdd:TIGR03269 227 HWPEVIEDLSDKAIWLENGEIKE 249
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-228 |
3.39e-21 |
|
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: 88.24 E-value: 3.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 2 TDAILQVSDLSVYY--NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDlnpevTTTGSVVYNGHNIYSprT 79
Cdd:cd03369 3 EHGEIEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLE-----AEEGKIEIDGIDIST--I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 80 DTVELRKEIGMVFQQPNPFPMTIYENVvyglrinGIKDKQVlDEAVEKALqgasiwdevkdRLYDSAIGLSGGQQQRVCV 159
Cdd:cd03369 76 PLEDLRSSLTIIPQDPTLFSGTIRSNL-------DPFDEYS-DEEIYGAL-----------RVSEGGLNLSQGQRQLLCL 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2038545162 160 ARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTMLLVtrsmqqASRIS-----DKTGFFLDGDLIEF 228
Cdd:cd03369 137 ARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTI------AHRLRtiidyDKILVMDAGEVKEY 204
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
5-243 |
3.57e-21 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 90.54 E-value: 3.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYYNKK-------------KALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrmgdLNPEVTTTGSVVYNG 71
Cdd:PRK15079 8 LLEVADLKVHFDIKdgkqwfwqppktlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAI-----IGLVKATDGEVAWLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 72 HNIYSPRTDTV-ELRKEIGMVFQQP----NPfPMTIYENVVYGLRINGIKDKQvldeavekalqgasiwDEVKDRLYD-- 144
Cdd:PRK15079 83 KDLLGMKDDEWrAVRSDIQMIFQDPlaslNP-RMTIGEIIAEPLRTYHPKLSR----------------QEVKDRVKAmm 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 145 SAIGL------------SGGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTMLLV--TRSMQQA 210
Cdd:PRK15079 146 LKVGLlpnlinryphefSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIfiAHDLAVV 225
|
250 260 270
....*....|....*....|....*....|...
gi 2038545162 211 SRISDKTGFFLDGDLIEFNDTKQMFLDPQHKET 243
Cdd:PRK15079 226 KHISDRVLVMYLGHAVELGTYDEVYHNPLHPYT 258
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
16-204 |
3.75e-21 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 92.03 E-value: 3.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 16 NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEVTTTGSVVYNGHNIYSPrtdtvELRKEIGMVFQQP 95
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNAL--AFRSPKGVKGSGSVLLNGMPIDAK-----EMRAISAYVQQDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 96 NPFPM-TIYENVVYG--LRINGIKDKQVLDEAVEKALQGASIWDEVKDRL--YDSAIGLSGGQQQRVCVARVLATSPKII 170
Cdd:TIGR00955 109 LFIPTlTVREHLMFQahLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIgvPGRVKGLSGGERKRLAFASELLTDPPLL 188
|
170 180 190
....*....|....*....|....*....|....
gi 2038545162 171 LLDEPTSALDPISAGKIEETLYGLKDKYTMLLVT 204
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICT 222
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-180 |
5.37e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 88.69 E-value: 5.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 2 TDAILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdlnpEVTTTGSVVYNGHNIYSprTDT 81
Cdd:PRK10575 8 SDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRH-----QPPSEGEILLDAQPLES--WSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 82 VELRKEIGMVFQQ-PNPFPMTIYENVVYG-------LRINGIKDKQVLDEAVekALQGASiwdEVKDRLYDSaigLSGGQ 153
Cdd:PRK10575 81 KAFARKVAYLPQQlPAAEGMTVRELVAIGrypwhgaLGRFGAADREKVEEAI--SLVGLK---PLAHRLVDS---LSGGE 152
|
170 180
....*....|....*....|....*..
gi 2038545162 154 QQRVCVARVLATSPKIILLDEPTSALD 180
Cdd:PRK10575 153 RQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-188 |
6.13e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 88.91 E-value: 6.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLksLNRMGDLNPEvttTGSVVYNGHNIYSPRTDTVEL 84
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLF--MNLSGLLRPQ---KGAVLWQGKPLDYSKRGLLAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 85 RKEIGMVFQQPNP--FPMTIYENVVYGLRINGIKDKQVLdEAVEKALqgaSIWDEVKDRlYDSAIGLSGGQQQRVCVARV 162
Cdd:PRK13638 76 RQQVATVFQDPEQqiFYTDIDSDIAFSLRNLGVPEAEIT-RRVDEAL---TLVDAQHFR-HQPIQCLSHGQKKRVAIAGA 150
|
170 180
....*....|....*....|....*.
gi 2038545162 163 LATSPKIILLDEPTSALDPisAGKIE 188
Cdd:PRK13638 151 LVLQARYLLLDEPTAGLDP--AGRTQ 174
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-228 |
9.53e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.51 E-value: 9.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYnGHNIysprtdtvel 84
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLL--AGELEP---DSGTVKL-GETV---------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 85 rkEIGMVFQQPNPFP--MTIYENVvyglringikdKQVLDEAVEKAL---------QGASIWDEVKDrlydsaigLSGGQ 153
Cdd:COG0488 379 --KIGYFDQHQEELDpdKTVLDEL-----------RDGAPGGTEQEVrgylgrflfSGDDAFKPVGV--------LSGGE 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038545162 154 QQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLyglkDKY--TMLLVTRSMQQASRISDKTGFFLDGDLIEF 228
Cdd:COG0488 438 KARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEAL----DDFpgTVLLVSHDRYFLDRVATRILEFEDGGVREY 510
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-216 |
1.87e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 87.94 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 1 MTDAILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEvttTGSVVYNGHNI--YSPR 78
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRML--LGLTHPD---AGSISLCGEPVpsRARH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 79 TdtvelRKEIGMVFQQPNPFP-MTIYENVVYGLRINGIKDKQVlDEAVEKALQGASIWDEVKDRLYDsaigLSGGQQQRV 157
Cdd:PRK13537 78 A-----RQRVGVVPQFDNLDPdFTVRENLLVFGRYFGLSAAAA-RALVPPLLEFAKLENKADAKVGE----LSGGMKRRL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 158 CVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDK-YTMLLVTRSMQQASRISDK 216
Cdd:PRK13537 148 TLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARgKTILLTTHFMEEAERLCDR 207
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-234 |
2.66e-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: 2.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 3 DAILQVSDLSVYY-----NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSV-VYNGH---N 73
Cdd:TIGR03269 277 EPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKII--AGVLEP---TSGEVnVRVGDewvD 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 74 IYSPRTDTV-ELRKEIGMVFQQPNPFP-MTIYENVVYGLRIngikdkQVLDE-AVEKA---LQGASIWDE----VKDRLY 143
Cdd:TIGR03269 352 MTKPGPDGRgRAKRYIGILHQEYDLYPhRTVLDNLTEAIGL------ELPDElARMKAvitLKMVGFDEEkaeeILDKYP 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 144 DSaigLSGGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQQASRISDKTGFFL 221
Cdd:TIGR03269 426 DE---LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMeqTFIIVSHDMDFVLDVCDRAALMR 502
|
250
....*....|...
gi 2038545162 222 DGDLIEFNDTKQM 234
Cdd:TIGR03269 503 DGKIVKIGDPEEI 515
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
6-226 |
3.94e-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: 85.53 E-value: 3.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPevtTTGSVVYNGHNIysPRTDTvelr 85
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMIT--GILRP---TSGEIIFDGHPW--TRKDL---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 86 KEIGMVFQQPNPFP-MTIYENVVYGLRINGIKDKQVlDEAVEKALQGASIWDEVKDrlydsaigLSGGQQQRVCVARVLA 164
Cdd:TIGR03740 70 HKIGSLIESPPLYEnLTARENLKVHTTLLGLPDSRI-DEVLNIVDLTNTGKKKAKQ--------FSLGMKQRLGIAIALL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038545162 165 TSPKIILLDEPTSALDPISAGKIEETLYGLKDK-YTMLLVTRSMQQASRISDKTGFFLDGDLI 226
Cdd:TIGR03740 141 NHPKLLILDEPTNGLDPIGIQELRELIRSFPEQgITVILSSHILSEVQQLADHIGIISEGVLG 203
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
4-241 |
5.96e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 85.72 E-value: 5.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 4 AILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEvttTGSVVYNGHNIySPRTDTVE 83
Cdd:PRK10895 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMV--VGIVPRD---AGNIIIDDEDI-SLLPLHAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 84 LRKEIGMVFQQPNPFP-MTIYENVVYGLRINGIKDKQVLDEAVEKALQGASIwDEVKDRLYDSaigLSGGQQQRVCVARV 162
Cdd:PRK10895 76 ARRGIGYLPQEASIFRrLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHI-EHLRDSMGQS---LSGGERRRVEIARA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 163 LATSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTMLLVT-RSMQQASRISDKTGFFLDGDLIEFNDTKQMFLDPQHK 241
Cdd:PRK10895 152 LAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVK 231
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
5-226 |
5.97e-20 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 86.03 E-value: 5.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPE-----VTTTGSVVYNGHNIYspRT 79
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKAL--AGDLTGGgaprgARVTGDVTLNGEPLA--AI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 80 DTVELRKEIGMVFQQPNP-FPMTIYENVVYG----LRING---IKDKQVLDEAVEKAlqGASIWDEvKDrlydsAIGLSG 151
Cdd:PRK13547 77 DAPRLARLRAVLPQAAQPaFAFSAREIVLLGryphARRAGaltHRDGEIAWQALALA--GATALVG-RD-----VTTLSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 152 GQQQRVCVARVLA---------TSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTM--LLVTRSMQQASRISDKTGFF 220
Cdd:PRK13547 149 GELARVQFARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgvLAIVHDPNLAARHADRIAML 228
|
....*.
gi 2038545162 221 LDGDLI 226
Cdd:PRK13547 229 ADGAIV 234
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-225 |
1.11e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 85.11 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdlnpEVTTTGSVVynghniySPRTDTVELR 85
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGL-----ETPSAGELL-------AGTAPLAEAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 86 KEIGMVFQQPNPFP-MTIYENVVYGLRINgikdkqvLDEAVEKALQGASIwdevKDRLYDSAIGLSGGQQQRVCVARVLA 164
Cdd:PRK11247 81 EDTRLMFQDARLLPwKKVIDNVGLGLKGQ-------WRDAALQALAAVGL----ADRANEWPAALSGGQKQRVALARALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038545162 165 TSPKIILLDEPTSALDPISagKIE-----ETLYgLKDKYTMLLVTRSMQQASRISDKTGFFLDGDL 225
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALT--RIEmqdliESLW-QQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-194 |
1.24e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 87.56 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 2 TDAILQVSDLSVY-YNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmgdlnpevtttgsvvynGhnIYSPRTD 80
Cdd:COG4178 359 EDGALALEDLTLRtPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIA------------------G--LWPYGSG 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 81 TVELRKEIGMVF--QQPNpFPM-TIYENVVYGLRingikDKQVLDEAVEKALQGASIwDEVKDRLYDSA---IGLSGGQQ 154
Cdd:COG4178 419 RIARPAGARVLFlpQRPY-LPLgTLREALLYPAT-----AEAFSDAELREALEAVGL-GHLAERLDEEAdwdQVLSLGEQ 491
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2038545162 155 QRVCVARVLATSPKIILLDEPTSALDPISagkiEETLYGL 194
Cdd:COG4178 492 QRLAFARLLLHKPDWLFLDEATSALDEEN----EAALYQL 527
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
5-180 |
1.67e-19 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 87.08 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYY--NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDLnpevtTTGSVVYNGHNIYSPRTDtv 82
Cdd:PRK10789 313 ELDVNIRQFTYpqTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDV-----SEGDIRFHDIPLTKLQLD-- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 83 ELRKEIGMVFQQPNPFPMTIYENVVYGlRINGIKdkqvldEAVEKALQGASIWDEVKdRL---YDSAIG-----LSGGQQ 154
Cdd:PRK10789 386 SWRSRLAVVSQTPFLFSDTVANNIALG-RPDATQ------QEIEHVARLASVHDDIL-RLpqgYDTEVGergvmLSGGQK 457
|
170 180
....*....|....*....|....*.
gi 2038545162 155 QRVCVARVLATSPKIILLDEPTSALD 180
Cdd:PRK10789 458 QRISIARALLLNAEILILDDALSAVD 483
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
7-213 |
2.06e-19 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 86.86 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 7 QVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEvTTTGSVVYNGhniyspRTDTVELRK 86
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNAL--AGRIQGN-NFTGTILANN------RKPTKQILK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 87 EIGMVFQQPNPFP-MTIYENVVYG--LRINGIKDKQvldeavEKALQGASIWDEVKDRLYDSAI-------GLSGGQQQR 156
Cdd:PLN03211 141 RTGFVTQDDILYPhLTVRETLVFCslLRLPKSLTKQ------EKILVAESVISELGLTKCENTIignsfirGISGGERKR 214
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2038545162 157 VCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKyTMLLVTRSMQQASRI 213
Cdd:PLN03211 215 VSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQPSSRV 270
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
5-244 |
2.15e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 86.83 E-value: 2.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYYNKKK----ALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdlnpeVTTTGSVVYNGHNIYSPRTD 80
Cdd:PRK10261 12 VLAVENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRL------LEQAGGLVQCDKMLLRRRSR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 81 TV-ELRK------------EIGMVFQQP----NPFpMTIYENVVYGLRIN-GIKDKQVLDEAvEKALQGASIwDEVKDRL 142
Cdd:PRK10261 86 QViELSEqsaaqmrhvrgaDMAMIFQEPmtslNPV-FTVGEQIAESIRLHqGASREEAMVEA-KRMLDQVRI-PEAQTIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 143 YDSAIGLSGGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTM--LLVTRSMQQASRISDKTGFF 220
Cdd:PRK10261 163 SRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgvIFITHDMGVVAEIADRVLVM 242
|
250 260
....*....|....*....|....
gi 2038545162 221 LDGDLIEFNDTKQMFLDPQHKETE 244
Cdd:PRK10261 243 YQGEAVETGSVEQIFHAPQHPYTR 266
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
6-214 |
1.61e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 84.38 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNK-KKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNI--YSPRTdtv 82
Cdd:PRK10790 341 IDIDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLL--MGYYPL---TEGEIRLDGRPLssLSHSV--- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 83 eLRKEIGMVFQQPNPFPMTIYENVVYGLRINGIKDKQVLdEAVEKALQGASIWDEVKDRLYDSAIGLSGGQQQRVCVARV 162
Cdd:PRK10790 413 -LRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQAL-ETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARV 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2038545162 163 LATSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTMLLVtrsmqqASRIS 214
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVI------AHRLS 536
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-233 |
1.62e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 81.67 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 1 MTDAIlQVSDLSVYY----------------------NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdLN 58
Cdd:COG1134 1 MSSMI-EVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGI--LE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 59 PevtTTGSVVYNGhNIYSPrtdtveLrkEIGMVFqQPNpfpMTIYENVVYGLRINGIKDKQV---LDEAVEKAlqgasiw 135
Cdd:COG1134 78 P---TSGRVEVNG-RVSAL------L--ELGAGF-HPE---LTGRENIYLNGRLLGLSRKEIdekFDEIVEFA------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 136 dEVKD------RLYdsaiglSGGQQQRVCVARVLATSPKIILLDEPTSALDPI----SAGKIEEtlygLKDKY-TMLLVT 204
Cdd:COG1134 135 -ELGDfidqpvKTY------SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRE----LRESGrTVIFVS 203
|
250 260 270
....*....|....*....|....*....|
gi 2038545162 205 RSMQQASRISDKtGFFLD-GDLIEFNDTKQ 233
Cdd:COG1134 204 HSMGAVRRLCDR-AIWLEkGRLVMDGDPEE 232
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
15-216 |
2.38e-18 |
|
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: 81.22 E-value: 2.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 15 YNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPevtTTGSVVYNGhniYSPRTDTVELRKEIGMVFQQ 94
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILS--GLLQP---TSGEVRVAG---LVPWKRRKKFLRRIGVVFGQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 95 PNP--FPMTIYENVVYGLRINGIKD---KQVLDEAVEkALQgasiwdeVKDRLYDSAIGLSGGQQQRVCVARVLATSPKI 169
Cdd:cd03267 103 KTQlwWDLPVIDSFYLLAAIYDLPParfKKRLDELSE-LLD-------LEELLDTPVRQLSLGQRMRAEIAAALLHEPEI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2038545162 170 ILLDEPTSALDPISAGKIEETL--YGLKDKYTMLLVTRSMQQASRISDK 216
Cdd:cd03267 175 LFLDEPTIGLDVVAQENIRNFLkeYNRERGTTVLLTSHYMKDIEALARR 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-176 |
3.31e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.14 E-value: 3.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 3 DAILQVSDLSVyynkKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGH--NIYSPRtD 80
Cdd:COG1129 254 EVVLEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARAL--FGADPA---DSGEIRLDGKpvRIRSPR-D 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 81 TVEL--------RKEIGMVFqqpnpfPMTIYENVVYG----LRINGIKDKQVLDEAVEKALQG-----ASIWDEVKDrly 143
Cdd:COG1129 324 AIRAgiayvpedRKGEGLVL------DLSIRENITLAsldrLSRGGLLDRRRERALAEEYIKRlriktPSPEQPVGN--- 394
|
170 180 190
....*....|....*....|....*....|...
gi 2038545162 144 dsaigLSGGQQQRVCVARVLATSPKIILLDEPT 176
Cdd:COG1129 395 -----LSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
6-180 |
4.30e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 80.65 E-value: 4.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVyynkKKALNSVSLSFQPKEITALIGPSGSGKSTLlksLNRMGDLNPEvttTGSVVYNGHNI--YSPRtdtvE 83
Cdd:COG4138 1 LQLNDVAV----AGRLGPISAQVNAGELIHLIGPNGAGKSTL---LARMAGLLPG---QGEILLNGRPLsdWSAA----E 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 84 LRKEIGMVFQQ-PNPFPMTIYENVVYGLRingikdKQVLDEAVEKALQgasiwdEVKDRL-----YDSAIG-LSGGQQQR 156
Cdd:COG4138 67 LARHRAYLSQQqSPPFAMPVFQYLALHQP------AGASSEAVEQLLA------QLAEALgledkLSRPLTqLSGGEWQR 134
|
170 180 190
....*....|....*....|....*....|.
gi 2038545162 157 VCVARVL-----ATSP--KIILLDEPTSALD 180
Cdd:COG4138 135 VRLAAVLlqvwpTINPegQLLLLDEPMNSLD 165
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-208 |
4.42e-18 |
|
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: 80.07 E-value: 4.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 21 LNSVSLSFQPKEITALIGPSGSGKSTLLksLNRMGDLNpevTTTGSVVYNGHNIYSPRTDTVELRKEIGMVF--QQPNPF 98
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLL--LAILGEMQ---TLEGKVHWSNKNESEPSFEATRSRNRYSVAYaaQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 99 PMTIYENVVYGLRINGIKDKQVLDE-AVEKALQGASIWDEVKdrLYDSAIGLSGGQQQRVCVARVLATSPKIILLDEPTS 177
Cdd:cd03290 92 NATVEENITFGSPFNKQRYKAVTDAcSLQPDIDLLPFGDQTE--IGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190
....*....|....*....|....*....|....
gi 2038545162 178 ALD-PISAGKIEETLYGL--KDKYTMLLVTRSMQ 208
Cdd:cd03290 170 ALDiHLSDHLMQEGILKFlqDDKRTLVLVTHKLQ 203
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
6-180 |
7.68e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.15 E-value: 7.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEvttTGSVVYNGHNIYSP--RTDTVE 83
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLI--AGLLPPA---AGTIKLDGGDIDDPdvAEACHY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 84 LRKEIGMvfqqpNPFpMTIYENVVYGLRINGIKDKQVlDEAVEK-ALQGasiwdeVKDRLYDSaigLSGGQQQRVCVARV 162
Cdd:PRK13539 78 LGHRNAM-----KPA-LTVAENLEFWAAFLGGEELDI-AAALEAvGLAP------LAHLPFGY---LSAGQKRRVALARL 141
|
170
....*....|....*...
gi 2038545162 163 LATSPKIILLDEPTSALD 180
Cdd:PRK13539 142 LVSNRPIWILDEPTAALD 159
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
4-244 |
8.97e-18 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 80.94 E-value: 8.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 4 AILQVSDLSVYYNKK----KALNSVSLSFQPKEITALIGPSGSGKStlLKSLNRMGDLN-PEVTTTGSVVYNGHNIYspR 78
Cdd:PRK11022 2 ALLNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKS--VSSLAIMGLIDyPGRVMAEKLEFNGQDLQ--R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 79 TDTVELRK----EIGMVFQQP----NPfPMTIYENVVYGLRINGIKDKQVLDEAVEKALQGASIWDEvKDRLYDSAIGLS 150
Cdd:PRK11022 78 ISEKERRNlvgaEVAMIFQDPmtslNP-CYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDP-ASRLDVYPHQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 151 GGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKYTM--LLVTRSMQQASRISDKTGFFLDGDLIEF 228
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMalVLITHDLALVAEAAHKIIVMYAGQVVET 235
|
250
....*....|....*.
gi 2038545162 229 NDTKQMFLDPQHKETE 244
Cdd:PRK11022 236 GKAHDIFRAPRHPYTQ 251
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
18-225 |
1.20e-17 |
|
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: 81.98 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 18 KKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPevtTTGSVVYNGHNIyspRTDTVELRKEIGMVFQQPNP 97
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILT--GLLPP---TSGTVLVGGKDI---ETNLDAVRQSLGMCPQHNIL 1014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 98 FP-MTIYENVVYGLRINGIKDKQVLDEaVEKALQGASIWDEVKDRLYDsaigLSGGQQQRVCVARVLATSPKIILLDEPT 176
Cdd:TIGR01257 1015 FHhLTVAEHILFYAQLKGRSWEEAQLE-MEAMLEDTGLHHKRNEEAQD----LSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2038545162 177 SALDPISAGKIEETLYGLKDKYTMLLVTRSMQQASRISDKTGFFLDGDL 225
Cdd:TIGR01257 1090 SGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
24-243 |
1.42e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 79.36 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 24 VSLSFQPKEITALIGPSGSGKStlLKSLNRMGDLNPEVT-TTGSVVYNGHNIySPRtdtvELR-KEIGMVFQQP----NP 97
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRqTAGRVLLDGKPV-APC----ALRgRKIATIMQNPrsafNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 98 FpMTIYENVVYGLRINGikdKQVLDEAVEKALQGASIWDevKDRLYDS-AIGLSGGQQQRVCVARVLATSPKIILLDEPT 176
Cdd:PRK10418 95 L-HTMHTHARETCLALG---KPADDATLTAALEAVGLEN--AARVLKLyPFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038545162 177 SALDPISAGKIEETLYGLKDKYT--MLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQMFLDPQHKET 243
Cdd:PRK10418 169 TDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVT 237
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-217 |
1.57e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 79.54 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 1 MTDAILQVSDLSVYY-NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDL---NPEVTTTGSVVYNG--HNI 74
Cdd:PRK15056 2 MQQAGIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKAL--MGFVrlaSGKISILGQPTRQAlqKNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 75 --YSPRTDTVELRkeigmvfqqpnpFPMTIyENVV----YG----LRINGIKDKQVLDEAVEKAlqgasiwDEVKDRlyD 144
Cdd:PRK15056 80 vaYVPQSEEVDWS------------FPVLV-EDVVmmgrYGhmgwLRRAKKRDRQIVTAALARV-------DMVEFR--H 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2038545162 145 SAIG-LSGGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDK-YTMLLVTRSMQQASRISDKT 217
Cdd:PRK15056 138 RQIGeLSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYT 212
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
14-224 |
1.65e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 79.65 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 14 YYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPEvttTGSVVYNGHNIYSPrTDTVELRKEIGMVFQ 93
Cdd:PRK13644 11 YPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLN--GLLRPQ---KGKVLVSGIDTGDF-SKLQGIRKLVGIVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 94 QPNP--FPMTIYENVVYG---LRINGIKDKQVLDEAV-EKALQgasiwdevKDRlYDSAIGLSGGQQQRVCVARVLATSP 167
Cdd:PRK13644 85 NPETqfVGRTVEEDLAFGpenLCLPPIEIRKRVDRALaEIGLE--------KYR-HRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038545162 168 KIILLDEPTSALDPISAGKIEETLYGLKDK-YTMLLVTRSMQQ---ASRI--SDKTGFFLDGD 224
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEElhdADRIivMDRGKIVLEGE 218
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-180 |
1.82e-17 |
|
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: 77.47 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 3 DAILQVSDLSVyynkKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEvttTGSVVYNGH--NIYSPRtD 80
Cdd:cd03215 2 EPVLEVRGLSV----KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEAL--FGLRPPA---SGEITLDGKpvTRRSPR-D 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 81 TVEL--------RKEIGMVFQqpnpfpMTIYENVVYGLRingikdkqvldeavekalqgasiwdevkdrlydsaigLSGG 152
Cdd:cd03215 72 AIRAgiayvpedRKREGLVLD------LSVAENIALSSL-------------------------------------LSGG 108
|
170 180
....*....|....*....|....*...
gi 2038545162 153 QQQRVCVARVLATSPKIILLDEPTSALD 180
Cdd:cd03215 109 NQQKVVLARWLARDPRVLILDEPTRGVD 136
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-204 |
5.42e-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: 75.18 E-value: 5.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPE--VTTTGSVVYNGHniysprtdtve 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLI--AGELEPDegIVTWGSTVKIGY----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 84 lrkeigmvFQQpnpfpmtiyenvvyglringikdkqvldeavekalqgasiwdevkdrlydsaigLSGGQQQRVCVARVL 163
Cdd:cd03221 68 --------FEQ------------------------------------------------------LSGGEKMRLALAKLL 85
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2038545162 164 ATSPKIILLDEPTSALDPISAGKIEETLYGLKDkyTMLLVT 204
Cdd:cd03221 86 LENPNLLLLDEPTNHLDLESIEALEEALKEYPG--TVILVS 124
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-230 |
7.99e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.18 E-value: 7.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 2 TDAILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPevtTTGSVVYNGHNIYSPRTdT 81
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILS--GNYQP---DAGSILIDGQEMRFAST-T 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 82 VELRKEIGMVFQQPNPFP-MTIYENVVYGLRIN--GIKDKQVLDEAVEKALQ--GASIWDEVKDRLydsaigLSGGQQQR 156
Cdd:PRK11288 75 AALAAGVAIIYQELHLVPeMTVAENLYLGQLPHkgGIVNRRLLNYEAREQLEhlGVDIDPDTPLKY------LSIGQRQM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 157 VCVARVLATSPKIILLDEPTSALdpiSAGKIEEtLYG----LKDKYTMLL-VTRSMQQASRISDKTGFFLDGDLIE-FND 230
Cdd:PRK11288 149 VEIAKALARNARVIAFDEPTSSL---SAREIEQ-LFRvireLRAEGRVILyVSHRMEEIFALCDAITVFKDGRYVAtFDD 224
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-179 |
1.33e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 78.51 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 2 TDAILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDLNpevttTGSVVYNGH--NIYSPRt 79
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRD-----AGSILYLGKevTFNGPK- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 80 DTVElrKEIGMVFQQPNPFP-MTIYENVVYGL----RINGIKDKQVLDEAvEKALQGASIWDEVKDRLYDsaigLSGGQQ 154
Cdd:PRK10762 75 SSQE--AGIGIIHQELNLIPqLTIAENIFLGRefvnRFGRIDWKKMYAEA-DKLLARLNLRFSSDKLVGE----LSIGEQ 147
|
170 180
....*....|....*....|....*
gi 2038545162 155 QRVCVARVLATSPKIILLDEPTSAL 179
Cdd:PRK10762 148 QMVEIAKVLSFESKVIIMDEPTDAL 172
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
6-191 |
1.60e-16 |
|
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: 76.82 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNK--KKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMgdlnpeVTTTGSVVYNGHNiysprTDTVE 83
Cdd:cd03289 3 MTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL------LNTEGDIQIDGVS-----WNSVP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 84 L---RKEIGMVFQQPNPFPMTIYENV-VYGLRingiKDKQVLDEAVEKALQgaSIWDEVKDRL----YDSAIGLSGGQQQ 155
Cdd:cd03289 72 LqkwRKAFGVIPQKVFIFSGTFRKNLdPYGKW----SDEEIWKVAEEVGLK--SVIEQFPGQLdfvlVDGGCVLSHGHKQ 145
|
170 180 190
....*....|....*....|....*....|....*.
gi 2038545162 156 RVCVARVLATSPKIILLDEPTSALDPISAGKIEETL 191
Cdd:cd03289 146 LMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTL 181
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-208 |
2.16e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 77.05 E-value: 2.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 15 YNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPevtTTGSVVYNGHNiysPRTDTVELRKEIGMVFQQ 94
Cdd:COG4586 32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLT--GILVP---TSGEVRVLGYV---PFKRRKEFARRIGVVFGQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 95 PN------PfpmtiyenVVYGLRIN----GIKD---KQVLDEAVEkALqgasiwdEVKDRLYDSAIGLSGGQQQRVCVAR 161
Cdd:COG4586 104 RSqlwwdlP--------AIDSFRLLkaiyRIPDaeyKKRLDELVE-LL-------DLGELLDTPVRQLSLGQRMRCELAA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2038545162 162 VLATSPKIILLDEPTSALDPISAGKIEETLYGLKDKY--TMLLVTRSMQ 208
Cdd:COG4586 168 ALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMD 216
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
24-180 |
2.45e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 77.22 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 24 VSLSFQPKEITALIGPSGSGKSTLLkslNRMGDL-NPEvttTGSVVYNGHNIYSPRTD---TVELRKeIGMVFQQPNPFP 99
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLI---NAISGLtRPQ---KGRIVLNGRVLFDAEKGiclPPEKRR-IGYVFQDARLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 100 -MTIYENVVYGLRIngiKDKQVLDEAVEkaLQGAsiwDEVKDRLydsAIGLSGGQQQRVCVARVLATSPKIILLDEPTSA 178
Cdd:PRK11144 90 hYKVRGNLRYGMAK---SMVAQFDKIVA--LLGI---EPLLDRY---PGSLSGGEKQRVAIGRALLTAPELLLMDEPLAS 158
|
..
gi 2038545162 179 LD 180
Cdd:PRK11144 159 LD 160
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-179 |
4.12e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 77.28 E-value: 4.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 1 MTDAILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmgDLNPEVTTTGSVVYNG-----HNIy 75
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLS---GVYPHGTYEGEIIFEGeelqaSNI- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 76 sprTDTvElRKEIGMVFQQ----PNpfpMTIYENVVYGLRI--NGIKDKQVLDEAVEKALQGASIWDEVKDRLYDsaigL 149
Cdd:PRK13549 77 ---RDT-E-RAGIAIIHQElalvKE---LSVLENIFLGNEItpGGIMDYDAMYLRAQKLLAQLKLDINPATPVGN----L 144
|
170 180 190
....*....|....*....|....*....|
gi 2038545162 150 SGGQQQRVCVARVLATSPKIILLDEPTSAL 179
Cdd:PRK13549 145 GLGQQQLVEIAKALNKQARLLILDEPTASL 174
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
16-184 |
6.77e-16 |
|
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: 73.84 E-value: 6.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 16 NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPEVTTTGSVVYNGHNIyspRTDTVELRKEIGMVFQQP 95
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALA--NRTEGNVSVEGDIHYNGIPY---KEFAEKYPGEIIYVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 96 NPFP-MTIYENVVYGLRINGikdkqvlDEAVEkalqgasiwdevkdrlydsaiGLSGGQQQRVCVARVLATSPKIILLDE 174
Cdd:cd03233 93 VHFPtLTVRETLDFALRCKG-------NEFVR---------------------GISGGERKRVSIAEALVSRASVLCWDN 144
|
170
....*....|
gi 2038545162 175 PTSALDPISA 184
Cdd:cd03233 145 STRGLDSSTA 154
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-207 |
5.69e-15 |
|
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: 74.21 E-value: 5.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 21 LNSVSLSFQPKEITALIGPSGSGKSTLLKSL-NRMGDLNPEVTTTGSVVYnghniysprtdtvelrkeigmVFQQPNPFP 99
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALlAEMDKVEGHVHMKGSVAY---------------------VPQQAWIQN 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 100 MTIYENVVYGLRINGIKDKQVLDE-AVEKALQGASIWDEVKdrLYDSAIGLSGGQQQRVCVARVLATSPKIILLDEPTSA 178
Cdd:TIGR00957 713 DSLRENILFGKALNEKYYQQVLEAcALLPDLEILPSGDRTE--IGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSA 790
|
170 180 190
....*....|....*....|....*....|...
gi 2038545162 179 LDPISAGKIEETLYG----LKDKyTMLLVTRSM 207
Cdd:TIGR00957 791 VDAHVGKHIFEHVIGpegvLKNK-TRILVTHGI 822
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
5-248 |
6.13e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 73.71 E-value: 6.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmgDLNPEVTTTGSVVYNGHNIYSPRTDTVEl 84
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILS---GVYPHGTWDGEIYWSGSPLKASNIRDTE- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 85 RKEIGMVFQQPNPFP-MTIYENVVYGLRIN---GIKDKQVLDEAVEKALQGASIwDEVKDRLYDSAIGlsGGQQQRVCVA 160
Cdd:TIGR02633 77 RAGIVIIHQELTLVPeLSVAENIFLGNEITlpgGRMAYNAMYLRAKNLLRELQL-DADNVTRPVGDYG--GGQQQLVEIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 161 RVLATSPKIILLDEPTSALdpiSAGKIEETLYGLKD----KYTMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQMfl 236
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSL---TEKETEILLDIIRDlkahGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM-- 228
|
250
....*....|..
gi 2038545162 237 dpqhkETEDYIT 248
Cdd:TIGR02633 229 -----SEDDIIT 235
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6-191 |
1.03e-14 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 73.41 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNK--KKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDLNPEVTTTGsVVYNGHNIYsprtdtvE 83
Cdd:TIGR01271 1218 MDVQGLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDG-VSWNSVTLQ-------T 1289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 84 LRKEIGMVFQQPNPFPMTIYENVVYGLRINgikDKQVLDEAVEKALQgaSIWDEVKDRL----YDSAIGLSGGQQQRVCV 159
Cdd:TIGR01271 1290 WRKAFGVIPQKVFIFSGTFRKNLDPYEQWS---DEEIWKVAEEVGLK--SVIEQFPDKLdfvlVDGGYVLSNGHKQLMCL 1364
|
170 180 190
....*....|....*....|....*....|..
gi 2038545162 160 ARVLATSPKIILLDEPTSALDPISAGKIEETL 191
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLDPVTLQIIRKTL 1396
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
17-191 |
1.30e-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: 69.96 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 17 KKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDLNpevTTTGSVVYNGhniySPRTDTveLRKEIGMVFQQPN 96
Cdd:cd03232 19 KRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAG---VITGEILING----RPLDKN--FQRSTGYVEQQDV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 97 PFPM-TIYENVVYG--LRingikdkqvldeavekalqgasiwdevkdrlydsaiGLSGGQQQRVCVARVLATSPKIILLD 173
Cdd:cd03232 90 HSPNlTVREALRFSalLR------------------------------------GLSVEQRKRLTIGVELAAKPSILFLD 133
|
170
....*....|....*...
gi 2038545162 174 EPTSALDPISAGKIEETL 191
Cdd:cd03232 134 EPTSGLDSQAAYNIVRFL 151
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
3-216 |
1.36e-14 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 73.02 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 3 DAILQVSDLSVYYNKkkALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNIYSPRTDTV 82
Cdd:TIGR01271 426 DDGLFFSNFSLYVTP--VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMI--MGELEP---SEGKIKHSGRISFSPQTSWI 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 83 elrkeigmvfqqpnpFPMTIYENVVYGLRINGIKDKQVLdeaveKALQ---GASIWDEvKDR--LYDSAIGLSGGQQQRV 157
Cdd:TIGR01271 499 ---------------MPGTIKDNIIFGLSYDEYRYTSVI-----KACQleeDIALFPE-KDKtvLGEGGITLSGGQRARI 557
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 158 CVARVLATSPKIILLDEPTSALDPISAGKI-EETLYGLKDKYTMLLVTRSMQQASRiSDK 216
Cdd:TIGR01271 558 SLARAVYKDADLYLLDSPFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKK-ADK 616
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
6-205 |
1.46e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.14 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVS-LSFQPKE--ITALIGPSGSGKSTLLKSLNRMGDlnpevTTTGSVVYN-GHNIysprtDT 81
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVEIYKdLNFTLTEgkTYAFVGESGCGKSTILKLIERLYD-----PTEGDIIINdSHNL-----KD 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 82 VEL---RKEIGMVFQQPNPFPMTIYENVVYGLRinGIKDKQVLDEAVEK------------------------------- 127
Cdd:PTZ00265 453 INLkwwRSKIGVVSQDPLLFSNSIKNNIKYSLY--SLKDLEALSNYYNEdgndsqenknkrnscrakcagdlndmsnttd 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 128 ---ALQGASIWDEVKDR--------------------LYDSAIG-----LSGGQQQRVCVARVLATSPKIILLDEPTSAL 179
Cdd:PTZ00265 531 sneLIEMRKNYQTIKDSevvdvskkvlihdfvsalpdKYETLVGsnaskLSGGQKQRISIARAIIRNPKILILDEATSSL 610
|
250 260
....*....|....*....|....*....
gi 2038545162 180 DPISAGKIEETLYGLK---DKYTMLLVTR 205
Cdd:PTZ00265 611 DNKSEYLVQKTINNLKgneNRITIIIAHR 639
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
6-193 |
1.72e-14 |
|
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: 69.83 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPEvttTGSVVYNGHNIYSPRTdtvELR 85
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILA--GLSPPL---AGRVLLNGGPLDFQRD---SIA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 86 KEIGMVFQQPN-PFPMTIYENVVYGLRINGikdkqvlDEAVEKALqgasiwDEVKDRLYDSAI--GLSGGQQQRVCVARV 162
Cdd:cd03231 73 RGLLYLGHAPGiKTTLSVLENLRFWHADHS-------DEQVEEAL------ARVGLNGFEDRPvaQLSAGQQRRVALARL 139
|
170 180 190
....*....|....*....|....*....|.
gi 2038545162 163 LATSPKIILLDEPTSALDPISAGKIEETLYG 193
Cdd:cd03231 140 LLSGRPLWILDEPTTALDKAGVARFAEAMAG 170
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-204 |
2.56e-14 |
|
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: 68.72 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 21 LNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrmGDLNPevtttgsvVYNGhNIYSPRtdtvelRKEIGMVFQQPNPFPM 100
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRAL---AGLWP--------WGSG-RIGMPE------GEDLLFLPQRPYLPLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 101 TIYENVVYGlringikdkqvldeavekalqgasiWDEVkdrlydsaigLSGGQQQRVCVARVLATSPKIILLDEPTSALD 180
Cdd:cd03223 79 TLREQLIYP-------------------------WDDV----------LSGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
170 180
....*....|....*....|....
gi 2038545162 181 PisagKIEETLYGLKDKYTMLLVT 204
Cdd:cd03223 124 E----ESEDRLYQLLKELGITVIS 143
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
17-196 |
5.66e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 71.29 E-value: 5.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 17 KKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPEVTTTGSVVYNGHniysPRTDTVELRkeIGMVFQQPN 96
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVITGGDRLVNGR----PLDSSFQRS--IGYVQQQDL 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 97 PFP-MTIYENVVYGLRIN-----GIKDKQVLDEAVEKALQGASIWDEVkdrLYDSAIGLSGGQQQRVCVARVLATSPKII 170
Cdd:TIGR00956 847 HLPtSTVRESLRFSAYLRqpksvSKSEKMEYVEEVIKLLEMESYADAV---VGVPGEGLNVEQRKRLTIGVELVAKPKLL 923
|
170 180
....*....|....*....|....*..
gi 2038545162 171 L-LDEPTSALDPISAGKIEETLYGLKD 196
Cdd:TIGR00956 924 LfLDEPTSGLDSQTAWSICKLMRKLAD 950
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
6-180 |
6.58e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.19 E-value: 6.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVyynkKKALNSVSLSFQPKEITALIGPSGSGKSTLLKslnRMGDLNPevtTTGSVVYNGHNI--YSPRtdtvE 83
Cdd:PRK03695 1 MQLNDVAV----STRLGPLSAEVRAGEILHLVGPNGAGKSTLLA---RMAGLLP---GSGSIQFAGQPLeaWSAA----E 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 84 LRKEIGMVFQQPNP-FPMTIYEnvvY-------GLRINGIKDkqVLDEAVEkALQgasiwdeVKDRLYDSAIGLSGGQQQ 155
Cdd:PRK03695 67 LARHRAYLSQQQTPpFAMPVFQ---YltlhqpdKTRTEAVAS--ALNEVAE-ALG-------LDDKLGRSVNQLSGGEWQ 133
|
170 180 190
....*....|....*....|....*....|..
gi 2038545162 156 RVCVARV-LATSPKI------ILLDEPTSALD 180
Cdd:PRK03695 134 RVRLAAVvLQVWPDInpagqlLLLDEPMNSLD 165
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
13-204 |
7.08e-14 |
|
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: 70.73 E-value: 7.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 13 VYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSlnrMGDLNPEvtttgsvvYNGHNIYSPRTdtvelrkEIGMVF 92
Cdd:TIGR03719 13 VVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRI---MAGVDKD--------FNGEARPQPGI-------KVGYLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 93 QQPNPFP-MTIYENVVYGL--------RINGIKDK---------QVLDE--AVEKALQGASIWD-----EVK-DRL---- 142
Cdd:TIGR03719 75 QEPQLDPtKTVRENVEEGVaeikdaldRFNEISAKyaepdadfdKLAAEqaELQEIIDAADAWDldsqlEIAmDALrcpp 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038545162 143 YDSAIG-LSGGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDkyTMLLVT 204
Cdd:TIGR03719 155 WDADVTkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG--TVVAVT 215
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-180 |
7.72e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.99 E-value: 7.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 1 MTDAIlQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGhniysprtd 80
Cdd:PRK09544 1 MTSLV-SLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVV--LGLVAP---DEGVIKRNG--------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 81 tvELRkeIGMVFQQPNPFPmTIYENVVYGLRIN-GIKDKQVLdeAVEKALQGASIWDEVKDRlydsaigLSGGQQQRVCV 159
Cdd:PRK09544 66 --KLR--IGYVPQKLYLDT-TLPLTVNRFLRLRpGTKKEDIL--PALKRVQAGHLIDAPMQK-------LSGGETQRVLL 131
|
170 180
....*....|....*....|.
gi 2038545162 160 ARVLATSPKIILLDEPTSALD 180
Cdd:PRK09544 132 ARALLNRPQLLVLDEPTQGVD 152
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
19-247 |
8.12e-14 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 69.83 E-value: 8.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 19 KALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDLNPEVTTTgSVVYNGHNIY--SPRtdtvELRKEIG----MVF 92
Cdd:PRK15093 21 KAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTAD-RMRFDDIDLLrlSPR----ERRKLVGhnvsMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 93 QQP----NP-----------FPMTIYENVVYGlRINGIKDKqvldeAVEkALQGASIWDEvKDRLYDSAIGLSGGQQQRV 157
Cdd:PRK15093 96 QEPqsclDPservgrqlmqnIPGWTYKGRWWQ-RFGWRKRR-----AIE-LLHRVGIKDH-KDAMRSFPYELTEGECQKV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 158 CVARVLATSPKIILLDEPTSALDPISAGKIEETLYGL--KDKYTMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQMF 235
Cdd:PRK15093 168 MIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnqNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELV 247
|
250
....*....|..
gi 2038545162 236 LDPQHKETEDYI 247
Cdd:PRK15093 248 TTPHHPYTQALI 259
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-181 |
1.74e-13 |
|
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: 67.00 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEvttTGSVVYNGHNIYSPRTdtvELR 85
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRIL--AGLLRPD---SGEVRWNGTPLAEQRD---EPH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 86 KEIGMVFQQPNPFP-MTIYENVVYGLRINGIKDKQVLDEAVEKALQGASiwdevkDRLydsAIGLSGGQQQRVCVARVLA 164
Cdd:TIGR01189 73 ENILYLGHLPGLKPeLSALENLHFWAAIHGGAQRTIEDALAAVGLTGFE------DLP---AAQLSAGQQRRLALARLWL 143
|
170
....*....|....*..
gi 2038545162 165 TSPKIILLDEPTSALDP 181
Cdd:TIGR01189 144 SRRPLWILDEPTTALDK 160
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-180 |
1.91e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 69.29 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 3 DAILQVSDLSVY-YNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEvttTGSVVYNGHNI--YSPRt 79
Cdd:COG3845 255 EVVLEVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEAL--AGLRPPA---SGSIRLDGEDItgLSPR- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 80 DTVEL--------RKEIGMVfqqPNpfpMTIYENVV------YGLRINGIKDKQVLDEAVEKALQ-----GASIWDEVKd 140
Cdd:COG3845 329 ERRRLgvayipedRLGRGLV---PD---MSVAENLIlgryrrPPFSRGGFLDRKAIRAFAEELIEefdvrTPGPDTPAR- 401
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2038545162 141 rlydsaiGLSGGQQQRVCVARVLATSPKIILLDEPTSALD 180
Cdd:COG3845 402 -------SLSGGNQQKVILARELSRDPKLLIAAQPTRGLD 434
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
3-216 |
4.91e-13 |
|
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: 67.19 E-value: 4.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 3 DAILQVSDLSVYYNKkkALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVVYNGHNIYSPRTDTV 82
Cdd:cd03291 37 DNNLFFSNLCLVGAP--VLKNINLKIEKGEMLAITGSTGSGKTSLLMLI--LGELEP---SEGKIKHSGRISFSSQFSWI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 83 elrkeigmvfqqpnpFPMTIYENVVYGLRINGIKDKQVLdEAVEKALQGASIWDEVKDRLYDSAIGLSGGQQQRVCVARV 162
Cdd:cd03291 110 ---------------MPGTIKENIIFGVSYDEYRYKSVV-KACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2038545162 163 LATSPKIILLDEPTSALDPISAGKI-EETLYGLKDKYTMLLVTRSMQQAsRISDK 216
Cdd:cd03291 174 VYKDADLYLLDSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHL-KKADK 227
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
19-244 |
6.22e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 67.24 E-value: 6.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 19 KALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEVTTTGS-VVYNGHNI--YSPRTDTVELRKEIGMVFQQP 95
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAI--CGITKDNWHVTADrFRWNGIDLlkLSPRERRKIIGREIAMIFQEP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 96 NPF--PM-TIyenvvyglringikDKQvLDEAVEKALQGASIWDEVKDRlYDSAIGL--------------------SGG 152
Cdd:COG4170 99 SSCldPSaKI--------------GDQ-LIEAIPSWTFKGKWWQRFKWR-KKRAIELlhrvgikdhkdimnsyphelTEG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 153 QQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLK--DKYTMLLVTRSMQQASRISDKTGFFLDGDLIEFND 230
Cdd:COG4170 163 ECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNqlQGTSILLISHDLESISQWADTITVLYCGQTVESGP 242
|
250
....*....|....
gi 2038545162 231 TKQMFLDPQHKETE 244
Cdd:COG4170 243 TEQILKSPHHPYTK 256
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
15-228 |
7.39e-13 |
|
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: 65.63 E-value: 7.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 15 YNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRmgdlnpevtttgsvvynghnIYSPRTDTVELRK------EI 88
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAG--------------------IYPPDSGTVTVRGrvssllGL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 89 GMVFqQPNpfpMTIYENVVYGLRINGIKDK---QVLDEAVEKALQGASIWDEVKdrlydsaiGLSGGQQQRVCVARVLAT 165
Cdd:cd03220 92 GGGF-NPE---LTGRENIYLNGRLLGLSRKeidEKIDEIIEFSELGDFIDLPVK--------TYSSGMKARLAFAIATAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2038545162 166 SPKIILLDEPTSALDPI----SAGKIEETlygLKDKYTMLLVTRSMQQASRISDKTGFFLDGDLIEF 228
Cdd:cd03220 160 EPDILLIDEVLAVGDAAfqekCQRRLREL---LKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-182 |
3.17e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.84 E-value: 3.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEvttTGSVVYNGHNiYSPRTDTVEL 84
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKII--AGIVPPD---SGTLEIGGNP-CARLTPAKAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 85 RKEIGMVFQQPNPFP-MTIYENVVYGLringiKDKQVLDEAVEKALQ--GASIwdevkdRLYDSAIGLSGGQQQRVCVAR 161
Cdd:PRK15439 85 QLGIYLVPQEPLLFPnLSVKENILFGL-----PKRQASMQKMKQLLAalGCQL------DLDSSAGSLEVADRQIVEILR 153
|
170 180
....*....|....*....|.
gi 2038545162 162 VLATSPKIILLDEPTSALDPI 182
Cdd:PRK15439 154 GLMRDSRILILDEPTASLTPA 174
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-179 |
3.33e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.58 E-value: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 1 MTDAILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPevtTTGSVVYNGHNiYSPRTD 80
Cdd:PRK09700 1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLS--GIHEP---TKGTITINNIN-YNKLDH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 81 TVELRKEIGMVFQQPNPF-PMTIYENVVYG-LRINGIKDKQVLDEAvEKALQGASIWDEV--KDRLYDSAIGLSGGQQQR 156
Cdd:PRK09700 75 KLAAQLGIGIIYQELSVIdELTVLENLYIGrHLTKKVCGVNIIDWR-EMRVRAAMMLLRVglKVDLDEKVANLSISHKQM 153
|
170 180
....*....|....*....|...
gi 2038545162 157 VCVARVLATSPKIILLDEPTSAL 179
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSL 176
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-201 |
4.40e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.57 E-value: 4.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 21 LNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDlnpevTTTGSVVYNGHNI--YSPRtdtvELRKEIGMVFQQPNPF 98
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVE-----VCGGEIRVNGREIgaYGLR----ELRRQFSMIPQDPVLF 1396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 99 PMTIYENVVYGLringikdkQVLDEAVEKALQ--G-----ASIWDEVKDRLYDSAIGLSGGQQQRVCVAR-VLATSPKII 170
Cdd:PTZ00243 1397 DGTVRQNVDPFL--------EASSAEVWAALElvGlrervASESEGIDSRVLEGGSNYSVGQRQLMCMARaLLKKGSGFI 1468
|
170 180 190
....*....|....*....|....*....|.
gi 2038545162 171 LLDEPTSALDPISAGKIEETLYGLKDKYTML 201
Cdd:PTZ00243 1469 LMDEATANIDPALDRQIQATVMSAFSAYTVI 1499
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
13-180 |
5.91e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 64.75 E-value: 5.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 13 VYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSlnrMGDLNPEvtttgsvvYNGHNIYSPRTdtvelrkEIGMVF 92
Cdd:PRK11819 15 VVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRI---MAGVDKE--------FEGEARPAPGI-------KVGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 93 QQP--NPfPMTIYENVVYGL--------RINGIKDK---------QVLDE--AVEKALQGASIWD-----EVK-DRL--- 142
Cdd:PRK11819 77 QEPqlDP-EKTVRENVEEGVaevkaaldRFNEIYAAyaepdadfdALAAEqgELQEIIDAADAWDldsqlEIAmDALrcp 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2038545162 143 -YDSAIG-LSGGQQQRVCVARVLATSPKIILLDEPTSALD 180
Cdd:PRK11819 156 pWDAKVTkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-184 |
5.92e-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: 5.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 16 NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSL-NRMGDLnpevtttgsvvynghniysPRTDTVELrkeigmvfqQ 94
Cdd:COG2401 41 VERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLaGALKGT-------------------PVAGCVDV---------P 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 95 PNPFPmtiyENVVYglrINGIKDKQVLDEAVEkALQGASIWDEVK-DRLYDSaigLSGGQQQRVCVARVLATSPKIILLD 173
Cdd:COG2401 93 DNQFG----REASL---IDAIGRKGDFKDAVE-LLNAVGLSDAVLwLRRFKE---LSTGQKFRFRLALLLAERPKLLVID 161
|
170
....*....|.
gi 2038545162 174 EPTSALDPISA 184
Cdd:COG2401 162 EFCSHLDRQTA 172
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-180 |
6.63e-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: 64.85 E-value: 6.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 3 DAILQVSDLSVYY---NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLnpEVTTTGSVVYNGH--NIYSP 77
Cdd:TIGR02633 255 DVILEARNLTCWDvinPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQAL--FGAY--PGKFEGNVFINGKpvDIRNP 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 78 ----RTDTV---ELRKEIGMVFQqpnpfpMTIYENVVYGLrINGIKDKQVLDEAVEKALQGASIWD-EVKDRLYDSAIG- 148
Cdd:TIGR02633 331 aqaiRAGIAmvpEDRKRHGIVPI------LGVGKNITLSV-LKSFCFKMRIDAAAELQIIGSAIQRlKVKTASPFLPIGr 403
|
170 180 190
....*....|....*....|....*....|..
gi 2038545162 149 LSGGQQQRVCVARVLATSPKIILLDEPTSALD 180
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-208 |
1.04e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 64.61 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 18 KKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEVTTtgSVVYNGHNIYSPrtdtvelrkeigmvfQQPNP 97
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAM--LGELSHAETS--SVVIRGSVAYVP---------------QVSWI 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 98 FPMTIYENVVYGLRINGIKDKQVLD-EAVEKALQGASIWD--EVKDRlydsAIGLSGGQQQRVCVARVLATSPKIILLDE 174
Cdd:PLN03232 691 FNATVRENILFGSDFESERYWRAIDvTALQHDLDLLPGRDltEIGER----GVNISGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190
....*....|....*....|....*....|....*.
gi 2038545162 175 PTSALDPISAGKIEETL--YGLKDKyTMLLVTRSMQ 208
Cdd:PLN03232 767 PLSALDAHVAHQVFDSCmkDELKGK-TRVLVTNQLH 801
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
25-206 |
1.74e-11 |
|
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: 63.61 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 25 SLSFQPKEITAL--IGPSGSGKSTLLKSLnrmGDLNPevtttgsvVYNGhniysprTDTVELRKEIGMVFQQPNPFPMTI 102
Cdd:TIGR00954 470 SLSFEVPSGNNLliCGPNGCGKSSLFRIL---GELWP--------VYGG-------RLTKPAKGKLFYVPQRPYMTLGTL 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 103 YENVVYGLRINGIKDKQVLDEAVEKALQGASIWDEVKDRLYDSAIG-----LSGGQQQRVCVARVLATSPKIILLDEPTS 177
Cdd:TIGR00954 532 RDQIIYPDSSEDMKRRGLSDKDLEQILDNVQLTHILEREGGWSAVQdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTS 611
|
170 180
....*....|....*....|....*....
gi 2038545162 178 ALDPisagKIEETLYGLKDKYTMLLVTRS 206
Cdd:TIGR00954 612 AVSV----DVEGYMYRLCREFGITLFSVS 636
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-227 |
1.80e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 63.27 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 19 KALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmgDLNPEVTTTGSVVYNG-----HNIY-SPRTDTVELRKEIGMVf 92
Cdd:NF040905 15 KALDDVNLSVREGEIHALCGENGAGKSTLMKVLS---GVYPHGSYEGEILFDGevcrfKDIRdSEALGIVIIHQELALI- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 93 qqpnPFpMTIYENVVYGlriNGIKDKQVLDeavekalqgasiWDEVKDR---------LYDSA------IGLsgGQQQRV 157
Cdd:NF040905 91 ----PY-LSIAENIFLG---NERAKRGVID------------WNETNRRarellakvgLDESPdtlvtdIGV--GKQQLV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038545162 158 CVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDK-YTMLLVTRSMQQASRISDKTGFFLDGDLIE 227
Cdd:NF040905 149 EIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQgITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-204 |
3.00e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 61.73 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEVtTTGSVVYNGHniysprtDTVEL 84
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATL--AGREDYEV-TGGTVEFKGK-------DLLEL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 85 RKE------IGMVFQQP-------NPFPMTIYENVVYGLRINGIKDKQVLDEAVEKALQgasIWDEVKDRLYDSA-IGLS 150
Cdd:PRK09580 71 SPEdragegIFMAFQYPveipgvsNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIA---LLKMPEDLLTRSVnVGFS 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2038545162 151 GGQQQRVCVARVLATSPKIILLDEPTSALDpISAGKI-EETLYGLKD-KYTMLLVT 204
Cdd:PRK09580 148 GGEKKRNDILQMAVLEPELCILDESDSGLD-IDALKIvADGVNSLRDgKRSFIIVT 202
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-248 |
9.75e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.66 E-value: 9.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 16 NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNP-EVTTTGSVVYNGHniySPRTDTVELRKEIGMVFQQ 94
Cdd:TIGR00956 72 KTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIA--SNTDGfHIGVEGVITYDGI---TPEEIKKHYRGDVVYNAET 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 95 PNPFP-MTIYENVVY-------GLRINGIkDKQVLDE---AVEKALQGASIWDEVKdrLYDSAI-GLSGGQQQRVCVARV 162
Cdd:TIGR00956 147 DVHFPhLTVGETLDFaarcktpQNRPDGV-SREEYAKhiaDVYMATYGLSHTRNTK--VGNDFVrGVSGGERKRVSIAEA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 163 LATSPKIILLDEPTSALDP------ISAGKIEETLygLKDKYTMLLVTRSmQQASRISDKTGFFLDGDLIEFND---TKQ 233
Cdd:TIGR00956 224 SLGGAKIQCWDNATRGLDSatalefIRALKTSANI--LDTTPLVAIYQCS-QDAYELFDKVIVLYEGYQIYFGPadkAKQ 300
|
250 260
....*....|....*....|
gi 2038545162 234 MFLD-----PQHKETEDYIT 248
Cdd:TIGR00956 301 YFEKmgfkcPDRQTTADFLT 320
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-227 |
1.14e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.95 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 2 TDAILQVSDLSVYYNKKkaLNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrmgdLNPEVTTTGSVVYNGHNIySPRTDT 81
Cdd:PRK09700 262 HETVFEVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCL-----FGVDKRAGGEIRLNGKDI-SPRSPL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 82 VELRKEIGMVFQQPNP---FP-MTIYENV-------------VYGLrINGIKDKQVLDEAVEK-ALQGASIWDEVKDrly 143
Cdd:PRK09700 334 DAVKKGMAYITESRRDngfFPnFSIAQNMaisrslkdggykgAMGL-FHEVDEQRTAENQRELlALKCHSVNQNITE--- 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 144 dsaigLSGGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETLYGLKDK-YTMLLVTRSMQQASRISDKTGFFLD 222
Cdd:PRK09700 410 -----LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVFCE 484
|
....*
gi 2038545162 223 GDLIE 227
Cdd:PRK09700 485 GRLTQ 489
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
6-180 |
1.29e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.05 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDlnpevTTTGSVVYNGHNIyspRTDTVELR 85
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLAR-----PDAGEVLWQGEPI---RRQRDEYH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 86 KE---IGmvfQQPNPFP-MTIYENVVYGLRINGIKDkqvlDEAVEKALQGASIwdevKDRLYDSAIGLSGGQQQRVCVAR 161
Cdd:PRK13538 74 QDllyLG---HQPGIKTeLTALENLRFYQRLHGPGD----DEALWEALAQVGL----AGFEDVPVRQLSAGQQRRVALAR 142
|
170
....*....|....*....
gi 2038545162 162 VLATSPKIILLDEPTSALD 180
Cdd:PRK13538 143 LWLTRAPLWILDEPFTAID 161
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
6-216 |
1.57e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.79 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSvyynkKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLnPEvtTTGSVVYNGHNIY--SPRtDTV- 82
Cdd:PRK10762 258 LKVDNLS-----GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVL--YGAL-PR--TSGYVTLDGHEVVtrSPQ-DGLa 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 83 -------ELRKEIGMVFQqpnpfpMTIYENVV-----YGLRINGIKDKQVLDEAVEKALQGASIwdevKDRLYDSAIG-L 149
Cdd:PRK10762 327 ngivyisEDRKRDGLVLG------MSVKENMSltalrYFSRAGGSLKHADEQQAVSDFIRLFNI----KTPSMEQAIGlL 396
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2038545162 150 SGGQQQRVCVARVLATSPKIILLDEPTSALDpISAGKieeTLYGLKDKY-----TMLLVTRSMQQASRISDK 216
Cdd:PRK10762 397 SGGNQQKVAIARGLMTRPKVLILDEPTRGVD-VGAKK---EIYQLINQFkaeglSIILVSSEMPEVLGMSDR 464
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-203 |
1.96e-10 |
|
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: 60.73 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 21 LNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDlnpevTTTGSVVYNGHNIysPRTDTVELRKEIGMVFQQPNPFPM 100
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINE-----SAEGEIIIDGLNI--AKIGLHDLRFKITIIPQDPVLFSG 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 101 TiyenvvygLRINGIKDKQVLDEAVEKALQGASIWDEVK---DRL-YDSAIG---LSGGQQQRVCVARVLATSPKIILLD 173
Cdd:TIGR00957 1375 S--------LRMNLDPFSQYSDEEVWWALELAHLKTFVSalpDKLdHECAEGgenLSVGQRQLVCLARALLRKTKILVLD 1446
|
170 180 190
....*....|....*....|....*....|
gi 2038545162 174 EPTSALDPISAGKIEETLYGLKDKYTMLLV 203
Cdd:TIGR00957 1447 EATAAVDLETDNLIQSTIRTQFEDCTVLTI 1476
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-216 |
2.28e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.92 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 24 VSLSFQPKEITALIGPSGSGKSTLLKSL---NRMgdlnpevtTTGSVVYNGH--NIYSPRtDTV--------ELRKEIGM 90
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLygaTRR--------TAGQVYLDGKpiDIRSPR-DAIragimlcpEDRKAEGI 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 91 VfqqpnpfPM-TIYENVVYGLRINGIKDKQVLDEAVEKALQGASIWD-EVKDRLYDSAIG-LSGGQQQRVCVARVLATSP 167
Cdd:PRK11288 343 I-------PVhSVADNINISARRHHLRAGCLINNRWEAENADRFIRSlNIKTPSREQLIMnLSGGNQQKAILGRWLSEDM 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2038545162 168 KIILLDEPTSALDPISAGKIEETLYGL-KDKYTMLLVTRSMQQASRISDK 216
Cdd:PRK11288 416 KVILLDEPTRGIDVGAKHEIYNVIYELaAQGVAVLFVSSDLPEVLGVADR 465
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-184 |
2.38e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.06 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSvyynkKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGdLNPevTTTGSVVYNGHNIyspRTDTVEL 84
Cdd:PRK15439 268 VLTVEDLT-----GEGFRNISLEVRAGEILGLAGVVGAGRTELAETL--YG-LRP--ARGGRIMLNGKEI---NALSTAQ 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 85 RKEIGMVF-----QQPNPF-PMTIYENVV------YGLRINGIKDKQVLdEAVEKALQgasiwdeVKDRLYDSAI-GLSG 151
Cdd:PRK15439 335 RLARGLVYlpedrQSSGLYlDAPLAWNVCalthnrRGFWIKPARENAVL-ERYRRALN-------IKFNHAEQAArTLSG 406
|
170 180 190
....*....|....*....|....*....|...
gi 2038545162 152 GQQQRVCVARVLATSPKIILLDEPTSALDpISA 184
Cdd:PRK15439 407 GNQQKVLIAKCLEASPQLLIVDEPTRGVD-VSA 438
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-204 |
3.32e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.50 E-value: 3.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 1 MTDAILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGdlNPEVT-TTGSVVYNGHNIYSprt 79
Cdd:CHL00131 3 KNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVI--AG--HPAYKiLEGDILFKGESILD--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 80 DTVELRKEIG--MVFQQPNPFP--------MTIYEN--VVYGL-RINGIKDKQVLDEAVEKA-LQGASIWDEVKDrlyds 145
Cdd:CHL00131 76 LEPEERAHLGifLAFQYPIEIPgvsnadflRLAYNSkrKFQGLpELDPLEFLEIINEKLKLVgMDPSFLSRNVNE----- 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2038545162 146 aiGLSGGQQQRVCVARVLATSPKIILLDEPTSALDpISAGK-IEETLYGLKDKYT-MLLVT 204
Cdd:CHL00131 151 --GFSGGEKKRNEILQMALLDSELAILDETDSGLD-IDALKiIAEGINKLMTSENsIILIT 208
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
14-226 |
3.39e-10 |
|
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: 58.57 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 14 YYNKKKALNSVSL-----SFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEVTTTG----SVVYNGHNIYSPRTDTVE- 83
Cdd:cd03237 3 YPTMKKTLGEFTLeveggSISESEVIGILGPNGIGKTTFIKML--AGVLKPDEGDIEieldTVSYKPQYIKADYEGTVRd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 84 -LRKEIGMVFQQPNpfpmtiYEN-VVYGLRINGIKDKQVLDeavekalqgasiwdevkdrlydsaigLSGGQQQRVCVAR 161
Cdd:cd03237 81 lLSSITKDFYTHPY------FKTeIAKPLQIEQILDREVPE--------------------------LSGGELQRVAIAA 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2038545162 162 VLATSPKIILLDEPTSALDpisagkIEETlyglkdkytmLLVTRSMQQASRISDKTGFFLDGDLI 226
Cdd:cd03237 129 CLSKDADIYLLDEPSAYLD------VEQR----------LMASKVIRRFAENNEKTAFVVEHDII 177
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
6-236 |
4.53e-10 |
|
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: 58.38 E-value: 4.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYY--NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDLnpevtTTGSVVYNGHNIYSPRTDTve 83
Cdd:cd03288 20 IKIHDLCVRYenNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDI-----FDGKIVIDGIDISKLPLHT-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 84 LRKEIGMVFQQPNPFPMTIyenvvyglRINGIKDKQVLDEAVEKALQGASIWDEVKDR-------LYDSAIGLSGGQQQR 156
Cdd:cd03288 93 LRSRLSIILQDPILFSGSI--------RFNLDPECKCTDDRLWEALEIAQLKNMVKSLpggldavVTEGGENFSVGQRQL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 157 VCVARVLATSPKIILLDEPTSALDPISAG---KIEETLYGLKDKYTMLLVTRSMQQAsrisDKTGFFLDGDLIEFNDTKQ 233
Cdd:cd03288 165 FCLARAFVRKSSILIMDEATASIDMATENilqKVVMTAFADRTVVTIAHRVSTILDA----DLVLVLSRGILVECDTPEN 240
|
...
gi 2038545162 234 MFL 236
Cdd:cd03288 241 LLA 243
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-196 |
4.60e-10 |
|
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: 59.18 E-value: 4.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 3 DAILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEvttTGSVVYNghniysprtDTV 82
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMI--TGQEQPD---SGTIEIG---------ETV 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 83 ELrkeiGMVFQQ-----PNPfpmTIYENVVYGLRINGIKDKQVLDEAVEKA--LQGASIWDEVKDrlydsaigLSGGQQQ 155
Cdd:TIGR03719 386 KL----AYVDQSrdaldPNK---TVWEEISGGLDIIKLGKREIPSRAYVGRfnFKGSDQQKKVGQ--------LSGGERN 450
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2038545162 156 RVCVARVLATSPKIILLDEPTSALDPisagkieETLYGLKD 196
Cdd:TIGR03719 451 RVHLAKTLKSGGNVLLLDEPTNDLDV-------ETLRALEE 484
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
5-189 |
5.63e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.27 E-value: 5.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEvttTGSVVYNGHNIyspRTDTVEL 84
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLI--AGLLNPE---KGEILFERQSI---KKDLCTY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 85 RKEIGMVFQQP--NPFpMTIYENVVYGLRINgiKDKQVLDEAVEKALQGasiwdevkdRLYDSAIG-LSGGQQQRVCVAR 161
Cdd:PRK13540 73 QKQLCFVGHRSgiNPY-LTLRENCLYDIHFS--PGAVGITELCRLFSLE---------HLIDYPCGlLSSGQKRQVALLR 140
|
170 180 190
....*....|....*....|....*....|..
gi 2038545162 162 VLATSPKIILLDEPTSALDPIS----AGKIEE 189
Cdd:PRK13540 141 LWMSKAKLWLLDEPLVALDELSlltiITKIQE 172
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-223 |
8.12e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 58.87 E-value: 8.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYY--NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDlnpEVTTTGSVVYNGHNIYsprTDTV 82
Cdd:TIGR01257 1937 ILRLNELTKVYsgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLT--GD---TTVTSGDATVAGKSIL---TNIS 2008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 83 ELRKEIGMV--FQQPNPFpMTIYENVVYGLRINGIKDKQVlDEAVEKALQ--GASIWdevKDRLydsAIGLSGGQQQRVC 158
Cdd:TIGR01257 2009 DVHQNMGYCpqFDAIDDL-LTGREHLYLYARLRGVPAEEI-EKVANWSIQslGLSLY---ADRL---AGTYSGGNKRKLS 2080
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2038545162 159 VARVLATSPKIILLDEPTSALDPISAGKIEETLYG-LKDKYTMLLVTRSMQQASRISDKTGFFLDG 223
Cdd:TIGR01257 2081 TAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSiIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-180 |
8.58e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 58.64 E-value: 8.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 18 KKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLnpEVTTtGSVvynghniYSPRTdtvelrkeIGMVFQQPNP 97
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSL--LSQF--EISE-GRV-------WAERS--------IAYVPQQAWI 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 98 FPMTIYENVVYGLRingiKDKQVLDEAV-------EKALQGASIWDEVKDRlydsAIGLSGGQQQRVCVARVLATSPKII 170
Cdd:PTZ00243 733 MNATVRGNILFFDE----EDAARLADAVrvsqleaDLAQLGGGLETEIGEK----GVNLSGGQKARVSLARAVYANRDVY 804
|
170
....*....|
gi 2038545162 171 LLDEPTSALD 180
Cdd:PTZ00243 805 LLDDPLSALD 814
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
21-180 |
8.92e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 58.70 E-value: 8.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 21 LNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEVTTTGSVVYNGH--NIYSPRTDTVELRK---EIGMvfqqp 95
Cdd:PLN03140 181 LKDASGIIKPSRMTLLLGPPSSGKTTLLLAL--AGKLDPSLKVSGEITYNGYrlNEFVPRKTSAYISQndvHVGV----- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 96 npfpMTIYENVVYGLRINGI--------------KDKQVLDEAVEKALQGASIWDEVKDRLY--------------DSAI 147
Cdd:PLN03140 254 ----MTVKETLDFSARCQGVgtrydllselarreKDAGIFPEAEVDLFMKATAMEGVKSSLItdytlkilgldickDTIV 329
|
170 180 190
....*....|....*....|....*....|....*....
gi 2038545162 148 ------GLSGGQQQRVCVARVLATSPKIILLDEPTSALD 180
Cdd:PLN03140 330 gdemirGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLD 368
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-207 |
1.53e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.06 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 21 LNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDLNpevttTGSVVYNGHNIysPRTDTVELRKEIGMVFQQPNPFPM 100
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELE-----KGRIMIDDCDV--AKFGLTDLRRVLSIIPQSPVLFSG 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 101 TIyenvvyglRINGIKDKQVLDEAVEKALQGASIWDEVKD-------RLYDSAIGLSGGQQQRVCVARVLATSPKIILLD 173
Cdd:PLN03232 1325 TV--------RFNIDPFSEHNDADLWEALERAHIKDVIDRnpfgldaEVSEGGENFSVGQRQLLSLARALLRRSKILVLD 1396
|
170 180 190
....*....|....*....|....*....|....
gi 2038545162 174 EPTSALDPISAGKIEETLYGLKDKYTMLLVTRSM 207
Cdd:PLN03232 1397 EATASVDVRTDSLIQRTIREEFKSCTMLVIAHRL 1430
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-180 |
2.23e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.25 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 3 DAILQVSDLSVYY---NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSL-----NRmgdlnpevtTTGSVVYNGH-- 72
Cdd:PRK13549 257 EVILEVRNLTAWDpvnPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLfgaypGR---------WEGEIFIDGKpv 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 73 NIYSPRtDTV--------ELRKEIGMVFQQPNPFPMTI--YENVVYGLRINGIKDKQVLDEAVEKAlqgasiwdEVKDRL 142
Cdd:PRK13549 328 KIRNPQ-QAIaqgiamvpEDRKRDGIVPVMGVGKNITLaaLDRFTGGSRIDDAAELKTILESIQRL--------KVKTAS 398
|
170 180 190
....*....|....*....|....*....|....*....
gi 2038545162 143 YDSAIG-LSGGQQQRVCVARVLATSPKIILLDEPTSALD 180
Cdd:PRK13549 399 PELAIArLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-203 |
2.35e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.44 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 21 LNSVSLSFQPKEITALIGPSGSGKSTLLKSLNRMGDLNpevttTGSVVYNGHNIysPRTDTVELRKEIGMVFQQPNPFPM 100
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELE-----RGRILIDGCDI--SKFGLMDLRKVLGIIPQAPVLFSG 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 101 TIYENVVyglRINGIKDKQvLDEAVEKAlqgasiwdEVKDRLYDSAIGL-----------SGGQQQRVCVARVLATSPKI 169
Cdd:PLN03130 1328 TVRFNLD---PFNEHNDAD-LWESLERA--------HLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKI 1395
|
170 180 190
....*....|....*....|....*....|....
gi 2038545162 170 ILLDEPTSALDPISAGKIEETLYGLKDKYTMLLV 203
Cdd:PLN03130 1396 LVLDEATAAVDVRTDALIQKTIREEFKSCTMLII 1429
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
13-182 |
2.44e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.95 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 13 VYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLkSLnRMGD----LNPEVTTTGSVVYNGHNIYsprtdtvELRKEI 88
Cdd:PRK10938 268 VSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLL-SL-ITGDhpqgYSNDLTLFGRRRGSGETIW-------DIKKHI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 89 GMVfqqPNPFPM-----TIYENVVyglrINGIKDKQVLDEAVEKALQG-ASIWDE---VKDRLYDSAI-GLSGGQQQRVC 158
Cdd:PRK10938 339 GYV---SSSLHLdyrvsTSVRNVI----LSGFFDSIGIYQAVSDRQQKlAQQWLDilgIDKRTADAPFhSLSWGQQRLAL 411
|
170 180
....*....|....*....|....
gi 2038545162 159 VARVLATSPKIILLDEPTSALDPI 182
Cdd:PRK10938 412 IVRALVKHPTLLILDEPLQGLDPL 435
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-204 |
3.66e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.06 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 16 NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPevTTTGSVVYNGHNIYSPRTDTVelrkeigmvfqqp 95
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAM--LGELPP--RSDASVVIRGTVAYVPQVSWI------------- 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 96 npFPMTIYENVVYGLRINGIKDKQVLD-EAVEKALQGASIWD--EVKDRlydsAIGLSGGQQQRVCVARVLATSPKIILL 172
Cdd:PLN03130 691 --FNATVRDNILFGSPFDPERYERAIDvTALQHDLDLLPGGDltEIGER----GVNISGGQKQRVSMARAVYSNSDVYIF 764
|
170 180 190
....*....|....*....|....*....|....*
gi 2038545162 173 DEPTSALDPISAGKIEETLygLKD---KYTMLLVT 204
Cdd:PLN03130 765 DDPLSALDAHVGRQVFDKC--IKDelrGKTRVLVT 797
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-237 |
1.17e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 21 LNSVSLSFQPKEITALIGPSGSGKSTLLKSLNR---MGDlnpevtttGSVVYNghniysprTDTVELRkeigmvFQQ--P 95
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevlLDD--------GRIIYE--------QDLIVAR------LQQdpP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 96 NPFPMTIYENVVYGLRING--IKD-----KQVLDEAVEKALQGASIWDEVKDRL----YDSAI----------------G 148
Cdd:PRK11147 77 RNVEGTVYDFVAEGIEEQAeyLKRyhdisHLVETDPSEKNLNELAKLQEQLDHHnlwqLENRInevlaqlgldpdaalsS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 149 LSGGQQQRVCVARVLATSPKIILLDEPTSALDpISAgkIE--ETLygLKD-KYTMLLVT------RSMqqASRISDktgf 219
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLD-IET--IEwlEGF--LKTfQGSIIFIShdrsfiRNM--ATRIVD---- 225
|
250
....*....|....*....
gi 2038545162 220 fLD-GDLIEFNDTKQMFLD 237
Cdd:PRK11147 226 -LDrGKLVSYPGNYDQYLL 243
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
18-225 |
2.43e-08 |
|
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: 54.02 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 18 KKALNSVSLSFQP-----KEITALIGPSGSGKSTLLKSLNrmGDLNP---EVTTTGSVVYNGHNIYSPRTDTVE--LRKE 87
Cdd:COG1245 348 TKSYGGFSLEVEGgeireGEVLGIVGPNGIGKTTFAKILA--GVLKPdegEVDEDLKISYKPQYISPDYDGTVEefLRSA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 88 IGmvfqqpNPFPMTIYEN-VVYGLRINGIKDKQVLDeavekalqgasiwdevkdrlydsaigLSGGQQQRVCVARVLATS 166
Cdd:COG1245 426 NT------DDFGSSYYKTeIIKPLGLEKLLDKNVKD--------------------------LSGGELQRVAIAACLSRD 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2038545162 167 PKIILLDEPTSALDpisagkIEETlyglkdkytmLLVTRSMQQASRISDKTGFFLDGDL 225
Cdd:COG1245 474 ADLYLLDEPSAHLD------VEQR----------LAVAKAIRRFAENRGKTAMVVDHDI 516
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-237 |
2.96e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.97 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 19 KALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEvttTGSVVYNGHNIySPRTDTVELRKEIGMVFQQPNpf 98
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCL--FGIYQKD---SGSILFQGKEI-DFKSSKEALENGISMVHQELN-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 99 pMTIYENVVYGLRINGIKDKQVLDEAVEKALQGASIWDEVKDRL--YDSAIGLSGGQQQRVCVARVLATSPKIILLDEPT 176
Cdd:PRK10982 84 -LVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIdpRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2038545162 177 SALDPISAGKIEETLYGLKDK-YTMLLVTRSMQQASRISDKTGFFLDGDLIEFNDTKQMFLD 237
Cdd:PRK10982 163 SSLTEKEVNHLFTIIRKLKERgCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMD 224
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-180 |
1.86e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.33 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 3 DAILQVSDLSVY---YNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSL--NRMGdlnpeVTTTGSVVYNGHNIysp 77
Cdd:NF040905 255 EVVFEVKNWTVYhplHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgRSYG-----RNISGTVFKDGKEV--- 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 78 RTDTV------------ELRKEIGMVFQQpnpfpmTIYENVVYGlRINGIKDKQVLDEAVEkalqgASIWDEVKDRL--- 142
Cdd:NF040905 327 DVSTVsdaidaglayvtEDRKGYGLNLID------DIKRNITLA-NLGKVSRRGVIDENEE-----IKVAEEYRKKMnik 394
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2038545162 143 ----YDSAIGLSGGQQQRVCVARVLATSPKIILLDEPTSALD 180
Cdd:NF040905 395 tpsvFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
18-225 |
1.87e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.35 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 18 KKALNSVSLSFQP-----KEITALIGPSGSGKSTLLKSLNrmGDLNP---EVTTTGSVVYNGHNIYSPRTDTVELrkeig 89
Cdd:PRK13409 347 TKKLGDFSLEVEGgeiyeGEVIGIVGPNGIGKTTFAKLLA--GVLKPdegEVDPELKISYKPQYIKPDYDGTVED----- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 90 MVFQQPNPFPMTIYEN-VVYGLRINGIKDKQVLDeavekalqgasiwdevkdrlydsaigLSGGQQQRVCVARVLATSPK 168
Cdd:PRK13409 420 LLRSITDDLGSSYYKSeIIKPLQLERLLDKNVKD--------------------------LSGGELQRVAIAACLSRDAD 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2038545162 169 IILLDEPTSALDpisagkIEETlyglkdkytmLLVTRSMQQASRISDKTGFFLDGDL 225
Cdd:PRK13409 474 LYLLDEPSAHLD------VEQR----------LAVAKAIRRIAEEREATALVVDHDI 514
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
16-191 |
2.51e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.39 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 16 NKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSL-NRM------GDLN----PEVTTTGSVV--YNGHN-IYSPRtdt 81
Cdd:PLN03140 891 DRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLaGRKtggyieGDIRisgfPKKQETFARIsgYCEQNdIHSPQ--- 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 82 velrkeigmvfqqpnpfpMTIYENVVYG--LRIngikDKQVLDEavEKAlqgaSIWDEVK-----DRLYDSAIGLSG--- 151
Cdd:PLN03140 968 ------------------VTVRESLIYSafLRL----PKEVSKE--EKM----MFVDEVMelvelDNLKDAIVGLPGvtg 1019
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2038545162 152 ---GQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEETL 191
Cdd:PLN03140 1020 lstEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTV 1062
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-180 |
7.32e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.51 E-value: 7.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 6 LQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEvttTGSVVY--NGHNIYSPRTDTVE 83
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL--VGELEPD---SGTVKWseNANIGYYAQDHAYD 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 84 LRKEIGMV-----FQQPNpfpmtiyenvvyglringiKDKQVLDEAVEKALQGAsiwDEVKdrlyDSAIGLSGGQQQRVC 158
Cdd:PRK15064 395 FENDLTLFdwmsqWRQEG-------------------DDEQAVRGTLGRLLFSQ---DDIK----KSVKVLSGGEKGRML 448
|
170 180
....*....|....*....|..
gi 2038545162 159 VARVLATSPKIILLDEPTSALD 180
Cdd:PRK15064 449 FGKLMMQKPNVLVMDEPTNHMD 470
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
145-249 |
7.93e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 49.35 E-value: 7.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 145 SAIGLSGGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKI-EETLYGLKDKYTMLLVTRSMQQASRIS------DKT 217
Cdd:NF000106 141 AAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVwDEVRSMVRDGATVLLTTQYMEEAEQLAheltviDRG 220
|
90 100 110
....*....|....*....|....*....|....*
gi 2038545162 218 GFFLDGDLIEFNDT---KQMFLDPQHKETEDYITG 249
Cdd:NF000106 221 RVIADGKVDELKTKvggRTLQIRPAHAAELDRMVG 255
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
35-208 |
8.56e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.56 E-value: 8.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 35 ALIGPSGSGKSTLLKSLnrMGDLNPevtTTGSVvynghniyspRTDTvelRKEIGMvFQQ------PNPfpmTIYENVVY 108
Cdd:PRK11147 349 ALIGPNGCGKTTLLKLM--LGQLQA---DSGRI----------HCGT---KLEVAY-FDQhraeldPEK---TVMDNLAE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 109 G---LRINGiKDKQVLDeavekALQgasiwdevkDRLYDSA------IGLSGGQQQRVCVARVLATSPKIILLDEPTSAL 179
Cdd:PRK11147 407 GkqeVMVNG-RPRHVLG-----YLQ---------DFLFHPKramtpvKALSGGERNRLLLARLFLKPSNLLILDEPTNDL 471
|
170 180 190
....*....|....*....|....*....|...
gi 2038545162 180 DpisagkIE--ETLYGLKDKY--TMLLVTRSMQ 208
Cdd:PRK11147 472 D------VEtlELLEELLDSYqgTVLLVSHDRQ 498
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-196 |
1.69e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.58 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 3 DAILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEvttTGSVVYNghniysprtDTV 82
Cdd:PRK11819 322 DKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMI--TGQEQPD---SGTIKIG---------ETV 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 83 ELrkeiGMVFQQ-----PNPfpmTIYENVVYGLRIngIKDKQVldeavekalqgasiwdEVKDRLYDSAIG--------- 148
Cdd:PRK11819 388 KL----AYVDQSrdaldPNK---TVWEEISGGLDI--IKVGNR----------------EIPSRAYVGRFNfkggdqqkk 442
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2038545162 149 ---LSGGQQQRVCVARVLATSPKIILLDEPTSALDPisagkieETLYGLKD 196
Cdd:PRK11819 443 vgvLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV-------ETLRALEE 486
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
18-180 |
2.12e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.79 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 18 KKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPevtTTGSVVYNGHNIYS-PRTDTVELRKEIGMVFQqpn 96
Cdd:PRK13541 13 QKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIA--GIMQP---SSGNIYYKNCNINNiAKPYCTYIGHNLGLKLE--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 97 pfpMTIYENVVYGLRINgikdkqvldEAVEkALQGASIWDEVKDRLYDSAIGLSGGQQQRVCVARVLATSPKIILLDEPT 176
Cdd:PRK13541 85 ---MTVFENLKFWSEIY---------NSAE-TLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVE 151
|
....
gi 2038545162 177 SALD 180
Cdd:PRK13541 152 TNLS 155
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
2-181 |
2.51e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.15 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 2 TDAILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEvttTGSVVYNGH-NIYSPRTD 80
Cdd:PRK13543 8 APPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVL--AGLLHVE---SGQIQIDGKtATRGDRSR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 81 TVELRKEIGMVFQQpnpfpMTIYENVVYGLRINGIKDKQVLDEAVekALQGASIWDEVKDRlydsaiGLSGGQQQRVCVA 160
Cdd:PRK13543 83 FMAYLGHLPGLKAD-----LSTLENLHFLCGLHGRRAKQMPGSAL--AIVGLAGYEDTLVR------QLSAGQKKRLALA 149
|
170 180
....*....|....*....|.
gi 2038545162 161 RVLATSPKIILLDEPTSALDP 181
Cdd:PRK13543 150 RLWLSPAPLWLLDEPYANLDL 170
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-180 |
3.75e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.47 E-value: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 30 PKE--ITALIGPSGSGKSTLLKSLNrmGDLNPevtttgsvvyN-GHNIYSPRTDTVeLRK----EIGMVFQQpnpfpmtI 102
Cdd:COG1245 96 PKKgkVTGILGPNGIGKSTALKILS--GELKP----------NlGDYDEEPSWDEV-LKRfrgtELQDYFKK-------L 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 103 YEN---VVYglringiKDKQVldEAVEKALQG-----------ASIWDEVKDRL-----YDSAIG-LSGGQQQRVCVARV 162
Cdd:COG1245 156 ANGeikVAH-------KPQYV--DLIPKVFKGtvrellekvdeRGKLDELAEKLgleniLDRDISeLSGGELQRVAIAAA 226
|
170
....*....|....*...
gi 2038545162 163 LATSPKIILLDEPTSALD 180
Cdd:COG1245 227 LLRDADFYFFDEPSSYLD 244
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
138-180 |
5.44e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.03 E-value: 5.44e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2038545162 138 VKDRLYDSAIG-LSGGQQQRVCVARVLATSPKIILLDEPTSALD 180
Cdd:PRK10982 380 VKTPGHRTQIGsLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-183 |
5.94e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.04 E-value: 5.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLkSL----NRMgdlnpevtTTGSVVYNGHNIYSPRtd 80
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLL-SLiagaRKI--------QQGRVEVLGGDMADAR-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 81 tveLRKEIG-----MvfqqP-----NPFP-MTIYENVVYGLRINGikdkqvLDEAvEKAlqgASIwdevkDRLYDS---- 145
Cdd:NF033858 70 ---HRRAVCpriayM----PqglgkNLYPtLSVFENLDFFGRLFG------QDAA-ERR---RRI-----DELLRAtgla 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2038545162 146 ------AIGLSGGQQQRV--CVArvLATSPKIILLDEPTSALDPIS 183
Cdd:NF033858 128 pfadrpAGKLSGGMKQKLglCCA--LIHDPDLLILDEPTTGVDPLS 171
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-197 |
7.47e-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: 44.67 E-value: 7.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 30 PKEITALIGPSGSGKSTLLKSLnrmgdlnpevtttgsvvyngHNIYSPRTDTVelrkeigmvfqqpnpfpmtiyenvvyg 109
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARAL--------------------ARELGPPGGGV--------------------------- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 110 LRINGIKDKQVLDEAVEKALQGasiwdevkdrlyDSAIGLSGGQQQRVCVARVLATSPKIILLDEPTSALDPISAGKIEE 189
Cdd:smart00382 34 IYIDGEDILEEVLDQLLLIIVG------------GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLL 101
|
....*...
gi 2038545162 190 TLYGLKDK 197
Cdd:smart00382 102 LEELRLLL 109
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
35-180 |
8.62e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 8.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 35 ALIGPSGSGKSTLLKSLNrmGDLNPevtTTGSVVynghniyspRTDTVELrkeigMVFQQPNPFPMTIYEN-VVYGLR-I 112
Cdd:PLN03073 539 AMVGPNGIGKSTILKLIS--GELQP---SSGTVF---------RSAKVRM-----AVFSQHHVDGLDLSSNpLLYMMRcF 599
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038545162 113 NGIKDKQVLDEAVEKALQGasiwdevkDRLYDSAIGLSGGQQQRVCVARVLATSPKIILLDEPTSALD 180
Cdd:PLN03073 600 PGVPEQKLRAHLGSFGVTG--------NLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
7-230 |
9.27e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.58 E-value: 9.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 7 QVSDLSVYYNKKK---ALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNrmGDLNPevtTTGSVVYNGhniysprtDTVE 83
Cdd:PRK13546 23 RMKDALIPKHKNKtffALDDISLKAYEGDVIGLVGINGSGKSTLSNIIG--GSLSP---TVGKVDRNG--------EVSV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 84 LRKEIGMVFQqpnpfpMTIYENVVYGLRINGIKDKQVldeaveKALQGASI-WDEVKDRLYDSAIGLSGGQQQRVCVARV 162
Cdd:PRK13546 90 IAISAGLSGQ------LTGIENIEFKMLCMGFKRKEI------KAMTPKIIeFSELGEFIYQPVKKYSSGMRAKLGFSIN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2038545162 163 LATSPKIILLDEPTSALDPISAGKIEETLYGLKD-KYTMLLVTRSMQQASRISDKTGFFLDGDLIEFND 230
Cdd:PRK13546 158 ITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEqNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGE 226
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
30-180 |
1.03e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.96 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 30 PKE--ITALIGPSGSGKSTLLKSLNrmGDLNPEVTTTGSvvynghniySPRTDTVeLRKEIGMVFQqpnpfpmtiyeNVV 107
Cdd:PRK13409 96 PKEgkVTGILGPNGIGKTTAVKILS--GELIPNLGDYEE---------EPSWDEV-LKRFRGTELQ-----------NYF 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 108 YGLRINGIK--------DK--QVLDEAVEKALQGA---SIWDEVKDRL-----YDSAIG-LSGGQQQRVCVARVLATSPK 168
Cdd:PRK13409 153 KKLYNGEIKvvhkpqyvDLipKVFKGKVRELLKKVderGKLDEVVERLgleniLDRDISeLSGGELQRVAIAAALLRDAD 232
|
170
....*....|..
gi 2038545162 169 IILLDEPTSALD 180
Cdd:PRK13409 233 FYFFDEPTSYLD 244
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
33-117 |
1.49e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 45.07 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 33 ITALIGPSGSGKSTLLKSLNRMGDLNPEVTTTGSVVYNGHNIYSPRTDTVELRKEIGMVFQqpnpFPMTIYENVVYGLRI 112
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFE----ISEFLEDGVRYRYGL 76
|
....*
gi 2038545162 113 NGIKD 117
Cdd:pfam13304 77 DLERE 81
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-180 |
2.00e-05 |
|
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: 44.66 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 29 QPKEITALIGPSGSGKSTLLKSLNrmGDLNPEVTTTGS------VV--YNG---HNIYSP-RTDTVELRKEIGMVFQQPN 96
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILA--GKLKPNLGKFDDppdwdeILdeFRGselQNYFTKlLEGDVKVIVKPQYVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 97 PFPMTIYENvvyglrINGIKDKQVLDEAVEK-ALQGasiwdeVKDRLYDSaigLSGGQQQRVCVARVLATSPKIILLDEP 175
Cdd:cd03236 102 AVKGKVGEL------LKKKDERGKLDELVDQlELRH------VLDRNIDQ---LSGGELQRVAIAAALARDADFYFFDEP 166
|
....*
gi 2038545162 176 TSALD 180
Cdd:cd03236 167 SSYLD 171
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
5-180 |
2.39e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.16 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 5 ILQVSDLSVYYNKKKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEVTTTGSV------VYNGHNIYSPR 78
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLL--AGELAPVSGEIGLAkgiklgYFAQHQLEFLR 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 79 TDTVELRKEIGMVFQQPnpfpmtiyenvvyglringikDKQVLDEAVEKALQGasiwdevkDRLYDSAIGLSGGQQQRVC 158
Cdd:PRK10636 390 ADESPLQHLARLAPQEL---------------------EQKLRDYLGGFGFQG--------DKVTEETRRFSGGEKARLV 440
|
170 180
....*....|....*....|..
gi 2038545162 159 VARVLATSPKIILLDEPTSALD 180
Cdd:PRK10636 441 LALIVWQRPNLLLLDEPTNHLD 462
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
14-181 |
6.71e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 43.81 E-value: 6.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 14 YYNKKKALNSVSLSFQPKEITALIGPSGSGKST---LLKSLNRmgdlnpevTTTGSVVYNGHNIYSprTDTVELRKEIGM 90
Cdd:PRK10522 332 YQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTlamLLTGLYQ--------PQSGEILLDGKPVTA--EQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 91 VFQQPNPFPmtiyenvvyglRINGIKDKQVLDEAVEKALQGASIWDEVK---DRLYDsaIGLSGGQQQRVCVARVLATSP 167
Cdd:PRK10522 402 VFTDFHLFD-----------QLLGPEGKPANPALVEKWLERLKMAHKLEledGRISN--LKLSKGQKKRLALLLALAEER 468
|
170
....*....|....
gi 2038545162 168 KIILLDEPTSALDP 181
Cdd:PRK10522 469 DILLLDEWAADQDP 482
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
24-48 |
7.80e-05 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 39.51 E-value: 7.80e-05
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
25-204 |
9.94e-05 |
|
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: 41.58 E-value: 9.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 25 SLSFQPKEITALIGPSGSGKSTLLKSlnrmgdlnpevtttgsvvynghniysprtdtvelrkeIGMVFqqpnpfpmtiye 104
Cdd:cd03227 15 DVTFGEGSLTIITGPNGSGKSTILDA-------------------------------------IGLAL------------ 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 105 nvvyGLRINGIKDKQVLDEAVEKALQGAsiwdevkdRLYDSAIGLSGGQQQRVCVARVLA----TSPKIILLDEPTSALD 180
Cdd:cd03227 46 ----GGAQSATRRRSGVKAGCIVAAVSA--------ELIFTRLQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLD 113
|
170 180
....*....|....*....|....
gi 2038545162 181 PISAGKIEETLYGLKDKYTMLLVT 204
Cdd:cd03227 114 PRDGQALAEAILEHLVKGAQVIVI 137
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
149-215 |
1.18e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 41.54 E-value: 1.18e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2038545162 149 LSGGQQQRVCVARVLATSPK--IILLDEPTSALDPISAGKIEETLYGLKD-KYTMLLVTRS---MQQASRISD 215
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDlGNTVILIEHNldvLSSADWIID 160
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
149-247 |
1.87e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 149 LSGGQQQRVCVARVLATSPKII--LLDEPTSALDPISAGKIEETLYGLKDK-YTMLLVTRSMQQ---ASRISD---KTGF 219
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQgNTVLLVEHDEQMislADRIIDigpGAGI 556
|
90 100
....*....|....*....|....*...
gi 2038545162 220 FldGDLIEFNDTKQMFLDPQHKETEDYI 247
Cdd:PRK00635 557 F--GGEVLFNGSPREFLAKSDSLTAKYL 582
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
141-215 |
3.45e-04 |
|
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: 40.70 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 141 RLYDSAIGLSGGQQQRVCVARVLAT--SPKIILLDEPTSALDPISAGKIEETLYGLKDKYTMLLVTR----SMQQASRIS 214
Cdd:cd03270 130 TLSRSAPTLSGGEAQRIRLATQIGSglTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEhdedTIRAADHVI 209
|
.
gi 2038545162 215 D 215
Cdd:cd03270 210 D 210
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
125-226 |
3.77e-04 |
|
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: 40.25 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 125 VEKALQGASIWDEVKDRLYDSAIGLSGGQQQRVCVARVLATSPKIILLDEPTSALDpisagkIEETLYglkdkytmllVT 204
Cdd:cd03222 48 QLIPNGDNDEWDGITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLD------IEQRLN----------AA 111
|
90 100
....*....|....*....|..
gi 2038545162 205 RSMQQASRISDKTGFFLDGDLI 226
Cdd:cd03222 112 RAIRRLSEEGKKTALVVEHDLA 133
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
19-57 |
4.81e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 40.68 E-value: 4.81e-04
10 20 30
....*....|....*....|....*....|....*....
gi 2038545162 19 KALNSVSLSFQPkeITALIGPSGSGKSTLLKSLNRMGDL 57
Cdd:COG4637 11 KSLRDLELPLGP--LTVLIGANGSGKSNLLDALRFLSDA 47
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
19-150 |
7.89e-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: 39.99 E-value: 7.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 19 KALNSVSLSFQPKeITALIGPSGSGKSTLLKSLNRMgdLNPEVTTTgsvvYNGHNIYSPRtDTVELRKEIGMVFQQPnpf 98
Cdd:COG3593 12 RSIKDLSIELSDD-LTVLVGENNSGKSSILEALRLL--LGPSSSRK----FDEEDFYLGD-DPDLPEIEIELTFGSL--- 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2038545162 99 PMTIYENVVYGLRINGIKDK-QVLDEAVEKALQGASiwDEVKDRLYDSAIGLS 150
Cdd:COG3593 81 LSRLLRLLLKEEDKEELEEAlEELNEELKEALKALN--ELLSEYLKELLDGLD 131
|
|
| ATPase_2 |
pfam01637 |
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is ... |
14-88 |
1.17e-03 |
|
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is involved in binding ATP. There are eukaryote members as well as archaeal members in this family.
Pssm-ID: 376582 [Multi-domain] Cd Length: 222 Bit Score: 39.23 E-value: 1.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2038545162 14 YYNKKKALNSVS--LSFQPKEITALIGPSGSGKSTLLK-SLNRMGDLNPEVtttgSVVYNGHNIYSPRTDTVELRKEI 88
Cdd:pfam01637 1 FVDREKELKELEewAERGPNLIYVIYGPEGCGKTALLReSIENLLDLGYYV----IYYDPLRRYFISKLDRFEEVRRL 74
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
24-72 |
1.23e-03 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 39.78 E-value: 1.23e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2038545162 24 VSLSFQPKEITALIGPSGSGKSTLLKSLnrMGDLNPEvttTGSVVYNGH 72
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLL--TGLYRPE---SGEILLDGQ 394
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
28-67 |
1.90e-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: 38.53 E-value: 1.90e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2038545162 28 FQPKeITALIGPSGSGKSTLLKSLnrMGDLNpevTTTGSV 67
Cdd:cd01854 83 LKGK-TSVLVGQSGVGKSTLLNAL--LPELV---LATGEI 116
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
19-52 |
2.37e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 38.44 E-value: 2.37e-03
10 20 30
....*....|....*....|....*....|....*
gi 2038545162 19 KALNSVSLSF-QPKEITALIGPSGSGKSTLLKSLN 52
Cdd:COG3950 12 RGFEDLEIDFdNPPRLTVLVGENGSGKTTLLEAIA 46
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
141-197 |
2.43e-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: 38.84 E-value: 2.43e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 141 RLYDSAIGLSGGQQQRVCVARVL---ATSPKIILLDEPTSALDPISAGKIEETLYGLKDK 197
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDK 881
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
150-180 |
2.66e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 38.69 E-value: 2.66e-03
10 20 30
....*....|....*....|....*....|.
gi 2038545162 150 SGGQQQRVCVARVLATSPKIILLDEPTSALD 180
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
33-142 |
3.79e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 36.55 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2038545162 33 ITALIGPSGSGKSTLLKSLNRMgdlnpevtttgsvvyngHNIYSPRTDTVELrkeigmvfqqPNPF-PMTIYENVV--YG 109
Cdd:pfam13401 7 ILVLTGESGTGKTTLLRRLLEQ-----------------LPEVRDSVVFVDL----------PSGTsPKDLLRALLraLG 59
|
90 100 110
....*....|....*....|....*....|....*...
gi 2038545162 110 LRINGIKDKQVLDEAVEKALQGAS-----IWDEVkDRL 142
Cdd:pfam13401 60 LPLSGRLSKEELLAALQQLLLALAvavvlIIDEA-QHL 96
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
30-53 |
4.05e-03 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 36.73 E-value: 4.05e-03
|
| NK |
cd02019 |
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ... |
33-75 |
4.77e-03 |
|
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.
Pssm-ID: 238977 [Multi-domain] Cd Length: 69 Bit Score: 35.00 E-value: 4.77e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2038545162 33 ITALIGPSGSGKSTLLKSL-NRMGDLNPEVTTTGsVVYNGHNIY 75
Cdd:cd02019 1 IIAITGGSGSGKSTVAKKLaEQLGGRSVVVLDEI-VILEGLYAS 43
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
33-97 |
5.06e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 37.46 E-value: 5.06e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2038545162 33 ITALIGPSGSGKSTLLKSLnrMGDLNPEVTttgsVVYnghnIYSPRTDTVELRKEIGMVFQQPNP 97
Cdd:COG3267 45 FVVLTGEVGTGKTTLLRRL--LERLPDDVK----VAY----IPNPQLSPAELLRAIADELGLEPK 99
|
|
| Rad17 |
pfam03215 |
Rad17 P-loop domain; |
10-53 |
6.52e-03 |
|
Rad17 P-loop domain;
Pssm-ID: 367398 [Multi-domain] Cd Length: 186 Bit Score: 36.47 E-value: 6.52e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2038545162 10 DLSVYYNK----KKALNSVSLSFQPKEITALIGPSGSGKSTLLKSLNR 53
Cdd:pfam03215 20 QLAVHKRKikdvQEWLDAMFLENAKHRILLISGPSGCGKSTVIKELSK 67
|
|
| |
