|
Name |
Accession |
Description |
Interval |
E-value |
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
34-290 |
0e+00 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 523.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 34 TLSDRERRVVYSTQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELVPTVKTSGKILYRDQNIF 113
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGARVEGEILLDGEDIY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 114 DKSYPVEKLRTNVGMVFQQPNPFPKSIYDNITYGPRIHGIKDKKILDEIVEKSLRGAAIWDELKDRLDQNAYGLSGGQQQ 193
Cdd:COG1117 82 DPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDEVKDRLKKSALGLSGGQQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 194 RVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDYSIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIF 273
Cdd:COG1117 162 RLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIF 241
|
250
....*....|....*..
gi 1374671911 274 SNPSDKQTEDYISGRFG 290
Cdd:COG1117 242 TNPKDKRTEDYITGRFG 258
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
43-289 |
6.30e-167 |
|
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: 462.53 E-value: 6.30e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 43 VYSTQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELVPTVKTSGKILYRDQNIFDKSYPVEKL 122
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPGVRIEGKVLFDGQDIYDKKIDVVEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 123 RTNVGMVFQQPNPFPKSIYDNITYGPRIHGIKDKKILDEIVEKSLRGAAIWDELKDRLDQNAYGLSGGQQQRVCIARCLA 202
Cdd:TIGR00972 81 RRRVGMVFQKPNPFPMSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALWDEVKDRLHDSALGLSGGQQQRLCIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 203 IEPDVILMDEPTSALDPISTLRVEELVQDLKKDYSIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNPSDKQTE 282
Cdd:TIGR00972 161 VEPEVLLLDEPTSALDPIATGKIEELIQELKKKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKRTE 240
|
....*..
gi 1374671911 283 DYISGRF 289
Cdd:TIGR00972 241 DYISGRF 247
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
45-272 |
2.21e-137 |
|
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: 386.92 E-value: 2.21e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 45 STQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELVPTVKTSGKILYRDQNIFDKSYPVEKLRT 124
Cdd:cd03260 2 ELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLLDGKDIYDLDVDVLELRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 125 NVGMVFQQPNPFPKSIYDNITYGPRIHGIKDKKILDEIVEKSLRGAAIWDELKDRLDqnAYGLSGGQQQRVCIARCLAIE 204
Cdd:cd03260 82 RVGMVFQKPNPFPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRLH--ALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1374671911 205 PDVILMDEPTSALDPISTLRVEELVQDLKKDYSIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKI 272
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
43-290 |
2.15e-130 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 370.26 E-value: 2.15e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 43 VYSTQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELVPTVKTSGKILYRDQNIFDKSYPVEKL 122
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 123 RTNVGMVFQQPNPFPKSIYDNITYGPRIHGIKDKKILDEIVEKSLRGAAIWDELKDRLDQNAYGLSGGQQQRVCIARCLA 202
Cdd:PRK14239 85 RKEIGMVFQQPNPFPMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIARVLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 203 IEPDVILMDEPTSALDPISTLRVEELVQDLKKDYSIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNPSDKQTE 282
Cdd:PRK14239 165 TSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETE 244
|
....*...
gi 1374671911 283 DYISGRFG 290
Cdd:PRK14239 245 DYISGKFG 252
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
42-290 |
1.19e-127 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 363.72 E-value: 1.19e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 42 VVYSTQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELVPTVKTSGKILYRDQNIFDKSY-PVE 120
Cdd:PRK14243 9 TVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGKVTFHGKNLYAPDVdPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 121 kLRTNVGMVFQQPNPFPKSIYDNITYGPRIHGIKDKkiLDEIVEKSLRGAAIWDELKDRLDQNAYGLSGGQQQRVCIARC 200
Cdd:PRK14243 89 -VRRRIGMVFQKPNPFPKSIYDNIAYGARINGYKGD--MDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 201 LAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDYSIIIVTHNMQQAARVSDKTAFF---------LNGYVNEYDDTDK 271
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEK 245
|
250
....*....|....*....
gi 1374671911 272 IFSNPSDKQTEDYISGRFG 290
Cdd:PRK14243 246 IFNSPQQQATRDYVSGRFG 264
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
47-290 |
5.87e-91 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 270.75 E-value: 5.87e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELVPTVKTSGKILYRDQNIFDKSYPVEKLRTNV 126
Cdd:PRK14258 11 NNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIYERRVNLNRLRRQV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 127 GMVFQQPNPFPKSIYDNITYGPRIHGIKDKKILDEIVEKSLRGAAIWDELKDRLDQNAYGLSGGQQQRVCIARCLAIEPD 206
Cdd:PRK14258 91 SMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 207 VILMDEPTSALDPISTLRVEELVQD--LKKDYSIIIVTHNMQQAARVSDKTAFFLN-----GYVNEYDDTDKIFSNPSDK 279
Cdd:PRK14258 171 VLLMDEPCFGLDPIASMKVESLIQSlrLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHDS 250
|
250
....*....|.
gi 1374671911 280 QTEDYISGRFG 290
Cdd:PRK14258 251 RTREYVLSRLG 261
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
46-290 |
3.80e-87 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 260.54 E-value: 3.80e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 46 TQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELVPTVKTSGKILYRDQNIFDKSYPVEKLRTN 125
Cdd:PRK14267 7 TVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSPDVDPIEVRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 126 VGMVFQQPNPFPK-SIYDNITYGPRIHG-IKDKKILDEIVEKSLRGAAIWDELKDRLDQNAYGLSGGQQQRVCIARCLAI 203
Cdd:PRK14267 87 VGMVFQYPNPFPHlTIYDNVAIGVKLNGlVKSKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 204 EPDVILMDEPTSALDPISTLRVEELVQDLKKDYSIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNPSDKQTED 283
Cdd:PRK14267 167 KPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEK 246
|
....*..
gi 1374671911 284 YISGRFG 290
Cdd:PRK14267 247 YVTGALG 253
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
47-288 |
1.09e-84 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 254.45 E-value: 1.09e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELVPTVKTSGKILYRDQNIFdkSYPVEKLRTNV 126
Cdd:PRK14247 7 RDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIF--KMDVIELRRRV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 127 GMVFQQPNPFPK-SIYDNITYGPRIHGI-KDKKILDEIVEKSLRGAAIWDELKDRLDQNAYGLSGGQQQRVCIARCLAIE 204
Cdd:PRK14247 85 QMVFQIPNPIPNlSIFENVALGLKLNRLvKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 205 PDVILMDEPTSALDPISTLRVEELVQDLKKDYSIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNPSDKQTEDY 284
Cdd:PRK14247 165 PEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEKY 244
|
....
gi 1374671911 285 ISGR 288
Cdd:PRK14247 245 VTGR 248
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
47-286 |
1.03e-77 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 236.04 E-value: 1.03e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQNIFDKSYPVEKLRTNV 126
Cdd:COG1126 5 ENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEP-----DSGTITVDGEDLTDSKKDINKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 127 GMVFQQPNPFP-KSIYDNITYGPRIHGIKDKKILDEIVEKSLR--GaaiwdeLKDRLDQNAYGLSGGQQQRVCIARCLAI 203
Cdd:COG1126 80 GMVFQQFNLFPhLTVLENVTLAPIKVKKMSKAEAEERAMELLErvG------LADKADAYPAQLSGGQQQRVAIARALAM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 204 EPDVILMDEPTSALDPISTLRVEELVQDLKKD-YSIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNPSDKQTE 282
Cdd:COG1126 154 EPKVMLFDEPTSALDPELVGEVLDVMRDLAKEgMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTR 233
|
....
gi 1374671911 283 DYIS 286
Cdd:COG1126 234 AFLS 237
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
43-288 |
1.07e-75 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 231.86 E-value: 1.07e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 43 VYSTQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELVPT-VKTSGKILYRDQNIFdkSYPVEK 121
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSkIKVDGKVLYFGKDIF--QIDAIK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 122 LRTNVGMVFQQPNPFPK-SIYDNITYGPRIHGIKDKKILDEIVEKSLRGAAIWDELKDRLDQNAYGLSGGQQQRVCIARC 200
Cdd:PRK14246 88 LRKEVGMVFQQPNPFPHlSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 201 LAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDYSIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNPSDKQ 280
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNEL 247
|
....*...
gi 1374671911 281 TEDYISGR 288
Cdd:PRK14246 248 TEKYVIGR 255
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
48-290 |
1.63e-69 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 216.50 E-value: 1.63e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 48 NLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELVPTVKTSGKILYRDQNIFDKSYPVEkLRTNVG 127
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDVLE-FRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 128 MVFQQPNPFPKSIYDNITYGPRIHGIKDKKILDEIVEKSLRGAAIWDELKDRLDQNAYGLSGGQQQRVCIARCLAIEPDV 207
Cdd:PRK14271 105 MLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 208 ILMDEPTSALDPISTLRVEELVQDLKKDYSIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNPSDKQTEDYISG 287
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAG 264
|
...
gi 1374671911 288 RFG 290
Cdd:PRK14271 265 LSG 267
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
45-263 |
1.87e-63 |
|
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: 198.91 E-value: 1.87e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 45 STQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQNIFDKSYPVEKLRT 124
Cdd:cd03262 2 EIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEP-----DSGTIIIDGLKLTDDKKNINELRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 125 NVGMVFQQPNPFP-KSIYDNITYGPRIHGIKDKKILDEIVEKSLR--GaaiwdeLKDRLDQNAYGLSGGQQQRVCIARCL 201
Cdd:cd03262 77 KVGMVFQQFNLFPhLTVLENITLAPIKVKGMSKAEAEERALELLEkvG------LADKADAYPAQLSGGQQQRVAIARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1374671911 202 AIEPDVILMDEPTSALDPISTLRVEELVQDLKKD-YSIIIVTHNMQQAARVSDKTAFFLNGYV 263
Cdd:cd03262 151 AMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEgMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
48-261 |
1.66e-60 |
|
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: 190.09 E-value: 1.66e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 48 NLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIFDKSYPVEKLRTNVG 127
Cdd:cd03229 5 NVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEE-----PDSGSILIDGEDLTDLEDELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 128 MVFQQPNPFP-KSIYDNItygprihgikdkkildeivekslrgaaiwdelkdrldqnAYGLSGGQQQRVCIARCLAIEPD 206
Cdd:cd03229 80 MVFQDFALFPhLTVLENI---------------------------------------ALGLSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1374671911 207 VILMDEPTSALDPISTLRVEELVQDLKKD--YSIIIVTHNMQQAARVSDKTAFFLNG 261
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
50-276 |
5.27e-59 |
|
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: 187.92 E-value: 5.27e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 50 DLWY---GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMveLVPTvktSGKILYRDQNIFDKSypVEKLRTNV 126
Cdd:COG1122 5 NLSFsypGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGL--LKPT---SGEVLVDGKDITKKN--LRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 127 GMVFQqpNP----FPKSIYDNITYGPRIHGIKDKKIlDEIVEKSLR--GaaiwdeLKDRLDQNAYGLSGGQQQRVCIARC 200
Cdd:COG1122 78 GLVFQ--NPddqlFAPTVEEDVAFGPENLGLPREEI-RERVEEALElvG------LEHLADRPPHELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1374671911 201 LAIEPDVILMDEPTSALDPISTLRVEELVQDLKKD-YSIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNP 276
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEgKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
54-278 |
1.54e-56 |
|
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: 189.73 E-value: 1.54e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 54 GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvPTvktSGKILYRDQNIFDKSYP-VEKLRTNVGMVFQQ 132
Cdd:COG1123 276 GGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR--PT---SGSILFDGKDLTKLSRRsLRELRRRVQMVFQD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 133 P----NPFpKSIYDNITYGPRIHGIKDKKILDEIVEKSLRGAAIWDELKDRLdqnAYGLSGGQQQRVCIARCLAIEPDVI 208
Cdd:COG1123 351 PysslNPR-MTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRY---PHELSGGQRQRVAIARALALEPKLL 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1374671911 209 LMDEPTSALDPISTLRVEELVQDLKKDY--SIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNPSD 278
Cdd:COG1123 427 ILDEPTSALDVSVQAQILNLLRDLQRELglTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQH 498
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
45-255 |
2.52e-56 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 180.40 E-value: 2.52e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 45 STQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQNIfdKSYPVEKLRT 124
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPP-----TSGEIYLDGKPL--SAMPPPEWRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 125 NVGMVFQQPNPFPKSIYDNITYGPRIHGIK-DKKILDEIVEKSLRGAAIwdelkdrLDQNAYGLSGGQQQRVCIARCLAI 203
Cdd:COG4619 75 QVAYVPQEPALWGGTVRDNLPFPFQLRERKfDRERALELLERLGLPPDI-------LDKPVERLSGGERQRLALIRALLL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1374671911 204 EPDVILMDEPTSALDPISTLRVEELVQDLKKDY--SIIIVTHNMQQAARVSDKT 255
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYLAEEgrAVLWVSHDPEQIERVADRV 201
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
50-261 |
1.86e-54 |
|
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: 175.73 E-value: 1.86e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 50 DLWY----GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIfdKSYPVEKLRTN 125
Cdd:cd03225 4 NLSFsypdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLG-----PTSGEVLVDGKDL--TKLSLKELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 126 VGMVFQQPNP--FPKSIYDNITYGPRIHGIKDKKIlDEIVEKSLRGAaiwdELKDRLDQNAYGLSGGQQQRVCIARCLAI 203
Cdd:cd03225 77 VGLVFQNPDDqfFGPTVEEEVAFGLENLGLPEEEI-EERVEEALELV----GLEGLRDRSPFTLSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1374671911 204 EPDVILMDEPTSALDPISTLRVEELVQDLKKD-YSIIIVTHNMQQAARVSDKTAFFLNG 261
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
47-257 |
4.82e-54 |
|
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: 174.63 E-value: 4.82e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQNIFDKsyPVEklRTNV 126
Cdd:cd03259 4 KGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERP-----DSGEILIDGRDVTGV--PPE--RRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 127 GMVFQQPNPFP-KSIYDNITYGPRIHGIKDKKIlDEIVEKSLRGAAIWDELKDRLDQnaygLSGGQQQRVCIARCLAIEP 205
Cdd:cd03259 75 GMVFQDYALFPhLTVAENIAFGLKLRGVPKAEI-RARVRELLELVGLEGLLNRYPHE----LSGGQQQRVALARALAREP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1374671911 206 DVILMDEPTSALDPISTLRVEELVQDLKK--DYSIIIVTHNMQQAARVSDKTAF 257
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEEALALADRIAV 203
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
47-273 |
5.37e-53 |
|
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: 172.69 E-value: 5.37e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKAlnrMVELVPtvKTSGKILYRDQNIFDKSyPVE--KLRT 124
Cdd:cd03261 4 RGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRL---IVGLLR--PDSGEVLIDGEDISGLS-EAElyRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 125 NVGMVFQQPNPF-PKSIYDNITYGPRIHGIKDKKILDEIVEKSLRGAaiwdELKDRLDQNAYGLSGGQQQRVCIARCLAI 203
Cdd:cd03261 78 RMGMLFQSGALFdSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAV----GLRGAEDLYPAELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1374671911 204 EPDVILMDEPTSALDPISTLRVEELVQDLKKDY--SIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIF 273
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRSLKKELglTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
54-285 |
1.14e-52 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 174.12 E-value: 1.14e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 54 GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQNIfdKSYPVEKLRTNVGMVFQQP 133
Cdd:COG1125 13 DGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEP-----TSGRILIDGEDI--RDLDPVELRRRIGYVIQQI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 134 NPFP-KSIYDNITYGPRIHGIKDKKIlDEIVekslrgaaiwDELKDR--LDQNAYG------LSGGQQQRVCIARCLAIE 204
Cdd:COG1125 86 GLFPhMTVAENIATVPRLLGWDKERI-RARV----------DELLELvgLDPEEYRdrypheLSGGQQQRVGVARALAAD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 205 PDVILMDEPTSALDPIS--TLRVE--ELVQDLKKdySIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNPSDKQ 280
Cdd:COG1125 155 PPILLMDEPFGALDPITreQLQDEllRLQRELGK--TIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDF 232
|
....*
gi 1374671911 281 TEDYI 285
Cdd:COG1125 233 VADFV 237
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
53-285 |
2.29e-52 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 171.33 E-value: 2.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 53 YGEQH-SLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIfdKSYPVEKLRTNVGMVFQ 131
Cdd:cd03295 10 YGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIE-----PTSGEIFIDGEDI--REQDPVELRRKIGYVIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 132 QPNPFP-KSIYDNITYGPRIHGIKDKKILDEIVEK-SLRGAAIwDELKDRLdqnAYGLSGGQQQRVCIARCLAIEPDVIL 209
Cdd:cd03295 83 QIGLFPhMTVEENIALVPKLLKWPKEKIRERADELlALVGLDP-AEFADRY---PHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1374671911 210 MDEPTSALDPISTLRVEELVQDLKKDY--SIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNPSDKQTEDYI 285
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQELgkTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFV 236
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
48-266 |
9.95e-52 |
|
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: 169.22 E-value: 9.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 48 NLDLWYGEQHS----LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIFDKSYPVEKLR 123
Cdd:cd03257 6 NLSVSFPTGGGsvkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLK-----PTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 124 -TNVGMVFQQP----NPFpKSIYDNITYGPRIHGIKDKK-ILDEIVEKSLRGAaiwDELKDRLDQNAYGLSGGQQQRVCI 197
Cdd:cd03257 81 rKEIQMVFQDPmsslNPR-MTIGEQIAEPLRIHGKLSKKeARKEAVLLLLVGV---GLPEEVLNRYPHELSGGQRQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1374671911 198 ARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDY--SIIIVTHNMQQAARVSDKTAFFLNGYVNEY 266
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
47-278 |
1.35e-50 |
|
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: 166.90 E-value: 1.35e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHS----LKNVNLDILEKNVTAIIGPSGSGKSTYVKALnrmVELVPtvKTSGKILYRDQNI---FDKSYpv 119
Cdd:COG1124 5 RNLSVSYGQGGRrvpvLKDVSLEVAPGESFGLVGESGSGKSTLLRAL---AGLER--PWSGEVTFDGRPVtrrRRKAF-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 120 eklRTNVGMVFQQP----NPFpKSIYDNITYGPRIHGIKDKkilDEIVEKSLRGAAIWDELKDRL-DQnaygLSGGQQQR 194
Cdd:COG1124 78 ---RRRVQMVFQDPyaslHPR-HTVDRILAEPLRIHGLPDR---EERIAELLEQVGLPPSFLDRYpHQ----LSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 195 VCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDY--SIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKI 272
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226
|
....*.
gi 1374671911 273 FSNPSD 278
Cdd:COG1124 227 LAGPKH 232
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
55-276 |
2.54e-49 |
|
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: 164.55 E-value: 2.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 55 EQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMveLVPTvktSGKILYRDQNIF-DKSYPVEKLRTNVGMVFQQP 133
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGL--LKPT---SGTVTIDGRDITaKKKKKLKDLRKKVGLVFQFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 134 NP--FPKSIYDNITYGPRIHGIKDKKIlDEIVEKSLRGAAIWDELKDRldqNAYGLSGGQQQRVCIARCLAIEPDVILMD 211
Cdd:TIGR04521 92 EHqlFEETVYKDIAFGPKNLGLSEEEA-EERVKEALELVGLDEEYLER---SPFELSGGQMRRVAIAGVLAMEPEVLILD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1374671911 212 EPTSALDPISTLRVEELVQDLKKDY--SIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNP 276
Cdd:TIGR04521 168 EPTAGLDPKGRKEILDLFKRLHKEKglTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
54-254 |
1.49e-48 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 162.18 E-value: 1.49e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 54 GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTyvkaLNRMVE-LVPTvkTSGKILYRDQnifdksyPVEKLRTNVGMVFQQ 132
Cdd:COG1116 22 GGVTALDDVSLTVAAGEFVALVGPSGCGKST----LLRLIAgLEKP--TSGEVLVDGK-------PVTGPGPDRGVVFQE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 133 PNPFP-KSIYDNITYGPRIHGIKDKKIlDEIVEKSLR--GaaiwdeLKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVIL 209
Cdd:COG1116 89 PALLPwLTVLDNVALGLELRGVPKAER-RERARELLElvG------LAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1374671911 210 MDEPTSALDPISTLRVEELVQDLKKDY--SIIIVTHNMQQAARVSDK 254
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRLWQETgkTVLFVTHDVDEAVFLADR 208
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
41-276 |
3.84e-48 |
|
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: 162.92 E-value: 3.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 41 RVVYSTQNldlwyGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvPTVKTSGKILYRDQNIFDKSYP-V 119
Cdd:COG0444 8 KVYFPTRR-----GVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLP--PPGITSGEILFDGEDLLKLSEKeL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 120 EKLRTN-VGMVFQQP----NPFpKSIYDNITYGPRIHGIKDKKILDEIVEKSLRGAAIWDElKDRLDQNAYGLSGGQQQR 194
Cdd:COG0444 81 RKIRGReIQMIFQDPmtslNPV-MTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDP-ERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 195 VCIARCLAIEPDVILMDEPTSALDPisTLRVE--ELVQDLKKDY--SIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTD 270
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDV--TIQAQilNLLKDLQRELglAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVE 236
|
....*.
gi 1374671911 271 KIFSNP 276
Cdd:COG0444 237 ELFENP 242
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
47-263 |
4.11e-48 |
|
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: 159.58 E-value: 4.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQ----HSLKNVNLDILEKNVTAIIGPSGSGKSTyvkaLNRMVELVPTVkTSGKILYRDQNIFDKSyPVEK- 121
Cdd:cd03255 4 KNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKST----LLNILGGLDRP-TSGEVRVDGTDISKLS-EKELa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 122 --LRTNVGMVFQQPNPFPK-SIYDNITYGPRIHGIKDKKIlDEIVEKSLRGAaiwdELKDRLDQNAYGLSGGQQQRVCIA 198
Cdd:cd03255 78 afRRRHIGFVFQSFNLLPDlTALENVELPLLLAGVPKKER-RERAEELLERV----GLGDRLNHYPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1374671911 199 RCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDY--SIIIVTHNMqQAARVSDKTAFFLNGYV 263
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
47-263 |
4.53e-48 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 160.14 E-value: 4.53e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKAlnrMVELVPtvKTSGKILYRDQNIFDKSYP-VEKLRTN 125
Cdd:COG1127 9 RNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKL---IIGLLR--PDSGEILVDGQDITGLSEKeLYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 126 VGMVFQQPNPF-PKSIYDNITYGPRIHGIKDKKILDEIV-EK----SLRGAAiwdelkdrlDQNAYGLSGGQQQRVCIAR 199
Cdd:COG1127 84 IGMLFQGGALFdSLTVFENVAFPLREHTDLSEAEIRELVlEKlelvGLPGAA---------DKMPSELSGGMRKRVALAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1374671911 200 CLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDY--SIIIVTHNMQQAARVSDKTAFFLNGYV 263
Cdd:COG1127 155 ALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
45-254 |
9.50e-48 |
|
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: 159.82 E-value: 9.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 45 STQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRmvELVPTvktSGKILYRDQNIfdKSYPVEKLRT 124
Cdd:COG1120 3 EAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAG--LLKPS---SGEVLLDGRDL--ASLSRRELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 125 NVGMVFQQPN-PFPKSIYDNITYG--PRIHGI-KDKKILDEIVEKSLRGAAIWDeLKDR-LDQnaygLSGGQQQRVCIAR 199
Cdd:COG1120 76 RIAYVPQEPPaPFGLTVRELVALGryPHLGLFgRPSAEDREAVEEALERTGLEH-LADRpVDE----LSGGERQRVLIAR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1374671911 200 CLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDY--SIIIVTHNMQQAARVSDK 254
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERgrTVVMVLHDLNLAARYADR 207
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
54-265 |
1.19e-47 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 158.67 E-value: 1.19e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 54 GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTyvkALNRMVEL-VPTvktSGKILYRDQNIFDKSypvEKLRT-----NVG 127
Cdd:COG1136 19 GEVTALRGVSLSIEAGEFVAIVGPSGSGKST---LLNILGGLdRPT---SGEVLIDGQDISSLS---ERELArlrrrHIG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 128 MVFQQPNPFPK-SIYDNITYGPRIHGIKDKKILDEIVE--KSLrgaaiwdELKDRLDQNAYGLSGGQQQRVCIARCLAIE 204
Cdd:COG1136 90 FVFQFFNLLPElTALENVALPLLLAGVSRKERRERAREllERV-------GLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1374671911 205 PDVILMDEPTSALDPISTLRVEELVQDLKKDY--SIIIVTHNMQQAARvSDKTAFFLNGYVNE 265
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRELgtTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
54-277 |
1.97e-47 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 158.51 E-value: 1.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 54 GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNrMVELvPTvktSGKILYRDQNIFDKSYP-VEKLRTNVGMVFQQ 132
Cdd:cd03258 16 GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCIN-GLER-PT---SGSVLVDGTDLTLLSGKeLRKARRRIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 133 PNPF-PKSIYDNITYGPRIHGIKDKKILDEIVEK-SLRGaaiwdeLKDRLDqnAY--GLSGGQQQRVCIARCLAIEPDVI 208
Cdd:cd03258 91 FNLLsSRTVFENVALPLEIAGVPKAEIEERVLELlELVG------LEDKAD--AYpaQLSGGQKQRVGIARALANNPKVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1374671911 209 LMDEPTSALDPISTLRVEELVQDLKK--DYSIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNPS 277
Cdd:cd03258 163 LCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
47-276 |
4.42e-47 |
|
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: 164.69 E-value: 4.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWY--GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRmveLVP-TVKTSGKILYRDQNIFDksYPVEKLR 123
Cdd:COG1123 8 RDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG---LLPhGGRISGEVLLDGRDLLE--LSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 124 TNVGMVFQQP--NPFPKSIYDNITYGPRIHGIKDKKIlDEIVEKSLRGAAIwdelKDRLDQNAYGLSGGQQQRVCIARCL 201
Cdd:COG1123 83 RRIGMVFQDPmtQLNPVTVGDQIAEALENLGLSRAEA-RARVLELLEAVGL----ERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1374671911 202 AIEPDVILMDEPTSALDPISTLRVEELVQDLKKDY--SIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNP 276
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP 234
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
45-261 |
4.48e-47 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 157.53 E-value: 4.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 45 STQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIFDKSypvEKLRT 124
Cdd:COG1131 2 EVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLR-----PTSGEVRVLGEDVARDP---AEVRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 125 NVGMVFQQPNPFPK-SIYDNITYGPRIHGIkDKKILDEIVEKSLRGAaiwdELKDRLDQNAYGLSGGQQQRVCIARCLAI 203
Cdd:COG1131 74 RIGYVPQEPALYPDlTVRENLRFFARLYGL-PRKEARERIDELLELF----GLTDAADRKVGTLSGGMKQRLGLALALLH 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1374671911 204 EPDVILMDEPTSALDPISTLRVEELVQDLKKD-YSIIIVTHNMQQAARVSDKTAFFLNG 261
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLCDRVAIIDKG 207
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
47-278 |
6.56e-47 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 160.65 E-value: 6.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTyvkaLNRMV---ELVptvkTSGKILYRDQNIFDKsyPVEKlR 123
Cdd:COG3842 9 ENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTT----LLRMIagfETP----DSGRILLDGRDVTGL--PPEK-R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 124 tNVGMVFQQPNPFP-KSIYDNITYGPRIHGIKDKKIlDEIVEKSLRGAAIwDELKDRL-DQnaygLSGGQQQRVCIARCL 201
Cdd:COG3842 78 -NVGMVFQDYALFPhLTVAENVAFGLRMRGVPKAEI-RARVAELLELVGL-EGLADRYpHQ----LSGGQQQRVALARAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 202 AIEPDVILMDEPTSALDPisTLRvEELVQDLK---KDYSI--IIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNP 276
Cdd:COG3842 151 APEPRVLLLDEPLSALDA--KLR-EEMREELRrlqRELGItfIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERP 227
|
..
gi 1374671911 277 SD 278
Cdd:COG3842 228 AT 229
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
47-285 |
7.10e-47 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 157.18 E-value: 7.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQNIFDKSYPVEKLRTNV 126
Cdd:PRK09493 5 KNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEI-----TSGDLIVDGLKVNDPKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 127 GMVFQQPNPFPK-SIYDNITYGP-RIHGIKdKKILDEIVEKSLRGAAiwdeLKDRLDQNAYGLSGGQQQRVCIARCLAIE 204
Cdd:PRK09493 80 GMVFQQFYLFPHlTALENVMFGPlRVRGAS-KEEAEKQARELLAKVG----LAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 205 PDVILMDEPTSALDPisTLRVEEL--VQDLKKD-YSIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNPSDKQT 281
Cdd:PRK09493 155 PKLMLFDEPTSALDP--ELRHEVLkvMQDLAEEgMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRL 232
|
....
gi 1374671911 282 EDYI 285
Cdd:PRK09493 233 QEFL 236
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
54-254 |
2.13e-46 |
|
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: 155.32 E-value: 2.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 54 GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTyvkaLNRMV--ELVPTvktSGKILYRDQnifdksyPVEKLRTNVGMVFQ 131
Cdd:cd03293 15 GAVTALEDISLSVEEGEFVALVGPSGCGKST----LLRIIagLERPT---SGEVLVDGE-------PVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 132 QPNPFP-KSIYDNITYGPRIHGIKDKKIlDEIVEKSLR--GaaiwdeLKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVI 208
Cdd:cd03293 81 QDALLPwLTVLDNVALGLELQGVPKAEA-RERAEELLElvG------LSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1374671911 209 LMDEPTSALDPISTLRVEELVQDLKKDY--SIIIVTHNMQQAARVSDK 254
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDEAVFLADR 201
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
53-277 |
1.18e-45 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 154.57 E-value: 1.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 53 YGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNrMVElVPTvktSGKILYRDQNIFDKS------YP-----VEK 121
Cdd:COG4598 18 FGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCIN-LLE-TPD---SGEIRVGGEEIRLKPdrdgelVPadrrqLQR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 122 LRTNVGMVFQQPNPFP-KSIYDNITYGPrIHGIKDKKilDEIVEkslRGAAIWDE--LKDRLDQNAYGLSGGQQQRVCIA 198
Cdd:COG4598 93 IRTRLGMVFQSFNLWShMTVLENVIEAP-VHVLGRPK--AEAIE---RAEALLAKvgLADKRDAYPAHLSGGQQQRAAIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 199 RCLAIEPDVILMDEPTSALDPistlrveELV-------QDLKKD-YSIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTD 270
Cdd:COG4598 167 RALAMEPEVMLFDEPTSALDP-------ELVgevlkvmRDLAEEgRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPA 239
|
....*..
gi 1374671911 271 KIFSNPS 277
Cdd:COG4598 240 EVFGNPK 246
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
54-287 |
1.32e-45 |
|
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: 157.32 E-value: 1.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 54 GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIFDKSyPVE---KLRTNVGMVF 130
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIE-----PTAGQIFIDGENIMKQS-PVElreVRRKKIGMVF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 131 QQPNPFP-KSIYDNITYGPRIHGIKDKkildEIVEKSLRGAAIWDeLKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVIL 209
Cdd:TIGR01186 78 QQFALFPhMTILQNTSLGPELLGWPEQ----ERKEKALELLKLVG-LEEYEHRYPDELSGGMQQRVGLARALAAEPDILL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 210 MDEPTSALDPISTLRVEELVQDLKKDY--SIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNPSDKQTEDYISG 287
Cdd:TIGR01186 153 MDEAFSALDPLIRDSMQDELKKLQATLqkTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGK 232
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
47-286 |
2.12e-45 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 153.24 E-value: 2.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMvelvpTVKTSGKILYRDQNiFD-KSYPVEK---- 121
Cdd:COG4161 6 KNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLL-----ETPDSGQLNIAGHQ-FDfSQKPSEKairl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 122 LRTNVGMVFQQPNPFPK-SIYDNITYGP-RIHGIKDKKILDEIVE--KSLRgaaiwdeLKDRLDQNAYGLSGGQQQRVCI 197
Cdd:COG4161 80 LRQKVGMVFQQYNLWPHlTVMENLIEAPcKVLGLSKEQAREKAMKllARLR-------LTDKADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 198 ARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKK-DYSIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDkIFSNP 276
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS-HFTQP 231
|
250
....*....|
gi 1374671911 277 SDKQTEDYIS 286
Cdd:COG4161 232 QTEAFAHYLS 241
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
59-215 |
2.95e-45 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 150.11 E-value: 2.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIFDKSYPveKLRTNVGMVFQQPNPFP- 137
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLS-----PTEGTILLDGQDLTDDERK--SLRKEIGYVFQDPQLFPr 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1374671911 138 KSIYDNITYGPRIHGIkDKKILDEIVEKSLRGAAIWDELKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPTS 215
Cdd:pfam00005 74 LTVRENLRLGLLLKGL-SKREKDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
47-261 |
3.11e-45 |
|
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: 150.09 E-value: 3.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIFDKsyPVEKLRTNV 126
Cdd:cd00267 3 ENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK-----PTSGEILIDGKDIAKL--PLEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 127 GMVFQqpnpfpksiydnitygprihgikdkkildeivekslrgaaiwdelkdrldqnaygLSGGQQQRVCIARCLAIEPD 206
Cdd:cd00267 76 GYVPQ-------------------------------------------------------LSGGQRQRVALARALLLNPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1374671911 207 VILMDEPTSALDPISTLRVEELVQDL-KKDYSIIIVTHNMQQAARVSDKTAFFLNG 261
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
47-278 |
5.00e-45 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 155.62 E-value: 5.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTyvkaLNRMV---ELVptvkTSGKILYRDQNIFDKsyPVEKlR 123
Cdd:COG3839 7 ENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKST----LLRMIaglEDP----TSGEILIGGRDVTDL--PPKD-R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 124 tNVGMVFQQPNPFP-KSIYDNITYGPRIHGIKDKKIlDEIVEKSlrgAAIWDeLKDRLDQNAYGLSGGQQQRVCIARCLA 202
Cdd:COG3839 76 -NIAMVFQSYALYPhMTVYENIAFPLKLRKVPKAEI-DRRVREA---AELLG-LEDLLDRKPKQLSGGQRQRVALGRALV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 203 IEPDVILMDEPTSALDPisTLRVE------ELVQDLKKdySIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNP 276
Cdd:COG3839 150 REPKVFLLDEPLSNLDA--KLRVEmraeikRLHRRLGT--TTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRP 225
|
..
gi 1374671911 277 SD 278
Cdd:COG3839 226 AN 227
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
54-286 |
1.50e-44 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 154.08 E-value: 1.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 54 GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRmveL-VPTvktSGKILYRDQNIfdKSYPVEKLRT---NVGMV 129
Cdd:COG1135 16 GPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL---LeRPT---SGSVLVDGVDL--TALSERELRAarrKIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 130 FQQPNPFP-KSIYDNITYGPRIHGIKDKKIL---DEIVEksLRGaaiwdeLKDRldQNAY--GLSGGQQQRVCIARCLAI 203
Cdd:COG1135 88 FQHFNLLSsRTVAENVALPLEIAGVPKAEIRkrvAELLE--LVG------LSDK--ADAYpsQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 204 EPDVILMDEPTSALDPISTLRVEELVQDLKKDY--SIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNPSDKQT 281
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRSILDLLKDINRELglTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELT 237
|
....*
gi 1374671911 282 EDYIS 286
Cdd:COG1135 238 RRFLP 242
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
56-286 |
3.15e-44 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 150.67 E-value: 3.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 56 QHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIfDKSYP-------VEKLRTNVGM 128
Cdd:PRK11264 16 QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQ-----PEAGTIRVGDITI-DTARSlsqqkglIRQLRQHVGF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 129 VFQQPNPFP-KSIYDNITYGPRIhgikdkkildeiVEKSLRGAAIwdELKDRL--------DQNAYG--LSGGQQQRVCI 197
Cdd:PRK11264 90 VFQNFNLFPhRTVLENIIEGPVI------------VKGEPKEEAT--ARARELlakvglagKETSYPrrLSGGQQQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 198 ARCLAIEPDVILMDEPTSALDP------ISTLRveELVQDLKkdySIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDK 271
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDPelvgevLNTIR--QLAQEKR---TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKA 230
|
250
....*....|....*
gi 1374671911 272 IFSNPSDKQTEDYIS 286
Cdd:PRK11264 231 LFADPQQPRTRQFLE 245
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
54-261 |
3.89e-44 |
|
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: 147.91 E-value: 3.89e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 54 GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQNIfdKSYPVEKLRTNVGMVFQQP 133
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDP-----TSGEILIDGVDL--RDLDLESLRKNIAYVPQDP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 134 NPFPKSIYDNItygprihgikdkkildeivekslrgaaiwdelkdrldqnaygLSGGQQQRVCIARCLAIEPDVILMDEP 213
Cdd:cd03228 86 FLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPILILDEA 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1374671911 214 TSALDPISTLRVEELVQDLKKDYSIIIVTHNMQQAARVsDKTAFFLNG 261
Cdd:cd03228 124 TSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDA-DRIIVLDDG 170
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
59-243 |
4.22e-44 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 159.23 E-value: 4.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQNIfdKSYPVEKLRTNVGMVFQQPNPFPK 138
Cdd:COG2274 491 LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEP-----TSGRILIDGIDL--RQIDPASLRRQIGVVLQDVFLFSG 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 139 SIYDNITYGprihgikDKKILDEIVEKSLRGAAIWDELKD-------RLDQNAYGLSGGQQQRVCIARCLAIEPDVILMD 211
Cdd:COG2274 564 TIRENITLG-------DPDATDEEIIEAARLAGLHDFIEAlpmgydtVVGEGGSNLSGGQRQRLAIARALLRNPRILILD 636
|
170 180 190
....*....|....*....|....*....|..
gi 1374671911 212 EPTSALDPISTLRVEELVQDLKKDYSIIIVTH 243
Cdd:COG2274 637 EATSALDAETEAIILENLRRLLKGRTVIIIAH 668
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
47-286 |
1.14e-43 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 149.01 E-value: 1.14e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMvelvpTVKTSGKiLYRDQNIFD-KSYPVEK---- 121
Cdd:PRK11124 6 NGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLL-----EMPRSGT-LNIAGNHFDfSKTPSDKaire 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 122 LRTNVGMVFQQPNPFPK-SIYDNITYGP-RIHGIKDKKILDEIVE--KSLRgaaiwdeLKDRLDQNAYGLSGGQQQRVCI 197
Cdd:PRK11124 80 LRRNVGMVFQQYNLWPHlTVQQNLIEAPcRVLGLSKDQALARAEKllERLR-------LKPYADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 198 ARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKD-YSIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKiFSNP 276
Cdd:PRK11124 153 ARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETgITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQP 231
|
250
....*....|
gi 1374671911 277 SDKQTEDYIS 286
Cdd:PRK11124 232 QTEAFKNYLS 241
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
59-287 |
3.39e-43 |
|
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: 148.56 E-value: 3.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvPTvktSGKILYRDQNI--FDKSYPVEKLRTNVGMVFQQPNPF 136
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIE--PT---SGKVLIDGQDIaaMSRKELRELRRKKISMVFQSFALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 137 P-KSIYDNITYGPRIHGIkDKKILDEIVEKSLRGAAiwdeLKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPTS 215
Cdd:cd03294 115 PhRTVLENVAFGLEVQGV-PRAEREERAAEALELVG----LEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1374671911 216 ALDPisTLRVE------ELVQDLKKdySIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNPSDKQTEDYISG 287
Cdd:cd03294 190 ALDP--LIRREmqdellRLQAELQK--TIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRG 263
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
54-243 |
1.03e-42 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 153.78 E-value: 1.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 54 GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQNIfdKSYPVEKLRTNVGMVFQQP 133
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDP-----TSGRILIDGVDI--RDLTLESLRRQIGVVPQDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 134 NPFPKSIYDNITYGprihgikDKKILDEIVEKSLRGAAIWD---ELKDRLD----QNAYGLSGGQQQRVCIARCLAIEPD 206
Cdd:COG1132 424 FLFSGTIRENIRYG-------RPDATDEEVEEAAKAAQAHEfieALPDGYDtvvgERGVNLSGGQRQRIAIARALLKDPP 496
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1374671911 207 VILMDEPTSALDPIStlrvEELVQD----LKKDYSIIIVTH 243
Cdd:COG1132 497 ILILDEATSALDTET----EALIQEalerLMKGRTTIVIAH 533
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
45-263 |
7.59e-42 |
|
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: 143.73 E-value: 7.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 45 STQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALnrmVELVPTvkTSGKILYRDQNIFDKSyPVEKLRT 124
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTI---MGLLPP--RSGSIRFDGRDITGLP-PHERARA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 125 NVGMVFQQPNPFPK-SIYDNITYGPRIHGIKDKK-ILDEIVEkslrgaaIWDELKDRLDQNAYGLSGGQQQRVCIARCLA 202
Cdd:cd03224 76 GIGYVPEGRRIFPElTVEENLLLGAYARRRAKRKaRLERVYE-------LFPRLKERRKQLAGTLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1374671911 203 IEPDVILMDEPTSALDPISTLRVEELVQDLKKD-YSIIIVTHNMQQAARVSDktafflNGYV 263
Cdd:cd03224 149 SRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEgVTILLVEQNARFALEIAD------RAYV 204
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
47-274 |
8.05e-42 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 144.08 E-value: 8.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKAlnrMVELVPtvKTSGKILyrdqnIFDKsyPVEKLRTNV 126
Cdd:COG1121 10 ENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKA---ILGLLP--PTSGTVR-----LFGK--PPRRARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 127 GMVFQQPN---PFPKSIYDNITYG-------PRIHGIKDKkildEIVEKSLR--GAAiwdELKDRLdqnaYG-LSGGQQQ 193
Cdd:COG1121 78 GYVPQRAEvdwDFPITVRDVVLMGrygrrglFRRPSRADR----EAVDEALErvGLE---DLADRP----IGeLSGGQQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 194 RVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKK-DYSIIIVTHNMQQAARVSDKTAfFLNGYVNEYDDTDKI 272
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRReGKTILVVTHDLGAVREYFDRVL-LLNRGLVAHGPPEEV 225
|
..
gi 1374671911 273 FS 274
Cdd:COG1121 226 LT 227
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
54-277 |
3.07e-41 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 143.34 E-value: 3.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 54 GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMveLVPTvktSGKILYRDQNIFDKSYpVEKLRTNVGMVFQQP 133
Cdd:TIGR04520 13 SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGL--LLPT---SGKVTVDGLDTLDEEN-LWEIRKKVGMVFQNP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 134 -NPFPKSIY-DNITYGPRIHGIKDKKILdEIVEKSLRGAaiwdELKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMD 211
Cdd:TIGR04520 87 dNQFVGATVeDDVAFGLENLGVPREEMR-KRVDEALKLV----GMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1374671911 212 EPTSALDPISTLRVEELVQDLKKDY--SIIIVTHNMQQAARvSDKTAFFLNGYVnEYDDTDK-IFSNPS 277
Cdd:TIGR04520 162 EATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEAVL-ADRVIVMNKGKI-VAEGTPReIFSQVE 228
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
47-254 |
4.68e-41 |
|
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: 141.94 E-value: 4.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQ-HSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQNI-FDKSYPVEKLRT 124
Cdd:cd03256 4 ENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEP-----TSGSVLIDGTDInKLKGKALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 125 NVGMVFQQPNPFPK-SIYDNITYG--PRIHGIK---------DKKILDEIVEKSlrgaaiwdELKDRLDQNAYGLSGGQQ 192
Cdd:cd03256 79 QIGMIFQQFNLIERlSVLENVLSGrlGRRSTWRslfglfpkeEKQRALAALERV--------GLLDKAYQRADQLSGGQQ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1374671911 193 QRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDL--KKDYSIIIVTHNMQQAARVSDK 254
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREYADR 214
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
54-253 |
7.35e-41 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 141.73 E-value: 7.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 54 GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQNIF-DKSYPVEKLRTNVGMVFQQ 132
Cdd:COG3638 14 GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEP-----TSGEILVDGQDVTaLRGRALRRLRRRIGMIFQQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 133 PNPFPK-SIYDNITYG--PRIHGIKdkkildeivekSLRG--------AAIW--DE--LKDRLDQNAYGLSGGQQQRVCI 197
Cdd:COG3638 89 FNLVPRlSVLTNVLAGrlGRTSTWR-----------SLLGlfppedreRALEalERvgLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1374671911 198 ARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDYSI--IIVTHNMQQAARVSD 253
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGItvVVNLHQVDLARRYAD 215
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
45-256 |
1.44e-40 |
|
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: 139.98 E-value: 1.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 45 STQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALnrmVELVPtvKTSGKIlyrdqNIFDKsyPVEKLRT 124
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAI---LGLLK--PTSGSI-----RVFGK--PLEKERK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 125 NVGMVFQQPN---PFPKSIYDNITYGPRIHGI-------KDKKILDEIVEKSlrGAAiwdELKDR-LDQnaygLSGGQQQ 193
Cdd:cd03235 69 RIGYVPQRRSidrDFPISVRDVVLMGLYGHKGlfrrlskADKAKVDEALERV--GLS---ELADRqIGE----LSGGQQQ 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1374671911 194 RVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKD-YSIIIVTHNMQQAARVSDKTA 256
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEYFDRVL 203
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
55-254 |
2.04e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 141.72 E-value: 2.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 55 EQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIFDKSYPVEKLRTNVGMVFQQP- 133
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLK-----PTSGKIIIDGVDITDKKVKLSDIRKKVGLVFQYPe 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 134 -NPFPKSIYDNITYGPRIHGIKDKKILDEiVEKSLRGAAI-WDELKDRldqNAYGLSGGQQQRVCIARCLAIEPDVILMD 211
Cdd:PRK13637 94 yQLFEETIEKDIAFGPINLGLSEEEIENR-VKRAMNIVGLdYEDYKDK---SPFELSGGQKRRVAIAGVVAMEPKILILD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1374671911 212 EPTSALDPISTLRVEELVQDLKKDY--SIIIVTHNMQQAARVSDK 254
Cdd:PRK13637 170 EPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKLADR 214
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
47-286 |
2.23e-40 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 140.16 E-value: 2.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHsLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIFDksYPVEKlrTNV 126
Cdd:cd03299 4 ENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIK-----PDSGKILLNGKDITN--LPPEK--RDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 127 GMVFQQPNPFP-KSIYDNITYGPRIHGIKDKKILDEIVEKSlRGAAIwDELkdrLDQNAYGLSGGQQQRVCIARCLAIEP 205
Cdd:cd03299 74 SYVPQNYALFPhMTVYKNIAYGLKKRKVDKKEIERKVLEIA-EMLGI-DHL---LNRKPETLSGGEQQRVAIARALVVNP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 206 DVILMDEPTSALDPISTLRVEELVQDLKKDYS--IIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNPSDKQTED 283
Cdd:cd03299 149 KILLLDEPFSALDVRTKEKLREELKKIRKEFGvtVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAE 228
|
...
gi 1374671911 284 YIS 286
Cdd:cd03299 229 FLG 231
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
45-261 |
8.96e-40 |
|
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: 136.80 E-value: 8.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 45 STQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQNIfdKSYPVEKLRT 124
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKP-----SSGEILLDGKDL--ASLSPKELAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 125 NVGMVFQqpnpfpksiydnitygprihgikdkkILDEIvekslrGAAiwdELKDR-LDQnaygLSGGQQQRVCIARCLAI 203
Cdd:cd03214 74 KIAYVPQ--------------------------ALELL------GLA---HLADRpFNE----LSGGERQRVLLARALAQ 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 204 EPDVILMDEPTSALDPISTLRVEELVQDLKKDY--SIIIVTHNMQQAARVSDKTAFFLNG 261
Cdd:cd03214 115 EPPILLLDEPTSHLDIAHQIELLELLRRLARERgkTVVMVLHDLNLAARYADRVILLKDG 174
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
48-254 |
1.13e-39 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 138.59 E-value: 1.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 48 NLDLWYGEQH-SLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQNIFD-KSYPVEKLRTN 125
Cdd:TIGR02315 6 NLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEP-----SSGSILLEGTDITKlRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 126 VGMVFQQPNPFP-KSIYDNITYG-----PRIHGI------KDKKILDEIVEKSlrgaaiwdELKDRLDQNAYGLSGGQQQ 193
Cdd:TIGR02315 81 IGMIFQHYNLIErLTVLENVLHGrlgykPTWRSLlgrfseEDKERALSALERV--------GLADKAYQRADQLSGGQQQ 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1374671911 194 RVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDYSIIIVT--HNMQQAARVSDK 254
Cdd:TIGR02315 153 RVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIInlHQVDLAKKYADR 215
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
45-254 |
4.23e-39 |
|
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: 136.80 E-value: 4.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 45 STQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMveLVPTvktSGKILYRDQNIFDKSyPVEKLRT 124
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGF--LRPT---SGSVLFDGEDITGLP-PHEIARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 125 NVGMVFQQPNPFPK-SIYDNI------TYGPRIHGIKDKKILDEIVEKSLRGAAIWdELKDRLDQNAYGLSGGQQQRVCI 197
Cdd:cd03219 76 GIGRTFQIPRLFPElTVLENVmvaaqaRTGSGLLLARARREEREARERAEELLERV-GLADLADRPAGELSYGQQRRLEI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1374671911 198 ARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLK-KDYSIIIVTHNMQQAARVSDK 254
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLNPEETEELAELIRELReRGITVLLVEHDMDVVMSLADR 212
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
59-289 |
5.18e-39 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 140.62 E-value: 5.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvPTvktSGKILYRDQNIFdkSYPVEKL----RTNVGMVFQQ-- 132
Cdd:COG4175 43 VNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIE--PT---AGEVLIDGEDIT--KLSKKELrelrRKKMSMVFQHfa 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 133 --PNpfpKSIYDNITYGPRIHGIkDKKILDEIVEKSLR--GaaiwdeLKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVI 208
Cdd:COG4175 116 llPH---RTVLENVAFGLEIQGV-PKAERRERAREALElvG------LAGWEDSYPDELSGGMQQRVGLARALATDPDIL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 209 LMDEPTSALDPIstLRVE------ELVQDLKKdySIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNPSDkqte 282
Cdd:COG4175 186 LMDEAFSALDPL--IRREmqdellELQAKLKK--TIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPAN---- 257
|
....*..
gi 1374671911 283 DYISgRF 289
Cdd:COG4175 258 DYVA-DF 263
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
59-265 |
7.63e-39 |
|
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: 136.13 E-value: 7.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQNIfdKSYPVEKLRTNVGMVFQQPNPFPK 138
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDP-----TSGEILLDGVDI--RDLNLRWLRSQIGLVSQEPVLFDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 139 SIYDNITYGprihgikDKKILDEIVEKSLRGAAIWD---ELKDRLD----QNAYGLSGGQQQRVCIARCLAIEPDVILMD 211
Cdd:cd03249 92 TIAENIRYG-------KPDATDEEVEEAAKKANIHDfimSLPDGYDtlvgERGSQLSGGQKQRIAIARALLRNPKILLLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1374671911 212 EPTSALDPISTLRVEELVQDLKKDYSIIIVTHNMqQAARVSDKTAFFLNGYVNE 265
Cdd:cd03249 165 EATSALDAESEKLVQEALDRAMKGRTTIVIAHRL-STIRNADLIAVLQNGQVVE 217
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
45-261 |
7.68e-39 |
|
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: 134.06 E-value: 7.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 45 STQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIFDKSypvEKLRT 124
Cdd:cd03230 2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLK-----PDSGEIKVLGKDIKKEP---EEVKR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 125 NVGMVFQQPNPFPK-SIYDNITYgprihgikdkkildeivekslrgaaiwdelkdrldqnayglSGGQQQRVCIARCLAI 203
Cdd:cd03230 74 RIGYLPEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLH 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1374671911 204 EPDVILMDEPTSALDPISTLRVEELVQDLKKDY-SIIIVTHNMQQAARVSDKTAFFLNG 261
Cdd:cd03230 113 DPELLILDEPTSGLDPESRREFWELLRELKKEGkTILLSSHILEEAERLCDRVAILNNG 171
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
48-285 |
3.15e-38 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 134.50 E-value: 3.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 48 NLDLWYGEQHslKNVNLDILEKNVTAIIGPSGSGKSTYvkaLNRMVELVPTvkTSGKILYRDQNIfDKSYPVEKLrtnVG 127
Cdd:COG3840 6 DLTYRYGDFP--LRFDLTIAAGERVAILGPSGAGKSTL---LNLIAGFLPP--DSGRILWNGQDL-TALPPAERP---VS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 128 MVFQQPNPFPK-SIYDNITYG--PRIH-GIKDKKILDEIVEK-SLrgaaiwDELKDRL-DQnaygLSGGQQQRVCIARCL 201
Cdd:COG3840 75 MLFQENNLFPHlTVAQNIGLGlrPGLKlTAEQRAQVEQALERvGL------AGLLDRLpGQ----LSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 202 AIEPDVILMDEPTSALDPIstLRVE--ELVQDLKKDY--SIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNPS 277
Cdd:COG3840 145 VRKRPILLLDEPFSALDPA--LRQEmlDLVDELCRERglTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEP 222
|
....*...
gi 1374671911 278 DKQTEDYI 285
Cdd:COG3840 223 PPALAAYL 230
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
47-251 |
3.40e-38 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 134.02 E-value: 3.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHS-LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRmvELVPTvktSGKILYRDQNIFD-KSYPVEKLRT 124
Cdd:COG2884 5 ENVSKRYPGGREaLSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYG--EERPT---SGQVLVNGQDLSRlKRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 125 NVGMVFQQ----PNpfpKSIYDNITYGPRIHGIKDKKILDEiVEKSLRgaaiWDELKDRLDQNAYGLSGGQQQRVCIARC 200
Cdd:COG2884 80 RIGVVFQDfrllPD---RTVYENVALPLRVTGKSRKEIRRR-VREVLD----LVGLSDKAKALPHELSGGEQQRVAIARA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1374671911 201 LAIEPDVILMDEPTSALDPISTLRVEELVQDL-KKDYSIIIVTHNM----QQAARV 251
Cdd:COG2884 152 LVNRPELLLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLelvdRMPKRV 207
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
53-285 |
5.02e-38 |
|
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: 133.90 E-value: 5.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 53 YGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTyvkaLNRMVELVPTVkTSGKILYRDQNIfdksYPVEKLRTNVGMVFQQ 132
Cdd:cd03300 10 YGGFVALDGVSLDIKEGEFFTLLGPSGCGKTT----LLRLIAGFETP-TSGEILLDGKDI----TNLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 133 PNPFPK-SIYDNITYGPRIHGIkDKKILDEIVEKSLRGAAIWDELKDRLDQnaygLSGGQQQRVCIARCLAIEPDVILMD 211
Cdd:cd03300 81 YALFPHlTVFENIAFGLRLKKL-PKAEIKERVAEALDLVQLEGYANRKPSQ----LSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1374671911 212 EPTSALDpiSTLRvEELVQDLKK-----DYSIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNPSDKQTEDYI 285
Cdd:cd03300 156 EPLGALD--LKLR-KDMQLELKRlqkelGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFI 231
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
47-276 |
7.80e-38 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 136.43 E-value: 7.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTyvkaLNRMVE--LVPTvktSGKILYRDQNIFDKSyPVEKlRt 124
Cdd:COG1118 6 RNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTT----LLRIIAglETPD---SGRIVLNGRDLFTNL-PPRE-R- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 125 NVGMVFQQPNPFPK-SIYDNITYGPRIHGIKDKKIlDEIVEKSLR--GAaiwDELKDRL-DQnaygLSGGQQQRVCIARC 200
Cdd:COG1118 76 RVGFVFQHYALFPHmTVAENIAFGLRVRPPSKAEI-RARVEELLElvQL---EGLADRYpSQ----LSGGQRQRVALARA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 201 LAIEPDVILMDEPTSALDpiSTLRVE--ELVQDLKKDYSI--IIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNP 276
Cdd:COG1118 148 LAVEPEVLLLDEPFGALD--AKVRKElrRWLRRLHDELGGttVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRP 225
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
53-287 |
8.12e-38 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 134.33 E-value: 8.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 53 YGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALN---RMVELVPTVKTSGKILYRDQN----IFDKSyPVEKLRTN 125
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINfleKPSEGSIVVNGQTINLVRDKDgqlkVADKN-QLRLLRTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 126 VGMVFQQPNPFPK-SIYDNITYGP-RIHGIKdKKILDEIVEKSLRGAAIWDELKDRLDQNaygLSGGQQQRVCIARCLAI 203
Cdd:PRK10619 94 LTMVFQHFNLWSHmTVLENVMEAPiQVLGLS-KQEARERAVKYLAKVGIDERAQGKYPVH---LSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 204 EPDVILMDEPTSALDPISTLRVEELVQDLKKD-YSIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNPSDKQTE 282
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQ 249
|
....*
gi 1374671911 283 DYISG 287
Cdd:PRK10619 250 QFLKG 254
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
53-263 |
1.00e-36 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 130.07 E-value: 1.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 53 YGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTyvkaLNRMVELVPTVkTSGKILYRDQNIFDkSYPVEKlrtNVGMVFQQ 132
Cdd:cd03301 10 FGNVTALDDLNLDIADGEFVVLLGPSGCGKTT----TLRMIAGLEEP-TSGRIYIGGRDVTD-LPPKDR---DIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 133 PNPFP-KSIYDNITYGPRIHGIKDkkilDEIVEKSLRGAAIWDeLKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMD 211
Cdd:cd03301 81 YALYPhMTVYDNIAFGLKLRKVPK----DEIDERVREVAELLQ-IEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1374671911 212 EPTSALDpiSTLRVE---ELVQDLKK-DYSIIIVTHNMQQAARVSDKTAFFLNGYV 263
Cdd:cd03301 156 EPLSNLD--AKLRVQmraELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
55-278 |
2.33e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 131.30 E-value: 2.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 55 EQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMveLVPTvktSGKILYRDQNIFD--KSYPVEKLRTNVGMVFQQ 132
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGL--LQPT---SGTVTIGERVITAgkKNKKLKPLRKKVGIVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 133 PNP--FPKSIYDNITYGPRIHGIKDkkildeivEKSLRGAAIWDEL----KDRLDQNAYGLSGGQQQRVCIARCLAIEPD 206
Cdd:PRK13634 94 PEHqlFEETVEKDICFGPMNFGVSE--------EDAKQKAREMIELvglpEELLARSPFELSGGQMRRVAIAGVLAMEPE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1374671911 207 VILMDEPTSALDPISTLRVEELVQDL--KKDYSIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNPSD 278
Cdd:PRK13634 166 VLVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDE 239
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
59-261 |
3.45e-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: 128.57 E-value: 3.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDI---LEKNVTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQNIFDKS----YPVEKLRtnVGMVFQ 131
Cdd:cd03297 10 LPDFTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEKP-----DGGTIVLNGTVLFDSRkkinLPPQQRK--IGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 132 QPNPFPK-SIYDNITYGPRIHGIKDKKILdeiVEKSLRGAAIwDELKDRldqNAYGLSGGQQQRVCIARCLAIEPDVILM 210
Cdd:cd03297 83 QYALFPHlNVRENLAFGLKRKRNREDRIS---VDELLDLLGL-DHLLNR---YPAQLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1374671911 211 DEPTSALDPISTLRVEELVQDLKKDYSI--IIVTHNMQQAARVSDKTAFFLNG 261
Cdd:cd03297 156 DEPFSALDRALRLQLLPELKQIKKNLNIpvIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
47-251 |
7.13e-36 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 134.89 E-value: 7.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWY-GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQNIfdKSYPVEKLRTN 125
Cdd:COG4988 340 EDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP-----YSGSILINGVDL--SDLDPASWRRQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 126 VGMVFQQPNPFPKSIYDNITYGprihgikDKKILDEIVEKSLRGAAIWD---ELKDRLD----QNAYGLSGGQQQRVCIA 198
Cdd:COG4988 413 IAWVPQNPYLFAGTIRENLRLG-------RPDASDEELEAALEAAGLDEfvaALPDGLDtplgEGGRGLSGGQAQRLALA 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1374671911 199 RCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDYSIIIVTH---NMQQAARV 251
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHrlaLLAQADRI 541
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
54-261 |
1.05e-35 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 127.62 E-value: 1.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 54 GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMvelvpTVKTSGKILYRDQNIfdkSYPVEKLRTNVGMVFQQP 133
Cdd:cd03263 13 GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGE-----LRPTSGTAYINGYSI---RTDRKAARQSLGYCPQFD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 134 NPFPK-SIYDNITYGPRIHGIKDKKIlDEIVEKSLRGaaiwDELKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDE 212
Cdd:cd03263 85 ALFDElTVREHLRFYARLKGLPKSEI-KEEVELLLRV----LGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1374671911 213 PTSALDPISTLRVEELVQDLKKDYSIIIVTHNMQQAARVSDKTAFFLNG 261
Cdd:cd03263 160 PTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDG 208
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
54-286 |
3.10e-35 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 129.54 E-value: 3.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 54 GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvPTvktSGKILYRDQNIfdKSYPVEKLRT---NVGMVF 130
Cdd:PRK11153 16 RTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLER--PT---SGRVLVDGQDL--TALSEKELRKarrQIGMIF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 131 QQPNPFP-KSIYDNITYGPRIHGIKDKKI------LDEIVEKSlrgaaiwdELKDRLDQNaygLSGGQQQRVCIARCLAI 203
Cdd:PRK11153 89 QHFNLLSsRTVFDNVALPLELAGTPKAEIkarvteLLELVGLS--------DKADRYPAQ---LSGGQKQRVAIARALAS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 204 EPDVILMDEPTSALDPISTLRVEELVQDLKKDYSIIIV--THNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNPSDKQT 281
Cdd:PRK11153 158 NPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVliTHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLT 237
|
....*
gi 1374671911 282 EDYIS 286
Cdd:PRK11153 238 REFIQ 242
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
45-263 |
8.76e-34 |
|
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: 122.78 E-value: 8.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 45 STQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQNIFDKSyPVEKLRT 124
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPP-----RSGSIRFDGEDITGLP-PHRIARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 125 NVGMVFQQPNPFPK-SIYDNITYGPRIHGIKD--KKILDEIVEkslrgaaIWDELKDRLDQNAYGLSGGQQQRVCIARCL 201
Cdd:COG0410 79 GIGYVPEGRRIFPSlTVEENLLLGAYARRDRAevRADLERVYE-------LFPRLKERRRQRAGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1374671911 202 AIEPDVILMDEPTSALDPISTLRVEELVQDLKKD-YSIIIVTHNMQQAARVSDKtafflnGYV 263
Cdd:COG0410 152 MSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREgVTILLVEQNARFALEIADR------AYV 208
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
45-274 |
9.42e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 123.97 E-value: 9.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 45 STQNLDLWY--GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMveLVP---TVKTSGKILyRDQNIFDksypv 119
Cdd:PRK13635 7 RVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGL--LLPeagTITVGGMVL-SEETVWD----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 120 ekLRTNVGMVFQQP-NPFPKS-IYDNITYGPRIHGIKDkkilDEIVEKsLRGAAIWDELKDRLDQNAYGLSGGQQQRVCI 197
Cdd:PRK13635 79 --VRRQVGMVFQNPdNQFVGAtVQDDVAFGLENIGVPR----EEMVER-VDQALRQVGMEDFLNREPHRLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1374671911 198 ARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLK--KDYSIIIVTHNMQQAARvSDKTAFFLNGYVNEYDDTDKIFS 274
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKeqKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
47-276 |
2.41e-33 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 127.49 E-value: 2.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYG----EQHSLKNVNLDILEKNVTAIIGPSGSGKStyVKALNRMvELVP--TVKTSGKILYRDQNIFDKSYPV- 119
Cdd:COG4172 10 EDLSVAFGqgggTVEAVKGVSFDIAAGETLALVGESGSGKS--VTALSIL-RLLPdpAAHPSGSILFDGQDLLGLSEREl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 120 EKLRTN-VGMVFQQP----NPFpKSIYDNITYGPRIH-GIKDKKILDEIVEkSLRGAAIwDELKDRLDQNAYGLSGGQQQ 193
Cdd:COG4172 87 RRIRGNrIAMIFQEPmtslNPL-HTIGKQIAEVLRLHrGLSGAAARARALE-LLERVGI-PDPERRLDAYPHQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 194 RVCIARCLAIEPDVILMDEPTSALDPisTLRVE--ELVQDLKKDY--SIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDT 269
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDV--TVQAQilDLLKDLQRELgmALLLITHDLGVVRRFADRVAVMRQGEIVEQGPT 241
|
....*..
gi 1374671911 270 DKIFSNP 276
Cdd:COG4172 242 AELFAAP 248
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
55-253 |
2.66e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 122.93 E-value: 2.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 55 EQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMveLVPTvktSGKILYRDQNIF--DKSYPVEKLRTNVGMVFQQ 132
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGL--HVPT---QGSVRVDDTLITstSKNKDIKQIRKKVGLVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 133 PNP--FPKSIYDNITYGPRIHGIKDKKIlDEIVEKSLRGAAIWDELKDRldqNAYGLSGGQQQRVCIARCLAIEPDVILM 210
Cdd:PRK13649 94 PESqlFEETVLKDVAFGPQNFGVSQEEA-EALAREKLALVGISESLFEK---NPFELSGGQMRRVAIAGILAMEPKILVL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1374671911 211 DEPTSALDPISTLRVEELVQDLKKD-YSIIIVTHNMQQAARVSD 253
Cdd:PRK13649 170 DEPTAGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVANYAD 213
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
45-254 |
3.28e-33 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 122.07 E-value: 3.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 45 STQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMveLVPTvktSGKILYRDQNIFDKSyPVEklRT 124
Cdd:COG0411 6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGF--YRPT---SGRILFDGRDITGLP-PHR--IA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 125 NVGMV--FQQPNPFPK-SIYDNITYGPRIHG-----------IKDKKILDEIVEKSLRGAAIWDeLKDRLDQNAYGLSGG 190
Cdd:COG0411 78 RLGIArtFQNPRLFPElTVLENVLVAAHARLgrgllaallrlPRARREEREARERAEELLERVG-LADRADEPAGNLSYG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1374671911 191 QQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKD--YSIIIVTHNMQQAARVSDK 254
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErgITILLIEHDMDLVMGLADR 222
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
55-276 |
6.17e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 122.25 E-value: 6.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 55 EQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMveLVPTvktSGKILYRDQNIFDK--SYPVEKLRTNVGMVFQQ 132
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNAL--LKPS---SGTITIAGYHITPEtgNKNLKKLRKKVSLVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 133 PNP--FPKSIYDNITYGPRIHGIKDKKILDEIVeKSLRGAAIWDELkdrLDQNAYGLSGGQQQRVCIARCLAIEPDVILM 210
Cdd:PRK13641 94 PEAqlFENTVLKDVEFGPKNFGFSEDEAKEKAL-KWLKKVGLSEDL---ISKSPFELSGGQMRRVAIAGVMAYEPEILCL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1374671911 211 DEPTSALDPISTLRVEELVQDLKKD-YSIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNP 276
Cdd:PRK13641 170 DEPAAGLDPEGRKEMMQLFKDYQKAgHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
59-275 |
1.74e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 121.35 E-value: 1.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMveLVPTvktSGKI--LYRDQNIFDKSYPVEK--------------- 121
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNAL--LLPD---TGTIewIFKDEKNKKKTKEKEKvleklviqktrfkki 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 122 -----LRTNVGMVFQ--QPNPFPKSIYDNITYGPRIHGIKDKkildEIVEKSLRGAAIWDELKDRLDQNAYGLSGGQQQR 194
Cdd:PRK13651 98 kkikeIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKE----EAKKRAAKYIELVGLDESYLQRSPFELSGGQKRR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 195 VCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDL-KKDYSIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIF 273
Cdd:PRK13651 174 VALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDIL 253
|
..
gi 1374671911 274 SN 275
Cdd:PRK13651 254 SD 255
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
55-245 |
2.29e-32 |
|
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: 118.85 E-value: 2.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 55 EQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMveLVPTvktSGKILYRDQNIfdKSYPVEKLRTNVGMVFQQPN 134
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGL--YKPT---SGSVLLDGTDI--RQLDPADLRRNIGYVPQDVT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 135 PFPKSIYDNITYGPRIHgiKDKKIL--------DEIVEKSLRGaaiwdeLKDRLDQNAYGLSGGQQQRVCIARCLAIEPD 206
Cdd:cd03245 89 LFYGTLRDNITLGAPLA--DDERILraaelagvTDFVNKHPNG------LDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1374671911 207 VILMDEPTSALDPISTLRVEELVQDLKKDYSIIIVTHNM 245
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRP 199
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
57-245 |
2.45e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 120.72 E-value: 2.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 57 HSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIFDKSYPVEKLRTNVGMVFQQPNP- 135
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILK-----PSSGRILFDGKPIDYSRKGLMKLRESVGMVFQDPDNq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 136 -FPKSIYDNITYGPRIHGIKDKKIlDEIVEKSLRGAAIwDELKDRldqNAYGLSGGQQQRVCIARCLAIEPDVILMDEPT 214
Cdd:PRK13636 95 lFSASVYQDVSFGAVNLKLPEDEV-RKRVDNALKRTGI-EHLKDK---PTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPT 169
|
170 180 190
....*....|....*....|....*....|...
gi 1374671911 215 SALDPISTLRVEELVQDLKK--DYSIIIVTHNM 245
Cdd:PRK13636 170 AGLDPMGVSEIMKLLVEMQKelGLTIIIATHDI 202
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
48-243 |
7.40e-32 |
|
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: 117.71 E-value: 7.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 48 NLDLWYGEQHS-LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIfdKSYPVEKLRTNV 126
Cdd:cd03254 7 NVNFSYDEKKPvLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYD-----PQKGQILIDGIDI--RDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 127 GMVFQQPNPFPKSIYDNITYGprihgikDKKILDEIVEKSLRGAAIWDELKDR-------LDQNAYGLSGGQQQRVCIAR 199
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLG-------RPNATDEEVIEAAKEAGAHDFIMKLpngydtvLGENGGNLSQGERQLLAIAR 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1374671911 200 CLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDYSIIIVTH 243
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAH 196
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
46-276 |
8.66e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 119.14 E-value: 8.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 46 TQNLDLWY-GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMveLVPTvktSGKILYRDQNIFDKSypVEKLRT 124
Cdd:PRK13652 6 TRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGI--LKPT---SGSVLIRGEPITKEN--IREVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 125 NVGMVFQQPNP--FPKSIYDNITYGPRIHGIkDKKILDEIVEKSLRGAAIwDELKDRLDQNaygLSGGQQQRVCIARCLA 202
Cdd:PRK13652 79 FVGLVFQNPDDqiFSPTVEQDIAFGPINLGL-DEETVAHRVSSALHMLGL-EELRDRVPHH---LSGGEKKRVAIAGVIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1374671911 203 IEPDVILMDEPTSALDPISTLRVEELVQDLKKDYSIIIV--THNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNP 276
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIfsTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
47-277 |
1.03e-31 |
|
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: 117.83 E-value: 1.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTyvkaLNRMVELVPTvKTSGKILYRDQNIFDKsyPVEKlrTNV 126
Cdd:cd03296 6 RNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTT----LLRLIAGLER-PDSGTILFGGEDATDV--PVQE--RNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 127 GMVFQQPNPFPK-SIYDNITYGPRIHGIKDKKILDEIVEK--SLRGAAIWDELKDRLDQNaygLSGGQQQRVCIARCLAI 203
Cdd:cd03296 77 GFVFQHYALFRHmTVFDNVAFGLRVKPRSERPPEAEIRAKvhELLKLVQLDWLADRYPAQ---LSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1374671911 204 EPDVILMDEPTSALDpiSTLRvEEL---VQDLKKDYSI--IIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNPS 277
Cdd:cd03296 154 EPKVLLLDEPFGALD--AKVR-KELrrwLRRLHDELHVttVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPA 229
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
59-251 |
1.41e-31 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 122.95 E-value: 1.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQNIfdKSYPVEKLRTNVGMVFQQPNPFPK 138
Cdd:COG4987 351 LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDP-----QSGSITLGGVDL--RDLDEDDLRRRIAVVPQRPHLFDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 139 SIYDNITYGprihgikDKKILDEIVEKSLRGAAIWD---ELKDRLD----QNAYGLSGGQQQRVCIARCLAIEPDVILMD 211
Cdd:COG4987 424 TLRENLRLA-------RPDATDEELWAALERVGLGDwlaALPDGLDtwlgEGGRRLSGGERRRLALARALLRDAPILLLD 496
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1374671911 212 EPTSALDPISTLRVEELVQDLKKDYSIIIVTHNMQQAARV 251
Cdd:COG4987 497 EPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERM 536
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
37-276 |
3.00e-31 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 121.72 E-value: 3.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 37 DRERRVVYSTQNLDLWY-----------GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvkTSGKI 105
Cdd:COG4172 269 PPDAPPLLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP------SEGEI 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 106 LYRDQNIFDKSypvEK----LRTNVGMVFQqpNPF----PK-SIYDNITYGPRIHGIK-DKKILDEIVEKSLRGAAIWDE 175
Cdd:COG4172 343 RFDGQDLDGLS---RRalrpLRRRMQVVFQ--DPFgslsPRmTVGQIIAEGLRVHGPGlSAAERRARVAEALEEVGLDPA 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 176 LKDRldqnaY--GLSGGQQQRVCIARCLAIEPDVILMDEPTSALDpiSTLRVE--ELVQDLKKDY--SIIIVTHNMQQAA 249
Cdd:COG4172 418 ARHR-----YphEFSGGQRQRIAIARALILEPKLLVLDEPTSALD--VSVQAQilDLLRDLQREHglAYLFISHDLAVVR 490
|
250 260
....*....|....*....|....*..
gi 1374671911 250 RVSDKTAFFLNGYVNEYDDTDKIFSNP 276
Cdd:COG4172 491 ALAHRVMVMKDGKVVEQGPTEQVFDAP 517
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
59-261 |
3.33e-31 |
|
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: 115.43 E-value: 3.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIFDKsypveKLRTNVGMVFQQPNP--F 136
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIK-----ESSGSILLNGKPIKAK-----ERRKSIGYVMQDVDYqlF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 137 PKSIYDNITYGprihgIKDKKILDEIVEKSLRGAAIWDeLKDRLDQNaygLSGGQQQRVCIARCLAIEPDVILMDEPTSA 216
Cdd:cd03226 86 TDSVREELLLG-----LKELDAGNEQAETVLKDLDLYA-LKERHPLS---LSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1374671911 217 LDPISTLRVEELVQDLKK-DYSIIIVTHNMQQAARVSDKTAFFLNG 261
Cdd:cd03226 157 LDYKNMERVGELIRELAAqGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
53-263 |
4.14e-31 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 118.98 E-value: 4.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 53 YGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTyvkaLNRMVELVPTVkTSGKILYRDQNIFDksypVEKLRTNVGMVFQQ 132
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKST----LLRMIAGLEDI-TSGDLFIGEKRMND----VPPAERGVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 133 PNPFPK-SIYDNITYGPRIHGIKDKKIldeivEKSLRGAAIWDELKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMD 211
Cdd:PRK11000 84 YALYPHlSVAENMSFGLKLAGAKKEEI-----NQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1374671911 212 EPTSALDpiSTLRVE------ELVQDLKKdySIIIVTHNMQQAARVSDKTAFFLNGYV 263
Cdd:PRK11000 159 EPLSNLD--AALRVQmrieisRLHKRLGR--TMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
57-276 |
5.13e-31 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 117.91 E-value: 5.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 57 HSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIFDKS-YPVEKLRTNVGMVFQQP-- 133
Cdd:COG4608 32 KAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEE-----PTSGEILFDGQDITGLSgRELRPLRRRMQMVFQDPya 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 134 --NPfPKSIYDNITYGPRIHGIKDKKILDEIVEKSLRgaaiwdelKDRLDQNAYG-----LSGGQQQRVCIARCLAIEPD 206
Cdd:COG4608 107 slNP-RMTVGDIIAEPLRIHGLASKAERRERVAELLE--------LVGLRPEHADrypheFSGGQRQRIGIARALALNPK 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1374671911 207 VILMDEPTSALDpIStlrVE----ELVQDLKKDYSI--IIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNP 276
Cdd:COG4608 178 LIVCDEPVSALD-VS---IQaqvlNLLEDLQDELGLtyLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARP 249
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
48-261 |
8.79e-31 |
|
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: 114.60 E-value: 8.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 48 NLDLWYGEQHSLKNVNLdILEKNVTAIIGPSGSGKSTYVKALnrmVELVPTvkTSGKILYRDQNIFDKsypVEKLRTNVG 127
Cdd:cd03264 5 NLTKRYGKKRALDGVSL-TLGPGMYGLLGPNGAGKTTLMRIL---ATLTPP--SSGTIRIDGQDVLKQ---PQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 128 MVFQQPNPFPK-SIYDNITYGPRIHGIKDKKIlDEIVEKSLRGAAIWDELKDRLDQnaygLSGGQQQRVCIARCLAIEPD 206
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDYIAWLKGIPSKEV-KARVDEVLELVNLGDRAKKKIGS----LSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1374671911 207 VILMDEPTSALDPISTLRVEELVQDLKKDYSIIIVTHNMQQAARVSDKTAFFLNG 261
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKG 205
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
37-275 |
1.10e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 115.86 E-value: 1.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 37 DRERRVVYSTQNLDLWYGEQHS--LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILyrdqnIFD 114
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNSENnaLKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLK-----PQSGEIK-----IDG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 115 KSYP---VEKLRTNVGMVFQQP-NPF-PKSIYDNITYG---PRIHGIKDKKILDEIVEKSlrgaaiwdELKDRLDQNAYG 186
Cdd:PRK13632 71 ITISkenLKEIRKKIGIIFQNPdNQFiGATVEDDIAFGlenKKVPPKKMKDIIDDLAKKV--------GMEDYLDKEPQN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 187 LSGGQQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKK--DYSIIIVTHNMQQAARvSDKTAFFLNGYVN 264
Cdd:PRK13632 143 LSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrKKTLISITHDMDEAIL-ADKVIVFSEGKLI 221
|
250
....*....|.
gi 1374671911 265 EYDDTDKIFSN 275
Cdd:PRK13632 222 AQGKPKEILNN 232
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
47-248 |
4.18e-30 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 114.19 E-value: 4.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYG----EQHSLKNVNLDILEKNVTAIIGPSGSGKSTYvkaLNRMVELVPTvkTSGKILyRDQNifdksyPVEKL 122
Cdd:COG4525 7 RHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTL---LNLIAGFLAP--SSGEIT-LDGV------PVTGP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 123 RTNVGMVFQQPNPFP-KSIYDNITYGPRIHGIkDKKILDEIVEKSLR--GaaiwdeLKDRLDQNAYGLSGGQQQRVCIAR 199
Cdd:COG4525 75 GADRGVVFQKDALLPwLNVLDNVAFGLRLRGV-PKAERRARAEELLAlvG------LADFARRRIWQLSGGMRQRVGIAR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1374671911 200 CLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDY--SIIIVTHNMQQA 248
Cdd:COG4525 148 ALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTgkGVFLITHSVEEA 198
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
55-249 |
5.16e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 114.41 E-value: 5.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 55 EQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMveLVPTvktSGKILYRDQNIFDKSYpVEKLRTNVGMVFQQP- 133
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNAL--LIPS---EGKVYVDGLDTSDEEN-LWDIRNKAGMVFQNPd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 134 NPFPKSIYD-NITYGPRIHGIKDKKIlDEIVEKSLRGAAIWdELKDrldQNAYGLSGGQQQRVCIARCLAIEPDVILMDE 212
Cdd:PRK13633 96 NQIVATIVEeDVAFGPENLGIPPEEI-RERVDESLKKVGMY-EYRR---HAPHLLSGGQKQRVAIAGILAMRPECIIFDE 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 1374671911 213 PTSALDPISTLRVEELVQDLKKDY--SIIIVTHNMQQAA 249
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAV 209
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
46-261 |
7.95e-30 |
|
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: 112.08 E-value: 7.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 46 TQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMveLVPTvktSGKILYrdqNIFDKSYPVEKLRTN 125
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTL--LKPT---SGRATV---AGHDVVREPREVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 126 VGMVFQQPNPFPK-SIYDNITYGPRIHGIKDKKiLDEIVEKSLRGAAIWdELKDRLDQNaygLSGGQQQRVCIARCLAIE 204
Cdd:cd03265 75 IGIVFQDLSVDDElTGWENLYIHARLYGVPGAE-RRERIDELLDFVGLL-EAADRLVKT---YSGGMRRRLEIARSLVHR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1374671911 205 PDVILMDEPTSALDPISTLRVEELVQDLKKDY--SIIIVTHNMQQAARVSDKTAFFLNG 261
Cdd:cd03265 150 PEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAEQLCDRVAIIDHG 208
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
54-248 |
8.68e-30 |
|
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: 111.36 E-value: 8.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 54 GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMveLVPTvktSGKILYRDQNI-FDKSyPVEKLRTNVGMVFQQ 132
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGL--LRPQ---SGAVLIDGEPLdYSRK-GLLERRQRVGLVFQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 133 PNP--FPKSIYDNITYGPRIHGIKDKKIlDEIVEKSLRGAAIwDELKDRLDQNaygLSGGQQQRVCIARCLAIEPDVILM 210
Cdd:TIGR01166 77 PDDqlFAADVDQDVAFGPLNLGLSEAEV-ERRVREALTAVGA-SGLRERPTHC---LSGGEKKRVAIAGAVAMRPDVLLL 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 1374671911 211 DEPTSALDPISTLRVEELVQDLKKD-YSIIIVTHNMQQA 248
Cdd:TIGR01166 152 DEPTAGLDPAGREQMLAILRRLRAEgMTVVISTHDVDLA 190
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
59-265 |
1.03e-29 |
|
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: 112.32 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQNIfdKSYPVEKLRTNVGMVFQQPNPFPK 138
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDV-----SSGSILIDGQDI--REVTLDSLRRAIGVVPQDTVLFND 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 139 SIYDNITYGprihgikDKKILDEIVEKSLRGAAIWDELKdRLDQnAYG---------LSGGQQQRVCIARCLAIEPDVIL 209
Cdd:cd03253 90 TIGYNIRYG-------RPDATDEEVIEAAKAAQIHDKIM-RFPD-GYDtivgerglkLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1374671911 210 MDEPTSALDPISTLRVEELVQDLKKDYSIIIVTHNMQQAARvSDKTAFFLNGYVNE 265
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVE 215
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
47-243 |
1.16e-29 |
|
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: 112.32 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHS--LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQNIFDksYPVEKLRT 124
Cdd:cd03251 4 KNVTFRYPGDGPpvLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDV-----DSGRILIDGHDVRD--YTLASLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 125 NVGMVFQQPNPFPKSIYDNITYGPRihgikdkKILDEIVEKSLRGAAIWD---ELKDRLD----QNAYGLSGGQQQRVCI 197
Cdd:cd03251 77 QIGLVSQDVFLFNDTVAENIAYGRP-------GATREEVEEAARAANAHEfimELPEGYDtvigERGVKLSGGQRQRIAI 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1374671911 198 ARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDYSIIIVTH 243
Cdd:cd03251 150 ARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAH 195
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
61-276 |
1.73e-29 |
|
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: 114.43 E-value: 1.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 61 NVNLDILEKNVTAIIGPSGSGKSTYVKA---LNRmvelvptvKTSGKILYRDQNIFDKSY----PVEKLRtnVGMVFQQP 133
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLER--------PDSGRIRLGGEVLQDSARgiflPPHRRR--IGYVFQEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 134 NPFP-KSIYDNITYG-PRIHGIKDKKILDEIVEkslrgaaiWDELKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMD 211
Cdd:COG4148 87 RLFPhLSVRGNLLYGrKRAPRAERRISFDEVVE--------LLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1374671911 212 EPTSALDPISTLRVEELVQDLKKDYSI--IIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNP 276
Cdd:COG4148 159 EPLAALDLARKAEILPYLERLRDELDIpiLYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
58-249 |
1.93e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 112.54 E-value: 1.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 58 SLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQNIFDKSYpvEKLRTNVGMVFQQP-NPF 136
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKV-----KSGEIFYNNQAITDDNF--EKLRKHIGIVFQNPdNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 137 PKSI--YDnITYGPRIHGIKDKKiLDEIVEKSLRGAaiwdELKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPT 214
Cdd:PRK13648 97 VGSIvkYD-VAFGLENHAVPYDE-MHRRVSEALKQV----DMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEAT 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 1374671911 215 SALDPISTLRVEELVQDLK--KDYSIIIVTHNMQQAA 249
Cdd:PRK13648 171 SMLDPDARQNLLDLVRKVKseHNITIISITHDLSEAM 207
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
48-243 |
2.51e-29 |
|
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: 116.23 E-value: 2.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 48 NLDLWY-GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIFDksYPVEKLRTNV 126
Cdd:TIGR02857 326 GVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVD-----PTEGSIAVNGVPLAD--ADADSWRDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 127 GMVFQQPNPFPKSIYDNITygpriHGIKDKKilDEIVEKSLRGAAIWDELKDR-------LDQNAYGLSGGQQQRVCIAR 199
Cdd:TIGR02857 399 AWVPQHPFLFAGTIAENIR-----LARPDAS--DAEIREALERAGLDEFVAALpqgldtpIGEGGAGLSGGQAQRLALAR 471
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1374671911 200 CLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDYSIIIVTH 243
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTH 515
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
45-285 |
3.18e-29 |
|
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: 113.59 E-value: 3.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 45 STQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMvelvpTVKTSGKILYRDQNIFDksYPVEKlrT 124
Cdd:TIGR03265 6 SIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGL-----ERQTAGTIYQGGRDITR--LPPQK--R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 125 NVGMVFQQPNPFPK-SIYDNITYGprIHGIKDKKilDEIVEKslrgAAIWDELKDRLDQ-NAY--GLSGGQQQRVCIARC 200
Cdd:TIGR03265 77 DYGIVFQSYALFPNlTVADNIAYG--LKNRGMGR--AEVAER----VAELLDLVGLPGSeRKYpgQLSGGQQQRVALARA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 201 LAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDYSI--IIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNPSD 278
Cdd:TIGR03265 149 LATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVttIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPAT 228
|
....*..
gi 1374671911 279 KQTEDYI 285
Cdd:TIGR03265 229 PFVADFV 235
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
58-244 |
3.60e-29 |
|
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: 110.19 E-value: 3.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 58 SLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIFD-KSYPVEKLRTNVGMVFQQPNPF 136
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEEL-----PTSGTIRVNGQDVSDlRGRAIPYLRRKIGVVFQDFRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 137 PK-SIYDNITYGPRIHGIKDKKIlDEIVEKSLRGAAiwdeLKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPTS 215
Cdd:cd03292 91 PDrNVYENVAFALEVTGVPPREI-RKRVPAALELVG----LSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTG 165
|
170 180 190
....*....|....*....|....*....|
gi 1374671911 216 ALDPISTLRVEELVQDL-KKDYSIIIVTHN 244
Cdd:cd03292 166 NLDPDTTWEIMNLLKKInKAGTTVVVATHA 195
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
45-254 |
5.00e-29 |
|
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: 108.28 E-value: 5.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 45 STQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIFDKSyPVEKLRT 124
Cdd:cd03216 2 ELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYK-----PDSGEILVDGKEVSFAS-PRDARRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 125 NVGMVFQqpnpfpksiydnitygprihgikdkkildeivekslrgaaiwdelkdrldqnaygLSGGQQQRVCIARCLAIE 204
Cdd:cd03216 76 GIAMVYQ-------------------------------------------------------LSVGERQMVEIARALARN 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1374671911 205 PDVILMDEPTSALDPISTLRVEELVQDLKKD-YSIIIVTHNMQQAARVSDK 254
Cdd:cd03216 101 ARLLILDEPTAALTPAEVERLFKVIRRLRAQgVAVIFISHRLDEVFEIADR 151
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
47-267 |
5.15e-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: 109.89 E-value: 5.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWY--GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQNIfdKSYPVEKLRT 124
Cdd:cd03244 6 KNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVEL-----SSGSILIDGVDI--SKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 125 NVGMVFQQPNPFPKSIYDNITygprIHGIKDKKILDEIVEKSlRGAAIWDELKDRLD----QNAYGLSGGQQQRVCIARC 200
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLD----PFGEYSDEELWQALERV-GLKEFVESLPGGLDtvveEGGENLSVGQRQLLCLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1374671911 201 LAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDYSIIIVTHnmqqaaRV-----SDKTAFFLNGYVNEYD 267
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAH------RLdtiidSDRILVLDKGRVVEFD 219
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
55-275 |
5.18e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 112.02 E-value: 5.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 55 EQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVelvptVKTSGKILYRDQNI---FDKSYPVEKLRTNVGMVFQ 131
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLI-----ISETGQTIVGDYAIpanLKKIKEVKRLRKEIGLVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 132 QP--NPFPKSIYDNITYGPrIHGIKDKKILDEIVEKSLRGAAIWDELKDRldqNAYGLSGGQQQRVCIARCLAIEPDVIL 209
Cdd:PRK13645 98 FPeyQLFQETIEKDIAFGP-VNLGENKQEAYKKVPELLKLVQLPEDYVKR---SPFELSGGQKRRVALAGIIAMDGNTLV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1374671911 210 MDEPTSALDPISTLRVEELVQDLKKDYS--IIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSN 275
Cdd:PRK13645 174 LDEPTGGLDPKGEEDFINLFERLNKEYKkrIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
57-263 |
8.25e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 110.98 E-value: 8.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 57 HSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMvelvpTVKTSGKILYRDQNIFDKSypVEKLRTNVGMVFQQPNP- 135
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGI-----YLPQRGRVKVMGREVNAEN--EKWVRSKVGLVFQDPDDq 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 136 -FPKSIYDNITYGPRIHGIkDKKILDEIVEKSLRGAAIWDeLKDRldqNAYGLSGGQQQRVCIARCLAIEPDVILMDEPT 214
Cdd:PRK13647 92 vFSSTVWDDVAFGPVNMGL-DKDEVERRVEEALKAVRMWD-FRDK---PPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1374671911 215 SALDPISTLRVEELVQDLKKD-YSIIIVTHNMQQAARVSDKTAFFLNGYV 263
Cdd:PRK13647 167 AYLDPRGQETLMEILDRLHNQgKTVIVATHDVDLAAEWADQVIVLKEGRV 216
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
59-287 |
8.99e-29 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 113.59 E-value: 8.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNI--FDKSYPVEKLRTNVGMVFQQPNPF 136
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIE-----PTRGQVLIDGVDIakISDAELREVRRKKIAMVFQSFALM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 137 PK-SIYDNITYGPRIHGIKdkkiLDEIVEKSLrgaaiwDELKD-RLDQNAYG----LSGGQQQRVCIARCLAIEPDVILM 210
Cdd:PRK10070 119 PHmTVLDNTAFGMELAGIN----AEERREKAL------DALRQvGLENYAHSypdeLSGGMRQRVGLARALAINPDILLM 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1374671911 211 DEPTSALDP-ISTLRVEELVQ-DLKKDYSIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNPSDKQTEDYISG 287
Cdd:PRK10070 189 DEAFSALDPlIRTEMQDELVKlQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRG 267
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
45-261 |
1.02e-28 |
|
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: 108.84 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 45 STQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKAlnrMVELVPtvKTSGKILYRDQNIFDKSYPVEKlrt 124
Cdd:cd03268 2 KTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKI---ILGLIK--PDSGEITFDGKSYQKNIEALRR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 125 nVGMVFQQPNPFPK-SIYDNITYGPRIHGIKDKKIlDEIVEKSlrgaaiwdELKDRLDQNAYGLSGGQQQRVCIARCLAI 203
Cdd:cd03268 74 -IGALIEAPGFYPNlTARENLRLLARLLGIRKKRI-DEVLDVV--------GLKDSAKKKVKGFSLGMKQRLGIALALLG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1374671911 204 EPDVILMDEPTSALDPISTLRVEELVQDLKKD-YSIIIVTHNMQQAARVSDKTAFFLNG 261
Cdd:cd03268 144 NPDLLILDEPTNGLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKVADRIGIINKG 202
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
59-250 |
1.50e-28 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 109.10 E-value: 1.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQNIFDksYPVEKLRTNVGMVFQQPNPFPK 138
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQP-----QGGQVLLDGKPISQ--YEHKYLHSKVSLVGQEPVLFAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 139 SIYDNITYGprihgIKDKKiLDEIVEKSLRGAA----------IWDELKDRLDQnaygLSGGQQQRVCIARCLAIEPDVI 208
Cdd:cd03248 103 SLQDNIAYG-----LQSCS-FECVKEAAQKAHAhsfiselasgYDTEVGEKGSQ----LSGGQKQRVAIARALIRNPQVL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1374671911 209 LMDEPTSALDPISTLRVEELVQDLKKDYSIIIVTHNMQQAAR 250
Cdd:cd03248 173 ILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVER 214
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
57-255 |
1.99e-28 |
|
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: 108.49 E-value: 1.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 57 HSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMveLVPTvktSGKILYRDQNIFD-KSYPVEKLRTNVGMVFQQPNP 135
Cdd:TIGR02673 16 AALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGA--LTPS---RGQVRIAGEDVNRlRGRQLPLLRRRIGVVFQDFRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 136 FP-KSIYDNITYGPRIHGIKDKKIlDEIVEKSLRgaaiWDELKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPT 214
Cdd:TIGR02673 91 LPdRTVYENVALPLEVRGKKEREI-QRRVGAALR----QVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPT 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1374671911 215 SALDPISTLRVEELVQDL-KKDYSIIIVTHNMQQAARVSDKT 255
Cdd:TIGR02673 166 GNLDPDLSERILDLLKRLnKRGTTVIVATHDLSLVDRVAHRV 207
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
45-281 |
2.38e-28 |
|
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: 108.78 E-value: 2.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 45 STQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTyvkALNRMVELVPTvkTSGKILYRDQNIfdKSYPVEKlRT 124
Cdd:cd03218 2 RAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTT---TFYMIVGLVKP--DSGKILLDGQDI--TKLPMHK-RA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 125 NVGMVF--QQPNPFPK-SIYDNITYGPRIHGiKDKKILDEIVEKSLrgaaiwDELK-DRL-DQNAYGLSGGQQQRVCIAR 199
Cdd:cd03218 74 RLGIGYlpQEASIFRKlTVEENILAVLEIRG-LSKKEREEKLEELL------EEFHiTHLrKSKASSLSGGERRRVEIAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 200 CLAIEPDVILMDEPTSALDPISTLRVEELVQDLK-KDYSIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNPSD 278
Cdd:cd03218 147 ALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKdRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELV 226
|
...
gi 1374671911 279 KQT 281
Cdd:cd03218 227 RKV 229
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
42-276 |
2.71e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 110.71 E-value: 2.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 42 VVYSTQNLDLWYGEQHS-----LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVE------LVPTVKTSGKILYRDQ 110
Cdd:PRK13631 20 IILRVKNLYCVFDEKQEnelvaLNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKskygtiQVGDIYIGDKKNNHEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 111 NIFDKSYPVE---KLRTNVGMVFQQP--NPFPKSIYDNITYGPRIHGIKdKKILDEIVEKSLRGAAIWDelkDRLDQNAY 185
Cdd:PRK13631 100 ITNPYSKKIKnfkELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVK-KSEAKKLAKFYLNKMGLDD---SYLERSPF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 186 GLSGGQQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKD-YSIIIVTHNMQQAARVSDKTAFFLNGYVN 264
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANnKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
250
....*....|..
gi 1374671911 265 EYDDTDKIFSNP 276
Cdd:PRK13631 256 KTGTPYEIFTDQ 267
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
47-280 |
3.83e-28 |
|
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: 108.13 E-value: 3.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTyvkALNRMVELVPtvKTSGKILYRDQNIFDKsyPV-EKLRTN 125
Cdd:TIGR04406 5 ENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTT---SFYMIVGLVR--PDAGKILIDGQDITHL--PMhERARLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 126 VGMVFQQPNPFPK-SIYDNItygprihgikdKKILdEIVEKsLRGAAIWDELKDRL---------DQNAYGLSGGQQQRV 195
Cdd:TIGR04406 78 IGYLPQEASIFRKlTVEENI-----------MAVL-EIRKD-LDRAEREERLEALLeefqishlrDNKAMSLSGGERRRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 196 CIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLK-KDYSIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFS 274
Cdd:TIGR04406 145 EIARALATNPKFILLDEPFAGVDPIAVGDIKKIIKHLKeRGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVA 224
|
....*.
gi 1374671911 275 NPSDKQ 280
Cdd:TIGR04406 225 NEKVRR 230
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
47-253 |
4.26e-28 |
|
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: 108.00 E-value: 4.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALnrmVELVPTvkTSGKILYRDQNIfDKSYPVEKLRTNV 126
Cdd:TIGR03410 4 SNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTL---MGLLPV--KSGSIRLDGEDI-TKLPPHERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 127 GMVFQQPNPFPK-SIYDNITYGPRIHGIKDKKILDEIVEkslrgaaIWDELKDRLDQNAYGLSGGQQQRVCIARCLAIEP 205
Cdd:TIGR03410 78 AYVPQGREIFPRlTVEENLLTGLAALPRRSRKIPDEIYE-------LFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRP 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1374671911 206 DVILMDEPTSALDPISTLRVEELVQDLKK--DYSIIIVTHNMQQAARVSD 253
Cdd:TIGR03410 151 KLLLLDEPTEGIQPSIIKDIGRVIRRLRAegGMAILLVEQYLDFARELAD 200
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
74-277 |
8.39e-28 |
|
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: 109.51 E-value: 8.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 74 IIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQNIFDksypVEKLRTNVGMVFQQPNPFPK-SIYDNITYGPRIHG 152
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQP-----DSGSIMLDGEDVTN----VPPHLRHINMVFQSYALFPHmTVEENVAFGLKMRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 153 IkDKKILDEIVEKSLRGAaiwdELKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDL 232
Cdd:TIGR01187 72 V-PRAEIKPRVLEALRLV----QLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTI 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1374671911 233 KKDYSI--IIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNPS 277
Cdd:TIGR01187 147 QEQLGItfVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPA 193
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
55-284 |
9.04e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 108.33 E-value: 9.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 55 EQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIFDKSYP--VEKLRTNVGMVFQQ 132
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLK-----PTTGTVTVDDITITHKTKDkyIRPVRKRIGMVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 133 PNP--FPKSIYDNITYGPRIHGIKdkkiLDEIVEKSLRGAAIWDELKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILM 210
Cdd:PRK13646 94 PESqlFEDTVEREIIFGPKNFKMN----LDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1374671911 211 DEPTSALDPISTLRVEELVQDL--KKDYSIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSnpSDKQTEDY 284
Cdd:PRK13646 170 DEPTAGLDPQSKRQVMRLLKSLqtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK--DKKKLADW 243
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
46-263 |
9.90e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 107.79 E-value: 9.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 46 TQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMveLVPtvkTSGKILYRDQNIfdKSYPVEKLRTN 125
Cdd:PRK11231 5 TENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARL--LTP---QSGTVFLGDKPI--SMLSSRQLARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 126 VGMVFQQPnPFPK--SIYDNITYGPRIH-------GIKDKkildEIVEKSLRGAAIwDELKDRLdqnAYGLSGGQQQRVC 196
Cdd:PRK11231 78 LALLPQHH-LTPEgiTVRELVAYGRSPWlslwgrlSAEDN----ARVNQAMEQTRI-NHLADRR---LTDLSGGQRQRAF 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 197 IARCLAIEPDVILMDEPTSALDpISTlRVE--ELVQDLK-KDYSIIIVTHNMQQAARVSDKTAFFLNGYV 263
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLD-INH-QVElmRLMRELNtQGKTVVTVLHDLNQASRYCDHLVVLANGHV 216
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
53-256 |
1.06e-27 |
|
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: 108.63 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 53 YGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMveLVPTvktSGKILYrdqNIFDKSYPVEKLRTNVGMVFQQ 132
Cdd:TIGR01188 3 YGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTL--LRPT---SGTARV---AGYDVVREPRKVRRSIGIVPQY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 133 PNPFPK-SIYDNITYGPRIHGIKdKKILDEIVEKSLRGAAIWDELKDRLDQnaygLSGGQQQRVCIARCLAIEPDVILMD 211
Cdd:TIGR01188 75 ASVDEDlTGRENLEMMGRLYGLP-KDEAEERAEELLELFELGEAADRPVGT----YSGGMRRRLDIAASLIHQPDVLFLD 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1374671911 212 EPTSALDPISTLRVEELVQDLKK-DYSIIIVTHNMQQAARVSDKTA 256
Cdd:TIGR01188 150 EPTTGLDPRTRRAIWDYIRALKEeGVTILLTTHYMEEADKLCDRIA 195
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
50-269 |
1.26e-27 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 106.10 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 50 DLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELVptvktSGKILYRDQNIFdKSYPVEKlrtNVGMV 129
Cdd:TIGR01277 5 KVRYEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPA-----SGSIKVNDQSHT-GLAPYQR---PVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 130 FQQPNPFPK-SIYDNITYGprIH-GIKDKKILDEIVEKSLRGAAIwDELKDRLDQNaygLSGGQQQRVCIARCLAIEPDV 207
Cdd:TIGR01277 76 FQENNLFAHlTVRQNIGLG--LHpGLKLNAEQQEKVVDAAQQVGI-ADYLDRLPEQ---LSGGQRQRVALARCLVRPNPI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1374671911 208 ILMDEPTSALDPIstLRVE--ELVQDL--KKDYSIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDT 269
Cdd:TIGR01277 150 LLLDEPFSALDPL--LREEmlALVKQLcsERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
42-254 |
1.84e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 106.78 E-value: 1.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 42 VVYSTQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRmvELVPtvkTSGKILYRDQNIfdKSYPVEK 121
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSG--ELSP---DSGEVRLNGRPL--ADWSPAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 122 LRTNVGMVFQQPN-PFPKSIYDNITYGPRIHGIKDKKiLDEIVEKSLRGAAIWDeLKDRLDQnayGLSGGQQQRVCIARC 200
Cdd:PRK13548 74 LARRRAVLPQHSSlSFPFTVEEVVAMGRAPHGLSRAE-DDALVAAALAQVDLAH-LAGRDYP---QLSGGEQQRVQLARV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1374671911 201 LA------IEPDVILMDEPTSALDPISTLRVEELVQDLKKD--YSIIIVTHNMQQAARVSDK 254
Cdd:PRK13548 149 LAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErgLAVIVVLHDLNLAARYADR 210
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
71-263 |
3.45e-27 |
|
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: 104.88 E-value: 3.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 71 VTAIIGPSGSGKSTYvkaLNrmveLVP--TVKTSGKILYRDQNIfDKSYPVEKlrtNVGMVFQQPNPFPK-SIYDNITYG 147
Cdd:cd03298 26 ITAIVGPSGSGKSTL---LN----LIAgfETPQSGRVLINGVDV-TAAPPADR---PVSMLFQENNLFAHlTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 148 pRIHGIKDKKILDEIVEKSLRGAAIWDELKDRLDQnaygLSGGQQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEE 227
Cdd:cd03298 95 -LSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGE----LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 1374671911 228 LVQDLKKD--YSIIIVTHNMQQAARVSDKTAFFLNGYV 263
Cdd:cd03298 170 LVLDLHAEtkMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
59-276 |
3.47e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 106.70 E-value: 3.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNI-FDKSYPVEkLRTNVGMVFQQPNP-- 135
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILK-----PTSGEVLIKGEPIkYDKKSLLE-VRKTVGIVFQNPDDql 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 136 FPKSIYDNITYGPRIHGIKDkkildEIVEKSLRGAAIWDELKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPTS 215
Cdd:PRK13639 92 FAPTVEEDVAFGPLNLGLSK-----EEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1374671911 216 ALDPISTLRVEELVQDL-KKDYSIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNP 276
Cdd:PRK13639 167 GLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
55-246 |
4.79e-27 |
|
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: 110.34 E-value: 4.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 55 EQHSLKNVNLDIL--EKnvTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQNIfdKSYPVEKLRTNVGMVFQQ 132
Cdd:TIGR03375 477 ETPALDNVSLTIRpgEK--VAIIGRIGSGKSTLLKLLLGLYQP-----TEGSVLLDGVDI--RQIDPADLRRNIGYVPQD 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 133 PNPFPKSIYDNITYGPRihGIKDKKILdEIVEKSlrGA-AIWDELKDRLD----QNAYGLSGGQQQRVCIARCLAIEPDV 207
Cdd:TIGR03375 548 PRLFYGTLRDNIALGAP--YADDEEIL-RAAELA--GVtEFVRRHPDGLDmqigERGRSLSGGQRQAVALARALLRDPPI 622
|
170 180 190
....*....|....*....|....*....|....*....
gi 1374671911 208 ILMDEPTSALDPISTLRVEELVQDLKKDYSIIIVTHNMQ 246
Cdd:TIGR03375 623 LLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHRTS 661
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
59-253 |
6.77e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 109.34 E-value: 6.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIFDKSyPVEKLRTNVGMVFQQPNPFPK 138
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQ-----PDSGEILLDGEPVRFRS-PRDAQAAGIAIIHQELNLVPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 139 -SIYDNITYG--PRIHGIKDKKILDEIVEKSLR--GAAIwdelkdRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEP 213
Cdd:COG1129 94 lSVAENIFLGrePRRGGLIDWRAMRRRARELLArlGLDI------DPDTPVGDLSVAQQQLVEIARALSRDARVLILDEP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1374671911 214 TSALDPISTLRVEELVQDLKKD-YSIIIVTHNMQQAARVSD 253
Cdd:COG1129 168 TASLTEREVERLFRIIRRLKAQgVAIIYISHRLDEVFEIAD 208
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
47-243 |
1.08e-26 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 109.04 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYG--EQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIFDksYPVEKLRT 124
Cdd:TIGR02203 334 RNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYE-----PDSGQILLDGHDLAD--YTLASLRR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 125 NVGMVFQQPNPFPKSIYDNITYGPRihgikdKKILDEIVEKSLRgAAIWDELKDRLD--------QNAYGLSGGQQQRVC 196
Cdd:TIGR02203 407 QVALVSQDVVLFNDTIANNIAYGRT------EQADRAEIERALA-AAYAQDFVDKLPlgldtpigENGVLLSGGQRQRLA 479
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1374671911 197 IARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDYSIIIVTH 243
Cdd:TIGR02203 480 IARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAH 526
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
59-265 |
1.90e-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: 103.72 E-value: 1.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVelvptVKTSGKILY--RDQNIFDKSYpvekLRTNVGMVFQQPNPF 136
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFY-----VPENGRVLVdgHDLALADPAW----LRRQVGVVLQENVLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 137 PKSIYDNITYGprihgiKDKKILDEIVE-KSLRGA-AIWDELKDRLDQ----NAYGLSGGQQQRVCIARCLAIEPDVILM 210
Cdd:cd03252 89 NRSIRDNIALA------DPGMSMERVIEaAKLAGAhDFISELPEGYDTivgeQGAGLSGGQRQRIAIARALIHNPRILIF 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1374671911 211 DEPTSALDPISTLRVEELVQDLKKDYSIIIVTHNMqQAARVSDKTAFFLNGYVNE 265
Cdd:cd03252 163 DEATSALDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVE 216
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
58-263 |
2.55e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 104.82 E-value: 2.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 58 SLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELVPTVKTSGKILYRDQNifdKSYPVEKLRTNVGMVFQQPNP-- 135
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTS---KQKEIKPVRKKVGVVFQFPESql 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 136 FPKSIYDNITYGPRIHGIKdKKILDEIVEKSLRGAAIWDELkdrLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPTS 215
Cdd:PRK13643 98 FEETVLKDVAFGPQNFGIP-KEKAEKIAAEKLEMVGLADEF---WEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1374671911 216 ALDPISTLRVEELVQDLKKD-YSIIIVTHNMQQAARVSDKTAFFLNGYV 263
Cdd:PRK13643 174 GLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
47-251 |
2.66e-26 |
|
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: 102.69 E-value: 2.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYvkaLNRMVELVPtvKTSGKILYRDQNI--FDKSYPVEKLRT 124
Cdd:TIGR03608 2 KNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTL---LNIIGLLEK--FDSGQVYLNGQETppLNSKKASKFRRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 125 NVGMVFQQPNPFP-KSIYDNITYGPRIHGIKDKKILDEIVE--KSLRgaaiwdeLKDRLDQNAYGLSGGQQQRVCIARCL 201
Cdd:TIGR03608 77 KLGYLFQNFALIEnETVEENLDLGLKYKKLSKKEKREKKKEalEKVG-------LNLKLKQKIYELSGGEQQRVALARAI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1374671911 202 AIEPDVILMDEPTSALDPISTLRVEELVQDLKKD-YSIIIVTHNM---QQAARV 251
Cdd:TIGR03608 150 LKPPPLILADEPTGSLDPKNRDEVLDLLLELNDEgKTIIIVTHDPevaKQADRV 203
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
55-243 |
2.89e-26 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 107.80 E-value: 2.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 55 EQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQNIFDksYPVEKLRTNVGMVFQQPN 134
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDI-----DEGEILLDGHDLRD--YTLASLRNQVALVSQNVH 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 135 PFPKSIYDNITYGprihgiKDKKILDEIVEKSLRGAAIWD---ELKDRLD----QNAYGLSGGQQQRVCIARCLAIEPDV 207
Cdd:PRK11176 428 LFNDTIANNIAYA------RTEQYSREQIEEAARMAYAMDfinKMDNGLDtvigENGVLLSGGQRQRIAIARALLRDSPI 501
|
170 180 190
....*....|....*....|....*....|....*.
gi 1374671911 208 ILMDEPTSALDPISTLRVEELVQDLKKDYSIIIVTH 243
Cdd:PRK11176 502 LILDEATSALDTESERAIQAALDELQKNRTSLVIAH 537
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
53-277 |
3.53e-26 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 105.55 E-value: 3.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 53 YGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTyvkaLNRMVELVPTvKTSGKILYRDQnifDKSYPVEKLRtNVGMVFQQ 132
Cdd:PRK10851 12 FGRTQVLNDISLDIPSGQMVALLGPSGSGKTT----LLRIIAGLEH-QTSGHIRFHGT---DVSRLHARDR-KVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 133 PNPFPK-SIYDNITYG---------PRIHGIKDKKI-LDEIVEKSlrgaaiwdELKDRLDQNaygLSGGQQQRVCIARCL 201
Cdd:PRK10851 83 YALFRHmTVFDNIAFGltvlprrerPNAAAIKAKVTqLLEMVQLA--------HLADRYPAQ---LSGGQKQRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 202 AIEPDVILMDEPTSALDpiSTLRVE------ELVQDLKkdYSIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSN 275
Cdd:PRK10851 152 AVEPQILLLDEPFGALD--AQVRKElrrwlrQLHEELK--FTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWRE 227
|
..
gi 1374671911 276 PS 277
Cdd:PRK10851 228 PA 229
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
55-281 |
5.85e-26 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 107.25 E-value: 5.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 55 EQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIFDKS-YPVEKLRTNVGMVFQQP 133
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVE-----SQGGEIIFNGQRIDTLSpGKLQALRRDIQFIFQDP 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 134 ----NPfPKSIYDNITYGPRIHGIKDKKILDEIVEKSLRGAAIWDELKDRLdqnAYGLSGGQQQRVCIARCLAIEPDVIL 209
Cdd:PRK10261 411 yaslDP-RQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRY---PHEFSGGQRQRICIARALALNPKVII 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1374671911 210 MDEPTSALDPISTLRVEELVQDLKKDYSI--IIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNPSDKQT 281
Cdd:PRK10261 487 ADEAVSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYT 560
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
48-261 |
7.62e-26 |
|
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: 100.47 E-value: 7.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 48 NLDLWYGEQ--HSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRmvELVPTvktSGKILYRDQNIfdkSYPVEKLRTN 125
Cdd:cd03247 5 NVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG--DLKPQ---QGEITLDGVPV---SDLEKALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 126 VGMVFQQPNPFPKSIYDNItyGPRihgikdkkildeivekslrgaaiwdelkdrldqnaygLSGGQQQRVCIARCLAIEP 205
Cdd:cd03247 77 ISVLNQRPYLFDTTLRNNL--GRR-------------------------------------FSGGERQRLALARILLQDA 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1374671911 206 DVILMDEPTSALDPISTLRVEELVQDLKKDYSIIIVTHNMQQAARVsDKTAFFLNG 261
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHM-DKILFLENG 172
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
47-249 |
1.32e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 100.63 E-value: 1.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRmvELVPTVKTSGKILYRDQNIFDKsyPVEKLRtnV 126
Cdd:COG4136 5 ENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAG--TLSPAFSASGEVLLNGRRLTAL--PAEQRR--I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 127 GMVFQQPNPFPK-SIYDNITYG--PRIHGiKDKKildEIVEKSLRGAaiwdELKDRLDQNAYGLSGGQQQRVCIARCLAI 203
Cdd:COG4136 79 GILFQDDLLFPHlSVGENLAFAlpPTIGR-AQRR---ARVEQALEEA----GLAGFADRDPATLSGGQRARVALLRALLA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1374671911 204 EPDVILMDEPTSALDPISTLRVEELVQDLKKDYSI--IIVTHNMQQAA 249
Cdd:COG4136 151 EPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIpaLLVTHDEEDAP 198
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
59-243 |
1.43e-25 |
|
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: 100.32 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKAL-NRmvelVPTVKTSGKILYRDQNIFDKSYpveklRTNVGMVFQqpnpfp 137
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALaGR----RTGLGVSGEVLINGRPLDKRSF-----RKIIGYVPQ------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 138 ksiyDNITYGprihgikdkkilDEIVEKSLRGAAiwdELKdrldqnayGLSGGQQQRVCIARCLAIEPDVILMDEPTSAL 217
Cdd:cd03213 90 ----DDILHP------------TLTVRETLMFAA---KLR--------GLSGGERKRVSIALELVSNPSLLFLDEPTSGL 142
|
170 180
....*....|....*....|....*..
gi 1374671911 218 DPISTLRVEELVQDLKKD-YSIIIVTH 243
Cdd:cd03213 143 DSSSALQVMSLLRRLADTgRTIICSIH 169
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
53-276 |
1.54e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 104.26 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 53 YGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTyvkaLNRMVELVPTVkTSGKILYRDQNIFDksYPVEKlrTNVGMVFQQ 132
Cdd:PRK09452 24 FDGKEVISNLDLTINNGEFLTLLGPSGCGKTT----VLRLIAGFETP-DSGRIMLDGQDITH--VPAEN--RHVNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 133 PNPFPK-SIYDNITYGPRIHGIKDKKIlDEIVEKSLRGAaiwdELKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMD 211
Cdd:PRK09452 95 YALFPHmTVFENVAFGLRMQKTPAAEI-TPRVMEALRMV----QLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1374671911 212 EPTSALDpiSTLRVE---ELVQdLKKDYSI--IIVTHNMQQAARVSDKTAFFLNGYVnEYDDTDK-IFSNP 276
Cdd:PRK09452 170 ESLSALD--YKLRKQmqnELKA-LQRKLGItfVFVTHDQEEALTMSDRIVVMRDGRI-EQDGTPReIYEEP 236
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
44-251 |
4.45e-25 |
|
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: 98.44 E-value: 4.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 44 YSTQNLDLWYG--EQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKAlnrMVELVPTvkTSGKILYRDQNIfdKSYPVEK 121
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARL---ILGLLRP--TSGRVRLDGADI--SQWDPNE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 122 LRTNVGMVFQQPNPFPKSIYDNItygprihgikdkkildeivekslrgaaiwdelkdrldqnaygLSGGQQQRVCIARCL 201
Cdd:cd03246 74 LGDHVGYLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARAL 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1374671911 202 AIEPDVILMDEPTSALDPISTLRVEELVQDLKK-DYSIIIVTHNM---QQAARV 251
Cdd:cd03246 112 YGNPRILVLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPetlASADRI 165
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
55-277 |
5.81e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 101.03 E-value: 5.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 55 EQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMveLVPTVKTSGKILYRDQNIFDKSypVEKLRTNVGMVFQQP- 133
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGL--LLPDDNPNSKITVDGITLTAKT--VWDIREKVGIVFQNPd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 134 NPF-PKSIYDNITYGPRIHGIKDKKILdEIVEKSLRGAAiwdeLKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDE 212
Cdd:PRK13640 95 NQFvGATVGDDVAFGLENRAVPRPEMI-KIVRDVLADVG----MLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1374671911 213 PTSALDPISTLRVEELVQDLKKD--YSIIIVTHNMQQAArVSDKTAFFLNGYVNEYDDTDKIFSNPS 277
Cdd:PRK13640 170 STSMLDPAGKEQILKLIRKLKKKnnLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
59-276 |
6.91e-25 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 104.03 E-value: 6.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNI--FDKSYpvekLRTNVGMVFQQPNPF 136
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQ-----PTGGQVLLDGVPLvqYDHHY----LHRQVALVGQEPVLF 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 137 PKSIYDNITYGPRihgikdkKILDEIVEKSLRGAAIWD---ELKDRLDQNAYG----LSGGQQQRVCIARCLAIEPDVIL 209
Cdd:TIGR00958 568 SGSVRENIAYGLT-------DTPDEEIMAAAKAANAHDfimEFPNGYDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLI 640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1374671911 210 MDEPTSALDpistLRVEELVQDLK--KDYSIIIVTHNMQQAARvSDKTAFFLNGYVNEYDDTDKIFSNP 276
Cdd:TIGR00958 641 LDEATSALD----AECEQLLQESRsrASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
59-242 |
9.10e-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: 98.88 E-value: 9.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELVPTvkTSGKILYRDQnifdksyPVEK--LRTNVGMVFQQPNPF 136
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGT--TSGQILFNGQ-------PRKPdqFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 137 PK-SIYDNITYGP--RIHGIKDKKILDEIVE-KSLRGAAIwdelKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDE 212
Cdd:cd03234 94 PGlTVRETLTYTAilRLPRKSSDAIRKKRVEdVLLRDLAL----TRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190
....*....|....*....|....*....|
gi 1374671911 213 PTSALDPISTLRVEELVQDLKKDYSIIIVT 242
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARRNRIVILT 199
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
47-254 |
9.73e-25 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 99.80 E-value: 9.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRmvELVPTvktSGKILYRDQNIFDKSyPVE--KLRT 124
Cdd:COG4559 5 ENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTG--ELTPS---SGEVRLNGRPLAAWS-PWElaRRRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 125 nvgmVFQQPNP--FPKSIYDNITYGpRIHGIKDKKILDEIVEKSLRGAAIWDeLKDRLDQnayGLSGGQQQRVCIARCLA 202
Cdd:COG4559 79 ----VLPQHSSlaFPFTVEEVVALG-RAPHGSSAAQDRQIVREALALVGLAH-LAGRSYQ---TLSGGEQQRVQLARVLA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 203 -------IEPDVILMDEPTSALDPISTLRVEELVQDL-KKDYSIIIVTHNMQQAARVSDK 254
Cdd:COG4559 150 qlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLaRRGGGVVAVLHDLNLAAQYADR 209
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
53-253 |
1.06e-24 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 101.33 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 53 YGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKalnrmveLVPTVK--TSGKILYRDQNIFDKSYPveklRTNVGMVF 130
Cdd:PRK11432 16 FGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLR-------LVAGLEkpTEGQIFIDGEDVTHRSIQ----QRDICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 131 QQPNPFPK-SIYDNITYGPRIHGIKDkkilDEIVEKSLRGAAIWD--ELKDR-LDQnaygLSGGQQQRVCIARCLAIEPD 206
Cdd:PRK11432 85 QSYALFPHmSLGENVGYGLKMLGVPK----EERKQRVKEALELVDlaGFEDRyVDQ----ISGGQQQRVALARALILKPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1374671911 207 VILMDEPTSALDpiSTLR--VEELVQDLKKDYSI--IIVTHNMQQAARVSD 253
Cdd:PRK11432 157 VLLFDEPLSNLD--ANLRrsMREKIRELQQQFNItsLYVTHDQSEAFAVSD 205
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
73-274 |
1.99e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 98.12 E-value: 1.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 73 AIIGPSGSGKSTYvkaLNRMVELVPTvkTSGKILYRDQNiFDKSYPVeklRTNVGMVFQQPNPFPK-SIYDNITYGprIH 151
Cdd:PRK10771 29 AILGPSGAGKSTL---LNLIAGFLTP--ASGSLTLNGQD-HTTTPPS---RRPVSMLFQENNLFSHlTVAQNIGLG--LN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 152 -GIK----DKKILDEIVEK-SLrgaaiwDELKDRLDQNaygLSGGQQQRVCIARCLAIEPDVILMDEPTSALDPisTLRV 225
Cdd:PRK10771 98 pGLKlnaaQREKLHAIARQmGI------EDLLARLPGQ---LSGGQRQRVALARCLVREQPILLLDEPFSALDP--ALRQ 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1374671911 226 E--ELVQDL--KKDYSIIIVTHNMQQAARVSDKTAFFLNGYVnEYD-DTDKIFS 274
Cdd:PRK10771 167 EmlTLVSQVcqERQLTLLMVSHSLEDAARIAPRSLVVADGRI-AWDgPTDELLS 219
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
50-244 |
2.67e-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: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 50 DLWY--GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRmvelVPTVK-TSGKILYRDQNIFDKSyPVEKLRTNV 126
Cdd:cd03217 5 DLHVsvGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG----HPKYEvTEGEILFKGEDITDLP-PEERARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 127 GMVFQQPnpfpksiydnitygPRIHGIKDKKILDEIVEkslrgaaiwdelkdrldqnayGLSGGQQQRVCIARCLAIEPD 206
Cdd:cd03217 80 FLAFQYP--------------PEIPGVKNADFLRYVNE---------------------GFSGGEKKRNEILQLLLLEPD 124
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1374671911 207 VILMDEPTSALDpISTLR-VEELVQDLK-KDYSIIIVTHN 244
Cdd:cd03217 125 LAILDEPDSGLD-IDALRlVAEVINKLReEGKSVLIITHY 163
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
47-243 |
2.78e-24 |
|
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: 97.16 E-value: 2.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALnrmVELVPtvKTSGKILYRDQNIFDksyPVEKLRTNV 126
Cdd:COG4133 6 ENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRIL---AGLLP--PSAGEVLWNGEPIRD---AREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 127 GMVFQQPNPFPK-SIYDNITYGPRIHGIkdkkildeivekSLRGAAIWD-----ELKDRLDQNAYGLSGGQQQRVCIARC 200
Cdd:COG4133 78 AYLGHADGLKPElTVRENLRFWAALYGL------------RADREAIDEaleavGLAGLADLPVRQLSAGQKRRVALARL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1374671911 201 LAIEPDVILMDEPTSALDPISTLRVEELVQD-LKKDYSIIIVTH 243
Cdd:COG4133 146 LLSPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTH 189
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
55-278 |
4.54e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 98.27 E-value: 4.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 55 EQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIFDKSypVEKLRTNVGMVFQQP- 133
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLE-----AESGQIIIDGDLLTEEN--VWDIRHKIGMVFQNPd 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 134 NPF-PKSIYDNITYGPRIHGIkDKKILDEIVEKSLRGAAIWDeLKDRldqNAYGLSGGQQQRVCIARCLAIEPDVILMDE 212
Cdd:PRK13650 92 NQFvGATVEDDVAFGLENKGI-PHEEMKERVNEALELVGMQD-FKER---EPARLSGGQKQRVAIAGAVAMRPKIIILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1374671911 213 PTSALDPISTLRVEELVQDLKKDY--SIIIVTHNMQQAArVSDKTAFFLNGYVNEYDDTDKIFSNPSD 278
Cdd:PRK13650 167 ATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFSRGND 233
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
28-277 |
6.39e-24 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 99.03 E-value: 6.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 28 QTEKHETLSD-RERRVVYSTQNldlwyGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALnrMVELVPTVKTSGKIL 106
Cdd:PRK09473 5 AQQQADALLDvKDLRVTFSTPD-----GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFAL--MGLLAANGRIGGSAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 107 YRDQNIFD-KSYPVEKLRT-NVGMVFQQP----NPFPKsIYDNITYGPRIHGIKDKKildEIVEKSLR--GAAIWDELKD 178
Cdd:PRK09473 78 FNGREILNlPEKELNKLRAeQISMIFQDPmtslNPYMR-VGEQLMEVLMLHKGMSKA---EAFEESVRmlDAVKMPEARK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 179 RLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDY--SIIIVTHNMQQAARVSDKTA 256
Cdd:PRK09473 154 RMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKVL 233
|
250 260
....*....|....*....|.
gi 1374671911 257 FFLNGYVNEYDDTDKIFSNPS 277
Cdd:PRK09473 234 VMYAGRTMEYGNARDVFYQPS 254
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
56-276 |
9.17e-24 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 98.79 E-value: 9.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 56 QHSLkNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMvelvpTVKTSGKILYRDQNIFDK----SYPVEKLRtnVGMVFQ 131
Cdd:PRK11144 12 DLCL-TVNLTLPAQGITAIFGRSGAGKTSLINAISGL-----TRPQKGRIVLNGRVLFDAekgiCLPPEKRR--IGYVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 132 QPNPFPK-SIYDNITYGPRIhgiKDKKILDEIVEksLRGaaiwdeLKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILM 210
Cdd:PRK11144 84 DARLFPHyKVRGNLRYGMAK---SMVAQFDKIVA--LLG------IEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLM 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1374671911 211 DEPTSALD-PistlRVEELV---QDLKKDYSIII--VTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNP 276
Cdd:PRK11144 153 DEPLASLDlP----RKRELLpylERLAREINIPIlyVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
53-276 |
1.63e-23 |
|
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: 98.26 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 53 YGEqHSLKnVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQNIFDKS----YPVEKLRtnVGM 128
Cdd:TIGR02142 9 LGD-FSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRP-----DEGEIVLNGRTLFDSRkgifLPPEKRR--IGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 129 VFQQPNPFPK-SIYDNITYGPRIHGIKDKKILDEIVEKSLrgaAIwDELKDRLDQNaygLSGGQQQRVCIARCLAIEPDV 207
Cdd:TIGR02142 80 VFQEARLFPHlSVRGNLRYGMKRARPSERRISFERVIELL---GI-GHLLGRLPGR---LSGGEKQRVAIGRALLSSPRL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1374671911 208 ILMDEPTSALDPISTLRVEELVQDLKKDYSI--IIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNP 276
Cdd:TIGR02142 153 LLMDEPLAALDDPRKYEILPYLERLHAEFGIpiLYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
45-253 |
1.80e-23 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 95.92 E-value: 1.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 45 STQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYvkaLNRMVELVPtvKTSGKILYRDQNIfdKSYPVEKLRT 124
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTL---LSMISRLLP--PDSGEVLVDGLDV--ATTPSRELAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 125 NVGmVFQQPNPFPK--SIYDNITYG--PRIHG---IKDKKILDEivekslrgaAI----WDELKDR-LDQnaygLSGGQQ 192
Cdd:COG4604 76 RLA-ILRQENHINSrlTVRELVAFGrfPYSKGrltAEDREIIDE---------AIayldLEDLADRyLDE----LSGGQR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1374671911 193 QRVCIARCLAIEPDVILMDEPTSALDP------ISTLRveELVQDLKKdySIIIVTHNMQQAARVSD 253
Cdd:COG4604 142 QRAFIAMVLAQDTDYVLLDEPLNNLDMkhsvqmMKLLR--RLADELGK--TVVIVLHDINFASCYAD 204
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
45-244 |
1.82e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 95.87 E-value: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 45 STQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKST--YVkalnrMVELVPTvkTSGKILYRDQNIFDksYPVEKl 122
Cdd:COG1137 5 EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTtfYM-----IVGLVKP--DSGRIFLDGEDITH--LPMHK- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 123 RTNVGMVF--QQPNPFPK-SIYDNI-----TYGPRIHGIKDKkiLDEIVEkslrgaaiwdELK--DRLDQNAYGLSGGQQ 192
Cdd:COG1137 75 RARLGIGYlpQEASIFRKlTVEDNIlavleLRKLSKKEREER--LEELLE----------EFGitHLRKSKAYSLSGGER 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1374671911 193 QRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLK-KDYSIIIVTHN 244
Cdd:COG1137 143 RRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKeRGIGVLITDHN 195
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
57-263 |
2.17e-23 |
|
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: 95.13 E-value: 2.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 57 HSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDqniFDKSYPVEKLRTNVGMVFQQPNPF 136
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLE-----PDAGFATVDG---FDVVKEPAEARRRLGFVSDSTGLY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 137 PK-SIYDNITYGPRIHGIKDKKILDEIvekslrgaaiwDELKDRLDQNAY------GLSGGQQQRVCIARCLAIEPDVIL 209
Cdd:cd03266 91 DRlTARENLEYFAGLYGLKGDELTARL-----------EELADRLGMEELldrrvgGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1374671911 210 MDEPTSALDPISTLRVEELVQDLKKD-YSIIIVTHNMQQAARVSDKTAFFLNGYV 263
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
67-276 |
3.41e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 96.96 E-value: 3.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 67 LEKNVT-AIIGPSGSGKSTyvkaLNRMVELVPTvKTSGKILYRDQNIFDKSYPVEK-LRTNVGMVFQQPnpfpksiydni 144
Cdd:PRK11308 38 LERGKTlAVVGESGCGKST----LARLLTMIET-PTGGELYYQGQDLLKADPEAQKlLRQKIQIVFQNP----------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 145 tYG---PRihgikdKKIlDEIVEKSLrgaAIWDEL--KDRLDQNA-----YGL------------SGGQQQRVCIARCLA 202
Cdd:PRK11308 102 -YGslnPR------KKV-GQILEEPL---LINTSLsaAERREKALammakVGLrpehydryphmfSGGQRQRIAIARALM 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1374671911 203 IEPDVILMDEPTSALDPISTLRVEELVQDLKKDY--SIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNP 276
Cdd:PRK11308 171 LDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELglSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
4-243 |
3.63e-23 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 99.25 E-value: 3.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 4 IKELEKHTEKVNDSHEKQPFIAKDQTEKHETLSDRERRVVYSTQNLDLWYG----EQHSLKNVNLDILEKNVTAIIGPSG 79
Cdd:TIGR03796 436 LQELEGDLNRLDDVLRNPVDPLLEEPEGSAATSEPPRRLSGYVELRNITFGysplEPPLIENFSLTLQPGQRVALVGGSG 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 80 SGKSTYVKALNRMVElvptvKTSGKILYRDQNIfdKSYPVEKLRTNVGMVFQQPNPFPKSIYDNITygprihgIKDKKIL 159
Cdd:TIGR03796 516 SGKSTIAKLVAGLYQ-----PWSGEILFDGIPR--EEIPREVLANSVAMVDQDIFLFEGTVRDNLT-------LWDPTIP 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 160 DEIVEKSLRGAAIWDELKDR-------LDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQdl 232
Cdd:TIGR03796 582 DADLVRACKDAAIHDVITSRpggydaeLAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLR-- 659
|
250
....*....|.
gi 1374671911 233 KKDYSIIIVTH 243
Cdd:TIGR03796 660 RRGCTCIIVAH 670
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
60-260 |
5.16e-23 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 98.95 E-value: 5.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 60 KNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVEL-------------------------------------------- 95
Cdd:PTZ00265 1185 KDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeg 1264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 96 -----VPTVKTSGKILYRDQNIFDksYPVEKLRTNVGMVFQQPNPFPKSIYDNITYGprihgiKDKKILDEiVEKSLRGA 170
Cdd:PTZ00265 1265 gsgedSTVFKNSGKILLDGVDICD--YNLKDLRNLFSIVSQEPMLFNMSIYENIKFG------KEDATRED-VKRACKFA 1335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 171 AIwDE----LKDRLDQNA--YG--LSGGQQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKK--DYSIII 240
Cdd:PTZ00265 1336 AI-DEfiesLPNKYDTNVgpYGksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIIT 1414
|
250 260
....*....|....*....|
gi 1374671911 241 VTHNMQQAARvSDKTAFFLN 260
Cdd:PTZ00265 1415 IAHRIASIKR-SDKIVVFNN 1433
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
45-286 |
6.49e-23 |
|
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: 94.51 E-value: 6.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 45 STQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNrmVELVPTvktSGKILYRDQN-----IFDKSYPV 119
Cdd:TIGR02323 5 QVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLA--GRLAPD---HGTATYIMRSgaeleLYQLSEAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 120 EK--LRTNVGMVFQQPNPFPK---SIYDNItyGPRIHGIKDKKILDeiveksLRGAAI-WDEL----KDRLDQNAYGLSG 189
Cdd:TIGR02323 80 RRrlMRTEWGFVHQNPRDGLRmrvSAGANI--GERLMAIGARHYGN------IRATAQdWLEEveidPTRIDDLPRAFSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 190 GQQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDY--SIIIVTHNMQQAARVSDKTAFFLNGYVNEYD 267
Cdd:TIGR02323 152 GMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLglAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
250
....*....|....*....
gi 1374671911 268 DTDKIFSNPSDKQTEDYIS 286
Cdd:TIGR02323 232 LTDQVLDDPQHPYTQLLVS 250
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
73-265 |
9.08e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 97.72 E-value: 9.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 73 AIIGPSGSGKSTYVKALNRMVElvPTvktSGKILYRDQNIFDKSypVEKLRTNVGMVFQQPNPFPKSIYDNItygpRIhG 152
Cdd:PRK13657 365 AIVGPTGAGKSTLINLLQRVFD--PQ---SGRILIDGTDIRTVT--RASLRRNIAVVFQDAGLFNRSIEDNI----RV-G 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 153 IKDKKilDEIVEKSLRGAAIWDELK---DRLDQNAyG-----LSGGQQQRVCIARCLAIEPDVILMDEPTSALDPISTLR 224
Cdd:PRK13657 433 RPDAT--DEEMRAAAERAQAHDFIErkpDGYDTVV-GergrqLSGGERQRLAIARALLKDPPILILDEATSALDVETEAK 509
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1374671911 225 VEELVQDLKKDYSIIIVTHNMqQAARVSDKTAFFLNGYVNE 265
Cdd:PRK13657 510 VKAALDELMKGRTTFIIAHRL-STVRNADRILVFDNGRVVE 549
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
54-274 |
1.53e-22 |
|
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: 97.13 E-value: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 54 GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALnrmVELVPTvkTSGKILYRDQNIFdkSYPVEKLRTNVGMVFQQP 133
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLL---VGVWPP--TAGSVRLDGADLS--QWDREELGRHIGYLPQDV 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 134 NPFPKSIYDNITygpRIhgikdKKILDEIVEKSLRGAAIWD---ELKD----RLDQNAYGLSGGQQQRVCIARCLAIEPD 206
Cdd:COG4618 416 ELFDGTIAENIA---RF-----GDADPEKVVAAAKLAGVHEmilRLPDgydtRIGEGGARLSGGQRQRIGLARALYGDPR 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1374671911 207 VILMDEPTSALDPISTLRVEELVQDLKKD-YSIIIVTHNMqQAARVSDKTAFFLNGYVNEYDDTDKIFS 274
Cdd:COG4618 488 LVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHRP-SLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
38-244 |
1.61e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 92.85 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 38 RERRVVYSTQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIfdKSY 117
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLIS-----PTSGTLLFEGEDI--STL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 118 PVEKLRTNVGMVFQQPNPFPKSIYDNITYGPRIHGIK--DKKILDEIVEKSLRgaaiwDELkdrLDQNAYGLSGGQQQRV 195
Cdd:PRK10247 75 KPEIYRQQVSYCAQTPTLFGDTVYDNLIFPWQIRNQQpdPAIFLDDLERFALP-----DTI---LTKNIAELSGGEKQRI 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1374671911 196 CIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDYSIII--VTHN 244
Cdd:PRK10247 147 SLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVlwVTHD 197
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
45-253 |
1.65e-22 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 92.34 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 45 STQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILyrdqniFDKSYPVEKLRT 124
Cdd:cd03269 2 EVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIIL-----PDSGEVL------FDGKPLDIAARN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 125 NVGMVFQQPNPFPK-SIYDNITYGPRIHGIKDKKILDEIvEKSLRGAAIWDELKDRLDQnaygLSGGQQQRVCIARCLAI 203
Cdd:cd03269 71 RIGYLPEERGLYPKmKVIDQLVYLAQLKGLKKEEARRRI-DEWLERLELSEYANKRVEE----LSKGNQQKVQFIAAVIH 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1374671911 204 EPDVILMDEPTSALDPISTLRVEELVQDLK-KDYSIIIVTHNMQQAARVSD 253
Cdd:cd03269 146 DPELLILDEPFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELVEELCD 196
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
59-244 |
3.16e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 92.44 E-value: 3.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKAL-NRmvelvPTVK-TSGKILYRDQNIFDKSyPVEKLRTNVGMVFQQPNPF 136
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmGH-----PKYEvTSGSILLDGEDILELS-PDERARAGIFLAFQYPVEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 137 P--------KSIYDNITyGPRIHGIKDKKILDEIVEK-SLRgaaiwDELKDRlDQNAyGLSGGQQQRVCIARCLAIEPDV 207
Cdd:COG0396 90 PgvsvsnflRTALNARR-GEELSAREFLKLLKEKMKElGLD-----EDFLDR-YVNE-GFSGGEKKRNEILQMLLLEPKL 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 1374671911 208 ILMDEPTSALDpISTLR-VEELVQDLK-KDYSIIIVTHN 244
Cdd:COG0396 162 AILDETDSGLD-IDALRiVAEGVNKLRsPDRGILIITHY 199
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
52-244 |
3.42e-22 |
|
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: 95.89 E-value: 3.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 52 WYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVE-LVPTVKTSGKILYrdqnifdkSYPVEKLRTNVGMVF 130
Cdd:TIGR02868 344 YPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDpLQGEVTLDGVPVS--------SLDQDEVRRRVSVCA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 131 QQPNPFPKSIYDNITYGprihgikDKKILDEIVEKSLRGA--AIW-DELKDRLD----QNAYGLSGGQQQRVCIARCLAI 203
Cdd:TIGR02868 416 QDAHLFDTTVRENLRLA-------RPDATDEELWAALERVglADWlRALPDGLDtvlgEGGARLSGGERQRLALARALLA 488
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1374671911 204 EPDVILMDEPTSALDPISTLRVEELVQDLKKDYSIIIVTHN 244
Cdd:TIGR02868 489 DAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
45-276 |
4.55e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 95.54 E-value: 4.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 45 STQNLDLWYGEQHSLK----NVNLDILEKNVTAIIGPSGSGKStyVKALN--RMVELVPTVKTSGKILYRDQNIFDKSYP 118
Cdd:PRK15134 7 AIENLSVAFRQQQTVRtvvnDVSLQIEAGETLALVGESGSGKS--VTALSilRLLPSPPVVYPSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 119 -VEKLRTN-VGMVFQQP----NPF---PKSIYDNITygprIH-GIKDKKILDEIVE----KSLRGAAiwdelkDRLDQNA 184
Cdd:PRK15134 85 tLRGVRGNkIAMIFQEPmvslNPLhtlEKQLYEVLS----LHrGMRREAARGEILNcldrVGIRQAA------KRLTDYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 185 YGLSGGQQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKK--DYSIIIVTHNMQQAARVSDKTAFFLNGY 262
Cdd:PRK15134 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
250
....*....|....
gi 1374671911 263 VNEYDDTDKIFSNP 276
Cdd:PRK15134 235 CVEQNRAATLFSAP 248
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
47-267 |
4.58e-22 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 91.32 E-value: 4.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHS--LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIfdKSYPVEKLRT 124
Cdd:cd03369 10 ENLSVRYAPDLPpvLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLE-----AEEGKIEIDGIDI--STIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 125 NVGMVFQQPNPFPKSIYDNItygprihgikdkKILDEIVEKSLRGAAiwdelkdRLDQNAYGLSGGQQQRVCIARCLAIE 204
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNL------------DPFDEYSDEEIYGAL-------RVSEGGLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1374671911 205 PDVILMDEPTSALDPISTLRVEELVQDLKKDYSIIIVTHNMQQAARVsDKTAFFLNGYVNEYD 267
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYD 205
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
52-290 |
6.10e-22 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 92.55 E-value: 6.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 52 WYGEQH--SLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIF--DKSYPVEKLRtnvg 127
Cdd:PRK15112 20 WFRRQTveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIE-----PTSGELLIDDHPLHfgDYSYRSQRIR---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 128 MVFQQP----NPfpksiydnityGPRIHGIKDKKI-LDEIVEKSLRGAAIWDELKD---RLDQNAY---GLSGGQQQRVC 196
Cdd:PRK15112 91 MIFQDPstslNP-----------RQRISQILDFPLrLNTDLEPEQREKQIIETLRQvglLPDHASYyphMLAPGQKQRLG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 197 IARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDYSI--IIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFS 274
Cdd:PRK15112 160 LARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLA 239
|
250
....*....|....*.
gi 1374671911 275 NPSDKQTEDYISGRFG 290
Cdd:PRK15112 240 SPLHELTKRLIAGHFG 255
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
47-250 |
6.56e-22 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 92.36 E-value: 6.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMveLVPTvktSGKILYRDQNIfdKSYPVEKLRTNV 126
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRL--MTPA---HGHVWLDGEHI--QHYASKEVARRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 127 GMVFQQPN-PFPKSIYDNITYGPRIHG---IKDKKILDEIVEKSLRGAAIwdelKDRLDQNAYGLSGGQQQRVCIARCLA 202
Cdd:PRK10253 84 GLLAQNATtPGDITVQELVARGRYPHQplfTRWRKEDEEAVTKAMQATGI----THLADQSVDTLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1374671911 203 IEPDVILMDEPTSALDPISTLRVEELVQDL--KKDYSIIIVTHNMQQAAR 250
Cdd:PRK10253 160 QETAIMLLDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNQACR 209
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
58-277 |
9.11e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 91.97 E-value: 9.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 58 SLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIFDKSyPVEKLRTNVGMVFQQPNP-- 135
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLR-----PQKGKVLVSGIDTGDFS-KLQGIRKLVGIVFQNPETqf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 136 FPKSIYDNITYGPR---IHGIKDKKILDEIVEKSlrgaaiwdELKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDE 212
Cdd:PRK13644 91 VGRTVEEDLAFGPEnlcLPPIEIRKRVDRALAEI--------GLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1374671911 213 PTSALDPISTLRVEELVQDL-KKDYSIIIVTHNMQQaARVSDKTAFFLNGYVNEYDDTDKIFSNPS 277
Cdd:PRK13644 163 VTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
46-275 |
9.52e-22 |
|
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: 90.92 E-value: 9.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 46 TQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKIlyrdqnIFDKSYPVEKLRTN 125
Cdd:TIGR03740 3 TKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILR-----PTSGEI------IFDGHPWTRKDLHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 126 VGMVFQQPNPFPK-SIYDNITYGPRIHGIKDKKIlDEIVEKSlrgaaiwdELKDRLDQNAYGLSGGQQQRVCIARCLAIE 204
Cdd:TIGR03740 72 IGSLIESPPLYENlTARENLKVHTTLLGLPDSRI-DEVLNIV--------DLTNTGKKKAKQFSLGMKQRLGIAIALLNH 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1374671911 205 PDVILMDEPTSALDPISTLRVEELVQDLKKD-YSIIIVTHNMQQAARVSDKTAFFLNGY------VNEYDDTDKIFSN 275
Cdd:TIGR03740 143 PKLLILDEPTNGLDPIGIQELRELIRSFPEQgITVILSSHILSEVQQLADHIGIISEGVlgyqgkINKSENLEKLFVE 220
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
45-276 |
1.02e-21 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 91.53 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 45 STQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRmvELVPTvktSGKILYRDQ-----NIFDKSYPV 119
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSA--RLAPD---AGEVHYRMRdgqlrDLYALSEAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 120 EK--LRTNVGMVFQQPNpfpksiyD----------NItyGPRIHGIKDKKILDeiveksLRGAAI-WDEL----KDRLDQ 182
Cdd:PRK11701 83 RRrlLRTEWGFVHQHPR-------DglrmqvsaggNI--GERLMAVGARHYGD------IRATAGdWLERveidAARIDD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 183 NAYGLSGGQQQRVCIARCLAIEPDVILMDEPTSALDpIST-------LRveELVQDLkkDYSIIIVTHNMQQAARVSDKT 255
Cdd:PRK11701 148 LPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD-VSVqarlldlLR--GLVREL--GLAVVIVTHDLAVARLLAHRL 222
|
250 260
....*....|....*....|.
gi 1374671911 256 AFFLNGYVNEYDDTDKIFSNP 276
Cdd:PRK11701 223 LVMKQGRVVESGLTDQVLDDP 243
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
59-254 |
1.09e-21 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 90.55 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQNIFDKSYPvEKL---RTNVGMVFQQPNP 135
Cdd:NF038007 21 LNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSL-----DSGSLTLAGKEVTNLSYS-QKIilrRELIGYIFQSFNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 136 FPK-SIYDNITYGPRIHGIKDKkildEIVEKSLRGAAIWDeLKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPT 214
Cdd:NF038007 95 IPHlSIFDNVALPLKYRGVAKK----ERIERVNQVLNLFG-IDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPT 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1374671911 215 SALDPISTLRVEELVQDL-KKDYSIIIVTHNmQQAARVSDK 254
Cdd:NF038007 170 GNLDSKNARAVLQQLKYInQKGTTIIMVTHS-DEASTYGNR 209
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
52-225 |
1.10e-21 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 92.98 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 52 WYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTyvkaLNRMVELVPTVkTSGKILYRDQNIFDKSyPVEKlrtNVGMVFQ 131
Cdd:PRK11650 13 YDGKTQVIKGIDLDVADGEFIVLVGPSGCGKST----LLRMVAGLERI-TSGEIWIGGRVVNELE-PADR---DIAMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 132 QPNPFPK-SIYDNITYGPRIHGIkDKkilDEIVEKSLRGAAIWdELKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILM 210
Cdd:PRK11650 84 NYALYPHmSVRENMAYGLKIRGM-PK---AEIEERVAEAARIL-ELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLF 158
|
170
....*....|....*
gi 1374671911 211 DEPTSALDpiSTLRV 225
Cdd:PRK11650 159 DEPLSNLD--AKLRV 171
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
29-286 |
1.27e-21 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 92.46 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 29 TEKHETLSDRERRVVYSTQNLDLWYGEQH-SLK---NVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGK 104
Cdd:PRK15079 3 EGKKVLLEVADLKVHFDIKDGKQWFWQPPkTLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVK-----ATDGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 105 ILYRDQNIFDKS-YPVEKLRTNVGMVFQQP----NPfPKSIYDNI-----TYGPRIHGIKDKKILDEIVEK-SLRGAAIw 173
Cdd:PRK15079 78 VAWLGKDLLGMKdDEWRAVRSDIQMIFQDPlaslNP-RMTIGEIIaeplrTYHPKLSRQEVKDRVKAMMLKvGLLPNLI- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 174 delkdrldqNAYG--LSGGQQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDY--SIIIVTHNMQQAA 249
Cdd:PRK15079 156 ---------NRYPheFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVK 226
|
250 260 270
....*....|....*....|....*....|....*..
gi 1374671911 250 RVSDKTAFFLNGYVNEYDDTDKIFSNPSDKQTEDYIS 286
Cdd:PRK15079 227 HISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMS 263
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
44-280 |
1.79e-21 |
|
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: 91.02 E-value: 1.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 44 YSTQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIFD-KSYPVEKL 122
Cdd:TIGR02769 12 YRTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEK-----PAQGTVSFRGQDLYQlDRKQRRAF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 123 RTNVGMVFQQ-PNPF-PKSIYDNITYGPRIHGIK-DKKILDEIVEKSLRGAAIWDELKDRLDQNaygLSGGQQQRVCIAR 199
Cdd:TIGR02769 87 RRDVQLVFQDsPSAVnPRMTVRQIIGEPLRHLTSlDESEQKARIAELLDMVGLRSEDADKLPRQ---LSGGQLQRINIAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 200 CLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDYSI--IIVTHNMQQAARVSDKTAFFLNG-YVNEYDDTDKI-FSN 275
Cdd:TIGR02769 164 ALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSFCQRVAVMDKGqIVEECDVAQLLsFKH 243
|
....*
gi 1374671911 276 PSDKQ 280
Cdd:TIGR02769 244 PAGRN 248
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
47-285 |
1.93e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 92.59 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTyvkaLNRMVELVPTvKTSGKILYRDQNIFDksypVEKLRTNV 126
Cdd:PRK11607 23 RNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKST----LLRMLAGFEQ-PTAGQIMLDGVDLSH----VPPYQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 127 GMVFQQPNPFPK-SIYDNITYGPRihgiKDKKILDEI---VEKSLRGAAIWDELKDRLDQnaygLSGGQQQRVCIARCLA 202
Cdd:PRK11607 94 NMMFQSYALFPHmTVEQNIAFGLK----QDKLPKAEIasrVNEMLGLVHMQEFAKRKPHQ----LSGGQRQRVALARSLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 203 IEPDVILMDEPTSALDPISTLRVEELVQDL--KKDYSIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNPSDKQ 280
Cdd:PRK11607 166 KRPKLLLLDEPMGALDKKLRDRMQLEVVDIleRVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRY 245
|
....*
gi 1374671911 281 TEDYI 285
Cdd:PRK11607 246 SAEFI 250
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
10-254 |
3.13e-21 |
|
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: 89.70 E-value: 3.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 10 HTEKVNDSHEKQPFIakdqTEKHETLSDRERRVVystqnldlwygeqHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKAL 89
Cdd:cd03267 5 NLSKSYRVYSKEPGL----IGSLKSLFKRKYREV-------------EALKGISFTIEKGEIVGFIGPNGAGKTTTLKIL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 90 NRMveLVPT---VKTSGKILYRDQNifdksypveKLRTNVGMVFQQPN------PFPKSIYDNitygPRIHGIKD---KK 157
Cdd:cd03267 68 SGL--LQPTsgeVRVAGLVPWKRRK---------KFLRRIGVVFGQKTqlwwdlPVIDSFYLL----AAIYDLPParfKK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 158 ILDEIVEKSlrgaaiwdELKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDY- 236
Cdd:cd03267 133 RLDELSELL--------DLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERg 204
|
250
....*....|....*....
gi 1374671911 237 -SIIIVTHNMQQAARVSDK 254
Cdd:cd03267 205 tTVLLTSHYMKDIEALARR 223
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
53-250 |
3.82e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 88.44 E-value: 3.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 53 YGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMveLVPTvktSGKIlyrdqnifdksypVEKLRTNVGMVFQQ 132
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGV--LRPT---SGTV-------------RRAGGARVAYVPQR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 133 ---PNPFPKSIYDNITYG-------PRIHGIKDKKIldeiVEKSLRGAAIWDELKDRLDQnaygLSGGQQQRVCIARCLA 202
Cdd:NF040873 64 sevPDSLPLTVRDLVAMGrwarrglWRRLTRDDRAA----VDDALERVGLADLAGRQLGE----LSGGQRQRALLAQGLA 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1374671911 203 IEPDVILMDEPTSALDPISTLRVEELVQDLKKD-YSIIIVTHNMQQAAR 250
Cdd:NF040873 136 QEADLLLLDEPTTGLDAESRERIIALLAEEHARgATVVVVTHDLELVRR 184
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
55-255 |
5.57e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 89.76 E-value: 5.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 55 EQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQNIfdKSYPVEKLRTNVGMVFQqpN 134
Cdd:COG1101 18 EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPP-----DSGSILIDGKDV--TKLPEYKRAKYIGRVFQ--D 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 135 PF----PK-SIYDNI--------TYGPRIhGIKDKKIlDEIVE--KSLR-GaaiwdeLKDRLDQNAYGLSGGQQQRVCIA 198
Cdd:COG1101 89 PMmgtaPSmTIEENLalayrrgkRRGLRR-GLTKKRR-ELFREllATLGlG------LENRLDTKVGLLSGGQRQALSLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1374671911 199 RCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDYSI--IIVTHNMQQAARVSDKT 255
Cdd:COG1101 161 MATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLttLMVTHNMEQALDYGNRL 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
53-254 |
5.59e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 92.40 E-value: 5.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 53 YGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIFDKSyPVEKLRTNVGMVFQQ 132
Cdd:COG3845 15 FGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQ-----PDSGEILIDGKPVRIRS-PRDAIALGIGMVHQH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 133 PNPFPK-SIYDNITYG--PRIHGIKD-KKILDEIVEKSLR-------GAAIWDelkdrldqnaygLSGGQQQRVCIARCL 201
Cdd:COG3845 89 FMLVPNlTVAENIVLGlePTKGGRLDrKAARARIRELSERygldvdpDAKVED------------LSVGEQQRVEILKAL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1374671911 202 AIEPDVILMDEPTSALDPISTLRVEELVQDLKKD-YSIIIVTHNMQQAARVSDK 254
Cdd:COG3845 157 YRGARILILDEPTAVLTPQEADELFEILRRLAAEgKSIIFITHKLREVMAIADR 210
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
47-243 |
7.69e-21 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 88.99 E-value: 7.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRmvELVPTvktSGKILYrdqnIFDKSY---PVEKLR 123
Cdd:COG1119 7 RNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG--DLPPT---YGNDVR----LFGERRggeDVWELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 124 TNVGMV---FQQPnpFPKSI----------YDNItygprihGIkDKKILDEIVEKSLRGAAIW--DELKDRLdqnaYG-L 187
Cdd:COG1119 78 KRIGLVspaLQLR--FPRDEtvldvvlsgfFDSI-------GL-YREPTDEQRERARELLELLglAHLADRP----FGtL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1374671911 188 SGGQQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDY--SIIIVTH 243
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGapTLVLVTH 201
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
39-282 |
7.85e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 92.23 E-value: 7.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 39 ERRVVYSTQNLDLWYGEQH----SLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELVPTVKTSGKILYRDQN--- 111
Cdd:PRK10261 8 DARDVLAVENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrqv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 112 IFDKSYPVEKLR----TNVGMVFQQP----NP-FPksIYDNITYGPRIH-GIKDKKILDEiVEKSLRGAAIwDELKDRLD 181
Cdd:PRK10261 88 IELSEQSAAQMRhvrgADMAMIFQEPmtslNPvFT--VGEQIAESIRLHqGASREEAMVE-AKRMLDQVRI-PEAQTILS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 182 QNAYGLSGGQQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDYS--IIIVTHNMQQAARVSDKTAFFL 259
Cdd:PRK10261 164 RYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRVLVMY 243
|
250 260
....*....|....*....|...
gi 1374671911 260 NGYVNEYDDTDKIFSNPSDKQTE 282
Cdd:PRK10261 244 QGEAVETGSVEQIFHAPQHPYTR 266
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
53-253 |
8.42e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 89.78 E-value: 8.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 53 YGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIfdksypVEKLRTNVG-Mvfq 131
Cdd:COG4152 11 FGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILA-----PDSGEVLWDGEPL------DPEDRRRIGyL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 132 qpnP-----FPK-SIYDNITYGPRIHGIKDKKI---LDEIVEKsLrgaaiwdELKDRLDQNAYGLSGGQQQRVCIARCLA 202
Cdd:COG4152 77 ---PeerglYPKmKVGEQLVYLARLKGLSKAEAkrrADEWLER-L-------GLGDRANKKVEELSKGNQQKVQLIAALL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1374671911 203 IEPDVILMDEPTSALDPISTLRVEELVQDLK-KDYSIIIVTHNMQQAARVSD 253
Cdd:COG4152 146 HDPELLILDEPFSGLDPVNVELLKDVIRELAaKGTTVIFSSHQMELVEELCD 197
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
47-280 |
9.75e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 88.41 E-value: 9.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTyvkALNRMVELVPtvKTSGKILYRDQNIfdKSYPV-EKLRTN 125
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTT---TFYMVVGIVP--RDAGNIIIDDEDI--SLLPLhARARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 126 VGMVFQQPNPFPK-SIYDNITYGPRIHGIKDKKILDEIVEKSLRGAAIwDELKDRLDQNaygLSGGQQQRVCIARCLAIE 204
Cdd:PRK10895 80 IGYLPQEASIFRRlSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHI-EHLRDSMGQS---LSGGERRRVEIARALAAN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1374671911 205 PDVILMDEPTSALDPISTLRVEELVQDLkKDY--SIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNPSDKQ 280
Cdd:PRK10895 156 PKFILLDEPFAGVDPISVIDIKRIIEHL-RDSglGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKR 232
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
53-272 |
1.00e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 88.60 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 53 YGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvPT---VKTSGKIlyrdqnifdkSYPVEklrtnVGMV 129
Cdd:COG1134 36 REEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILE--PTsgrVEVNGRV----------SALLE-----LGAG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 130 FQqpnpfPK-SIYDNITYGPRIHGIKDKKI---LDEIVEKSlrgaaiwdELKDRLDQ--NAYglSGGQQQRVCIARCLAI 203
Cdd:COG1134 99 FH-----PElTGRENIYLNGRLLGLSRKEIdekFDEIVEFA--------ELGDFIDQpvKTY--SSGMRARLAFAVATAV 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 204 EPDVILMDEPTSALDPISTLRVEELVQDLKKDY-SIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKI 272
Cdd:COG1134 164 DPDILLVDEVLAVGDAAFQKKCLARIRELRESGrTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEV 233
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
59-246 |
1.69e-20 |
|
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: 86.75 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALnrMVELVptvKTSGKIlyrdqnifdksypveKLRTNVGMVFQQPNPFPK 138
Cdd:cd03250 21 LKDINLEVPKGELVAIVGPVGSGKSSLLSAL--LGELE---KLSGSV---------------SVPGSIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 139 SIYDNITYGprihgikdKKILDEIVEKSLRGAAiwdeLKDRLDQNAYG-----------LSGGQQQRVCIARCLAIEPDV 207
Cdd:cd03250 81 TIRENILFG--------KPFDEERYEKVIKACA----LEPDLEILPDGdlteigekginLSGGQKQRISLARAVYSDADI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1374671911 208 ILMDEPTSALDP-ISTLRVEELVQ-DLKKDYSIIIVTHNMQ 246
Cdd:cd03250 149 YLLDDPLSAVDAhVGRHIFENCILgLLLNNKTRILVTHQLQ 189
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
59-218 |
1.72e-20 |
|
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: 91.03 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQNIfdKSYPVEKLRTNVGMVFQQPNPFPK 138
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDV-----TSGRILIDGQDI--RDVTQASLRAAIGIVPQDTVLFND 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 139 SIYDNITYGpRIHgikdkkILDEIVEKSLRGAAIwDELKDRLDQnAYG---------LSGGQQQRVCIARCLAIEPDVIL 209
Cdd:COG5265 447 TIAYNIAYG-RPD------ASEEEVEAAARAAQI-HDFIESLPD-GYDtrvgerglkLSGGEKQRVAIARTLLKNPPILI 517
|
....*....
gi 1374671911 210 MDEPTSALD 218
Cdd:COG5265 518 FDEATSALD 526
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
43-278 |
2.90e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 87.84 E-value: 2.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 43 VYSTQNLDLWYGEQ---HSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVE-LVPTVKTSGKILYRDQnifdksyp 118
Cdd:PRK13642 4 ILEVENLVFKYEKEsdvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEeFEGKVKIDGELLTAEN-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 119 VEKLRTNVGMVFQQP-NPF-PKSIYDNITYGPRIHGIKDKKILDEIVEkslrgAAIWDELKDRLDQNAYGLSGGQQQRVC 196
Cdd:PRK13642 76 VWNLRRKIGMVFQNPdNQFvGATVEDDVAFGMENQGIPREEMIKRVDE-----ALLAVNMLDFKTREPARLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 197 IARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDY--SIIIVTHNMQQAARvSDKTAFFLNGYVNEYDDTDKIFS 274
Cdd:PRK13642 151 VAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA 229
|
....
gi 1374671911 275 NPSD 278
Cdd:PRK13642 230 TSED 233
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
44-245 |
4.83e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 87.05 E-value: 4.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 44 YSTQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTyvkaLNRMveLVPTVK-TSGKILYRDQnifdksyPVEKL 122
Cdd:PRK10419 13 YAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKST----LARL--LVGLESpSQGNVSWRGE-------PLAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 123 --------RTNVGMVFQQP----NPfPKSIYDnITYGPRIHGIK-DKKILDEIVEKSLRGAAIWDELKDRLDQNaygLSG 189
Cdd:PRK10419 80 nraqrkafRRDIQMVFQDSisavNP-RKTVRE-IIREPLRHLLSlDKAERLARASEMLRAVDLDDSVLDKRPPQ---LSG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1374671911 190 GQQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDYSI--IIVTHNM 245
Cdd:PRK10419 155 GQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDL 212
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
41-275 |
6.03e-20 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 86.47 E-value: 6.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 41 RVVYSTQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALnrmveLVPTVKTSGKILYRDQNIFDksYPVE 120
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTL-----CGDPRATSGRIVFDGKDITD--WQTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 121 K-LRTNVGMVFQQPNPFPK-SIYDNITYGprihGIKDKKilDEIVEKSLRGAAIWDELKDRLDQNAYGLSGGQQQRVCIA 198
Cdd:PRK11614 76 KiMREAVAIVPEGRRVFSRmTVEENLAMG----GFFAER--DQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1374671911 199 RCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKD-YSIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSN 275
Cdd:PRK11614 150 RALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQgMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
54-253 |
7.71e-20 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 86.74 E-value: 7.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 54 GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTyvkaLNRMV--ELVPTvktSGKILYRDQNIFDKS----YPVeklRTNVG 127
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTT----LLRLIggQIAPD---HGEILFDGENIPAMSrsrlYTV---RKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 128 MVFQQPNPFPK-SIYDNITYGPRIHGIKDKKILDEIV-----EKSLRGAAiwdELKDRldqnayGLSGGQQQRVCIARCL 201
Cdd:PRK11831 88 MLFQSGALFTDmNVFDNVAYPLREHTQLPAPLLHSTVmmkleAVGLRGAA---KLMPS------ELSGGMARRAALARAI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1374671911 202 AIEPDVILMDEPTSALDPISTLRVEELVQDLKKDYSI--IIVTHNMQQAARVSD 253
Cdd:PRK11831 159 ALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVtcVVVSHDVPEVLSIAD 212
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
53-254 |
8.84e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 86.27 E-value: 8.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 53 YGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILyrdqnifDKSYPVEKLRTNVGMVFQQ 132
Cdd:PRK11247 22 YGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLET-----PSAGELL-------AGTAPLAEAREDTRLMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 133 PNPFP-KSIYDNITYGprihgikdkkildeiveksLRGAaiWDE----------LKDRLDQNAYGLSGGQQQRVCIARCL 201
Cdd:PRK11247 90 ARLLPwKKVIDNVGLG-------------------LKGQ--WRDaalqalaavgLADRANEWPAALSGGQKQRVALARAL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1374671911 202 AIEPDVILMDEPTSALDPISTLRVEELVQDL--KKDYSIIIVTHNMQQAARVSDK 254
Cdd:PRK11247 149 IHRPGLLLLDEPLGALDALTRIEMQDLIESLwqQHGFTVLLVTHDVSEAVAMADR 203
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
41-275 |
1.05e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 86.22 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 41 RVVYSTQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRM----------VELV-PTVKTSGKiLYRD 109
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdksagshIELLgRTVQREGR-LARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 110 qnifdksypVEKLRTNVGMVFQQPNPFPK-SIYDNITYGPR------------IHGIKDKKILDEIVEKSLRGAAiwdel 176
Cdd:PRK09984 81 ---------IRKSRANTGYIFQQFNLVNRlSVLENVLIGALgstpfwrtcfswFTREQKQRALQALTRVGMVHFA----- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 177 kdrlDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDYSIIIVT--HNMQQAARVSDK 254
Cdd:PRK09984 147 ----HQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVtlHQVDYALRYCER 222
|
250 260
....*....|....*....|.
gi 1374671911 255 TAFFLNGYVNeYDDTDKIFSN 275
Cdd:PRK09984 223 IVALRQGHVF-YDGSSQQFDN 242
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
59-251 |
1.18e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 88.63 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSG--KILYRDQNIFDKSYPVEKLRTNVGMVFQQPNPF 136
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDK-----PTSGtyRVAGQDVATLDADALAQLRREHFGFIFQRYHLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 137 PK-SIYDNITYgPRIHGIKDKKildeivEKSLRGAAIWDEL--KDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEP 213
Cdd:PRK10535 99 SHlTAAQNVEV-PAVYAGLERK------QRLLRAQELLQRLglEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1374671911 214 TSALDPISTLRVEELVQDLK-KDYSIIIVTHNMQ---QAARV 251
Cdd:PRK10535 172 TGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQvaaQAERV 213
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
59-261 |
1.21e-19 |
|
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: 85.21 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYvkaLNRMVELvpTVKTSGKILYRDQNIfDKSYPvEKLrtnvgMVFQQPNPFP- 137
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTL---LNLISGL--AQPTSGGVILEGKQI-TEPGP-DRM-----VVFQNYSLLPw 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 138 KSIYDNITYG-----PRIHGIKDKKILDEIVEK-SLRGAAiwdelKDRLDQnaygLSGGQQQRVCIARCLAIEPDVILMD 211
Cdd:TIGR01184 69 LTVRENIALAvdrvlPDLSKSERRAIVEEHIALvGLTEAA-----DKRPGQ----LSGGMKQRVAIARALSIRPKVLLLD 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1374671911 212 EPTSALDPISTLRVEELVQDLKKDY--SIIIVTHNMQQAARVSDKTAFFLNG 261
Cdd:TIGR01184 140 EPFGALDALTRGNLQEELMQIWEEHrvTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
59-255 |
1.33e-19 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 85.18 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNR--MVelvptvkTSGKILYRDQN-IFD--KSYPVEKL---RTNVGMVF 130
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnyLP-------DSGSILVRHDGgWVDlaQASPREILalrRRTIGYVS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 131 QqpnpFPKSIydnitygPRIHGIkdkkildEIVEKSL--RGAAIwDELKDR---------LDQNAYGL-----SGGQQQR 194
Cdd:COG4778 100 Q----FLRVI-------PRVSAL-------DVVAEPLleRGVDR-EEARARarellarlnLPERLWDLppatfSGGEQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1374671911 195 VCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKD-YSIIIVTHNMQQAARVSDKT 255
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARgTAIIGIFHDEEVREAVADRV 222
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
53-248 |
2.01e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 85.14 E-value: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 53 YGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYvkaLNRMVELVPTvkTSGKILYRDQnifdksyPVEKLRTNVGMVFQQ 132
Cdd:PRK11248 11 YGGKPALEDINLTLESGELLVVLGPSGCGKTTL---LNLIAGFVPY--QHGSITLDGK-------PVEGPGAERGVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 133 PNPFP-KSIYDNITYGPRIHGikdkkildeiVEKSLRGAAIWDELKdRLDQNAYG------LSGGQQQRVCIARCLAIEP 205
Cdd:PRK11248 79 EGLLPwRNVQDNVAFGLQLAG----------VEKMQRLEIAHQMLK-KVGLEGAEkryiwqLSGGQRQRVGIARALAANP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1374671911 206 DVILMDEPTSALDPISTLRVEELVQDLKKDY--SIIIVTHNMQQA 248
Cdd:PRK11248 148 QLLLLDEPFGALDAFTREQMQTLLLKLWQETgkQVLLITHDIEEA 192
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
59-252 |
3.26e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 84.10 E-value: 3.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMvelvpTVKTSGKILYRDQNIFDKSYPVE-KLRTN-VGMVFQQPNPF 136
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL-----DTPTSGDVIFNGQPMSKLSSAAKaELRNQkLGFIYQFHHLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 137 PK-SIYDNITYGPRIHGIKDKkildEIVEKSLRG-AAIwdELKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPT 214
Cdd:PRK11629 100 PDfTALENVAMPLLIGKKKPA----EINSRALEMlAAV--GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1374671911 215 SALDPISTLRVEELVQDL--KKDYSIIIVTHNMQQAARVS 252
Cdd:PRK11629 174 GNLDARNADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMS 213
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
45-250 |
3.31e-19 |
|
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: 84.02 E-value: 3.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 45 STQNLDLWY----GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTyvkALNRMVEL-VPTvktSGKILYRDQNIF----Dk 115
Cdd:COG4181 10 ELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKST---LLGLLAGLdRPT---SGTVRLAGQDLFaldeD- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 116 syPVEKLR-TNVGMVFQQ----PN---------PFPksiydnitygprIHGIKDKKIldeivekslRGAAIWDE--LKDR 179
Cdd:COG4181 83 --ARARLRaRHVGFVFQSfqllPTltalenvmlPLE------------LAGRRDARA---------RARALLERvgLGHR 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1374671911 180 LDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDY--SIIIVTHNMQQAAR 250
Cdd:COG4181 140 LDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgtTLVLVTHDPALAAR 212
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
47-274 |
9.24e-19 |
|
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: 86.01 E-value: 9.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELVPTvktSGKILYR------------------ 108
Cdd:TIGR03269 4 KNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPT---SGRIIYHvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 109 ------------DQNIFDKSYPVEK-LRTNVGMVFQQPNPF--PKSIYDNITYGPRIHGIKDKKILDeivekslRGAAIW 173
Cdd:TIGR03269 81 pcpvcggtlepeEVDFWNLSDKLRRrIRKRIAIMLQRTFALygDDTVLDNVLEALEEIGYEGKEAVG-------RAVDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 174 DE--LKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDY--SIIIVTHNMQQAA 249
Cdd:TIGR03269 154 EMvqLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEVIE 233
|
250 260
....*....|....*....|....*
gi 1374671911 250 RVSDKTAFFLNGYVNEYDDTDKIFS 274
Cdd:TIGR03269 234 DLSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
61-254 |
9.65e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 83.50 E-value: 9.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 61 NVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIfdKSYPVEKLrTNVGMV--FQQPNPFPK 138
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYK-----PTGGTILLRGQHI--EGLPGHQI-ARMGVVrtFQHVRLFRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 139 -SIYDNITYGPR-------IHGIKDKKILDEIVEKSLRGAAIWDE---LKDRLDQNAYGLSGGQQQRVCIARCLAIEPDV 207
Cdd:PRK11300 95 mTVIENLLVAQHqqlktglFSGLLKTPAFRRAESEALDRAATWLErvgLLEHANRQAGNLAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1374671911 208 ILMDEPTSALDPISTLRVEELVQDLKKDY--SIIIVTHNMQQAARVSDK 254
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGISDR 223
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-244 |
1.25e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 85.65 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 12 EKVNDSHEKQPFIAKDQTEKHETlsdreRRVVYSTQNLDLWY--GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKAL 89
Cdd:PRK11160 312 RRINEITEQKPEVTFPTTSTAAA-----DQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 90 NRmvELVPtvkTSGKILYRDQNIfdKSYPVEKLRTNVGMVFQQPNPFPKSIYDNITygprihgIKDKKILDEIVEKSLRG 169
Cdd:PRK11160 387 TR--AWDP---QQGEILLNGQPI--ADYSEAALRQAISVVSQRVHLFSATLRDNLL-------LAAPNASDEALIEVLQQ 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 170 AaiwdELKDRLDQ----NAY-G-----LSGGQQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDYSII 239
Cdd:PRK11160 453 V----GLEKLLEDdkglNAWlGeggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVL 528
|
....*
gi 1374671911 240 IVTHN 244
Cdd:PRK11160 529 MITHR 533
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
59-247 |
1.43e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 85.28 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALnrmvelvptvktSGKILYRDQ----NIFDKSYPVEKLRTNVGMVFQQPN 134
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNAL------------LGFLPYQGSlkinGIELRELDPESWRKHLSWVGQNPQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 135 PFPKSIYDNITYGprihgikDKKILDEIVEKSLRGAAIWD---ELKDRLD-----QNAyGLSGGQQQRVCIARCLAIEPD 206
Cdd:PRK11174 434 LPHGTLRDNVLLG-------NPDASDEQLQQALENAWVSEflpLLPQGLDtpigdQAA-GLSVGQAQRLALARALLQPCQ 505
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1374671911 207 VILMDEPTSALDPISTLRVEELVQDLKKDYSIIIVTHNMQQ 247
Cdd:PRK11174 506 LLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLED 546
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
53-267 |
1.93e-18 |
|
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: 81.81 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 53 YGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMveLVPT---VKTSGKIlyrdqnifdkSYPVEklrTNVGMv 129
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGI--YPPDsgtVTVRGRV----------SSLLG---LGGGF- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 130 fqQPNpfpKSIYDNITYGPRIHGIKDKKI---LDEIVEKSlrgaaiwdELKDRLDQNAYGLSGGQQQRVCIARCLAIEPD 206
Cdd:cd03220 96 --NPE---LTGRENIYLNGRLLGLSRKEIdekIDEIIEFS--------ELGDFIDLPVKTYSSGMKARLAFAIATALEPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1374671911 207 VILMDEPTSALDPISTLRVEELVQDLKKDYSIII-VTHNMQQAARVSDKTAFFLNGYVNEYD 267
Cdd:cd03220 163 ILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVIlVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-274 |
2.20e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 84.85 E-value: 2.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 1 MNNIKELEKHTEkvndSHEKQPFIAKDQTEKHETLSDRerrvvystqnldlwyGEQHSLKNVNLDILEKNVTAIIGPSGS 80
Cdd:TIGR03269 261 MEGVSEVEKECE----VEVGEPIIKVRNVSKRYISVDR---------------GVVKAVDNVSLEVKEGEIFGIVGTSGA 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 81 GKSTYVKALNRMVElvptvKTSGKILYR--DQNI-FDKSYPVEKLRTN--VGMVFQQPNPFP-KSIYDNITygprihgik 154
Cdd:TIGR03269 322 GKTTLSKIIAGVLE-----PTSGEVNVRvgDEWVdMTKPGPDGRGRAKryIGILHQEYDLYPhRTVLDNLT--------- 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 155 DKKILDEIVEKSLRGAAI------WDELKDR--LDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVE 226
Cdd:TIGR03269 388 EAIGLELPDELARMKAVItlkmvgFDEEKAEeiLDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVT 467
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1374671911 227 ELVQDLKKDY--SIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFS 274
Cdd:TIGR03269 468 HSILKAREEMeqTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
50-274 |
4.70e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 81.98 E-value: 4.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 50 DLW--YGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMveLVPTvktSGKILYRDQNIFDKSYPVEKLRTNVG 127
Cdd:PRK13638 6 DLWfrYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGL--LRPQ---KGAVLWQGKPLDYSKRGLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 128 MVFQQPNP--FPKSIYDNITYGPRIHGIKDkkilDEIVEKSLRGAAIWDELKDRlDQNAYGLSGGQQQRVCIARCLAIEP 205
Cdd:PRK13638 81 TVFQDPEQqiFYTDIDSDIAFSLRNLGVPE----AEITRRVDEALTLVDAQHFR-HQPIQCLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 206 DVILMDEPTSALDPISTLRVEELVQDL-KKDYSIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFS 274
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIvAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
59-243 |
4.86e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 83.70 E-value: 4.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNrmvELVPTvkTSGKILY-RDQNIF---DKSY-PVEKLRtnvgmvfqqp 133
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIA---GLWPY--GSGRIARpAGARVLflpQRPYlPLGTLR---------- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 134 npfpksiyDNITYgPRIHGikdkKILDEIVEKSLRGAAIwDELKDRLDQNA---YGLSGGQQQRVCIARCLAIEPDVILM 210
Cdd:COG4178 444 --------EALLY-PATAE----AFSDAELREALEAVGL-GHLAERLDEEAdwdQVLSLGEQQRLAFARLLLHKPDWLFL 509
|
170 180 190
....*....|....*....|....*....|...
gi 1374671911 211 DEPTSALDPISTLRVEELVQDLKKDYSIIIVTH 243
Cdd:COG4178 510 DEATSALDEENEAALYQLLREELPGTTVISVGH 542
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
45-290 |
1.49e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 81.81 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 45 STQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMveLVPTvktSGKILYRDQNIFDKSypVEKLRT 124
Cdd:PRK09536 5 DVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGT--LTPT---AGTVLVAGDDVEALS--ARAASR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 125 NVGMVFQQPN-PFPKSIYDNITYGPRIH-------GIKDKKILDEIVEKSlrGAAIWdelkdrLDQNAYGLSGGQQQRVC 196
Cdd:PRK09536 78 RVASVPQDTSlSFEFDVRQVVEMGRTPHrsrfdtwTETDRAAVERAMERT--GVAQF------ADRPVTSLSGGERQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 197 IARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKD-YSIIIVTHNMQQAARVSDKTAFFLNGYVNEyddtdkiFSN 275
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDLAARYCDELVLLADGRVRA-------AGP 222
|
250
....*....|....*
gi 1374671911 276 PSDKQTEDYISGRFG 290
Cdd:PRK09536 223 PADVLTADTLRAAFD 237
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
60-276 |
2.28e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 79.36 E-value: 2.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 60 KNVNLDILEKNVTAIIGPSGSGKSTYVKALnrmVELVP--TVKTSGKILYRDQnifdksyPVE--KLR-TNVGMVFQQPn 134
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAA---LGILPagVRQTAGRVLLDGK-------PVApcALRgRKIATIMQNP- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 135 pfpKSIYdNITYGPRIHGIKDKKIL-----DEIVEKSLRGAAIwDELKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVIL 209
Cdd:PRK10418 89 ---RSAF-NPLHTMHTHARETCLALgkpadDATLTAALEAVGL-ENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1374671911 210 MDEPTSALDPISTLRVEELVQDL--KKDYSIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNP 276
Cdd:PRK10418 164 ADEPTTDLDVVAQARILDLLESIvqKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAP 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
46-243 |
3.55e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 81.26 E-value: 3.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 46 TQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRmvELVPtvkTSGKILYRDqnifdksypveklRTN 125
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAG--ELEP---DSGEVSIPK-------------GLR 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 126 VGMVFQQPNPFP-KSIYDNITYG-PRIHGIKDK--KILDEIVEKSLRGAAIwDELKDRLDQ-NAYG-------------- 186
Cdd:COG0488 63 IGYLPQEPPLDDdLTVLDTVLDGdAELRALEAEleELEAKLAEPDEDLERL-AELQEEFEAlGGWEaearaeeilsglgf 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1374671911 187 -----------LSGGQQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKdySIIIVTH 243
Cdd:COG0488 142 peedldrpvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPG--TVLVVSH 207
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
47-261 |
8.19e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 78.69 E-value: 8.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALnrmveLVPTVKTSGKILYRDQNIFDKSypvEKLRTNV 126
Cdd:PRK13537 11 RNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRML-----LGLTHPDAGSISLCGEPVPSRA---RHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 127 GMVFQQPNPFPK-SIYDNITYGPRIHGIKDKKIlDEIVEKSLRGAaiwdELKDRLDQNAYGLSGGQQQRVCIARCLAIEP 205
Cdd:PRK13537 83 GVVPQFDNLDPDfTVRENLLVFGRYFGLSAAAA-RALVPPLLEFA----KLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1374671911 206 DVILMDEPTSALDPIST-LRVEELVQDLKKDYSIIIVTHNMQQAARVSDKTAFFLNG 261
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARhLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
40-281 |
8.81e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 80.13 E-value: 8.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 40 RRVVystqnldlwyGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVelvptvKTSGKILYRDQnifdksyPV 119
Cdd:PRK15134 293 KRTV----------DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI------NSQGEIWFDGQ-------PL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 120 EKL--------RTNVGMVFQQPNPF--PK-SIYDNITYGPRIHgikdkkildeivEKSLRGAAIWDELKDRLDQnaYGL- 187
Cdd:PRK15134 350 HNLnrrqllpvRHRIQVVFQDPNSSlnPRlNVLQIIEEGLRVH------------QPTLSAAQREQQVIAVMEE--VGLd 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 188 -----------SGGQQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDYSI--IIVTHNMQQAARVSDK 254
Cdd:PRK15134 416 petrhrypaefSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRALCHQ 495
|
250 260
....*....|....*....|....*..
gi 1374671911 255 TAFFLNGYVNEYDDTDKIFSNPSDKQT 281
Cdd:PRK15134 496 VIVLRQGEVVEQGDCERVFAAPQQEYT 522
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
59-250 |
8.94e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 77.51 E-value: 8.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNI--FDKSYPVEKLRTNVGMVFQQPNPF 136
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDD-----GSSGEVSLVGQPLhqMDEEARAKLRAKHVGFVFQSFMLI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 137 PK-SIYDNITYGPRIHGIKDKKILDEIVE--KSLrgaaiwdELKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEP 213
Cdd:PRK10584 101 PTlNALENVELPALLRGESSRQSRNGAKAllEQL-------GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 1374671911 214 TSALDPISTLRVEELVQDLKKDY--SIIIVTHNMQQAAR 250
Cdd:PRK10584 174 TGNLDRQTGDKIADLLFSLNREHgtTLILVTHDLQLAAR 212
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
52-250 |
2.32e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 76.07 E-value: 2.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 52 WYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKalnrmveLVPTVK--TSGKILYRDQNIFD-KSYPVEKLRTNVGM 128
Cdd:PRK10908 11 YLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLK-------LICGIErpSAGKIWFSGHDITRlKNREVPFLRRQIGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 129 VFQQPNPF-PKSIYDNITYGPRIHGIKDKKILDEiVEKSLRGAAIWDELKDRLDQnaygLSGGQQQRVCIARCLAIEPDV 207
Cdd:PRK10908 84 IFQDHHLLmDRTVYDNVAIPLIIAGASGDDIRRR-VSAALDKVGLLDKAKNFPIQ----LSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1374671911 208 ILMDEPTSALDPISTLRVEELVQDLKK-DYSIIIVTHNMQQAAR 250
Cdd:PRK10908 159 LLADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHDIGLISR 202
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
22-243 |
2.54e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 76.15 E-value: 2.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 22 PFIAKDQTEKH-ETLSDRERRVVYSTQNLDLWY--GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMvelvpt 98
Cdd:COG2401 6 PFFVLMRVTKVySSVLDLSERVAIVLEAFGVELrvVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 99 vktsgkilyrdqnifdksypvEKLRTNVGMVFQQPNPFP--KSIYDNItygPRIHGIKDKKILDEIVekSLRGAAIWdel 176
Cdd:COG2401 80 ---------------------LKGTPVAGCVDVPDNQFGreASLIDAI---GRKGDFKDAVELLNAV--GLSDAVLW--- 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1374671911 177 KDRLDQnaygLSGGQQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDL--KKDYSIIIVTH 243
Cdd:COG2401 131 LRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLarRAGITLVVATH 195
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-267 |
3.05e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.57 E-value: 3.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 4 IKELEKHTEKVNDSHEKQPFIAKDQTEkhetlsdRERRVVYSTQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKS 83
Cdd:COG0488 283 IKALEKLEREEPPRRDKTVEIRFPPPE-------RLGKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKS 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 84 TYVKALNRmvELVPTvktSGKIlyrdqnifdksypveKLRTNVGMVF--QQPNPFP--KSIYDNITYGprihgikdkkiL 159
Cdd:COG0488 356 TLLKLLAG--ELEPD---SGTV---------------KLGETVKIGYfdQHQEELDpdKTVLDELRDG-----------A 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 160 DEIVEKSLRGAaiwdeLK------DRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPTSALDpISTLRV-EELVQdl 232
Cdd:COG0488 405 PGGTEQEVRGY-----LGrflfsgDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD-IETLEAlEEALD-- 476
|
250 260 270
....*....|....*....|....*....|....*..
gi 1374671911 233 kkDY--SIIIVTHNMQQAARVSDKTAFFLNGYVNEYD 267
Cdd:COG0488 477 --DFpgTVLLVSHDRYFLDRVATRILEFEDGGVREYP 511
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
52-246 |
1.46e-15 |
|
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: 73.90 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 52 WYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALnrmveLVPTVKTSGKILYRDQNIFDKSYPVEKLRT--NVGMV 129
Cdd:cd03290 10 WGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAI-----LGEMQTLEGKVHWSNKNESEPSFEATRSRNrySVAYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 130 FQQPNPFPKSIYDNITYGPRIHGIKDKKILDEIvekSLRGAAiwdELKDRLDQNAYG-----LSGGQQQRVCIARCLAIE 204
Cdd:cd03290 85 AQKPWLLNATVEENITFGSPFNKQRYKAVTDAC---SLQPDI---DLLPFGDQTEIGerginLSGGQRQRICVARALYQN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1374671911 205 PDVILMDEPTSAL-----DPISTLRVEELVQDLKKdySIIIVTHNMQ 246
Cdd:cd03290 159 TNIVFLDDPFSALdihlsDHLMQEGILKFLQDDKR--TLVLVTHKLQ 203
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
53-254 |
1.86e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 75.25 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 53 YGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTyvkaLNRMVeLVPTVKTSGKILYRDQNIFDKsypVEKLRTNVGMVFQQ 132
Cdd:PRK13536 51 YGDKAVVNGLSFTVASGECFGLLGPNGAGKST----IARMI-LGMTSPDAGKITVLGVPVPAR---ARLARARIGVVPQF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 133 PNPFPK-SIYDNITYGPRIHGIKDKKIldEIVEKSLRGAAiwdELKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMD 211
Cdd:PRK13536 123 DNLDLEfTVRENLLVFGRYFGMSTREI--EAVIPSLLEFA---RLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1374671911 212 EPTSALDPIST-LRVEELVQDLKKDYSIIIVTHNMQQAARVSDK 254
Cdd:PRK13536 198 EPTTGLDPHARhLIWERLRSLLARGKTILLTTHFMEEAERLCDR 241
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
54-243 |
2.01e-15 |
|
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: 76.23 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 54 GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKAlnrMVELVPTvkTSGKI------LYR-DQNIFDKSypveklrtnV 126
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARL---IVGIWPP--TSGSVrldgadLKQwDRETFGKH---------I 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 127 GMVFQQPNPFPKSIYDNITygpRIHGIKDKkilDEIVEKS-LRGAaiwDELKDRLdQNAY---------GLSGGQQQRVC 196
Cdd:TIGR01842 395 GYLPQDVELFPGTVAENIA---RFGENADP---EKIIEAAkLAGV---HELILRL-PDGYdtvigpggaTLSGGQRQRIA 464
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1374671911 197 IARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKK-DYSIIIVTH 243
Cdd:TIGR01842 465 LARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKArGITVVVITH 512
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-245 |
3.06e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 75.84 E-value: 3.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 3 NIKELEKHTEKVNDSHE---KQPFIAKDQTEKheTLSDRERrvvYSTQNLDLWYGEQHSL---KNVNLDILEKNVTAIIG 76
Cdd:PTZ00265 344 NITEYMKSLEATNSLYEiinRKPLVENNDDGK--KLKDIKK---IQFKNVRFHYDTRKDVeiyKDLNFTLTEGKTYAFVG 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 77 PSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIFdKSYPVEKLRTNVGMVFQQPNPFPKSIYDNITYGprIHGIKDK 156
Cdd:PTZ00265 419 ESGCGKSTILKLIERLYD-----PTEGDIIINDSHNL-KDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYS--LYSLKDL 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 157 KILDEIVEK-------------SLRGAAIWD------------------------------------------ELKDRLD 181
Cdd:PTZ00265 491 EALSNYYNEdgndsqenknkrnSCRAKCAGDlndmsnttdsneliemrknyqtikdsevvdvskkvlihdfvsALPDKYE 570
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 182 ----QNAYGLSGGQQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDYS--IIIVTHNM 245
Cdd:PTZ00265 571 tlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENriTIIIAHRL 640
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
47-243 |
8.29e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 74.37 E-value: 8.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHS-LKNVNLDILEKNVTAIIGPSGSGKSTYVKALnrMVELVPTvktSGKILYRDQNIFDKSYPVekLRTN 125
Cdd:PRK10790 344 DNVSFAYRDDNLvLQNINLSVPSRGFVALVGHTGSGKSTLASLL--MGYYPLT---EGEIRLDGRPLSSLSHSV--LRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 126 VGMVFQQPNPFPKSIYDNITYGPRIHGIKDKKILdEIVEKSLRGAAIWDELKDRLDQNAYGLSGGQQQRVCIARCLAIEP 205
Cdd:PRK10790 417 VAMVQQDPVVLADTFLANVTLGRDISEEQVWQAL-ETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTP 495
|
170 180 190
....*....|....*....|....*....|....*...
gi 1374671911 206 DVILMDEPTSALDPISTLRVEELVQDLKKDYSIIIVTH 243
Cdd:PRK10790 496 QILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAH 533
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
68-276 |
9.56e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 73.24 E-value: 9.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 68 EKNVTAIIGPSGSGKSTYVKALNRMVELvPTVKTSGKILYRDQNIFDKSypvEKLR-----TNVGMVFQQP----NPFPK 138
Cdd:PRK11022 32 QGEVVGIVGESGSGKSVSSLAIMGLIDY-PGRVMAEKLEFNGQDLQRIS---EKERrnlvgAEVAMIFQDPmtslNPCYT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 139 SIYdNITYGPRIHGIKDKKILDEIVEKSLRGAAIWDElKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPTSALD 218
Cdd:PRK11022 108 VGF-QIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDP-ASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALD 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 219 PISTLRVEELVQDL--KKDYSIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNP 276
Cdd:PRK11022 186 VTIQAQIIELLLELqqKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
58-261 |
1.56e-14 |
|
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: 73.89 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 58 SLKNVNLDILEKNVTAIIGPSGSGKSTyvkALNRMVELVPtvKTSGKILYRDQNIfdkSYPVEKLRTNVGMVFQQPNPFP 137
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTT---TLSILTGLLP--PTSGTVLVGGKDI---ETNLDAVRQSLGMCPQHNILFH 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 138 K-SIYDNITYGPRIHGIKDKkildeivEKSLRGAAIWDE--LKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPT 214
Cdd:TIGR01257 1017 HlTVAEHILFYAQLKGRSWE-------EAQLEMEAMLEDtgLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1374671911 215 SALDPISTLRVEELVQDLKKDYSIIIVTHNMQQAARVSDKTAFFLNG 261
Cdd:TIGR01257 1090 SGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
71-245 |
1.91e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 73.30 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 71 VTAIIGPSGSGKSTYVKALNRmvELVP------------TV--KTSGKILyrdQNIFDKSY-----PVEKLRtnvgMVFQ 131
Cdd:PRK13409 101 VTGILGPNGIGKTTAVKILSG--ELIPnlgdyeeepswdEVlkRFRGTEL---QNYFKKLYngeikVVHKPQ----YVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 132 QPNPFPKSIYDNITygprihGIKDKKILDEIVEKSlrgaaiwdELKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMD 211
Cdd:PRK13409 172 IPKVFKGKVRELLK------KVDERGKLDEVVERL--------GLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190
....*....|....*....|....*....|....
gi 1374671911 212 EPTSALDPISTLRVEELVQDLKKDYSIIIVTHNM 245
Cdd:PRK13409 238 EPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
55-243 |
5.60e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 71.67 E-value: 5.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 55 EQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQNIFDksYPVEKLRTNVGMVFQQPN 134
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDV-----SEGDIRFHDIPLTK--LQLDSWRSRLAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 135 PFPKSIYDNITYGprihgiKDKKILDEIvEKSLRGAAIWDELKdRLDQnAYG---------LSGGQQQRVCIARCLAIEP 205
Cdd:PRK10789 400 LFSDTVANNIALG------RPDATQQEI-EHVARLASVHDDIL-RLPQ-GYDtevgergvmLSGGQKQRISIARALLLNA 470
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1374671911 206 DVILMDEPTSALDPistlRVE-ELVQDLK---KDYSIIIVTH 243
Cdd:PRK10789 471 EILILDDALSAVDG----RTEhQILHNLRqwgEGRTVIISAH 508
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
52-255 |
7.26e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.91 E-value: 7.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 52 WYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQnifdksyPVEK-LRTN-VGMV 129
Cdd:PRK15056 16 WRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRL-----ASGKISILGQ-------PTRQaLQKNlVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 130 FQQPN---PFPKSIYDNITYGP-------RIHGIKDKKILDEIVEKSlrgaaiwDELKDRLDQNAYgLSGGQQQRVCIAR 199
Cdd:PRK15056 84 PQSEEvdwSFPVLVEDVVMMGRyghmgwlRRAKKRDRQIVTAALARV-------DMVEFRHRQIGE-LSGGQKKRVFLAR 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1374671911 200 CLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDYSIIIV-THNMQQAARVSDKT 255
Cdd:PRK15056 156 AIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVsTHNLGSVTEFCDYT 212
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
59-243 |
8.61e-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: 67.56 E-value: 8.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNrmvELVPTvkTSGKIlyrdqnifdkSYPVeklRTNVGMVFQQPnpfpk 138
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALA---GLWPW--GSGRI----------GMPE---GEDLLFLPQRP----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 139 siydnitYGPRihGikdkkildeivekSLRGAAI--WDELkdrldqnaygLSGGQQQRVCIARCLAIEPDVILMDEPTSA 216
Cdd:cd03223 74 -------YLPL--G-------------TLREQLIypWDDV----------LSGGEQQRLAFARLLLHKPKFVFLDEATSA 121
|
170 180
....*....|....*....|....*..
gi 1374671911 217 LDPISTLRVEELVQDLKkdYSIIIVTH 243
Cdd:cd03223 122 LDEESEDRLYQLLKELG--ITVISVGH 146
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
53-254 |
1.34e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.58 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 53 YGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKIlyrdqNIFDKSYP--VEKLRTN--VGM 128
Cdd:PRK09700 15 FGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHE-----PTKGTI-----TINNINYNklDHKLAAQlgIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 129 VFQQPNPFPK-SIYDNITYG----PRIHGIKdkkILDeIVEKSLRGAAIWDE--LKDRLDQNAYGLSGGQQQRVCIARCL 201
Cdd:PRK09700 85 IYQELSVIDElTVLENLYIGrhltKKVCGVN---IID-WREMRVRAAMMLLRvgLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1374671911 202 AIEPDVILMDEPTSALDPISTLRVEELVQDLKKD-YSIIIVTHNMQQAARVSDK 254
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEgTAIVYISHKLAEIRRICDR 214
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
68-245 |
1.59e-13 |
|
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: 70.58 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 68 EKNVTAIIGPSGSGKSTYVKALNRmvELVPTV--------------KTSGKILyrdQNIFDKSYPvEKLRTNVgmvfqqp 133
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSG--ELKPNLgdydeepswdevlkRFRGTEL---QDYFKKLAN-GEIKVAH------- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 134 npfpKSIY-DNItygPRIHGIKDKKILDEIVEkslRGAaiWDELKDRL------DQNAYGLSGGQQQRVCIARCLAIEPD 206
Cdd:COG1245 165 ----KPQYvDLI---PKVFKGTVRELLEKVDE---RGK--LDELAEKLglenilDRDISELSGGELQRVAIAAALLRDAD 232
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1374671911 207 VILMDEPTSALDPISTLRVEELVQDL-KKDYSIIIVTHNM 245
Cdd:COG1245 233 FYFFDEPSSYLDIYQRLNVARLIRELaEEGKYVLVVEHDL 272
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
71-245 |
1.72e-13 |
|
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: 68.55 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 71 VTAIIGPSGSGKSTYVKALNRmvELVPTVKTSGK------IL--YRD---QNIFdksypvEKLRTNVGMVFQQP---NPF 136
Cdd:cd03236 28 VLGLVGPNGIGKSTALKILAG--KLKPNLGKFDDppdwdeILdeFRGselQNYF------TKLLEGDVKVIVKPqyvDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 137 PKSIYDNItyGPRIHGIKDKKILDEIVEKSlrgaaiwdELKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPTSA 216
Cdd:cd03236 100 PKAVKGKV--GELLKKKDERGKLDELVDQL--------ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
170 180 190
....*....|....*....|....*....|
gi 1374671911 217 LDPISTLRVEELVQDL-KKDYSIIIVTHNM 245
Cdd:cd03236 170 LDIKQRLNAARLIRELaEDDNYVLVVEHDL 199
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
47-261 |
1.84e-13 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 66.32 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRmvELVPTvktSGKILyRDQNIfdksypveklrtnv 126
Cdd:cd03221 4 ENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG--ELEPD---EGIVT-WGSTV-------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 127 gmvfqqpnpfpksiydNITYgprihgikdkkildeivekslrgaaiwdelkdrLDQnaygLSGGQQQRVCIARCLAIEPD 206
Cdd:cd03221 64 ----------------KIGY---------------------------------FEQ----LSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1374671911 207 VILMDEPTSALDPISTLRVEELVQDLKKdySIIIVTHNMQQAARVSDKTAFFLNG 261
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEALKEYPG--TVILVSHDRYFLDQVATKIIELEDG 143
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
59-244 |
2.57e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 67.21 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTyvkaLNR-MVELVPTVktSGKILYRDQNIFDksypveklrtnvgmvfqqPNPFP 137
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTT----LLRlIAGLLPPA--AGTIKLDGGDIDD------------------PDVAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 138 KSIY--------------DNITYGPRIHGIKDKKILDEIvekslrgAAIwdELKDRLDQNAYGLSGGQQQRVCIARCLAI 203
Cdd:PRK13539 74 ACHYlghrnamkpaltvaENLEFWAAFLGGEELDIAAAL-------EAV--GLAPLAHLPFGYLSAGQKRRVALARLLVS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1374671911 204 EPDVILMDEPTSALDPISTLRVEELVQD-LKKDYSIIIVTHN 244
Cdd:PRK13539 145 NRPIWILDEPTAALDAAAVALFAELIRAhLAQGGIVIAATHI 186
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
58-274 |
3.89e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 68.99 E-value: 3.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 58 SLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIFDKSYPvEKLRTNVGMVFQQPNPF- 136
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQ-----KDSGSILFQGKEIDFKSSK-EALENGISMVHQELNLVl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 137 PKSIYDNITYG--PRIHGIKD-KKILDEIvekslrgAAIWDELKDRLD--QNAYGLSGGQQQRVCIARCLAIEPDVILMD 211
Cdd:PRK10982 87 QRSVMDNMWLGryPTKGMFVDqDKMYRDT-------KAIFDELDIDIDprAKVATLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1374671911 212 EPTSALDPISTLRVEELVQDLK-KDYSIIIVTHNMQQAARVSDKTAFFLNG-YVNEYD----DTDKIFS 274
Cdd:PRK10982 160 EPTSSLTEKEVNHLFTIIRKLKeRGCGIVYISHKMEEIFQLCDEITILRDGqWIATQPlaglTMDKIIA 228
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
38-246 |
7.31e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 67.42 E-value: 7.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 38 RERRVVystqnldlwygeqHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMveLVPT---VKTSGKILYRDQNifd 114
Cdd:COG4586 30 REYREV-------------EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGI--LVPTsgeVRVLGYVPFKRRK--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 115 ksypveKLRTNVGMVFQQpnpfpKS-------IYDNITYGPRIHGIKD---KKILDEIVEKsLrgaaiwdELKDRLDQNA 184
Cdd:COG4586 92 ------EFARRIGVVFGQ-----RSqlwwdlpAIDSFRLLKAIYRIPDaeyKKRLDELVEL-L-------DLGELLDTPV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1374671911 185 YGLSGGQQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDY--SIIIVTHNMQ 246
Cdd:COG4586 153 RQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMD 216
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
59-261 |
1.20e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.72 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIFDKSyPVEKLRTNVGMVFQQPNPFPK 138
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYT-----RDAGSILYLGKEVTFNG-PKSSQEAGIGIIHQELNLIPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 139 -SIYDNITYG----PRIHGIKDKKILDEIvekslrgaaiwDELKDRL------DQNAYGLSGGQQQRVCIARCLAIEPDV 207
Cdd:PRK10762 94 lTIAENIFLGrefvNRFGRIDWKKMYAEA-----------DKLLARLnlrfssDKLVGELSIGEQQMVEIAKVLSFESKV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1374671911 208 ILMDEPTSALDPISTLRVEELVQDLK-KDYSIIIVTHNMQQAARVSDKTAFFLNG 261
Cdd:PRK10762 163 IIMDEPTDALTDTETESLFRVIRELKsQGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
59-268 |
1.67e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 67.24 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRmvELVPTvktSGKILYRDQNIFDKSyPVEKLRTNVGMVFQQPNPFPK 138
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSG--NYQPD---AGSILIDGQEMRFAS-TTAALAAGVAIIYQELHLVPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 139 -SIYDNITYG--PRIHGIKDKKILDEIVEKSLrgaaiwDELKDRLDQNA---YgLSGGQQQRVCIARCLAIEPDVILMDE 212
Cdd:PRK11288 94 mTVAENLYLGqlPHKGGIVNRRLLNYEAREQL------EHLGVDIDPDTplkY-LSIGQRQMVEIAKALARNARVIAFDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1374671911 213 PTSALDPISTLRVEELVQDLKKDYSIII-VTHNMQQAARVSDKTAFFLNG-YVNEYDD 268
Cdd:PRK11288 167 PTSSLSAREIEQLFRVIRELRAEGRVILyVSHRMEEIFALCDAITVFKDGrYVATFDD 224
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
47-243 |
2.02e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.43 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMvelvPTVK-TSGKILYRDQNIFDKSyPVEKLRTN 125
Cdd:CHL00131 11 KNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH----PAYKiLEGDILFKGESILDLE-PEERAHLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 126 VGMVFQQPNPFP--------KSIYDN--ITYG-PRIHGIKDKKILDEIVEKSlrgaaiwdELKDR-LDQNAY-GLSGGQQ 192
Cdd:CHL00131 86 IFLAFQYPIEIPgvsnadflRLAYNSkrKFQGlPELDPLEFLEIINEKLKLV--------GMDPSfLSRNVNeGFSGGEK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1374671911 193 QRVCIARCLAIEPDVILMDEPTSALDpISTLRV--EELVQDLKKDYSIIIVTH 243
Cdd:CHL00131 158 KRNEILQMALLDSELAILDETDSGLD-IDALKIiaEGINKLMTSENSIILITH 209
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
139-253 |
2.44e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 66.58 E-value: 2.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 139 SIYDNITYgPRIHGIKDKKILDEiveKSLRGAAiwDELKDRL-------DQNAYGLSGGQQQRVCIARCLAIEPDVILMD 211
Cdd:COG1129 346 SIRENITL-ASLDRLSRGGLLDR---RRERALA--EEYIKRLriktpspEQPVGNLSGGNQQKVVLAKWLATDPKVLILD 419
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1374671911 212 EPTSALDpISTlRVE--ELVQDLKKD-YSIIIVTHNMQQAARVSD 253
Cdd:COG1129 420 EPTRGID-VGA-KAEiyRLIRELAAEgKAVIVISSELPELLGLSD 462
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
54-218 |
3.64e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 66.69 E-value: 3.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 54 GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALnrMVELVPTVKTSGKIlyrdqnifdksypveklRTNVGMVFQQP 133
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAM--LGELPPRSDASVVI-----------------RGTVAYVPQVS 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 134 NPFPKSIYDNITYGPRIHGIKdkkildeiVEKSLRGAAIWDELkDRL---DQNAYG-----LSGGQQQRVCIARCLAIEP 205
Cdd:PLN03130 689 WIFNATVRDNILFGSPFDPER--------YERAIDVTALQHDL-DLLpggDLTEIGergvnISGGQKQRVSMARAVYSNS 759
|
170
....*....|...
gi 1374671911 206 DVILMDEPTSALD 218
Cdd:PLN03130 760 DVYIFDDPLSALD 772
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
71-218 |
4.32e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 64.48 E-value: 4.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 71 VTAIIGPSGSGKSTyvkALNRMVELVPTvktSGKILYRDQNIfdKSYPVEKLRTNVGMVFQQ-PNPFPKSIYDNIT-YGP 148
Cdd:COG4138 24 LIHLIGPNGAGKST---LLARMAGLLPG---QGEILLNGRPL--SDWSAAELARHRAYLSQQqSPPFAMPVFQYLAlHQP 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1374671911 149 RIHGI-KDKKILDEIVEKsLRgaaiwdeLKDRLDQNAYGLSGGQQQRVCIAR-CLAIEPDV------ILMDEPTSALD 218
Cdd:COG4138 96 AGASSeAVEQLLAQLAEA-LG-------LEDKLSRPLTQLSGGEWQRVRLAAvLLQVWPTInpegqlLLLDEPMNSLD 165
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
54-276 |
4.61e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 65.31 E-value: 4.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 54 GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALnrmvelVPTVKTSGKI-----LYRDQNIFDKSyPVEK---LRTN 125
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAI------CGITKDNWHVtadrfRWNGIDLLKLS-PRERrkiIGRE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 126 VGMVFQQPNpfpkSIYDnitygPrihgikDKKILDEIVE----KSLRGAaIWDELKDRLDQ-----------------NA 184
Cdd:COG4170 91 IAMIFQEPS----SCLD-----P------SAKIGDQLIEaipsWTFKGK-WWQRFKWRKKRaiellhrvgikdhkdimNS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 185 YG--LSGGQQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKK--DYSIIIVTHNMQQAARVSDKTAFFLN 260
Cdd:COG4170 155 YPheLTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlqGTSILLISHDLESISQWADTITVLYC 234
|
250
....*....|....*.
gi 1374671911 261 GYVNEYDDTDKIFSNP 276
Cdd:COG4170 235 GQTVESGPTEQILKSP 250
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
66-257 |
7.91e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.21 E-value: 7.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 66 ILEKNVTAIIGPSGSGKSTYVKALNRmvELVPT---VKTSGKILYRDQNIF-DKSYPVEKLrtnvgmVFQQPNPFPKSIY 141
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAG--VLKPDegeVDPELKISYKPQYIKpDYDGTVEDL------LRSITDDLGSSYY 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 142 DNitygprihgikdkkildEIVEKsLRgaaiwdeLKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPTSALDpis 221
Cdd:PRK13409 434 KS-----------------EIIKP-LQ-------LERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD--- 485
|
170 180 190
....*....|....*....|....*....|....*.
gi 1374671911 222 tlrVEELvqdlkkdysiIIVTHNMQQAARVSDKTAF 257
Cdd:PRK13409 486 ---VEQR----------LAVAKAIRRIAEEREATAL 508
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
47-263 |
9.31e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.08 E-value: 9.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRmvELVPTVKTSGKILYRDQNIFDK---SYPVEKLR 123
Cdd:PRK13547 5 DHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTGGGAPRGARVTGDVTLNGEplaAIDAPRLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 124 TNVGMVFQQPNP-FPKSIYDNITYGPRIHG-------IKDKKILDEIVEksLRGAaiwDELKDRldqNAYGLSGGQQQRV 195
Cdd:PRK13547 83 RLRAVLPQAAQPaFAFSAREIVLLGRYPHArragaltHRDGEIAWQALA--LAGA---TALVGR---DVTTLSGGELARV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1374671911 196 CIARCLA---------IEPDVILMDEPTSALDPISTLRVEELVQDLKKDYSI--IIVTHNMQQAARVSDKTAFFLNGYV 263
Cdd:PRK13547 155 QFARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgvLAIVHDPNLAARHADRIAMLADGAI 233
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
45-245 |
1.41e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.21 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 45 STQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQnifdksypvekLRt 124
Cdd:PRK09544 6 SLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVA-----PDEGVIKRNGK-----------LR- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 125 nVGMVFQQPN---PFPKSIYDNITYGPrihGIKDKKILDEIveKSLRGAAIwdelkdrLDQNAYGLSGGQQQRVCIARCL 201
Cdd:PRK09544 69 -IGYVPQKLYldtTLPLTVNRFLRLRP---GTKKEDILPAL--KRVQAGHL-------IDAPMQKLSGGETQRVLLARAL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1374671911 202 AIEPDVILMDEPTSALDPISTLRVEELVQDLKK--DYSIIIVTHNM 245
Cdd:PRK09544 136 LNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDL 181
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
71-254 |
2.02e-11 |
|
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: 64.04 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 71 VTAIIGPSGSGKSTYVKALNRmvELVPT---VKTSGKILYRDQNI-FDKSYPVEK-LRTNVGmvfqqpNPFPKSIYDNit 145
Cdd:COG1245 368 VLGIVGPNGIGKTTFAKILAG--VLKPDegeVDEDLKISYKPQYIsPDYDGTVEEfLRSANT------DDFGSSYYKT-- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 146 ygprihgikdkkildEIVEKsLRgaaiwdeLKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPTSALDpistlrV 225
Cdd:COG1245 438 ---------------EIIKP-LG-------LEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD------V 488
|
170 180 190
....*....|....*....|....*....|....*..
gi 1374671911 226 EELVQDLK--------KDYSIIIVTHNMQQAARVSDK 254
Cdd:COG1245 489 EQRLAVAKairrfaenRGKTAMVVDHDIYLIDYISDR 525
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
65-258 |
2.06e-11 |
|
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: 62.43 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 65 DILEKNVTAIIGPSGSGKSTYVKALNRMVElvPTVKTSG----KILYRDQNIFDKsypveklrtnvgmvfqqpnpFPKSI 140
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLK--PDEGDIEieldTVSYKPQYIKAD--------------------YEGTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 141 YDNITYGPRIHGIKDKKILDeiVEKSLrgaaiwdELKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPTSALDPI 220
Cdd:cd03237 79 RDLLSSITKDFYTHPYFKTE--IAKPL-------QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1374671911 221 STLRVEELVQD--LKKDYSIIIVTHNMQQAARVSDKTAFF 258
Cdd:cd03237 150 QRLMASKVIRRfaENNEKTAFVVEHDIIMIDYLADRLIVF 189
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
71-253 |
2.26e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 62.88 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 71 VTAIIGPSGSGKSTYVKALNRMvelvpTVKTSGKILYRDQNIfdKSYPVEKLRTNVGMVFQQ-PNPFPKSIYDNITYG-- 147
Cdd:PRK10575 39 VTGLIGHNGSGKSTLLKMLGRH-----QPPSEGEILLDAQPL--ESWSSKAFARKVAYLPQQlPAAEGMTVRELVAIGry 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 148 PrIHG------IKDKKILDEIVekSLRGaaiwdeLKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPTSALDPIS 221
Cdd:PRK10575 112 P-WHGalgrfgAADREKVEEAI--SLVG------LKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAH 182
|
170 180 190
....*....|....*....|....*....|....
gi 1374671911 222 TLRVEELVQDL--KKDYSIIIVTHNMQQAARVSD 253
Cdd:PRK10575 183 QVDVLALVHRLsqERGLTVIAVLHDINMAARYCD 216
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
59-274 |
2.47e-11 |
|
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: 62.62 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELVptvktSGKILYRDQNIfdKSYPVEKLRTNVGMVFQQPNPFPK 138
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIF-----DGKIVIDGIDI--SKLPLHTLRSRLSIILQDPILFSG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 139 SIYDNITygprihgiKDKKILDEIVEKSLRGAAIWDELKDR---LD----QNAYGLSGGQQQRVCIARCLAIEPDVILMD 211
Cdd:cd03288 110 SIRFNLD--------PECKCTDDRLWEALEIAQLKNMVKSLpggLDavvtEGGENFSVGQRQLFCLARAFVRKSSILIMD 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1374671911 212 EPTSALDPISTLRVEELVQDLKKDYSIIIVTHNMQQAARvSDKTAFFLNGYVNEYDDTDKIFS 274
Cdd:cd03288 182 EATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLA 243
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
59-277 |
2.80e-11 |
|
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: 62.56 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVelvptvKTSGKILYRDQNIfdKSYPVEKLRTNVGMVFQQPNPFPK 138
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL------NTEGDIQIDGVSW--NSVPLQKWRKAFGVIPQKVFIFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 139 SIYDNIT-YGPRihgiKDKKILDEIVEKSLRgaAIWDELKDRLD----QNAYGLSGGQQQRVCIARCLAIEPDVILMDEP 213
Cdd:cd03289 92 TFRKNLDpYGKW----SDEEIWKVAEEVGLK--SVIEQFPGQLDfvlvDGGCVLSHGHKQLMCLARSVLSKAKILLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1374671911 214 TSALDPISTLRVEELVQDLKKDYSIIIVTHNMQ-----QAARVSDKtafflnGYVNEYDDTDKIFSNPS 277
Cdd:cd03289 166 SAHLDPITYQVIRKTLKQAFADCTVILSEHRIEamlecQRFLVIEE------NKVRQYDSIQKLLNEKS 228
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
59-234 |
3.50e-11 |
|
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: 61.12 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNrmVELVPTVKTSGKILYR--DQNIFDKSYPVEklrtnVGMVFQQPNPF 136
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALA--NRTEGNVSVEGDIHYNgiPYKEFAEKYPGE-----IIYVSEEDVHF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 137 PksiydNITygprihgikdkkildeiVEKSLRGAaiwdeLKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPTSA 216
Cdd:cd03233 96 P-----TLT-----------------VRETLDFA-----LRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
170
....*....|....*...
gi 1374671911 217 LDPISTLrveELVQDLKK 234
Cdd:cd03233 149 LDSSTAL---EILKCIRT 163
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
41-253 |
7.81e-11 |
|
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: 59.75 E-value: 7.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 41 RVVYSTQNLDLWygeqHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALnrmVELVPTvkTSGKILYRDQNIFDKSyPVE 120
Cdd:cd03215 2 EPVLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEAL---FGLRPP--ASGEITLDGKPVTRRS-PRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 121 KLRTNVGMVfqqpnP--------FPK-SIYDNITygprihgikdkkildeivekslrgaaiwdelkdrldqNAYGLSGGQ 191
Cdd:cd03215 72 AIRAGIAYV-----PedrkreglVLDlSVAENIA-------------------------------------LSSLLSGGN 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1374671911 192 QQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKD-YSIIIVTHNMQQAARVSD 253
Cdd:cd03215 110 QQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAgKAVLLISSELDELLGLCD 172
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
71-251 |
1.14e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.82 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 71 VTAIIGPSGSGKSTYvkaLNRMVELVPTVKTSGKILYRDQNifdksyPVEKLRTNVGMVFQQPNPFP------KSIYDNI 144
Cdd:PLN03211 96 ILAVLGPSGSGKSTL---LNALAGRIQGNNFTGTILANNRK------PTKQILKRTGFVTQDDILYPhltvreTLVFCSL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 145 TYGPRIHGIKDKKILDEIVEKSLrGAAiwdELKDRLDQNAY--GLSGGQQQRVCIARCLAIEPDVILMDEPTSALDPIST 222
Cdd:PLN03211 167 LRLPKSLTKQEKILVAESVISEL-GLT---KCENTIIGNSFirGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAA 242
|
170 180 190
....*....|....*....|....*....|
gi 1374671911 223 LR-VEELVQDLKKDYSIIIVTHnmQQAARV 251
Cdd:PLN03211 243 YRlVLTLGSLAQKGKTIVTSMH--QPSSRV 270
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
62-285 |
1.20e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 60.97 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 62 VNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELVPTVkTSGKILYRDQNIFDKSyPVEKLRT---NVGMVFQQP----N 134
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRV-TADRMRFDDIDLLRLS-PRERRKLvghNVSMIFQEPqsclD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 135 P---FPKSIYDNI---TY-GP---RIHGIKDKKIldeiveKSLRGAAIWDElKDRLDQNAYGLSGGQQQRVCIARCLAIE 204
Cdd:PRK15093 104 PserVGRQLMQNIpgwTYkGRwwqRFGWRKRRAI------ELLHRVGIKDH-KDAMRSFPYELTEGECQKVMIAIALANQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 205 PDVILMDEPTSALDPISTLRVEELVQDLKKD--YSIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSNPSDKQTE 282
Cdd:PRK15093 177 PRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnnTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHPYTQ 256
|
...
gi 1374671911 283 DYI 285
Cdd:PRK15093 257 ALI 259
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
45-243 |
1.27e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.19 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 45 STQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELvptVKTSGKILYRDQNIFDKSyPVEKLRT 124
Cdd:PRK09580 3 SIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDY---EVTGGTVEFKGKDLLELS-PEDRAGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 125 NVGMVFQQP-------NPFPKSIYDNITYGPRIHGIKDKKILDEIVEKSLRGAAIWDELKDRldQNAYGLSGGQQQRVCI 197
Cdd:PRK09580 79 GIFMAFQYPveipgvsNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTR--SVNVGFSGGEKKRNDI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1374671911 198 ARCLAIEPDVILMDEPTSALDpISTLR-VEELVQDLKK-DYSIIIVTH 243
Cdd:PRK09580 157 LQMAVLEPELCILDESDSGLD-IDALKiVADGVNSLRDgKRSFIIVTH 203
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
74-275 |
1.38e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.92 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 74 IIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQNIfdKSYPVEKLRTNVGMVFQQPNPFPKSIYDNItygprihgi 153
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVEL-----EKGRIMIDDCDV--AKFGLTDLRRVLSIIPQSPVLFSGTVRFNI--------- 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 154 kdkkilDEIVEKSlrGAAIWDEL-----KDRLDQNAYGL-----------SGGQQQRVCIARCLAIEPDVILMDEPTSAL 217
Cdd:PLN03232 1331 ------DPFSEHN--DADLWEALerahiKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATASV 1402
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1374671911 218 DPISTLRVEELVQDLKKDYSIIIVTHNMQQAARVsDKTAFFLNGYVNEYDDTDKIFSN 275
Cdd:PLN03232 1403 DVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDC-DKILVLSSGQVLEYDSPQELLSR 1459
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
53-261 |
1.53e-10 |
|
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: 61.38 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 53 YGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNrmvELVPTVKTSGKILYRDQNIFDKSYPvEKLRTNVGMVFQQ 132
Cdd:TIGR02633 11 FGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILS---GVYPHGTWDGEIYWSGSPLKASNIR-DTERAGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 133 PNPFPK-SIYDNITYGpriHGIKDKKILDEIVEKSLRGAAIWDELKDRLDQNAYG---LSGGQQQRVCIARCLAIEPDVI 208
Cdd:TIGR02633 87 LTLVPElSVAENIFLG---NEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvgdYGGGQQQLVEIAKALNKQARLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1374671911 209 LMDEPTSALDPISTLRVEELVQDLK-KDYSIIIVTHNMQQAARVSDKTAFFLNG 261
Cdd:TIGR02633 164 ILDEPSSSLTEKETEILLDIIRDLKaHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
59-272 |
1.63e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.22 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKAlnrMVELVPtvKTSGKILYRDQNIFDKSyPVEKLRTNVGMVFQQPNPFPK 138
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKI---IAGIVP--PDSGTLEIGGNPCARLT-PAKAHQLGIYLVPQEPLLFPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 139 -SIYDNITYG-PRihGIKDKKILDEIVekslrgAAIWDELKdrLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPTSA 216
Cdd:PRK15439 101 lSVKENILFGlPK--RQASMQKMKQLL------AALGCQLD--LDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1374671911 217 LDPISTLRVEELVQDL-KKDYSIIIVTHNMQQAARVSDKTAFFLNGYV------NEYDDTDKI 272
Cdd:PRK15439 171 LTPAETERLFSRIRELlAQGVGIVFISHKLPEIRQLADRISVMRDGTIalsgktADLSTDDII 233
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
43-243 |
2.33e-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: 60.72 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 43 VYSTQNLDLWYGEQ-HSLKNVNLDILEKNVTAIIGPSGSGKSTYVKAlnrMVELvptvktsgkilyrDQNIFDKSYPVEK 121
Cdd:TIGR03719 4 IYTMNRVSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRI---MAGV-------------DKDFNGEARPQPG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 122 LRtnVGMVFQQPNPFP-KSIYDNITYGprIHGIKDK-KILDEIVEKSLRGAAIWD-------ELKDRL------------ 180
Cdd:TIGR03719 68 IK--VGYLPQEPQLDPtKTVRENVEEG--VAEIKDAlDRFNEISAKYAEPDADFDklaaeqaELQEIIdaadawdldsql 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1374671911 181 ------------DQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKdySIIIVTH 243
Cdd:TIGR03719 144 eiamdalrcppwDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG--TVVAVTH 216
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
59-261 |
4.46e-10 |
|
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: 60.31 E-value: 4.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALnrMVELVPT---VKTSGKILYRDQNifdksypveklrtnvgmvfqqPNP 135
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMI--MGELEPSegkIKHSGRISFSPQT---------------------SWI 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 136 FPKSIYDNITYGPRihgikdkkiLDEIVEKSLRGAAIWDE------LKDR--LDQNAYGLSGGQQQRVCIARCLAIEPDV 207
Cdd:TIGR01271 499 MPGTIKDNIIFGLS---------YDEYRYTSVIKACQLEEdialfpEKDKtvLGEGGITLSGGQRARISLARAVYKDADL 569
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1374671911 208 ILMDEPTSALDPISTLRV-EELVQDLKKDYSIIIVTHNMQQAARvSDKTAFFLNG 261
Cdd:TIGR01271 570 YLLDSPFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
33-285 |
4.56e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.80 E-value: 4.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 33 ETLSDRERRVVYSTQNLDLWygEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALnrmveLVPTVKTSGKILYRDQNI 112
Cdd:PRK09700 255 ENVSNLAHETVFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCL-----FGVDKRAGGEIRLNGKDI 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 113 FDKSyPVEKLRTNVGMVFQQPNP---FPK-SIYDNITYGPRI------------HGIKDKKILDEIVEK-SLRGAAIwde 175
Cdd:PRK09700 328 SPRS-PLDAVKKGMAYITESRRDngfFPNfSIAQNMAISRSLkdggykgamglfHEVDEQRTAENQRELlALKCHSV--- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 176 lkdrlDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKD-YSIIIVTHNMQQAARVSDK 254
Cdd:PRK09700 404 -----NQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDR 478
|
250 260 270
....*....|....*....|....*....|.
gi 1374671911 255 TAFFLNGYVNEyddtdkIFSNpSDKQTEDYI 285
Cdd:PRK09700 479 IAVFCEGRLTQ------ILTN-RDDMSEEEI 502
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
51-253 |
5.08e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.96 E-value: 5.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 51 LWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKIlyrdqnIFDKSYPVEKLrtnvgmvf 130
Cdd:PRK11147 11 LSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLL-----DDGRI------IYEQDLIVARL-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 131 QQ--PNPFPKSIYDNITYG--------PRIHGIKDKkILDEIVEKSLRGAAiwdELKDRLD-QNAY-------------- 185
Cdd:PRK11147 72 QQdpPRNVEGTVYDFVAEGieeqaeylKRYHDISHL-VETDPSEKNLNELA---KLQEQLDhHNLWqlenrinevlaqlg 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 186 --------GLSGGQQQRVCIARCLAIEPDVILMDEPTSALDpISTLrveELVQDLKKDY--SIIIVTH------NMqqAA 249
Cdd:PRK11147 148 ldpdaalsSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD-IETI---EWLEGFLKTFqgSIIFISHdrsfirNM--AT 221
|
....
gi 1374671911 250 RVSD 253
Cdd:PRK11147 222 RIVD 225
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
56-253 |
7.00e-10 |
|
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: 58.04 E-value: 7.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 56 QHSLKNVNLDILEKNVTAIIGPSGSGKST------YVKALNRMVELVPTvktsgkilYRDQNIFDKSYP----VEKLRTN 125
Cdd:cd03270 8 EHNLKNVDVDIPRNKLVVITGVSGSGKSSlafdtiYAEGQRRYVESLSA--------YARQFLGQMDKPdvdsIEGLSPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 126 VGMVFQQPNPFPKS-------IYD--NITYGpRIhGIKDKkiLDEIVEKSLrgaaiwDELkdRLDQNAYGLSGGQQQRVC 196
Cdd:cd03270 80 IAIDQKTTSRNPRStvgtvteIYDylRLLFA-RV-GIRER--LGFLVDVGL------GYL--TLSRSAPTLSGGEAQRIR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1374671911 197 IARCLAIEPDVIL--MDEPTSALDPISTLRVEELVQDLK-KDYSIIIVTHN---MQQAARVSD 253
Cdd:cd03270 148 LATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRdLGNTVLVVEHDedtIRAADHVID 210
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
74-243 |
1.02e-09 |
|
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: 57.12 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 74 IIGPSGSGKSTYVKALnrmVELVPtvKTSGKILYRDQnifdksypveklrtnvGMVFQQPnpfpkSIYDNITYGPRIHGI 153
Cdd:cd03231 31 VTGPNGSGKTTLLRIL---AGLSP--PLAGRVLLNGG----------------PLDFQRD-----SIARGLLYLGHAPGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 154 kdKKILDeiVEKSLR-------GAAIWDELkDRLDQNAYG------LSGGQQQRVCIARCLAIEPDVILMDEPTSALDPI 220
Cdd:cd03231 85 --KTTLS--VLENLRfwhadhsDEQVEEAL-ARVGLNGFEdrpvaqLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
170 180
....*....|....*....|....
gi 1374671911 221 STLRVEELV-QDLKKDYSIIIVTH 243
Cdd:cd03231 160 GVARFAEAMaGHCARGGMVVLTTH 183
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
54-242 |
1.20e-09 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 58.91 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 54 GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKAL-NRM---VELVPTVKTSGKILYRDQnifdksypvekLRTNVGMV 129
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALaFRSpkgVKGSGSVLLNGMPIDAKE-----------MRAISAYV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 130 FQQPNPFPK-SIYDNITYGPRI----HGIKDKKIL--DEIVEK-SLRGAA-----IWDELKdrldqnayGLSGGQQQRVC 196
Cdd:TIGR00955 105 QQDDLFIPTlTVREHLMFQAHLrmprRVTKKEKRErvDEVLQAlGLRKCAntrigVPGRVK--------GLSGGERKRLA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1374671911 197 IARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKDYSIIIVT 242
Cdd:TIGR00955 177 FASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICT 222
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
55-253 |
1.37e-09 |
|
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: 56.18 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 55 EQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVK------ALNRMVELVPTvktsgkiLYRDQNIFdksypVEKLRTNVGM 128
Cdd:cd03238 7 NVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNeglyasGKARLISFLPK-------FSRNKLIF-----IDQLQFLIDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 129 vfqqpnpfpksiydNITYGPrihgikdkkildeivekslrgaaiwdelkdrLDQNAYGLSGGQQQRVCIARCLA--IEPD 206
Cdd:cd03238 75 --------------GLGYLT-------------------------------LGQKLSTLSGGELQRVKLASELFsePPGT 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1374671911 207 VILMDEPTSALDPISTLRVEELVQDL-KKDYSIIIVTHN---MQQAARVSD 253
Cdd:cd03238 110 LFILDEPSTGLHQQDINQLLEVIKGLiDLGNTVILIEHNldvLSSADWIID 160
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
54-245 |
1.40e-09 |
|
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: 58.80 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 54 GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALnrmveLVPTVKTSGKIlyrdqnifdksypveKLRTNVGMVFQQP 133
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL-----LAEMDKVEGHV---------------HMKGSVAYVPQQA 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 134 NPFPKSIYDNITYGpriHGIKDKKildeiVEKSLRGAAIWDELK-----DRLDQNAYG--LSGGQQQRVCIARCLAIEPD 206
Cdd:TIGR00957 709 WIQNDSLRENILFG---KALNEKY-----YQQVLEACALLPDLEilpsgDRTEIGEKGvnLSGGQKQRVSLARAVYSNAD 780
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1374671911 207 VILMDEPTSALDPISTLRVEELV---QDLKKDYSIIIVTHNM 245
Cdd:TIGR00957 781 IYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGI 822
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
45-243 |
1.44e-09 |
|
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: 56.60 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 45 STQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQNIfdkSYPVEKLRT 124
Cdd:TIGR01189 2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRP-----DSGEVRWNGTPL---AEQRDEPHE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 125 NVGMVFQQPNPFPK-SIYDNITYGPRIHGIKDKKILDEIVEKSLRGAAiwdelkdrlDQNAYGLSGGQQQRVCIARCLAI 203
Cdd:TIGR01189 74 NILYLGHLPGLKPElSALENLHFWAAIHGGAQRTIEDALAAVGLTGFE---------DLPAAQLSAGQQRRLALARLWLS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1374671911 204 EPDVILMDEPTSALDPISTLRVEELVQD-LKKDYSIIIVTH 243
Cdd:TIGR01189 145 RRPLWILDEPTTALDKAGVALLAGLLRAhLARGGIVLLTTH 185
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
187-263 |
1.55e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.20 E-value: 1.55e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1374671911 187 LSGGQQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDL-KKDYSIIIVTHNMQQAARVSDKTAFFLNGYV 263
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
59-265 |
1.57e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 58.64 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELVptvktSGKILYRDQNIfdKSYPVEKLRTNVGMVFQQPNPFPK 138
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVC-----GGEIRVNGREI--GAYGLRELRRQFSMIPQDPVLFDG 1398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 139 SIYDNitygprihgikdkkiLDEIVEKSlrGAAIWDEL-----KDRLDQNAYGL-----------SGGQQQRVCIARCLA 202
Cdd:PTZ00243 1399 TVRQN---------------VDPFLEAS--SAEVWAALelvglRERVASESEGIdsrvleggsnySVGQRQLMCMARALL 1461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1374671911 203 IE-PDVILMDEPTSALDPISTLRVEELVQDLKKDYSIIIVTHNMQQAARVsDKTAFFLNGYVNE 265
Cdd:PTZ00243 1462 KKgSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQY-DKIIVMDHGAVAE 1524
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
55-275 |
2.07e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.45 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 55 EQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALnrMVELVPTVKTSGKIlyrdqnifdksypveklRTNVGMVFQQPN 134
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAM--LGELSHAETSSVVI-----------------RGSVAYVPQVSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 135 PFPKSIYDNITYGPRIHGIKDKKILDeivekslrGAAIWDEL-----KDRLDQNAYG--LSGGQQQRVCIARCLAIEPDV 207
Cdd:PLN03232 690 IFNATVRENILFGSDFESERYWRAID--------VTALQHDLdllpgRDLTEIGERGvnISGGQKQRVSMARAVYSNSDI 761
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1374671911 208 ILMDEPTSALDPISTLRV-EELVQDLKKDYSIIIVTHNMQQAARVsDKTAFFLNGYVNEYDDTDKIFSN 275
Cdd:PLN03232 762 YIFDDPLSALDAHVAHQVfDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSKS 829
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
59-275 |
2.25e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.21 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQNIfdKSYPVEKLRTNVGMVFQQPNPFPK 138
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVEL-----ERGRILIDGCDI--SKFGLMDLRKVLGIIPQAPVLFSG 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 139 SIYDNitygprihgikdkkiLDEIVEKSlrGAAIWD-----ELKDRLDQNAYGL-----------SGGQQQRVCIARCLA 202
Cdd:PLN03130 1328 TVRFN---------------LDPFNEHN--DADLWEsleraHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALL 1390
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1374671911 203 IEPDVILMDEPTSALDpistLRVEELVQ----DLKKDYSIIIVTHNMQQAARvSDKTAFFLNGYVNEYDDTDKIFSN 275
Cdd:PLN03130 1391 RRSKILVLDEATAAVD----VRTDALIQktirEEFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSN 1462
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
59-261 |
2.75e-09 |
|
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: 56.79 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALnrMVELVPT---VKTSGKILYRDQNIFdksypveklrtnvgmvfqqpnP 135
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLI--LGELEPSegkIKHSGRISFSSQFSW---------------------I 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 136 FPKSIYDNITYGPRIHGIKDKKILDEI-VEKSLrgAAIWDELKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPT 214
Cdd:cd03291 110 MPGTIKENIIFGVSYDEYRYKSVVKACqLEEDI--TKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPF 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1374671911 215 SALDPISTLRV-EELVQDLKKDYSIIIVTHNMQQaARVSDKTAFFLNG 261
Cdd:cd03291 188 GYLDVFTEKEIfESCVCKLMANKTRILVTSKMEH-LKKADKILILHEG 234
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
47-246 |
3.08e-09 |
|
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: 57.61 E-value: 3.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGE--QHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvkTSGKIlyRDQNIFDKSYPVEKLRT 124
Cdd:TIGR01271 1221 QGLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS------TEGEI--QIDGVSWNSVTLQTWRK 1292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 125 NVGMVFQQPNPFPKSIYDNITYGPRIHGIKDKKILDEIVEKSlrgaaIWDELKDRLD----QNAYGLSGGQQQRVCIARC 200
Cdd:TIGR01271 1293 AFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKS-----VIEQFPDKLDfvlvDGGYVLSNGHKQLMCLARS 1367
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1374671911 201 LAIEPDVILMDEPTSALDPIsTLRVeeLVQDLKKDYS---IIIVTHNMQ 246
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLDPV-TLQI--IRKTLKQSFSnctVILSEHRVE 1413
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
74-218 |
5.47e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 55.71 E-value: 5.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 74 IIGPSGSGKSTyvkALNRMVELVPtvkTSGKILYRDQNIFDksYPVEKL-RTNVGMVFQQPNPFPKSIYDNIT-YGP-RI 150
Cdd:PRK03695 27 LVGPNGAGKST---LLARMAGLLP---GSGSIQFAGQPLEA--WSAAELaRHRAYLSQQQTPPFAMPVFQYLTlHQPdKT 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1374671911 151 HGIKDKKILDEIVEkSLRgaaiwdeLKDRLDQNAYGLSGGQQQRVCIAR-CLAIEPDV------ILMDEPTSALD 218
Cdd:PRK03695 99 RTEAVASALNEVAE-ALG-------LDDKLGRSVNQLSGGEWQRVRLAAvVLQVWPDInpagqlLLLDEPMNSLD 165
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
59-232 |
6.92e-09 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 54.56 E-value: 6.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKAL-NRmvelvptvKTSGKIlyrDQNIFDKSYPVEK-LRTNVGMVFQQPNPF 136
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLaGR--------KTAGVI---TGEILINGRPLDKnFQRSTGYVEQQDVHS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 137 PKSIydnitygprihgikdkkildeiVEKSLRGAAiwdelkdrldqNAYGLSGGQQQRVCIARCLAIEPDVILMDEPTSA 216
Cdd:cd03232 92 PNLT----------------------VREALRFSA-----------LLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSG 138
|
170
....*....|....*.
gi 1374671911 217 LDPISTLRVEELVQDL 232
Cdd:cd03232 139 LDSQAAYNIVRFLKKL 154
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
60-254 |
1.11e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.83 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 60 KNVNLDILEKNVTAIIGPSGSGKSTYVKALnrmVELVPTVktSGKILYRDQNIFDKSyPVEKLRTnvGMVF-----QQPN 134
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETL---YGLRPAR--GGRIMLNGKEINALS-TAQRLAR--GLVYlpedrQSSG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 135 PF-PKSIYDNI---TYGPR---IHGIKDKKILdeivEKSLRGAAIwdELKDrLDQNAYGLSGGQQQRVCIARCLAIEPDV 207
Cdd:PRK15439 352 LYlDAPLAWNVcalTHNRRgfwIKPARENAVL----ERYRRALNI--KFNH-AEQAARTLSGGNQQKVLIAKCLEASPQL 424
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1374671911 208 ILMDEPTSALDPISTLRVEELVQDLKKD-YSIIIVTHNMQQAARVSDK 254
Cdd:PRK15439 425 LIVDEPTRGVDVSARNDIYQLIRSIAAQnVAVLFISSDLEEIEQMADR 472
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
180-254 |
1.27e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.39 E-value: 1.27e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1374671911 180 LDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKD-YSIIIVTHNMQQAARVSDK 254
Cdd:PRK10762 389 MEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEgLSIILVSSEMPEVLGMSDR 464
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
63-243 |
2.13e-08 |
|
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: 55.14 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 63 NLDILEKNVTAIIGPSGSGKSTYVKALNrmvELVPTVktsGKILY--RDQNIFdksypveklrtnvgMVFQQPNPFPKSI 140
Cdd:TIGR00954 472 SFEVPSGNNLLICGPNGCGKSSLFRILG---ELWPVY---GGRLTkpAKGKLF--------------YVPQRPYMTLGTL 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 141 YDNITYGPRIHGIKDKKILDEIVEKSL----------RGAAiWDELKDRLDQnaygLSGGQQQRVCIARCLAIEPDVILM 210
Cdd:TIGR00954 532 RDQIIYPDSSEDMKRRGLSDKDLEQILdnvqlthileREGG-WSAVQDWMDV----LSGGEKQRIAMARLFYHKPQFAIL 606
|
170 180 190
....*....|....*....|....*....|....*
gi 1374671911 211 DEPTSALDPistlRVEELVQDLKKDYSI--IIVTH 243
Cdd:TIGR00954 607 DECTSAVSV----DVEGYMYRLCREFGItlFSVSH 637
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
59-218 |
3.96e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.40 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKILyrdqnifdksypVEKlrtNVGMVFQQPNPFPK 138
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEI-----SEGRVW------------AER---SIAYVPQQAWIMNA 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 139 SIYDNITYgprihgikdkkiLDEIVEKSLRGAAIWDELKDRLDQNAYG-----------LSGGQQQRVCIARCLAIEPDV 207
Cdd:PTZ00243 736 TVRGNILF------------FDEEDAARLADAVRVSQLEADLAQLGGGleteigekgvnLSGGQKARVSLARAVYANRDV 803
|
170
....*....|.
gi 1374671911 208 ILMDEPTSALD 218
Cdd:PTZ00243 804 YLLDDPLSALD 814
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
59-254 |
6.89e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.39 E-value: 6.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNrmvELVPTVKTSGKILY-----RDQNIFDKSypveklRTNVGMVFQQP 133
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLS---GVYPHGTYEGEIIFegeelQASNIRDTE------RAGIAIIHQEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 134 NPFPK-SIYDNITYGPRI--HGIKDkkiLDEIVeksLRGAAIWDELKdrLDQNAY----GLSGGQQQRVCIARCLAIEPD 206
Cdd:PRK13549 92 ALVKElSVLENIFLGNEItpGGIMD---YDAMY---LRAQKLLAQLK--LDINPAtpvgNLGLGQQQLVEIAKALNKQAR 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1374671911 207 VILMDEPTSALDPISTLRVEELVQDLK-KDYSIIIVTHNMQQAARVSDK 254
Cdd:PRK13549 164 LLILDEPTASLTESETAVLLDIIRDLKaHGIACIYISHKLNEVKAISDT 212
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
59-267 |
8.74e-08 |
|
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: 53.41 E-value: 8.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIFDKSypVEKLRTNVGMVFQQPNPFPK 138
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINE-----SAEGEIIIDGLNIAKIG--LHDLRFKITIIPQDPVLFSG 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 139 SIYDNITygPrIHGIKDKKILDEIVEKSLRG--AAIWDELKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPTSA 216
Cdd:TIGR00957 1375 SLRMNLD--P-FSQYSDEEVWWALELAHLKTfvSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAA 1451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1374671911 217 LDpistLRVEELVQDLKK----DYSIIIVTHNMQQaarVSDKTAFFL--NGYVNEYD 267
Cdd:TIGR00957 1452 VD----LETDNLIQSTIRtqfeDCTVLTIAHRLNT---IMDYTRVIVldKGEVAEFG 1501
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
29-254 |
9.19e-08 |
|
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: 52.90 E-value: 9.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 29 TEKHETlsdreRRVVYSTQNLDLWYGEQHSLK---NVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptVKTSGKI 105
Cdd:TIGR02633 248 HEPHEI-----GDVILEARNLTCWDVINPHRKrvdDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYP----GKFEGNV 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 106 lYRDQNIFDKSYPVEKLRTNVGMVfqqPNPFPK-------SIYDNITYGPrIHGIKDKKILDEIVEKSLRGAAIwDELKD 178
Cdd:TIGR02633 319 -FINGKPVDIRNPAQAIRAGIAMV---PEDRKRhgivpilGVGKNITLSV-LKSFCFKMRIDAAAELQIIGSAI-QRLKV 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 179 RL---DQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDL-KKDYSIIIVTHNMQQAARVSDK 254
Cdd:TIGR02633 393 KTaspFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLaQEGVAIIVVSSELAEVLGLSDR 472
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
55-218 |
1.25e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 51.03 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 55 EQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVElvptvKTSGKILYRDQNIFDKSYP-VEKLRTNVGMVFQQp 133
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQ-----PSSGNIYYKNCNINNIAKPyCTYIGHNLGLKLEM- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 134 npfpkSIYDNITYGPRIHGikdkkildeiVEKSLRGAAIWDELKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEP 213
Cdd:PRK13541 86 -----TVFENLKFWSEIYN----------SAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEV 150
|
....*
gi 1374671911 214 TSALD 218
Cdd:PRK13541 151 ETNLS 155
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
47-250 |
3.75e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.28 E-value: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 47 QNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTyvkalnrMVELVPTVKT--SGKILYRDQNIFDKSYpveklRT 124
Cdd:NF033858 5 EGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSS-------LLSLIAGARKiqQGRVEVLGGDMADARH-----RR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 125 NVG-----MvfqqP-----NPFPK-SIYDNITYGPRIHGikdkkiLDeiveKSLRGAAIwDELKDR------LDQNAYGL 187
Cdd:NF033858 73 AVCpriayM----PqglgkNLYPTlSVFENLDFFGRLFG------QD----AAERRRRI-DELLRAtglapfADRPAGKL 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1374671911 188 SGGQQQRV--CIArcLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKD---YSIIIVTHNMQQAAR 250
Cdd:NF033858 138 SGGMKQKLglCCA--LIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpgMSVLVATAYMEEAER 203
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-266 |
4.03e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.10 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 25 AKDQTEKhetlSDRERRVVYSTQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKALnrMVELVPTvktSGK 104
Cdd:PRK11147 305 AKMQVEE----ASRSGKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLM--LGQLQAD---SGR 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 105 I--------LYRDQN--IFDksypveklrtnvgmvfqqPNpfpKSIYDNITYGPR---IHGiKDKKILDEivekslrgaa 171
Cdd:PRK11147 376 IhcgtklevAYFDQHraELD------------------PE---KTVMDNLAEGKQevmVNG-RPRHVLGY---------- 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 172 iwdeLKD------RLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPTSALDpISTLrveELVQDLKKDY--SIIIVTH 243
Cdd:PRK11147 424 ----LQDflfhpkRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD-VETL---ELLEELLDSYqgTVLLVSH 495
|
250 260
....*....|....*....|....*...
gi 1374671911 244 NMQqaarVSDKTA-----FFLNGYVNEY 266
Cdd:PRK11147 496 DRQ----FVDNTVtecwiFEGNGKIGRY 519
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
139-218 |
4.12e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.68 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 139 SIYDNITYGPRIHGIKDKKILDEIVEKSLRgaaiwDELKDRL-------DQNAYGLSGGQQQRVCIARCLAIEPDVILMD 211
Cdd:PRK11288 347 SVADNINISARRHHLRAGCLINNRWEAENA-----DRFIRSLniktpsrEQLIMNLSGGNQQKAILGRWLSEDMKVILLD 421
|
....*..
gi 1374671911 212 EPTSALD 218
Cdd:PRK11288 422 EPTRGID 428
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
57-272 |
4.15e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.20 E-value: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 57 HSLKNVNLDILEKNVTAIIGPSGSGKSTyvkaLNRMV--ELVPtvkTSGKIlyrdqnifDKSYPVEKLRTNVGMVFQQPN 134
Cdd:PRK13546 38 FALDDISLKAYEGDVIGLVGINGSGKST----LSNIIggSLSP---TVGKV--------DRNGEVSVIAISAGLSGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 135 pfpksiYDNITYGPRIHGIKDKKI---LDEIVEKSLRGAAIWDELKDrldqnaygLSGGQQQRVCIARCLAIEPDVILMD 211
Cdd:PRK13546 103 ------IENIEFKMLCMGFKRKEIkamTPKIIEFSELGEFIYQPVKK--------YSSGMRAKLGFSINITVNPDILVID 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1374671911 212 EPTSALDPISTLRVEELVQDLKK-DYSIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKI 272
Cdd:PRK13546 169 EALSVGDQTFAQKCLDKIYEFKEqNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
188-243 |
7.45e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.24 E-value: 7.45e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1374671911 188 SGGQQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVqdLKKDYSIIIVTH 243
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSH 399
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
187-243 |
8.14e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.12 E-value: 8.14e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1374671911 187 LSGGQQQRVCIARCLAIEPDVILMDEPTSALDPIStlrVEELVQDLkKDYS--IIIVTH 243
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES---VAWLEQFL-HDYPgtVVAVTH 218
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
56-245 |
1.14e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 48.76 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 56 QHSLKNVNLDILEKNVTAIIGPSGSGKSTYV-----KALNRMVELVPTVKTSGKILYRDQNIfDKsypveklrtnVGMVF 130
Cdd:cd03271 8 ENNLKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlyPALARRLHLKKEQPGNHDRIEGLEHI-DK----------VIVID 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 131 QQP-------NPFP-KSIYDNI--TYGPRIHGikdKKILDEIVEKSLRGAAIWD------------------------EL 176
Cdd:cd03271 77 QSPigrtprsNPATyTGVFDEIreLFCEVCKG---KRYNRETLEVRYKGKSIADvldmtveealeffenipkiarklqTL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1374671911 177 KD------RLDQNAYGLSGGQQQRVCIARCL---AIEPDVILMDEPTSALDPISTLRVEELVQDL-KKDYSIIIVTHNM 245
Cdd:cd03271 154 CDvglgyiKLGQPATTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLvDKGNTVVVIEHNL 232
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
59-218 |
2.73e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.48 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNRMVELvptvkTSGKILYRDQNIFDKSY-----------PVEKLRTnvG 127
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPP-----ASGSIRLDGEDITGLSPrerrrlgvayiPEDRLGR--G 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 128 MVfqqPNpFpkSIYDNIT----YGPRI--HGIKDKKIL----DEIVEK-SLRGAAIwdelkdrlDQNAYGLSGGQQQRVC 196
Cdd:COG3845 347 LV---PD-M--SVAENLIlgryRRPPFsrGGFLDRKAIrafaEELIEEfDVRTPGP--------DTPARSLSGGNQQKVI 412
|
170 180
....*....|....*....|..
gi 1374671911 197 IARCLAIEPDVILMDEPTSALD 218
Cdd:COG3845 413 LARELSRDPKLLIAAQPTRGLD 434
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
25-227 |
4.26e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 47.62 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 25 AKDQTEKHETLS------DRERRVVYSTQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGKSTyvkaLNRM------ 92
Cdd:TIGR03719 298 SQEFQKRNETAEiyippgPRLGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKST----LFRMitgqeq 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 93 -----VELVPTVKTSgkilYRDQNifdksypVEKLRTNvgmvfqqpnpfpKSIYDNITYGprihgikdkkiLDEI----V 163
Cdd:TIGR03719 374 pdsgtIEIGETVKLA----YVDQS-------RDALDPN------------KTVWEEISGG-----------LDIIklgkR 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1374671911 164 EKSLRGAAIWDELKDRLDQNAYG-LSGGQQQRVCIARCLAIEPDVILMDEPTSALDpISTLRVEE 227
Cdd:TIGR03719 420 EIPSRAYVGRFNFKGSDQQKKVGqLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD-VETLRALE 483
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
187-258 |
5.42e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.03 E-value: 5.42e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1374671911 187 LSGGQQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDL--KKDYSIIIVTHNMQQAARVSDKTAFF 258
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseEGKKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
56-245 |
6.14e-06 |
|
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: 47.32 E-value: 6.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 56 QHSLKNVNLDILEKNVTAIIGPSGSGKSTYV-----KALNRMVELVPTVKTSG----------KILYRDQNIFDK---SY 117
Cdd:TIGR00630 621 ENNLKNITVSIPLGLFTCITGVSGSGKSTLIndtlyPALANRLNGAKTVPGRYtsieglehldKVIHIDQSPIGRtprSN 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 118 PVE--KLRTNVGMVF-QQPNP----FPKSIYDNITYGPR-------------IHGIKD----------KKILDEIVEKSL 167
Cdd:TIGR00630 701 PATytGVFDEIRELFaETPEAkvrgYTPGRFSFNVKGGRceacqgdgvikieMHFLPDvyvpcevckgKRYNRETLEVKY 780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 168 RGAAIWD-------ELKD-----------------------RLDQNAYGLSGGQQQRVCIARCL---AIEPDVILMDEPT 214
Cdd:TIGR00630 781 KGKNIADvldmtveEAYEffeavpsisrklqtlcdvglgyiRLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPT 860
|
250 260 270
....*....|....*....|....*....|....
gi 1374671911 215 SAL--DPISTLRveELVQDL-KKDYSIIIVTHNM 245
Cdd:TIGR00630 861 TGLhfDDIKKLL--EVLQRLvDKGNTVVVIEHNL 892
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
187-254 |
9.33e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.85 E-value: 9.33e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1374671911 187 LSGGQQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDL-KKDYSIIIVTHNMQQAARVSDK 254
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLvQQGVAIIVISSELPEVLGLSDR 474
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
60-232 |
1.33e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 60 KNVNLDILEKNVTAIIGPSGSGKSTYVKALNRmvELVP---TVKTSGKIlyrDQNIFDKSYpVEKLRTNVGMVFQQPNPF 136
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISG--ELQPssgTVFRSAKV---RMAVFSQHH-VDGLDLSSNPLLYMMRCF 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 137 PksiydnitygprihGIKDKKILDEIVEKSLRGAAIWdelkdrldQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPTSA 216
Cdd:PLN03073 600 P--------------GVPEQKLRAHLGSFGVTGNLAL--------QPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNH 657
|
170
....*....|....*.
gi 1374671911 217 LDPIStlrVEELVQDL 232
Cdd:PLN03073 658 LDLDA---VEALIQGL 670
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
54-250 |
1.75e-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: 44.27 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 54 GEQHSLKNVNLDILEKNVTAIIGPSGSGKSTYVKAlnrmVELVPTVKTSgkilyrdqnifdksypveklRTNVGMVFQQP 133
Cdd:cd03227 6 RFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDA----IGLALGGAQS--------------------ATRRRSGVKAG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 134 npfpksiydnitygprihgikdkkildEIVekslrgAAIWDELKDRLDQnaygLSGGQQQRVCIARCLAI----EPDVIL 209
Cdd:cd03227 62 ---------------------------CIV------AAVSAELIFTRLQ----LSGGEKELSALALILALaslkPRPLYI 104
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1374671911 210 MDEPTSALDPISTLRVEELVQD-LKKDYSIIIVTHNMQQAAR 250
Cdd:cd03227 105 LDEIDRGLDPRDGQALAEAILEhLVKGAQVIVITHLPELAEL 146
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
73-261 |
2.12e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 46.16 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 73 AIIGPSGSGKSTYVKALNRmvelvPTVKTSGkilyrDQNIFDKSypvekLRTNVGMVFQQPNPFPK-SIYDNITYG---- 147
Cdd:TIGR01257 1969 GLLGVNGAGKTTTFKMLTG-----DTTVTSG-----DATVAGKS-----ILTNISDVHQNMGYCPQfDAIDDLLTGrehl 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 148 ---PRIHGIKDKKIlDEIVEKSLR--GAAIWdelKDRLdqnAYGLSGGQQQRVCIARCLAIEPDVILMDEPTSALDPIST 222
Cdd:TIGR01257 2034 ylyARLRGVPAEEI-EKVANWSIQslGLSLY---ADRL---AGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR 2106
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1374671911 223 LRV-EELVQDLKKDYSIIIVTHNMQQAARVSDKTAFFLNG 261
Cdd:TIGR01257 2107 RMLwNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
139-218 |
2.17e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.55 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 139 SIYDNITyGPRIHGIKDKKILDEIVEkslRGAAiwDELKDRL-------DQNAYGLSGGQQQRVCIARCLAIEPDVILMD 211
Cdd:NF040905 356 DIKRNIT-LANLGKVSRRGVIDENEE---IKVA--EEYRKKMniktpsvFQKVGNLSGGNQQKVVLSKWLFTDPDVLILD 429
|
....*..
gi 1374671911 212 EPTSALD 218
Cdd:NF040905 430 EPTRGID 436
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
68-243 |
2.51e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 44.14 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 68 EKNVTAIIGPSGSGKSTYVKALNrmVELVPTVKTSGKILYRDQNIFDKSypveKLRTNVGMVFQQPN--------PFpkS 139
Cdd:cd03240 21 FSPLTLIVGQNGAGKTTIIEALK--YALTGELPPNSKGGAHDPKLIREG----EVRAQVKLAFENANgkkytitrSL--A 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 140 IYDNITYgprIH-GIKDKKILDEIvekslrgaaiwdelkDRLdqnayglSGGQQQ------RVCIARCLAIEPDVILMDE 212
Cdd:cd03240 93 ILENVIF---CHqGESNWPLLDMR---------------GRC-------SGGEKVlasliiRLALAETFGSNCGILALDE 147
|
170 180 190
....*....|....*....|....*....|....
gi 1374671911 213 PTSALDPIS-TLRVEELV--QDLKKDYSIIIVTH 243
Cdd:cd03240 148 PTTNLDEENiEESLAEIIeeRKSQKNFQLIVITH 181
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
59-255 |
2.71e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.17 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 59 LKNVNLDILEKNVTAIIGPSGSGKSTYVKALNrmvELVPTVKTSGKILYRDQ-----NIFDKsypvEKLrtnvGMVF--Q 131
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLS---GVYPHGSYEGEILFDGEvcrfkDIRDS----EAL----GIVIihQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 132 QPNPFPK-SIYDNITYGPrihgikdkkildeivEKSLRGAAIWDELKDR---------LDQNAYGLSG----GQQQRVCI 197
Cdd:NF040905 86 ELALIPYlSIAENIFLGN---------------ERAKRGVIDWNETNRRarellakvgLDESPDTLVTdigvGKQQLVEI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 198 ARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKKD--YSIIIvTHNMQQAARVSDKT 255
Cdd:NF040905 151 AKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQgiTSIII-SHKLNEIRRVADSI 209
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
69-245 |
3.88e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 42.75 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 69 KNVTAIIGPSGSGKSTYVKALNRmvelvptvktsgkilyrdqNIFDKSYPVeklrtnvgmvfqqpnpfpksIYDNITygp 148
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALAR-------------------ELGPPGGGV--------------------IYIDGE--- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 149 rihgikdkkildeivekSLRGAAIWDELKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPTSALDPIST------ 222
Cdd:smart00382 40 -----------------DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEalllll 102
|
170 180
....*....|....*....|...
gi 1374671911 223 LRVEELVQDLKKDYSIIIVTHNM 245
Cdd:smart00382 103 EELRLLLLLKSEKNLTVILTTND 125
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
161-265 |
5.45e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.96 E-value: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 161 EIVEKSLRGAAiwDELKDRLD------QNAYGLSGGQQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDLKK 234
Cdd:NF000106 115 DLSRKDARARA--DELLERFSlteaagRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVR 192
|
90 100 110
....*....|....*....|....*....|....*...
gi 1374671911 235 D-YSIIIVTHNMQQAARVS------DKTAFFLNGYVNE 265
Cdd:NF000106 193 DgATVLLTTQYMEEAEQLAheltviDRGRVIADGKVDE 230
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
54-275 |
6.47e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.11 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 54 GEQH-SLKNVNLDILEKNVTAIIGPSGSGKSTyvkaLNRMVELVpTVKTSGKIlyrdqnifDKSYPVEKLRTNVGMVFQQ 132
Cdd:PRK13545 34 GEYHyALNNISFEVPEGEIVGIIGLNGSGKST----LSNLIAGV-TMPNKGTV--------DIKGSAALIAISSGLNGQL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 133 pnpfpkSIYDNITYGPRIHGIKDKKIlDEIVEKSLRGAaiwdELKDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDE 212
Cdd:PRK13545 101 ------TGIENIELKGLMMGLTKEKI-KEIIPEIIEFA----DIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1374671911 213 PTSALDPISTLRVEELVQDLK-KDYSIIIVTHNMQQAARVSDKTAFFLNGYVNEYDDTDKIFSN 275
Cdd:PRK13545 170 ALSVGDQTFTKKCLDKMNEFKeQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
67-250 |
7.08e-05 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 42.84 E-value: 7.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 67 LEKNVTAIIGPSGSGKSTYVKALnRMVelvpTVKTSGKILyRDQN----IFDKSYPVEKL-RTNVGMVFqqpnpfpksiy 141
Cdd:cd03278 20 FPPGLTAIVGPNGSGKSNIIDAI-RWV----LGEQSAKSL-RGEKmsdvIFAGSETRKPAnFAEVTLTF----------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 142 DNITygpRIHGIKDKKILDEIVE---KSLRgaaiwdelkdRLDQnaygLSGGQQQRVCIARCLAIE-----PDVILmDEP 213
Cdd:cd03278 83 DNSD---GRYSIISQGDVSEIIEapgKKVQ----------RLSL----LSGGEKALTALALLFAIFrvrpsPFCVL-DEV 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1374671911 214 TSALDPISTLRVEELVQDLKKDYSIIIVTHN---MQQAAR 250
Cdd:cd03278 145 DAALDDANVERFARLLKEFSKETQFIVITHRkgtMEAADR 184
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-268 |
1.27e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.34 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 5 KELEK-HTEKVNDSHEKQPFIAKDQTEK-HetlsdrerRVVYSTQNLDLWYGEQHSLKNVNLDILEKNVTAIIGPSGSGK 82
Cdd:PRK15064 287 KQIDKiKLEEVKPSSRQNPFIRFEQDKKlH--------RNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 83 STYVKALnrMVELVP---TVKTS--GKILY----------RDQNIFD--KSYPVEK-----LRTNVG-MVFQQpnpfpks 139
Cdd:PRK15064 359 TTLLRTL--VGELEPdsgTVKWSenANIGYyaqdhaydfeNDLTLFDwmSQWRQEGddeqaVRGTLGrLLFSQ------- 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 140 iydnitygprihgikdkkilDEIvEKSLRGaaiwdelkdrldqnaygLSGGQQQRVCIARCLAIEPDVILMDEPTSALDP 219
Cdd:PRK15064 430 --------------------DDI-KKSVKV-----------------LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDM 471
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1374671911 220 IStlrVEELVQDLKK-DYSIIIVTHNMQ----QAARVSDKTAFFLNGYVNEYDD 268
Cdd:PRK15064 472 ES---IESLNMALEKyEGTLIFVSHDREfvssLATRIIEITPDGVVDFSGTYEE 522
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
175-250 |
1.59e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.19 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 175 ELKDRLDQNAYGLSGGQQQRVCIArcLAI--EPDVILMDEPTSALDPISTLRVEELVQDL--KKDYSIIIVTHNMQQAAR 250
Cdd:NF033858 386 DLADVADALPDSLPLGIRQRLSLA--VAVihKPELLILDEPTSGVDPVARDMFWRLLIELsrEDGVTIFISTHFMNEAER 463
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
74-254 |
1.64e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 41.71 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 74 IIGPSGSGKSTyvkaLNRMVE-LVPTvkTSGKILYRDQnifdksyPVEKLRTnvgmvfqqpnpfpkSIYDNITY-GpriH 151
Cdd:PRK13538 32 IEGPNGAGKTS----LLRILAgLARP--DAGEVLWQGE-------PIRRQRD--------------EYHQDLLYlG---H 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 152 --GIKDkkilDEIVEKSLR----------GAAIWDEL-----KDRLDQNAYGLSGGQQQRVCIARCLAIEPDVILMDEPT 214
Cdd:PRK13538 82 qpGIKT----ELTALENLRfyqrlhgpgdDEALWEALaqvglAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1374671911 215 SALDPISTLRVEELV-QDLKKDYSIIIVTHnmQQAARVSDK 254
Cdd:PRK13538 158 TAIDKQGVARLEALLaQHAEQGGMVILTTH--QDLPVASDK 196
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
74-224 |
1.78e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.80 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 74 IIGPSGSGKSTyvkaLNRM-----------VELVPTVKTSgkilYRDQNifdksypveklRTNVgmvfqQPNpfpKSIYD 142
Cdd:PRK11819 355 IIGPNGAGKST----LFKMitgqeqpdsgtIKIGETVKLA----YVDQS-----------RDAL-----DPN---KTVWE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 143 NITYGprihgikdkkiLDEI----VEKSLR---------GAaiwdelkdrlDQN--AYGLSGGQQQRVCIARCLAIEPDV 207
Cdd:PRK11819 408 EISGG-----------LDIIkvgnREIPSRayvgrfnfkGG----------DQQkkVGVLSGGERNRLHLAKTLKQGGNV 466
|
170
....*....|....*..
gi 1374671911 208 ILMDEPTSALDpISTLR 224
Cdd:PRK11819 467 LLLDEPTNDLD-VETLR 482
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
186-248 |
2.50e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.31 E-value: 2.50e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1374671911 186 GLSGGQQQRVCIARCLAIEPDVILMDEPTSALDPISTLRVEELVQDL--KKDYSIIIVTHNMQQA 248
Cdd:PRK10938 401 SLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLisEGETQLLFVSHHAEDA 465
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
56-84 |
2.97e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.32 E-value: 2.97e-04
10 20
....*....|....*....|....*....
gi 1374671911 56 QHSLKNVNLDILEKNVTAIIGPSGSGKST 84
Cdd:COG0178 13 EHNLKNIDVDIPRNKLVVITGLSGSGKSS 41
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
186-218 |
3.20e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.14 E-value: 3.20e-04
10 20 30
....*....|....*....|....*....|...
gi 1374671911 186 GLSGGQQQRVCIARCLAIEPDVILMDEPTSALD 218
Cdd:PLN03140 1019 GLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
187-285 |
5.85e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 187 LSGGQQQRVCIARCLAIEPDVI--LMDEPTSALDPISTLRVEELVQDLK-KDYSIIIVTHNMQQ---AARVSD--KTAFF 258
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRdQGNTVLLVEHDEQMislADRIIDigPGAGI 556
|
90 100
....*....|....*....|....*..
gi 1374671911 259 LNGYVnEYDDTDKIFSNPSDKQTEDYI 285
Cdd:PRK00635 557 FGGEV-LFNGSPREFLAKSDSLTAKYL 582
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
64-101 |
6.20e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.19 E-value: 6.20e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1374671911 64 LDILEKNVTAIIGPSGSGKSTYVKALnrMVELVPTVKT 101
Cdd:pfam13555 17 IPIDPRGNTLLTGPSGSGKSTLLDAI--QTLLVPAKRA 52
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
56-91 |
7.06e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.17 E-value: 7.06e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1374671911 56 QHSLKNVNLDI-LEKnVTAIIGPSGSGKSTYV-----KALNR 91
Cdd:COG0178 618 ENNLKNVDVEIpLGV-LTCVTGVSGSGKSTLVndilyPALAR 658
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
56-91 |
7.67e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.83 E-value: 7.67e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1374671911 56 QHSLKNVNLDILEKNVTAIIGPSGSGKSTYV-----KALNR 91
Cdd:PRK00349 622 ENNLKNVDVEIPLGKFTCVTGVSGSGKSTLInetlyKALAR 662
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
194-243 |
1.30e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.88 E-value: 1.30e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1374671911 194 RVCIARCLAIEPDVILMDEPTSALDpISTLRVEELVQDlKKDYSIIIVTH 243
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLD-INTIRWLEDVLN-ERNSTMIIISH 210
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
58-243 |
1.53e-03 |
|
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: 39.60 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 58 SLKNVNLDiLEKNVTAIIGPSGSGKSTYVKALNRMVELVPTVKTSGKILYRDQNIFDKSYPVE-KLRTNVGMVF------ 130
Cdd:COG3593 13 SIKDLSIE-LSDDLTVLVGENNSGKSSILEALRLLLGPSSSRKFDEEDFYLGDDPDLPEIEIElTFGSLLSRLLrlllke 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 131 QQPNPFPKSIYD-NITYGPRIHGIKDKkiLDEIVEKSLRGAAI-----WDELKDRLDQ-----------NAYGLSGGQQQ 193
Cdd:COG3593 92 EDKEELEEALEElNEELKEALKALNEL--LSEYLKELLDGLDLelelsLDELEDLLKSlslriedgkelPLDRLGSGFQR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1374671911 194 RVCIARCLAI-------EPDVILMDEPTSALDPISTLRVEELVQDL-KKDYSIIIVTH 243
Cdd:COG3593 170 LILLALLSALaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELsEKPNQVIITTH 227
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
56-84 |
1.82e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.67 E-value: 1.82e-03
10 20
....*....|....*....|....*....
gi 1374671911 56 QHSLKNVNLDILEKNVTAIIGPSGSGKST 84
Cdd:PRK00349 13 EHNLKNIDLDIPRDKLVVFTGLSGSGKSS 41
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
56-84 |
3.35e-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: 3.35e-03
10 20
....*....|....*....|....*....
gi 1374671911 56 QHSLKNVNLDILEKNVTAIIGPSGSGKST 84
Cdd:TIGR00630 9 EHNLKNIDVEIPRDKLVVITGLSGSGKSS 37
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
187-248 |
4.99e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 38.50 E-value: 4.99e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 187 LSGGQQQRVCIARCLAI-----EPDVILmDEPTSALDPISTLRVEELVQDLKKDYSIIIVTHN---MQQA 248
Cdd:TIGR02168 1090 LSGGEKALTALALLFAIfkvkpAPFCIL-DEVDAPLDDANVERFANLLKEFSKNTQFIVITHNkgtMEVA 1158
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
58-89 |
5.84e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 37.99 E-value: 5.84e-03
10 20 30
....*....|....*....|....*....|..
gi 1374671911 58 SLKNVNLDIleKNVTAIIGPSGSGKSTYVKAL 89
Cdd:COG4637 12 SLRDLELPL--GPLTVLIGANGSGKSNLLDAL 41
|
|
| GPN2 |
cd17871 |
GPN-loop GTPase 2; GPN-loop GTPase 2 (GPN2) is a small GTPase required for proper localization ... |
73-95 |
6.80e-03 |
|
GPN-loop GTPase 2; GPN-loop GTPase 2 (GPN2) is a small GTPase required for proper localization of RNA polymerase II and III (RNAPII and RNAPIII). It forms heterodimers with GPN1 or GPN3.
Pssm-ID: 349780 Cd Length: 196 Bit Score: 36.75 E-value: 6.80e-03
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
147-244 |
7.35e-03 |
|
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: 37.37 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1374671911 147 GPRIHGIKDKKILDEIVEKSLRGA-AIWDELKDRLDQNAYGLSGGQQQRVCIA---RCLAIEPDVILMDEPTSALDP--I 220
Cdd:pfam13304 196 DLNLSDLGEGIEKSLLVDDRLRERgLILLENGGGGELPAFELSDGTKRLLALLaalLSALPKGGLLLIDEPESGLHPklL 275
|
90 100
....*....|....*....|....
gi 1374671911 221 STLrVEELVQDLKKDYSIIIVTHN 244
Cdd:pfam13304 276 RRL-LELLKELSRNGAQLILTTHS 298
|
|
| |
