|
Name |
Accession |
Description |
Interval |
E-value |
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-255 |
0e+00 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 506.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 1 MTLRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSL 80
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 81 LPQHHLTPEGITVQELVSYGRNPWLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVV 160
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 161 LLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMTPGLLRTVFSVEAE 240
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVEAE 240
|
250
....*....|....*
gi 16132108 241 IHPEPVSGRPMCLMR 255
Cdd:PRK11231 241 IHPEPVSGTPMCVVR 255
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-253 |
7.35e-138 |
|
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: 387.86 E-value: 7.35e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLP 82
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 83 QHHLTPEGITVQELVSYGRNPWLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLL 162
Cdd:COG1120 82 QEPPAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 163 DEPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMTPGLLRTVFSVEAEI 241
Cdd:COG1120 162 DEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEARV 241
|
250
....*....|..
gi 16132108 242 HPEPVSGRPMCL 253
Cdd:COG1120 242 IEDPVTGRPLVL 253
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-253 |
5.30e-108 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 312.02 E-value: 5.30e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 4 RTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLPQ 83
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 84 H-HLTPEgITVQELVSYGRNPWLSlwGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLL 162
Cdd:COG4604 83 EnHINSR-LTVRELVAFGRFPYSK--GRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 163 DEPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMTPGLLRTVFSVEAEI 241
Cdd:COG4604 160 DEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDTDIEV 239
|
250
....*....|..
gi 16132108 242 HpePVSGRPMCL 253
Cdd:COG4604 240 E--EIDGKRICV 249
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
3-251 |
5.51e-92 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 271.86 E-value: 5.51e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLP 82
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 83 QHHLTPEGITVQELVSYGRNPWLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLL 162
Cdd:PRK10253 88 QNATTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 163 DEPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMTPGLLRTVFSVEAEI 241
Cdd:PRK10253 168 DEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRCMI 247
|
250
....*....|
gi 16132108 242 HPEPVSGRPM 251
Cdd:PRK10253 248 IDDPVAGTPL 257
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-255 |
1.55e-88 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 262.79 E-value: 1.55e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 1 MTLRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSL 80
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 81 LPQH-HLT-PegITVQELVSYGRNPWlslwGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQ--- 155
Cdd:PRK13548 81 LPQHsSLSfP--FTVEEVVAMGRAPH----GLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQlwe 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 156 ---NTPVVLLDEPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMTPGLL 231
Cdd:PRK13548 155 pdgPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETL 234
|
250 260
....*....|....*....|....
gi 16132108 232 RTVFSVEAEIHPEPVSGRPMCLMR 255
Cdd:PRK13548 235 RRVYGADVLVQPHPETGAPLVLPR 258
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-251 |
6.38e-86 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 256.20 E-value: 6.38e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLP 82
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 83 QHHLTPEGITVQELVSYGRNPWlslwGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQ------N 156
Cdd:COG4559 82 QHSSLAFPFTVEEVVALGRAPH----GSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwepvdG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 157 TP-VVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMTPGLLRTVF 235
Cdd:COG4559 158 GPrWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERVY 237
|
250
....*....|....*.
gi 16132108 236 SVEAEIHPEPVSGRPM 251
Cdd:COG4559 238 GADLRVLAHPEGGCPQ 253
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-220 |
7.05e-86 |
|
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: 253.13 E-value: 7.05e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 4 RTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLPQ 83
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 84 hhltpegitvqelvsygrnpwlslwgrlsaednarvnvAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLD 163
Cdd:cd03214 81 --------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16132108 164 EPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQG 220
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-235 |
1.07e-81 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 245.00 E-value: 1.07e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPInmlssRQLARRLSLLP 82
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----RRARRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 83 QHHLTPEG--ITVQELVSYGRNPWLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVV 160
Cdd:COG1121 82 QRAEVDWDfpITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16132108 161 LLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMaNGHVMAQGTPEEVMTPGLLRTVF 235
Cdd:COG1121 162 LLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPENLSRAY 235
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-250 |
2.98e-78 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 241.67 E-value: 2.98e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 1 MTLRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSL 80
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 81 LPQHHLTPEGITVQELVSYGRNPWLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVV 160
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 161 LLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMTPGLLRTVFSVEAE 240
Cdd:PRK09536 162 LLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDARTA 241
|
250
....*....|
gi 16132108 241 IHPEPVSGRP 250
Cdd:PRK09536 242 VGTDPATGAP 251
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-251 |
8.04e-76 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 230.83 E-value: 8.04e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 2 TLRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLL 81
Cdd:PRK10575 11 TFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 82 PQHHLTPEGITVQELVSYGRNPWLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVL 161
Cdd:PRK10575 91 PQQLPAAEGMTVRELVAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 162 LDEPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMTPGLLRTVFSVEAE 240
Cdd:PRK10575 171 LDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGIPMG 250
|
250
....*....|.
gi 16132108 241 IHPEPVSGRPM 251
Cdd:PRK10575 251 ILPHPAGAAPV 261
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
3-251 |
1.43e-73 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 224.69 E-value: 1.43e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLP 82
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRRARARRVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 83 QHHLTPEGITVQELVSYGRNPWLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLL 162
Cdd:TIGR03873 82 QDSDTAVPLTVRDVVALGRIPHRSLWAGDSPHDAAVVDRALARTELSHLADRDMSTLSGGERQRVHVARALAQEPKLLLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 163 DEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMTPGLLRTVFSVEAEIH 242
Cdd:TIGR03873 162 DEPTNHLDVRAQLETLALVRELAATGVTVVAALHDLNLAASYCDHVVVLDGGRVVAAGPPREVLTPALIRAVYGVDATVL 241
|
....*....
gi 16132108 243 PEPVSGRPM 251
Cdd:TIGR03873 242 THPDTGRPI 250
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-220 |
6.70e-71 |
|
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: 216.25 E-value: 6.70e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 4 RTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSsrqlaRRLSLLPQ 83
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER-----KRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 84 HHLTPEG--ITVQELVSYGRNPWLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVL 161
Cdd:cd03235 76 RRSIDRDfpISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16132108 162 LDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQlVVMANGHVMAQG 220
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDR-VLLLNRTVVASG 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-227 |
4.05e-66 |
|
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: 204.87 E-value: 4.05e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSY-GTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLL 81
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 82 PQHhltPE----GITVQELVSYG-RNPWLSlwgrlSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQN 156
Cdd:COG1122 81 FQN---PDdqlfAPTVEEDVAFGpENLGLP-----REEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16132108 157 TPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMT 227
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-215 |
4.69e-61 |
|
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: 191.14 E-value: 4.69e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 4 RTENLTVSYGTD--KVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLL 81
Cdd:cd03225 1 ELKNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 82 PQHhltPE----GITVQELVSYGrnpwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNT 157
Cdd:cd03225 81 FQN---PDdqffGPTVEEEVAFG----LENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16132108 158 PVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGH 215
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-235 |
1.08e-60 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 191.05 E-value: 1.08e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINmLSSRQLARRLSLLP 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA-RDPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 83 QHHLTPEGITVQELVSYgrnpWLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLL 162
Cdd:COG1131 80 QEPALYPDLTVRENLRF----FARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16132108 163 DEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMTpGLLRTVF 235
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA-RLLEDVF 227
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-225 |
1.29e-58 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 186.22 E-value: 1.29e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTV-FLGDNPINmlSSRQLARRLSLL 81
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSIlIDGEDVRK--EPREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 82 PQHHLTPEGITVQELVSY-GRnpwlsLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVV 160
Cdd:COG4555 80 PDERGLYDRLTVRENIRYfAE-----LYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16132108 161 LLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-225 |
1.61e-55 |
|
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: 178.15 E-value: 1.61e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDK-VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSS---RQLARRL 78
Cdd:cd03256 1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 79 SLLPQHHLTPEGITVQELVSYGR----NPWLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLA 154
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRlgrrSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16132108 155 QNTPVVLLDEPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
3-227 |
3.28e-55 |
|
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: 177.24 E-value: 3.28e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARR----- 77
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgigrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 78 ---LSLLPqhHLTP-EGITVQELVSYGRNPWLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVL 153
Cdd:cd03219 81 fqiPRLFP--ELTVlENVMVAAQARTGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16132108 154 AQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMT 227
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-240 |
3.51e-55 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 177.56 E-value: 3.51e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDK-VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLA---RRL 78
Cdd:COG3638 3 LELRNLSKRYPGGTpALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRrlrRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 79 SLLPQHHLTPEGITVQELVSYGR----NPWLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLA 154
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLAGRlgrtSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 155 QNTPVVLLDEPTTYLDIN--HQVdlMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVmTPGLL 231
Cdd:COG3638 163 QEPKLILADEPVASLDPKtaRQV--MDLLRRIaREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL-TDAVL 239
|
....*....
gi 16132108 232 RTVFSVEAE 240
Cdd:COG3638 240 REIYGGEAE 248
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-203 |
4.55e-52 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 167.80 E-value: 4.55e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 11 SYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVflgdnpinmlsSRQLARRLSLLPQHHLTPEG 90
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQRSEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 91 --ITVQELVSYGRNPWLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTY 168
Cdd:NF040873 70 lpLTVRDLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|....*
gi 16132108 169 LDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASR 203
Cdd:NF040873 150 LDAESRERIIALLAEEHARGATVVVVTHDLELVRR 184
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-216 |
2.94e-51 |
|
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: 164.88 E-value: 2.94e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTV-FLGDNPINmlSSRQLARRLSLL 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIkVLGKDIKK--EPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 82 PQHhltpegitvqelvsygrnpwLSLWGRLSAEDNARvnvamnqtrinhlavrrlteLSGGQRQRAFLAMVLAQNTPVVL 161
Cdd:cd03230 79 PEE--------------------PSLYENLTVRENLK--------------------LSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16132108 162 LDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHV 216
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-227 |
5.32e-50 |
|
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: 171.24 E-value: 5.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTD-----KVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSS---RQL 74
Cdd:COG1123 261 LEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRrslREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 75 ARRLSLLPQHhltPEG-----ITVQELVSYGrnpwLSLWGRLSAED-NARVNVAMNQTRIN-HLAVRRLTELSGGQRQRA 147
Cdd:COG1123 341 RRRVQMVFQD---PYSslnprMTVGDIIAEP----LRLHGLLSRAErRERVAELLERVGLPpDLADRYPHELSGGQRQRV 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 148 FLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQ-GKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVM 226
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVF 493
|
.
gi 16132108 227 T 227
Cdd:COG1123 494 A 494
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
18-251 |
4.07e-49 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 161.93 E-value: 4.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 18 LNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLmPQSGTVFLGDNPINMLSSRQLARRLSLLPQHHLTPEGITVQELV 97
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 98 SygrnpwlslwgrLSAEDNArvNVAMNQTRINHLA---------VRRLTELSGGQRQRAFLAMVLAQNTPVV-------L 161
Cdd:COG4138 91 A------------LHQPAGA--SSEAVEQLLAQLAealgledklSRPLTQLSGGEWQRVRLAAVLLQVWPTInpegqllL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 162 LDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMTPGLLRTVFSVEAEI 241
Cdd:COG4138 157 LDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVKFRR 236
|
250
....*....|
gi 16132108 242 HpePVSGRPM 251
Cdd:COG4138 237 L--EVEGHRW 244
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-225 |
7.46e-49 |
|
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: 161.31 E-value: 7.46e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDK-VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSS---RQLARRL 78
Cdd:TIGR02315 2 LEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGkklRKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 79 SLLPQHHLTPEGITVQELVSYGR----NPWLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLA 154
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGRlgykPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16132108 155 QNTPVVLLDEPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKTSKQVMDYLKRInKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-215 |
8.03e-49 |
|
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: 158.18 E-value: 8.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 4 RTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLPQ 83
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 84 hhltpegitvqelvsygrnpwlslwgrlsaednarvnvamnqtrinhlavrrlteLSGGQRQRAFLAMVLAQNTPVVLLD 163
Cdd:cd00267 81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16132108 164 EPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGH 215
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-220 |
2.94e-48 |
|
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: 158.45 E-value: 2.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQlaRRLSLLP 82
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 83 QH-----HLtpegiTVQELVSYGrnpwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNT 157
Cdd:cd03259 79 QDyalfpHL-----TVAENIAFG----LKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16132108 158 PVVLLDEPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQG 220
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
3-226 |
5.31e-48 |
|
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: 159.43 E-value: 5.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARR----- 77
Cdd:COG0411 5 LEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLgiart 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 78 ---------LS-----LLPQHHLTPEGITvqelvsygrNPWLSLWGRLSAEDNARVNV--AMNQTRINHLAVRRLTELSG 141
Cdd:COG0411 85 fqnprlfpeLTvlenvLVAAHARLGRGLL---------AALLRLPRARREEREARERAeeLLERVGLADRADEPAGNLSY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 142 GQRQRAFLAMVLAQNTPVVLLDEPTTYLdiNHQ--VDLMRLMGELR-TQGKTVVAVLHDLNQASRYCDQLVVMANGHVMA 218
Cdd:COG0411 156 GQQRRLEIARALATEPKLLLLDEPAAGL--NPEetEELAELIRRLRdERGITILLIEHDMDLVMGLADRIVVLDFGRVIA 233
|
....*...
gi 16132108 219 QGTPEEVM 226
Cdd:COG0411 234 EGTPAEVR 241
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-219 |
5.85e-48 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 158.28 E-value: 5.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDK----VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLA--- 75
Cdd:COG1136 5 LELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 76 -RRLSLLPQ-HHLTPEgITVQELVSYGrnpwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVL 153
Cdd:COG1136 85 rRHIGFVFQfFNLLPE-LTALENVALP----LLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16132108 154 AQNTPVVLLDEPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASrYCDQLVVMANGHVMAQ 219
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHDPELAA-RADRVIRLRDGRIVSD 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-245 |
1.18e-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: 165.08 E-value: 1.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSY--GTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQ---SGTVFLGDNPINMLSSRQLARR 77
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 78 LSLLPQ---HHLTPegITVQELVSYG-RNPWLSlwgrlSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVL 153
Cdd:COG1123 85 IGMVFQdpmTQLNP--VTVGDQIAEAlENLGLS-----RAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 154 AQNTPVVLLDEPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMT-PGLL 231
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAaPQAL 237
|
250
....*....|....
gi 16132108 232 RTVFSVEAEIHPEP 245
Cdd:COG1123 238 AAVPRLGAARGRAA 251
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-216 |
2.43e-47 |
|
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: 156.50 E-value: 2.43e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDK----VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLA--- 75
Cdd:cd03255 1 IELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 76 -RRLSLLPQ-HHLTPEgITVQELVSYGrnpwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVL 153
Cdd:cd03255 81 rRHIGFVFQsFNLLPD-LTALENVELP----LLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16132108 154 AQNTPVVLLDEPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDlNQASRYCDQLVVMANGHV 216
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-220 |
2.48e-47 |
|
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: 156.90 E-value: 2.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTD----KVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTV-FLGDNPINMLSSRQLARR 77
Cdd:cd03257 2 LEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIiFDGKDLLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 78 --LSLLPQH---HLTPeGITVQELVsygRNPwLSLWGRLSAEDNARVNVAMNQTRINhLAVRRLT----ELSGGQRQRAF 148
Cdd:cd03257 82 keIQMVFQDpmsSLNP-RMTIGEQI---AEP-LRIHGKLSKKEARKEAVLLLLVGVG-LPEEVLNryphELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16132108 149 LAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQ-GKTVVAVLHDLNQASRYCDQLVVMANGHVMAQG 220
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-225 |
4.12e-47 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 159.54 E-value: 4.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 1 MTLRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDN--PINmLSSRQlaRRL 78
Cdd:COG1118 1 MSIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdlFTN-LPPRE--RRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 79 SLLPQH-----HLtpegiTVQELVSYGrnpwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVL 153
Cdd:COG1118 78 GFVFQHyalfpHM-----TVAENIAFG----LRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16132108 154 AQNTPVVLLDEPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:COG1118 149 AVEPEVLLLDEPFGALDAKVRKELRRWLRRLhDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
3-225 |
1.32e-46 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 158.34 E-value: 1.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQlaRRLSLLP 82
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK--RNVGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 83 QH-----HLtpegiTVQELVSYGrnpwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNT 157
Cdd:COG3842 84 QDyalfpHL-----TVAENVAFG----LRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16132108 158 PVVLLDEPTTYLDINH----QVDLMRLmgeLRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:COG3842 155 RVLLLDEPLSALDAKLreemREELRRL---QRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
6-227 |
7.33e-46 |
|
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: 153.21 E-value: 7.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLA---RRLSLLP 82
Cdd:COG1127 9 RNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrRRIGMLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 83 QHhltpeG-----ITVQELVSYGrnpwLSLWGRLSAED-NARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQN 156
Cdd:COG1127 89 QG-----GalfdsLTVFENVAFP----LREHTDLSEAEiRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16132108 157 TPVVLLDEPTTYLD-INHQVdLMRLMGELRTQ-GKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMT 227
Cdd:COG1127 160 PEILLYDEPTAGLDpITSAV-IDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-167 |
1.11e-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: 1.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 18 LNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLPQH-HLTPEgITVQEL 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDpQLFPR-LTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16132108 97 VSYGRNpwlsLWGRLSAEDNARVNVAMNQTRINHLAVRRL----TELSGGQRQRAFLAMVLAQNTPVVLLDEPTT 167
Cdd:pfam00005 80 LRLGLL----LKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-226 |
1.60e-45 |
|
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: 159.92 E-value: 1.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 2 TLRTENLTVSYGTDK-VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSL 80
Cdd:COG4988 336 SIELEDVSFSYPGGRpALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 81 LPQHHLTPEGiTVQElvsygrnpWLSLwGRLSAEDnARVNVAMNQTRINHLaVRRLTE------------LSGGQRQRAF 148
Cdd:COG4988 416 VPQNPYLFAG-TIRE--------NLRL-GRPDASD-EELEAALEAAGLDEF-VAALPDgldtplgeggrgLSGGQAQRLA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16132108 149 LAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRtQGKTVVAVLHDLNQASRyCDQLVVMANGHVMAQGTPEEVM 226
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELL 559
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-225 |
1.83e-45 |
|
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: 153.38 E-value: 1.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSY--GTD---KVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGD---NPINMLSSRQLARR 77
Cdd:TIGR04521 4 KNVSYIYqpGTPfekKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGrdiTAKKKKKLKDLRKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 78 LSLL---PQHHLTPEgiTVQELVSYG-RNPWLSLwgrlsAEDNARVNVAMNQTRINH-LAVRRLTELSGGQRQRAFLAMV 152
Cdd:TIGR04521 84 VGLVfqfPEHQLFEE--TVYKDIAFGpKNLGLSE-----EEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16132108 153 LAQNTPVVLLDEPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:TIGR04521 157 LAMEPEVLILDEPTAGLDPKGRKEILDLFKRLhKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREV 230
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-214 |
4.19e-45 |
|
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: 150.49 E-value: 4.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 4 RTENLTVSYG-TDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPInmlSSRQLARRLSLLP 82
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 83 Q---HHLTPEgiTVQELVSYGRnpwlslwgRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPV 159
Cdd:cd03226 78 QdvdYQLFTD--SVREELLLGL--------KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16132108 160 VLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANG 214
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-227 |
4.55e-45 |
|
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: 151.12 E-value: 4.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSS---RQLARRLSLLP 82
Cdd:cd03261 4 RGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelYRLRRRMGMLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 83 QHHLTPEGITVQELVSYgrnpWLSLWGRLSAED-NARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVL 161
Cdd:cd03261 84 QSGALFDSLTVFENVAF----PLREHTRLSEEEiREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16132108 162 LDEPTTYLD-INHQVdLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMT 227
Cdd:cd03261 160 YDEPTAGLDpIASGV-IDDLIRSLkKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-226 |
1.39e-44 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 149.91 E-value: 1.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVlnDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQlaRRLSLLP 82
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 83 Q-----HHLTpegitVQELVSYGRNPWLslwgRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNT 157
Cdd:COG3840 78 QennlfPHLT-----VAQNIGLGLRPGL----KLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 158 PVVLLDEPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVM 226
Cdd:COG3840 149 PILLLDEPFSALDPALRQEMLDLVDELcRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALL 218
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-226 |
5.27e-44 |
|
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: 148.80 E-value: 5.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTD----KVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRL 78
Cdd:COG1124 2 LEVRNLSVSYGQGgrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 79 SLLPQHhltPEGI-----TVQELVSygrnpwLSLWGRLSAEDNARVNVAMNQTRIN-HLAVRRLTELSGGQRQRAFLAMV 152
Cdd:COG1124 82 QMVFQD---PYASlhprhTVDRILA------EPLRIHGLPDREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16132108 153 LAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQ-GKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVM 226
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-215 |
6.22e-44 |
|
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: 146.56 E-value: 6.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLS--SRQLARRLSL 80
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 81 LPQHHltpegitvqelvsygrnpwlSLWGRLSAEDNarvnVAMNqtrinhlavrrlteLSGGQRQRAFLAMVLAQNTPVV 160
Cdd:cd03229 81 VFQDF--------------------ALFPHLTVLEN----IALG--------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16132108 161 LLDEPTTYLDINHQVDLMRLMGELRTQ-GKTVVAVLHDLNQASRYCDQLVVMANGH 215
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-226 |
2.90e-43 |
|
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: 154.15 E-value: 2.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 2 TLRTENLTVSY--GTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLS 79
Cdd:COG4987 333 SLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 80 LLPQH-HL--TpegiTVQElvsygrNpwLSLwGRLSAEDnARVNVAMNQTRINHLaVRRLTE------------LSGGQR 144
Cdd:COG4987 413 VVPQRpHLfdT----TLRE------N--LRL-ARPDATD-EELWAALERVGLGDW-LAALPDgldtwlgeggrrLSGGER 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 145 QRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELrTQGKTVVAVLHDLNQASRyCDQLVVMANGHVMAQGTPEE 224
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEE 555
|
..
gi 16132108 225 VM 226
Cdd:COG4987 556 LL 557
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-225 |
2.90e-43 |
|
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: 146.17 E-value: 2.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLM-----PQSGTVFLGDNPINMLSSRQLA-- 75
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVLElr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 76 RRLSLLPQhHLTPEGITVQELVSYGrnpwLSLWG-RLSAEDNARVNVAMNQTRINHLAVRRL--TELSGGQRQRAFLAMV 152
Cdd:cd03260 81 RRVGMVFQ-KPNPFPGSIYDNVAYG----LRLHGiKLKEELDERVEEALRKAALWDEVKDRLhaLGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16132108 153 LAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQgKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-215 |
5.27e-43 |
|
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: 143.68 E-value: 5.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTD--KVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSL 80
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 81 LPQhhltpegitvqelvsygrNPWL---SLWgrlsaeDNarvnvamnqtrInhlavrrlteLSGGQRQRAFLAMVLAQNT 157
Cdd:cd03228 81 VPQ------------------DPFLfsgTIR------EN-----------I----------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16132108 158 PVVLLDEPTTYLDINHQVDLMRLMGELRtQGKTVVAVLHDLNQAsRYCDQLVVMANGH 215
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALA-KGKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3-224 |
2.63e-42 |
|
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: 143.41 E-value: 2.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTD--KVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNpiNMLSSRQLARR-LS 79
Cdd:cd03263 1 LQIRNLTKTYKKGtkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGY--SIRTDRKAARQsLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 80 LLPQHHLTPEGITVQE-LVSYGRnpwlsLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTP 158
Cdd:cd03263 79 YCPQFDALFDELTVREhLRFYAR-----LKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16132108 159 VVLLDEPTTYLDINHQVDLMRLMGELRtQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEE 224
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-227 |
2.88e-42 |
|
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: 143.98 E-value: 2.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSY-GTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRL--- 78
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIgyv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 79 ----SLLPqhHLtpegiTVQELVsyGRNPWLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLA 154
Cdd:cd03295 81 iqqiGLFP--HM-----TVEENI--ALVPKLLKWPKEKIRERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16132108 155 QNTPVVLLDEPTTYLD----INHQVDLMRLMGELrtqGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMT 227
Cdd:cd03295 152 ADPPLLLMDEPFGALDpitrDQLQEEFKRLQQEL---GKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-197 |
5.57e-42 |
|
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: 142.23 E-value: 5.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 1 MTLRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINmLSSRQLARRLSL 80
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIR-DAREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 81 LPQHHLTPEGITVQELVSYgrnpWLSLWGRlsAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVV 160
Cdd:COG4133 80 LGHADGLKPELTVRENLRF----WAALYGL--RADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 16132108 161 LLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHD 197
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
3-237 |
2.49e-41 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 142.66 E-value: 2.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQ--------SGTVFLGDNPINMLSSRQL 74
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 75 ARRLSLLPQHHLTPEGITVQELVSYGRNPWLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLA 154
Cdd:PRK13547 82 ARLRAVLPQAAQPAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 155 QNTP---------VVLLDEPTTYLDINHQvdlMRLMGELRTQGKT----VVAVLHDLNQASRYCDQLVVMANGHVMAQGT 221
Cdd:PRK13547 162 QLWPphdaaqpprYLLLDEPTAALDLAHQ---HRLLDTVRRLARDwnlgVLAIVHDPNLAARHADRIAMLADGAIVAHGA 238
|
250
....*....|....*.
gi 16132108 222 PEEVMTPGLLRTVFSV 237
Cdd:PRK13547 239 PADVLTPAHIARCYGF 254
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
2-225 |
3.00e-41 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 144.45 E-value: 3.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 2 TLRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQlaRRLSLL 81
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--RNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 82 PQH-----HLtpegiTVQELVSYGrnpwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQN 156
Cdd:COG3839 81 FQSyalypHM-----TVYENIAFP----LKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVRE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16132108 157 TPVVLLDEPTTYLDinhqvdlMRLMGELRTQ--------GKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:COG3839 152 PKVFLLDEPLSNLD-------AKLRVEMRAEikrlhrrlGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-220 |
6.61e-41 |
|
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: 139.64 E-value: 6.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSYGTDKVLNDVSLSLPTGkITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPInmLSSRQLARR-LSLLPQH 84
Cdd:cd03264 4 ENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV--LKQPQKLRRrIGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 85 HLTPEGITVQELVSYgrNPWLSlwGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDE 164
Cdd:cd03264 81 FGVYPNFTVREFLDY--IAWLK--GIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16132108 165 PTTYLDINHQVDLMRLMGELrTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQG 220
Cdd:cd03264 157 PTAGLDPEERIRFRNLLSEL-GEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-225 |
5.53e-40 |
|
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: 138.24 E-value: 5.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 1 MTLRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQlaRRLSL 80
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 81 LPQHHLTPEGITVQELVSYG--------RNPwlslwgrlSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMV 152
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFGlrvkprseRPP--------EAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16132108 153 LAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQ-GKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-225 |
1.74e-39 |
|
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: 136.60 E-value: 1.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQlaRRLSLLP 82
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK--RPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 83 QHH-LTPEgITVQELVSYGrnpwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVL 161
Cdd:cd03300 79 QNYaLFPH-LTVFENIAFG----LRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16132108 162 LDEPTTYLDI----NHQVDLMRLMGELrtqGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:cd03300 154 LDEPLGALDLklrkDMQLELKRLQKEL---GITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-226 |
1.96e-39 |
|
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: 144.59 E-value: 1.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSYGTDK--VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLPQ 83
Cdd:COG2274 477 ENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 84 HHLTPEGiTVQElvsygrNpwLSLWgRLSAEDnARVNVAMNQTRInHLAVRRL------------TELSGGQRQRAFLAM 151
Cdd:COG2274 557 DVFLFSG-TIRE------N--ITLG-DPDATD-EEIIEAARLAGL-HDFIEALpmgydtvvgeggSNLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16132108 152 VLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRtQGKTVVAVLHDLNQAsRYCDQLVVMANGHVMAQGTPEEVM 226
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEELL 697
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-216 |
2.91e-39 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 135.33 E-value: 2.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLP 82
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 83 QH-HLTPEgiTVQELVSYgrnPWLSlwgRLSAEDNARVNVAMNQTRINHLAV-RRLTELSGGQRQRAFLAMVLAQNTPVV 160
Cdd:COG4619 81 QEpALWGG--TVRDNLPF---PFQL---RERKFDRERALELLERLGLPPDILdKPVERLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16132108 161 LLDEPTTYLDINHQVDLMRLMGELRTQ-GKTVVAVLHDLNQASRYCDQLVVMANGHV 216
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-216 |
1.13e-38 |
|
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: 134.14 E-value: 1.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTD----KVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINmlssrQLARRL 78
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT-----GPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 79 SLLPQHHLTPEGITVQELVSYGrnpwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTP 158
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALG----LELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16132108 159 VVLLDEPTTYLDI----NHQVDLMRLmgeLRTQGKTVVAVLHDLNQASRYCDQLVVMAN--GHV 216
Cdd:cd03293 152 VLLLDEPFSALDAltreQLQEELLDI---WRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRI 212
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
18-227 |
3.02e-38 |
|
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: 134.69 E-value: 3.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 18 LNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQL----ARRLSLLPQHH-LTPEgIT 92
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFaLLPH-RT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 93 VQELVSYGrnpwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLD-- 170
Cdd:cd03294 119 VLENVAFG----LEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDpl 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16132108 171 --INHQVDLMRLMGELRtqgKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMT 227
Cdd:cd03294 195 irREMQDELLRLQAELQ---KTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
3-226 |
7.92e-38 |
|
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: 132.17 E-value: 7.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARR-LSLL 81
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 82 PQhhltpegitvqelvsyGRNpwlsLWGRLSAEDNARVnVAMNQTRINHLAVR--------RLTE--------LSGGQRQ 145
Cdd:cd03224 81 PE----------------GRR----IFPELTVEENLLL-GAYARRRAKRKARLervyelfpRLKErrkqlagtLSGGEQQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 146 RAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:cd03224 140 MLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
.
gi 16132108 226 M 226
Cdd:cd03224 220 L 220
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-225 |
1.21e-37 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 132.04 E-value: 1.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINmLSSRQLA---RRLS 79
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINklrRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 80 LLPQH-----HLtpegiTVQELVSYGrnPWLSL-WGRLSAEDNARvnVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVL 153
Cdd:COG1126 81 MVFQQfnlfpHL-----TVLENVTLA--PIKVKkMSKAEAEERAM--ELLERVGLADKADAYPAQLSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16132108 154 AQNTPVVLLDEPTTYLD---INHQVDLMRlmgELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:COG1126 152 AMEPKVMLFDEPTSALDpelVGEVLDVMR---DLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEF 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
3-220 |
2.67e-37 |
|
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: 130.31 E-value: 2.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVlnDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLgdNPINMLSSRQLARRLSLLP 82
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLI--NGVDVTAAPPADRPVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 83 QHHLTPEGITVQELVSYGRNPWLslwgRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLL 162
Cdd:cd03298 77 QENNLFAHLTVEQNVGLGLSPGL----KLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16132108 163 DEPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQG 220
Cdd:cd03298 153 DEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
6-231 |
3.66e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 131.78 E-value: 3.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSY--GTdKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLPQ 83
Cdd:PRK13647 8 EDLHFRYkdGT-KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 84 hhlTPE----GITVQELVSYG-RNPWLSlwgrlSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTP 158
Cdd:PRK13647 87 ---DPDdqvfSSTVWDDVAFGpVNMGLD-----KDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16132108 159 VVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMTPGLL 231
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIV 231
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
6-227 |
3.93e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 131.65 E-value: 3.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSYGTDK--VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLPQ 83
Cdd:PRK13632 11 ENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 84 HhltPE----GITVQELVSYGRnpwlslwgrlsaeDNARVNVAMNQTRINHLAVRRLTE---------LSGGQRQRAFLA 150
Cdd:PRK13632 91 N---PDnqfiGATVEDDIAFGL-------------ENKKVPPKKMKDIIDDLAKKVGMEdyldkepqnLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16132108 151 MVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQG-KTVVAVLHDLNQASRyCDQLVVMANGHVMAQGTPEEVMT 227
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILN 231
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-242 |
5.25e-37 |
|
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: 130.59 E-value: 5.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSG-TVFLGDNPINMLSSRQLARRLSLL 81
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 82 -PQ-HHLTPEGITVQELVSYGRNPWLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPV 159
Cdd:COG1119 84 sPAlQLRFPRDETVLDVVLSGFFDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPEL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 160 VLLDEPTTYLDINHQVDLMRLMGELRTQG-KTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMTPGLLRTVFSVE 238
Cdd:COG1119 164 LILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTSENLSEAFGLP 243
|
....
gi 16132108 239 AEIH 242
Cdd:COG1119 244 VEVE 247
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-226 |
8.39e-37 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 136.45 E-value: 8.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSYGTDK-VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLPQH 84
Cdd:COG1132 343 ENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 85 -HLTPEgiTVQELVSYgrnpwlslwGRLSAEDnARVNVAMNQTRINHLaVRRL------------TELSGGQRQRAFLAM 151
Cdd:COG1132 423 tFLFSG--TIRENIRY---------GRPDATD-EEVEEAAKAAQAHEF-IEALpdgydtvvgergVNLSGGQRQRIAIAR 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16132108 152 VLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRtQGKTVVAVLHDLNQAsRYCDQLVVMANGHVMAQGTPEEVM 226
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTI-RNADRILVLDDGRIVEQGTHEELL 562
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
23-238 |
1.17e-36 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 129.20 E-value: 1.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 23 LSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPinmlsSRQLARRLSLLPQHHL----TPegITVQELVS 98
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS-----PGKGWRHIGYVPQRHEfawdFP--ISVAHTVM 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 99 YGRNPWLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLM 178
Cdd:TIGR03771 74 SGRTGHIGWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLT 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 179 RLMGELRTQGKTVVAVLHDLNQASRYCDQlVVMANGHVMAQGTPEEVMTPGLLRTVFSVE 238
Cdd:TIGR03771 154 ELFIELAGAGTAILMTTHDLAQAMATCDR-VVLLNGRVIADGTPQQLQDPAPWMTTFGVS 212
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-219 |
1.33e-36 |
|
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: 127.16 E-value: 1.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQlARRLsllp 82
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD-ARRA---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 83 qhhltpeGItvqELVSygrnpwlslwgrlsaednarvnvamnqtrinhlavrrltELSGGQRQRAFLAMVLAQNTPVVLL 162
Cdd:cd03216 76 -------GI---AMVY---------------------------------------QLSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 16132108 163 DEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQ 219
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-214 |
1.39e-36 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 129.82 E-value: 1.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDK----VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPInmlssRQLARRL 78
Cdd:COG1116 8 LELRGVSKRFPTGGggvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV-----TGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 79 SLLPQHHLTPEGITVQELVSYGrnpwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTP 158
Cdd:COG1116 83 GVVFQEPALLPWLTVLDNVALG----LELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 159 VVLLDEPTTYLD----INHQVDLMRLmgeLRTQGKTVVAVLHDLNQASRYCDQLVVMANG 214
Cdd:COG1116 159 VLLMDEPFGALDaltrERLQDELLRL---WQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
3-225 |
1.49e-36 |
|
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: 128.99 E-value: 1.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGtDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQlaRRLSLLP 82
Cdd:cd03299 1 LKVENLSKDWK-EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 83 QHH-LTPEgITVQELVSYGrnpwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVL 161
Cdd:cd03299 78 QNYaLFPH-MTVYKNIAYG----LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16132108 162 LDEPTTYLDINHQVDLMRLMGELRTQ-GKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:cd03299 153 LDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEV 217
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-211 |
1.62e-36 |
|
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: 135.11 E-value: 1.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 2 TLRTENLTVSY-GTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSL 80
Cdd:TIGR02857 321 SLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 81 LPQHHLTPEGiTVQELVsygrnpwlsLWGRLSAEDNARVNVAMN-------QTR---INHLAVRRLTELSGGQRQRAFLA 150
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENI---------RLARPDASDAEIREALERagldefvAALpqgLDTPIGEGGAGLSGGQAQRLALA 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16132108 151 MVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRtQGKTVVAVLHDLNQASRyCDQLVVM 211
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-251 |
2.44e-36 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 128.90 E-value: 2.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 21 VSLSLPTGKITALIGPNGCGKSTLLNCFSRLLmPQSGTVFLGDNPINMLSSRQLARRLSLLPQHHLTPEGITVQElvsyg 100
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQ----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 101 rnpWLSLW---GRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVV-------LLDEPTTYLD 170
Cdd:PRK03695 89 ---YLTLHqpdKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPDInpagqllLLDEPMNSLD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 171 INHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMTPGLLRTVFSVEAEIHpePVSGRP 250
Cdd:PRK03695 166 VAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVNFRRL--DVEGHP 243
|
.
gi 16132108 251 M 251
Cdd:PRK03695 244 M 244
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-225 |
3.36e-36 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 131.36 E-value: 3.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 1 MTLRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQlaRRLSL 80
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 81 LPQHHLTPEGITVQELVSYGrnpwLSLWGRL----SAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQN 156
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIAFG----LTVLPRRerpnAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 157 TPVVLLDEPTTYLDINHQVDLMRLMGELRTQGK-TVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-227 |
3.69e-36 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 128.62 E-value: 3.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRL--LMPQ---SGTVFLGDnpINMLSSR----Q 73
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEILLDG--EDIYDPDvdvvE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 74 LARRLSLLPQhHLTPEGITVQELVSYGrnpwLSLWGRLSAED-NARVNVAMNQT--------RINHLAvrrlTELSGGQR 144
Cdd:COG1117 90 LRRRVGMVFQ-KPNPFPKSIYDNVAYG----LRLHGIKSKSElDEIVEESLRKAalwdevkdRLKKSA----LGLSGGQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 145 QRAFLAMVLAQNTPVVLLDEPTTYLD-INHQV--DLMRlmgELRTQgKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGT 221
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALDpISTAKieELIL---ELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGP 236
|
....*.
gi 16132108 222 PEEVMT 227
Cdd:COG1117 237 TEQIFT 242
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
6-226 |
1.23e-35 |
|
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: 126.57 E-value: 1.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSYGTDK-VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLPQH 84
Cdd:cd03254 6 ENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 85 HLTPEGiTVQELVSYGRNpwlslwgrlSAEDnARVNVAMNQTRINHLaVRRLTE------------LSGGQRQRAFLAMV 152
Cdd:cd03254 86 TFLFSG-TIMENIRLGRP---------NATD-EEVIEAAKEAGAHDF-IMKLPNgydtvlgenggnLSQGERQLLAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16132108 153 LAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRtQGKTVVAVLHDLNqASRYCDQLVVMANGHVMAQGTPEEVM 226
Cdd:cd03254 154 MLRDPKILILDEATSNIDTETEKLIQEALEKLM-KGRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-250 |
1.35e-35 |
|
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: 129.02 E-value: 1.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTD----KVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQ---SGTVFLGDNPINMLSSRQL- 74
Cdd:COG0444 2 LEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 75 ---ARRLSLLPQ---HHLTPeGITVQELVSYGrnpwLSLWGRLSAED-NARVNVAMNQTRINHlAVRRLT----ELSGGQ 143
Cdd:COG0444 82 kirGREIQMIFQdpmTSLNP-VMTVGDQIAEP----LRIHGGLSKAEaRERAIELLERVGLPD-PERRLDryphELSGGM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 144 RQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQ-GKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTP 222
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPV 235
|
250 260 270
....*....|....*....|....*....|....*.
gi 16132108 223 EEVM-------TPGLLRTVFSVEAEIHP-EPVSGRP 250
Cdd:COG0444 236 EELFenprhpyTRALLSSIPRLDPDGRRlIPIPGEP 271
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-225 |
1.59e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 128.30 E-value: 1.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 2 TLRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINmlssRQLARRLSLL 81
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD----PEDRRRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 82 pqhhltPE--GI----TVQELVSY-GRnpwlsLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRA-FLAMVL 153
Cdd:COG4152 77 ------PEerGLypkmKVGEQLVYlAR-----LKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVqLIAALL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16132108 154 AQntPVVL-LDEPTTYLD-INhqVDLMR-LMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:COG4152 146 HD--PELLiLDEPFSGLDpVN--VELLKdVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-226 |
1.62e-35 |
|
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: 126.25 E-value: 1.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 1 MTLRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARR-LS 79
Cdd:COG0410 2 PMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 80 LLPQhhltpegitvqelvsyGRNpwlsLWGRLSAEDN---------ARVNVAMN-----------QTRINHLAvrrlTEL 139
Cdd:COG0410 82 YVPE----------------GRR----IFPSLTVEENlllgayarrDRAEVRADlervyelfprlKERRRQRA----GTL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 140 SGGQRQraFLAM--VLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVM 217
Cdd:COG0410 138 SGGEQQ--MLAIgrALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIV 215
|
....*....
gi 16132108 218 AQGTPEEVM 226
Cdd:COG0410 216 LEGTAAELL 224
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-220 |
1.50e-34 |
|
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: 123.63 E-value: 1.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSY----GTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMlSSRQLARRL 78
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 79 SLLPQHHLTPEGITVQELVSY-GRnpwlsLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNT 157
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYfAG-----LYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16132108 158 PVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQG 220
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-225 |
1.86e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 124.74 E-value: 1.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSY--GTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSL 80
Cdd:PRK13635 6 IRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 81 LPQHhltPE----GITVQELVSYGrnpwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQN 156
Cdd:PRK13635 86 VFQN---PDnqfvGATVQDDVAFG----LENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 157 TPVVLLDEPTTYLDINHQVDLMRLMGELRTQGK-TVVAVLHDLNQASRyCDQLVVMANGHVMAQGTPEEV 225
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-236 |
4.30e-34 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 123.84 E-value: 4.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 2 TLRTENLTVSY-GTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLarrLSL 80
Cdd:PRK15056 6 GIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 81 LPQHHLTPEG--ITVQELVSYGRNPWLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTP 158
Cdd:PRK15056 83 VPQSEEVDWSfpVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16132108 159 VVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDqLVVMANGHVMAQGTPEEVMTPGLLRTVFS 236
Cdd:PRK15056 163 VILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTFTAENLELAFS 239
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-220 |
4.31e-34 |
|
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: 122.00 E-value: 4.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRqlarRLSLLP 82
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARN----RIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 83 QHH-LTPEgITVQELVSYgrnpWLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVL 161
Cdd:cd03269 77 EERgLYPK-MKVIDQLVY----LAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 162 LDEPTTYLD-INHQVdLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQG 220
Cdd:cd03269 152 LDEPFSGLDpVNVEL-LKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
18-225 |
5.94e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 123.98 E-value: 5.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 18 LNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPI-------NMLSSRQLARRLSLLPQHHLTPEg 90
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkknkKLKPLRKKVGIVFQFPEHQLFEE- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 91 iTVQELVSYG-RNpwlslWGRLSAEDNARVNVAMNQTRINH-LAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTY 168
Cdd:PRK13634 102 -TVEKDICFGpMN-----FGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16132108 169 LDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-225 |
1.19e-33 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 121.67 E-value: 1.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 1 MTLRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARR-LS 79
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 80 LLPQHHLTPEGITVQE---LVsygrnpwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQN 156
Cdd:COG1137 82 YLPQEASIFRKLTVEDnilAV-------LELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATN 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16132108 157 TPVVLLDEPTTYLD---INhqvDLMRLMGELRTQGktvVAVL---HDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:COG1137 155 PKFILLDEPFAGVDpiaVA---DIQKIIRHLKERG---IGVLitdHNVRETLGICDRAYIISEGKVLAEGTPEEI 223
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-225 |
1.83e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 122.65 E-value: 1.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSY--GTDkVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPIN-----MLSSRQLA 75
Cdd:PRK13636 6 LKVEELNYNYsdGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysrkgLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 76 RRLSLLPQHHLTpeGITVQELVSYGRnpwLSLwGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQ 155
Cdd:PRK13636 85 GMVFQDPDNQLF--SASVYQDVSFGA---VNL-KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16132108 156 NTPVVLLDEPTTYLDINHQVDLMRLMGELRTQ-GKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-217 |
3.21e-33 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 120.05 E-value: 3.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQlaRRLSLLP 82
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 83 QHH-LTPEgITVQELVSYGrnpwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVL 161
Cdd:cd03301 79 QNYaLYPH-MTVYDNIAFG----LKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 162 LDEPTTYLDINHQVDlMRlmGEL----RTQGKTVVAVLHDLNQASRYCDQLVVMANGHVM 217
Cdd:cd03301 154 MDEPLSNLDAKLRVQ-MR--AELkrlqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
3-214 |
5.58e-33 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 119.38 E-value: 5.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDK----VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLA--- 75
Cdd:TIGR02211 2 LKCENLGKRYQEGKldtrVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAklr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 76 -RRLSLLPQ-HHLTPEgITVQELVSYgrnPwlSLWGRLSAEDNARVNVAMNQT-----RINHlavrRLTELSGGQRQRAF 148
Cdd:TIGR02211 82 nKKLGFIYQfHHLLPD-FTALENVAM---P--LLIGKKSVKEAKERAYEMLEKvglehRINH----RPSELSGGERQRVA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16132108 149 LAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRYcDQLVVMANG 214
Cdd:TIGR02211 152 IARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELnRELNTSFLVVTHDLELAKKL-DRVLEMKDG 217
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-225 |
2.79e-32 |
|
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: 118.07 E-value: 2.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGT----DKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQL---A 75
Cdd:cd03258 2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 76 RRLSLLPQHHLTPEGITVQELVSYgrnPwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQ 155
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVAL---P-LEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16132108 156 NTPVVLLDEPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-225 |
3.38e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 119.38 E-value: 3.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 1 MTLRTENLTVSY--GT---DKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPI--NMLSSRQ 73
Cdd:PRK13637 1 MSIKIENLTHIYmeGTpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 74 LARRLSLL---PQHHLTPEgiTVQELVSYG-RNPWLSlwgrlSAEDNARVNVAMNQTRINH--LAVRRLTELSGGQRQRA 147
Cdd:PRK13637 81 IRKKVGLVfqyPEYQLFEE--TIEKDIAFGpINLGLS-----EEEIENRVKRAMNIVGLDYedYKDKSPFELSGGQKRRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16132108 148 FLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGK-TVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNmTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-227 |
4.50e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 118.64 E-value: 4.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSY--GTdKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPI-----NMLSSRQLA 75
Cdd:PRK13639 2 LETRDLKYSYpdGT-EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydkkSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 76 RRLSLLPQHHL-TPegiTVQELVSYGrnPwLSLwgRLSAED-NARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVL 153
Cdd:PRK13639 81 GIVFQNPDDQLfAP---TVEEDVAFG--P-LNL--GLSKEEvEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16132108 154 AQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMT 227
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3-227 |
5.41e-32 |
|
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: 117.26 E-value: 5.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARR-LSLL 81
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 82 PQHHLTPEGITVQE---LVsygrnpwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTP 158
Cdd:cd03218 81 PQEASIFRKLTVEEnilAV-------LEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 159 VVLLDEPTTYLD-INHQvDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMT 227
Cdd:cd03218 154 FLLLDEPFAGVDpIAVQ-DIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
13-226 |
6.25e-32 |
|
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: 120.34 E-value: 6.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 13 GTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFL-GDNPINMlSSRQLA----RRLSLLPQHHLT 87
Cdd:TIGR01186 4 GGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIdGENIMKQ-SPVELRevrrKKIGMVFQQFAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 88 PEGITVQELVSYGrnPWLSLWGRLSAEDNARVnvAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTT 167
Cdd:TIGR01186 83 FPHMTILQNTSLG--PELLGWPEQERKEKALE--LLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 168 YLDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVM 226
Cdd:TIGR01186 159 ALDPLIRDSMQDELKKLqATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEIL 218
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-229 |
1.35e-31 |
|
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: 116.18 E-value: 1.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSYGTDK-VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLPQH 84
Cdd:cd03253 4 ENVTFAYDPGRpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 85 hlTPE-GITVQELVSYGRnpwlslwgrLSAEDNARVNVAmNQTRINHLAVR-----------RLTELSGGQRQRAFLAMV 152
Cdd:cd03253 84 --TVLfNDTIGYNIRYGR---------PDATDEEVIEAA-KAAQIHDKIMRfpdgydtivgeRGLKLSGGEKQRVAIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16132108 153 LAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTqGKTVVAVLHDLNQASRyCDQLVVMANGHVMAQGTPEEVMTPG 229
Cdd:cd03253 152 ILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAKG 226
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
16-201 |
1.38e-31 |
|
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: 114.83 E-value: 1.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 16 KVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSS--RQLARRLSLLPQHhltPE---- 89
Cdd:TIGR01166 6 EVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKglLERRQRVGLVFQD---PDdqlf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 90 GITVQELVSYG-RNPWLSlwgrlSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTY 168
Cdd:TIGR01166 83 AADVDQDVAFGpLNLGLS-----EAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAG 157
|
170 180 190
....*....|....*....|....*....|...
gi 16132108 169 LDINHQVDLMRLMGELRTQGKTVVAVLHDLNQA 201
Cdd:TIGR01166 158 LDPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-225 |
2.13e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 120.51 E-value: 2.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQlARRLsllp 82
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD-AQAA---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 83 qhhltpeGITV--QElvsygrnpwLSLWGRLS-AEdnarvNVAMNQT-----RINHLAVRRLT----------------- 137
Cdd:COG1129 80 -------GIAIihQE---------LNLVPNLSvAE-----NIFLGREprrggLIDWRAMRRRArellarlgldidpdtpv 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 138 -ELSGGQRQraflaMV-----LAQNTPVVLLDEPTTYLDiNHQVD-LMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVV 210
Cdd:COG1129 139 gDLSVAQQQ-----LVeiaraLSRDARVLILDEPTASLT-EREVErLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTV 212
|
250
....*....|....*
gi 16132108 211 MANGHVMAQGTPEEV 225
Cdd:COG1129 213 LRDGRLVGTGPVAEL 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-197 |
3.89e-31 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 120.17 E-value: 3.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 5 TENLTVSYGTDKVLNDVSLSLPTG-KItALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNpinmlssrqlaRRLSLLPQ 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGdRI-GLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-----------LRIGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 84 HHLTPEGITVQELVSYGRNPWLSLWGRLSA----------------------------EDNARVNVAMNQTRINHLAV-R 134
Cdd:COG0488 69 EPPLDDDLTVLDTVLDGDAELRALEAELEEleaklaepdedlerlaelqeefealggwEAEARAEEILSGLGFPEEDLdR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16132108 135 RLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINhqvDLMRLMGELRTQGKTVVAVLHD 197
Cdd:COG0488 149 PVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLE---SIEWLEEFLKNYPGTVLVVSHD 208
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-226 |
5.01e-31 |
|
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: 114.94 E-value: 5.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 16 KVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLPQHHLTPEGiTVQE 95
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDG-TIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 96 LVSYGRNPwlslwgrLSAEDNARVNVAMN------------QTRINhlavRRLTELSGGQRQRAFLAMVLAQNTPVVLLD 163
Cdd:cd03249 96 NIRYGKPD-------ATDEEVEEAAKKANihdfimslpdgyDTLVG----ERGSQLSGGQKQRIAIARALLRNPKILLLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16132108 164 EPTTYLDINH----QVDLMRLMgelrtQGKTVVAVLHDLNqASRYCDQLVVMANGHVMAQGTPEEVM 226
Cdd:cd03249 165 EATSALDAESeklvQEALDRAM-----KGRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDELM 225
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
22-220 |
6.54e-31 |
|
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: 113.80 E-value: 6.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 22 SLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDnpINMLSSRQLARRLSLLPQHHLTPEGITVQELVSYGR 101
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVND--QSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 102 NPWLslwgRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLM 181
Cdd:TIGR01277 96 HPGL----KLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16132108 182 GELRTQGK-TVVAVLHDLNQASRYCDQLVVMANGHVMAQG 220
Cdd:TIGR01277 172 KQLCSERQrTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
6-225 |
7.90e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 115.23 E-value: 7.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSYGTDK--VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLPQ 83
Cdd:PRK13648 11 KNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 84 HhltPE----GITVQELVSYGrnpwlsLWGRLSAEDNARVNVAMNQTRINHLAvRRLTE---LSGGQRQRAFLAMVLAQN 156
Cdd:PRK13648 91 N---PDnqfvGSIVKYDVAFG------LENHAVPYDEMHRRVSEALKQVDMLE-RADYEpnaLSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 157 TPVVLLDEPTTYLDINHQVDLMRLMGELR-TQGKTVVAVLHDLNQASRyCDQLVVMANGHVMAQGTPEEV 225
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVKsEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-216 |
1.03e-30 |
|
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: 113.39 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINmLSSRQLA---RRLSLLP 82
Cdd:cd03262 4 KNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT-DDKKNINelrQKVGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 83 QH-HLTPEgITVQELVSYGRnpwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVL 161
Cdd:cd03262 83 QQfNLFPH-LTVLENITLAP---IKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 16132108 162 LDEPTTYLD---INHQVDLMRlmgELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHV 216
Cdd:cd03262 159 FDEPTSALDpelVGEVLDVMK---DLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-220 |
1.04e-30 |
|
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: 112.64 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 1 MTLRTENLTV------SYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQ--SGTVFLGDNPinmLSSR 72
Cdd:cd03213 2 VTLSFRNLTVtvksspSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRP---LDKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 73 QLARRLSLLPQHHLTPEGITVQELVSYgrnpwlslwgrlSAEdnarvnvamnqtrinhlavrrLTELSGGQRQRAFLAMV 152
Cdd:cd03213 79 SFRKIIGYVPQDDILHPTLTVRETLMF------------AAK---------------------LRGLSGGERKRVSIALE 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16132108 153 LAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHdlnQAS----RYCDQLVVMANGHVMAQG 220
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIH---QPSseifELFDKLLLLSQGRVIYFG 194
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-221 |
1.23e-30 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 113.96 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 1 MTLRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDN------PINMLSSRQL 74
Cdd:PRK11124 1 MSIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdfskTPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 75 ARRLSLL-PQHHLTPEGITVQELVsygRNPwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVL 153
Cdd:PRK11124 81 RRNVGMVfQQYNLWPHLTVQQNLI---EAP-CRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16132108 154 AQNTPVVLLDEPTTYLD--INHQ-VDLMRlmgELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGT 221
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDpeITAQiVSIIR---ELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD 224
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-224 |
1.26e-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: 113.23 E-value: 1.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 5 TENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPInMLSSRQLARRLSLLPQH 84
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV-VREPREVRRRIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 85 HLTPEGITVQE-LVSYGRnpwlsLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLD 163
Cdd:cd03265 82 LSVDDELTGWEnLYIHAR-----LYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16132108 164 EPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEE 224
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-220 |
1.44e-30 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 112.02 E-value: 1.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYG--TDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSrQLARRLSL 80
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK-ALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 81 LPQhhltpegitvqelvsygrNPWLslwgrlsaednarvnvaMNQTRINHLAVRrlteLSGGQRQRAFLAMVLAQNTPVV 160
Cdd:cd03247 80 LNQ------------------RPYL-----------------FDTTLRNNLGRR----FSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 161 LLDEPTTYLDINHQVDLMRLMGELrTQGKTVVAVLHDLnQASRYCDQLVVMANGHVMAQG 220
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEV-LKDKTLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-216 |
1.62e-30 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 113.22 E-value: 1.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSYGTDK-VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLA---RRLSLL 81
Cdd:COG2884 5 ENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPylrRRIGVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 82 PQ-HHLTPEgITVQELVSYGrnpwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVV 160
Cdd:COG2884 85 FQdFRLLPD-RTVYENVALP----LRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16132108 161 LLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHV 216
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-216 |
2.84e-30 |
|
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: 111.15 E-value: 2.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDK--VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSL 80
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 81 LPQHHLTPEGiTVQElvsygrnpwlslwgrlsaednarvNVamnqtrinhlavrrlteLSGGQRQRAFLAMVLAQNTPVV 160
Cdd:cd03246 81 LPQDDELFSG-SIAE------------------------NI-----------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16132108 161 LLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRyCDQLVVMANGHV 216
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
7-225 |
2.90e-30 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 115.81 E-value: 2.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 7 NLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQlaRRLSLLPQHH- 85
Cdd:PRK09452 19 GISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN--RHVNTVFQSYa 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 86 LTPEgITVQELVSYGrnpwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEP 165
Cdd:PRK09452 97 LFPH-MTVFENVAFG----LRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16132108 166 TTYLDIN----HQVDLMRLMgelRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:PRK09452 172 LSALDYKlrkqMQNELKALQ---RKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-220 |
3.16e-30 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 111.93 E-value: 3.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTV-FLGDNPINMLSSrqLARRLSLL 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEItFDGKSYQKNIEA--LRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 82 PQHHLTPEgITVQElvsygrNpwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVL 161
Cdd:cd03268 79 EAPGFYPN-LTARE------N--LRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16132108 162 LDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQG 220
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-235 |
3.31e-30 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 112.68 E-value: 3.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 2 TLRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARR-LSL 80
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 81 LPQhhltpEGITVQELVSYGR-NPWLSLWGRLSAEDNA-RVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTP 158
Cdd:PRK10895 83 LPQ-----EASIFRRLSVYDNlMAVLQIRDDLSAEQREdRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16132108 159 VVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMTPGLLRTVF 235
Cdd:PRK10895 158 FILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVY 234
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
20-227 |
4.24e-30 |
|
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: 115.20 E-value: 4.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 20 DVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNP-------INMLSSRqlaRRL-------SLLPqhH 85
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsargIFLPPHR---RRIgyvfqeaRLFP--H 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 86 LTpegitVQELVSYGRnpwlslWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEP 165
Cdd:COG4148 92 LS-----VRGNLLYGR------KRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16132108 166 TTYLDINHQVDLMRLMGELRTQGKT-VVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMT 227
Cdd:COG4148 161 LAALDLARKAEILPYLERLRDELDIpILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLS 223
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
3-226 |
6.36e-30 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 111.94 E-value: 6.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDK--VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSL 80
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 81 LPQHHLTPEGiTVQELVSYGRnpwlSLWGRLSAEDNARVNVAMN---------QTRINHlavrRLTELSGGQRQRAFLAM 151
Cdd:cd03251 81 VSQDVFLFND-TVAENIAYGR----PGATREEVEEAARAANAHEfimelpegyDTVIGE----RGVKLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16132108 152 VLAQNTPVVLLDEPTTYLDINH----QVDLMRLMgelrtQGKTVVAVLHDLNQAsRYCDQLVVMANGHVMAQGTPEEVM 226
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESerlvQAALERLM-----KNRTTFVIAHRLSTI-ENADRIVVLEDGKIVERGTHEELL 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
7-227 |
6.37e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 112.11 E-value: 6.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 7 NLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLS---LLPQ 83
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEagmVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 84 HHLTPEgITVQELVSYG----RNPwlslwGRLSAEDNAR---VNVAMNQtRINHLAvrrlTELSGGQRQRAFLAMVLAQN 156
Cdd:PRK09493 86 FYLFPH-LTALENVMFGplrvRGA-----SKEEAEKQARellAKVGLAE-RAHHYP----SELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16132108 157 TPVVLLDEPTTYLD--INHQVdlMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMT 227
Cdd:PRK09493 155 PKLMLFDEPTSALDpeLRHEV--LKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-227 |
1.03e-29 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 112.98 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMlSSRQLARRLSLLP 82
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 83 Q-HHLTPEGITVQELVSYGRnpwlsLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVL 161
Cdd:PRK13537 87 QfDNLDPDFTVRENLLVFGR-----YFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16132108 162 LDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMT 227
Cdd:PRK13537 162 LDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-228 |
1.07e-29 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 111.64 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 1 MTLRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDN------PINMLSSRQL 74
Cdd:COG4161 1 MSIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 75 ARRLSLL-PQHHLTPEGITVQELVSygrNPwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVL 153
Cdd:COG4161 81 RQKVGMVfQQYNLWPHLTVMENLIE---AP-CKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16132108 154 AQNTPVVLLDEPTTYLD--INHQVdlMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMTP 228
Cdd:COG4161 157 MMEPQVLLFDEPTAALDpeITAQV--VEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHFTQP 231
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-227 |
2.09e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 111.84 E-value: 2.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 1 MTLRTENLTVSY--GT---DKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSS---- 71
Cdd:PRK13641 1 MSIKFENVDYIYspGTpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 72 RQLARRLSLL---PQHHLTPEgiTVQELVSYG-RNPWLSlwgrlsaEDNARV-------NVAMNQTRINHLAVrrltELS 140
Cdd:PRK13641 81 KKLRKKVSLVfqfPEAQLFEN--TVLKDVEFGpKNFGFS-------EDEAKEkalkwlkKVGLSEDLISKSPF----ELS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 141 GGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQG 220
Cdd:PRK13641 148 GGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHA 227
|
....*..
gi 16132108 221 TPEEVMT 227
Cdd:PRK13641 228 SPKEIFS 234
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
3-234 |
2.48e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 111.43 E-value: 2.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDK-VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLL 81
Cdd:PRK13652 4 IETRDLCYSYSGSKeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 82 PQHH----LTPegiTVQELVSYGRnpwLSLwGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNT 157
Cdd:PRK13652 84 FQNPddqiFSP---TVEQDIAFGP---INL-GLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16132108 158 PVVLLDEPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMT-PGLLRTV 234
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLqPDLLARV 235
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
3-226 |
2.76e-29 |
|
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: 115.23 E-value: 2.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSY-GTDK-VLNDVSLSLPTGKITALIGPNGCGKSTLLncfsRLLM----PQSGTVFLGDNPINMLSSRQLAR 76
Cdd:COG4618 331 LSVENLTVVPpGSKRpILRGVSFSLEPGEVLGVIGPSGSGKSTLA----RLLVgvwpPTAGSVRLDGADLSQWDREELGR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 77 RLSLLPQHhltPE--GITVQELVSygrnpwlslwgRLSAEDNARVNVAMNQTRInHLAVRRL-----TE-------LSGG 142
Cdd:COG4618 407 HIGYLPQD---VElfDGTIAENIA-----------RFGDADPEKVVAAAKLAGV-HEMILRLpdgydTRigeggarLSGG 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 143 QRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNqASRYCDQLVVMANGHVMAQGTP 222
Cdd:COG4618 472 QRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPR 550
|
....
gi 16132108 223 EEVM 226
Cdd:COG4618 551 DEVL 554
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-198 |
5.66e-29 |
|
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: 114.38 E-value: 5.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 2 TLRTENLTVSYGTD-KVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSL 80
Cdd:TIGR02868 334 TLELRDLSAGYPGApPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 81 LPQH-HLTpeGITVQELVSYGRnPWLS---LWGRLSA---EDNARVNVAMNQTRINHLAVRrlteLSGGQRQRAFLAMVL 153
Cdd:TIGR02868 414 CAQDaHLF--DTTVRENLRLAR-PDATdeeLWAALERvglADWLRALPDGLDTVLGEGGAR----LSGGERQRLALARAL 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16132108 154 AQNTPVVLLDEPTTYLDINHQVDLMRLMGELrTQGKTVVAVLHDL 198
Cdd:TIGR02868 487 LADAPILLLDEPTEHLDAETADELLEDLLAA-LSGRTVVLITHHL 530
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-226 |
6.20e-29 |
|
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: 114.43 E-value: 6.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTD--KVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSL 80
Cdd:TIGR02203 331 VEFRNVTFRYPGRdrPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 81 LPQH-HLTPEgiTVQELVSYGRnpwLSLWGRLSAEDNARVNVAMN---------QTRINHLAVRrlteLSGGQRQRAFLA 150
Cdd:TIGR02203 411 VSQDvVLFND--TIANNIAYGR---TEQADRAEIERALAAAYAQDfvdklplglDTPIGENGVL----LSGGQRQRLAIA 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 151 MVLAQNTPVVLLDEPTTYLDINH----QVDLMRLMgelrtQGKTVVAVLHDLNQASRyCDQLVVMANGHVMAQGTPEEVM 226
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESerlvQAALERLM-----QGRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNELL 555
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-227 |
7.37e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 109.62 E-value: 7.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 7 NLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRL--LMPQ---SGTVFLGDNPINMLSSRQLARRLSLL 81
Cdd:PRK14247 8 DLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEarvSGEVYLDGQDIFKMDVIELRRRVQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 82 PQHHLTPEGITVQELVSYGrnPWLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLT----ELSGGQRQRAFLAMVLAQNT 157
Cdd:PRK14247 88 FQIPNPIPNLSIFENVALG--LKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLDapagKLSGGQQQRLCIARALAFQP 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 158 PVVLLDEPTTYLDINHQVDLMRLMGELRTQgKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMT 227
Cdd:PRK14247 166 EVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-206 |
7.73e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 109.87 E-value: 7.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRL--LMPQ---SGTVFLGDNPINM--LSSRQLA 75
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGfrvEGKVTFHGKNLYApdVDPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 76 RRLSLLPQHHlTPEGITVQELVSYGrnpwlslwgrlsaednARVNVAmnQTRINHLAVRRLTE----------------- 138
Cdd:PRK14243 91 RRIGMVFQKP-NPFPKSIYDNIAYG----------------ARINGY--KGDMDELVERSLRQaalwdevkdklkqsgls 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16132108 139 LSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQgKTVVAVLHDLNQASRYCD 206
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSD 218
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1-225 |
9.67e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 110.25 E-value: 9.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 1 MTLRTENLTVSY--GTD---KVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSS---- 71
Cdd:PRK13646 1 MTIRFDNVSYTYqkGTPyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 72 RQLARRLSLL---PQHHLTPEgiTVQELVSYGRNpwlslwgrlsaednarvNVAMNQTRINHLAVRRLTEL--------- 139
Cdd:PRK13646 81 RPVRKRIGMVfqfPESQLFED--TVEREIIFGPK-----------------NFKMNLDEVKNYAHRLLMDLgfsrdvmsq 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 140 -----SGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRT-QGKTVVAVLHDLNQASRYCDQLVVMAN 213
Cdd:PRK13646 142 spfqmSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTdENKTIILVSHDMNEVARYADEVIVMKE 221
|
250
....*....|..
gi 16132108 214 GHVMAQGTPEEV 225
Cdd:PRK13646 222 GSIVSQTSPKEL 233
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
7-224 |
1.82e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 110.58 E-value: 1.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 7 NLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQlaRRLSLLPQHH- 85
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--RDICMVFQSYa 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 86 LTPEgITVQELVSYGrnpwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEP 165
Cdd:PRK11432 89 LFPH-MSLGENVGYG----LKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16132108 166 TTYLDINhqvdLMRLM----GELRTQ-GKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEE 224
Cdd:PRK11432 164 LSNLDAN----LRRSMrekiRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQE 223
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
20-220 |
3.01e-28 |
|
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: 107.00 E-value: 3.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 20 DVSLSLPTGkITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNP-----INM-LSSRQlaRRLSLLPQHH-LTPEgIT 92
Cdd:cd03297 16 KIDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrKKInLPPQQ--RKIGLVFQQYaLFPH-LN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 93 VQELVSYGrnpwlsLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDIN 172
Cdd:cd03297 92 VRENLAFG------LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16132108 173 HQVDLMRLMGELRTQ-GKTVVAVLHDLNQASRYCDQLVVMANGHVMAQG 220
Cdd:cd03297 166 LRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-225 |
3.94e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 111.66 E-value: 3.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQlARRL--SL 80
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRD-AIALgiGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 81 LPQHHLTPEGITVQELVSYGRNPWLSLWGRLSAEdNARVNVAMNQTrinHLAV---RRLTELSGGQRQRAFLAMVLAQNT 157
Cdd:COG3845 85 VHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAA-RARIRELSERY---GLDVdpdAKVEDLSVGEQQRVEILKALYRGA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16132108 158 PVVLLDEPTTYLDiNHQVD-LMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:COG3845 161 RILILDEPTAVLT-PQEADeLFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAET 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-228 |
6.38e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 107.17 E-value: 6.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRL--LMPQ---SGTVFLgdNPINMLSSR----Q 73
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVY--NGHNIYSPRtdtvD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 74 LARRLSLLPQHHlTPEGITVQELVSYGrnpwLSLWG-RLSAEDNARVNVAMNQTRINHLAVRRLTE----LSGGQRQRAF 148
Cdd:PRK14239 84 LRKEIGMVFQQP-NPFPMSIYENVVYG----LRLKGiKDKQVLDEAVEKSLKGASIWDEVKDRLHDsalgLSGGQQQRVC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 149 LAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQgKTVVAVLHDLNQASRYCDQLVVMANGHVMAQG-TPEEVMT 227
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNdTKQMFMN 237
|
.
gi 16132108 228 P 228
Cdd:PRK14239 238 P 238
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-224 |
6.83e-28 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 107.41 E-value: 6.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLL----MPQSGTVFLGDNpinMLSSRQLARRL 78
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdkSAGSHIELLGRT---VQREGRLARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 79 S--------LLPQHHLTPEgITVQELV---SYGRNP-WLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQR 146
Cdd:PRK09984 82 RksrantgyIFQQFNLVNR-LSVLENVligALGSTPfWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16132108 147 AFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEE 224
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
17-221 |
9.95e-28 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 106.05 E-value: 9.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 17 VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLA----RRLSLLPQ-HHLTPEgI 91
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnQKLGFIYQfHHLLPD-F 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 92 TVQELVSYgrnPWLsLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDI 171
Cdd:PRK11629 103 TALENVAM---PLL-IGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16132108 172 NHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLvVMANGHVMAQGT 221
Cdd:PRK11629 179 RNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQL-EMRDGRLTAELS 228
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-226 |
3.11e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 107.22 E-value: 3.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 7 NLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINmlSSRQLAR-RLSLLPQ-H 84
Cdd:PRK13536 46 GVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP--ARARLARaRIGVVPQfD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 85 HLTPEgITVQE-LVSYGRnpwlslWGRLSAED-NARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLL 162
Cdd:PRK13536 124 NLDLE-FTVREnLLVFGR------YFGMSTREiEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16132108 163 DEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVM 226
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-212 |
3.34e-27 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 105.33 E-value: 3.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 1 MTLRTENLTVSYGTDK----VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSsrqlAR 76
Cdd:COG4525 2 SMLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG----AD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 77 RLSLLPQHHLTPeGITVQELVSYGrnpwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQN 156
Cdd:COG4525 78 RGVVFQKDALLP-WLNVLDNVAFG----LRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAAD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 157 TPVVLLDEPTTYLDI----NHQVDLMRLMgelRTQGKTVVAVLHDLNQASRYCDQLVVMA 212
Cdd:COG4525 153 PRFLLMDEPFGALDAltreQMQELLLDVW---QRTGKGVFLITHSVEEALFLATRLVVMS 209
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-227 |
3.83e-27 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 105.27 E-value: 3.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 2 TLRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSR--------- 72
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRdgelvpadr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 73 -QLAR---RLSLLPQH-----HLTP-----EG-ITVQelvsyGRNpwlslwgRLSAEDNARVNVAmnqtRINhLAVRRLT 137
Cdd:COG4598 88 rQLQRirtRLGMVFQSfnlwsHMTVlenviEApVHVL-----GRP-------KAEAIERAEALLA----KVG-LADKRDA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 138 ---ELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANG 214
Cdd:COG4598 151 ypaHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQG 230
|
250
....*....|...
gi 16132108 215 HVMAQGTPEEVMT 227
Cdd:COG4598 231 RIEEQGPPAEVFG 243
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-226 |
3.93e-27 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 105.05 E-value: 3.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSS----------- 71
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 72 --RQLARRLSLLPQHHLTPEGITVQELVSYGRnpwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRL-TELSGGQRQRAF 148
Cdd:PRK10619 86 qlRLLRTRLTMVFQHFNLWSHMTVLENVMEAP---IQVLGLSKQEARERAVKYLAKVGIDERAQGKYpVHLSGGQQQRVS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16132108 149 LAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVM 226
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1-225 |
5.27e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 105.21 E-value: 5.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 1 MTLRTENLTVSY--GT---DKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSS---- 71
Cdd:PRK13649 1 MGINLQNVSYTYqaGTpfeGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 72 RQLARRLSLL---PQHHLTPEgiTVQELVSYG-RNPWLSlwgRLSAEDNARVNVAMNQTRINhLAVRRLTELSGGQRQRA 147
Cdd:PRK13649 81 KQIRKKVGLVfqfPESQLFEE--TVLKDVAFGpQNFGVS---QEEAEALAREKLALVGISES-LFEKNPFELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16132108 148 FLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-196 |
7.68e-27 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 103.03 E-value: 7.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 1 MTLRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSl 80
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 81 lPQHHLTPEgITVQElvsygrNpwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVV 160
Cdd:PRK13539 80 -HRNAMKPA-LTVAE------N--LEFWAAFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIW 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 16132108 161 LLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLH 196
Cdd:PRK13539 150 ILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATH 185
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
6-216 |
9.50e-27 |
|
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: 103.32 E-value: 9.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSYGT---DKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLP 82
Cdd:cd03248 15 QNVTFAYPTrpdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 83 QHHLTPEGiTVQELVSYGRnPWLSLWGRLSAED--NARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVV 160
Cdd:cd03248 95 QEPVLFAR-SLQDNIAYGL-QSCSFECVKEAAQkaHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16132108 161 LLDEPTTYLDINHQVDLMRLMGElRTQGKTVVAVLHDLNQASRyCDQLVVMANGHV 216
Cdd:cd03248 173 ILDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-225 |
9.59e-27 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 106.46 E-value: 9.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLG----------DNPINMlssr 72
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgvdlshvppyQRPINM---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 73 qLARRLSLLPQhhltpegITVQELVSYGRNPwlslwGRLS-AEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAM 151
Cdd:PRK11607 96 -MFQSYALFPH-------MTVEQNIAFGLKQ-----DKLPkAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16132108 152 VLAQNTPVVLLDEPTTYLDINHQvDLMRL--MGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:PRK11607 163 SLAKRPKLLLLDEPMGALDKKLR-DRMQLevVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-225 |
9.93e-27 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 105.55 E-value: 9.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSYGTDK----VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQL--ARR-L 78
Cdd:COG1135 5 ENLSKTFPTKGgpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraARRkI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 79 SLLPQH-HLTPEgITVQELVSYgrnPwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNT 157
Cdd:COG1135 85 GMIFQHfNLLSS-RTVAENVAL---P-LEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16132108 158 PVVLLDEPTTYLDIN--HQV-DLMRlmgELRTQ-GKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:COG1135 160 KVLLCDEATSALDPEttRSIlDLLK---DINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDV 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-216 |
1.28e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 107.46 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNpinmLssrqlarRLSLLP 82
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET----V-------KIGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 83 QHHLT-PEGITVQELVSYGrnpwlslwgrlsAEDNARVNV-----AMN------QTRINhlavrrltELSGGQRQRAFLA 150
Cdd:COG0488 385 QHQEElDPDKTVLDELRDG------------APGGTEQEVrgylgRFLfsgddaFKPVG--------VLSGGEKARLALA 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16132108 151 MVLAQNTPVVLLDEPTTYLDInhqvDLMRLMGE-LRT-QGkTVVAVLHDlnqasRY-----CDQLVVMANGHV 216
Cdd:COG0488 445 KLLLSPPNVLLLDEPTNHLDI----ETLEALEEaLDDfPG-TVLLVSHD-----RYfldrvATRILEFEDGGV 507
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
16-225 |
1.41e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 104.43 E-value: 1.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 16 KVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQ----LARRLSLL---PQHHLTP 88
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpVRKKVGVVfqfPESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 89 EgiTVQELVSYGRNPWlslwgRLSAEDNARVnvAMNQTRINHLAV----RRLTELSGGQRQRAFLAMVLAQNTPVVLLDE 164
Cdd:PRK13643 100 E--TVLKDVAFGPQNF-----GIPKEKAEKI--AAEKLEMVGLADefweKSPFELSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16132108 165 PTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:PRK13643 171 PTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDV 231
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-239 |
2.02e-26 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 105.19 E-value: 2.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 20 DVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINmlSSRQLA------RRLSLLPQH-HLTPEgIT 92
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLF--DSRKGIflppekRRIGYVFQEaRLFPH-LS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 93 VQELVSYGRnpwlslWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDIN 172
Cdd:TIGR02142 92 VRGNLRYGM------KRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16132108 173 HQVDLM----RLMGELRTqgkTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMTPGLLRTVFSVEA 239
Cdd:TIGR02142 166 RKYEILpyleRLHAEFGI---PILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLAREDQ 233
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-227 |
2.12e-26 |
|
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: 107.08 E-value: 2.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDK----VLNDVSLSLPTGKITALIGPNGCGKS----TLLncfsRLLMPQ----SGTVFLGDNPINMLS 70
Cdd:COG4172 7 LSVEDLSVAFGQGGgtveAVKGVSFDIAAGETLALVGESGSGKSvtalSIL----RLLPDPaahpSGSILFDGQDLLGLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 71 SRQLaRRL--------------SLLPQHhltpegiTVQELVSYGrnpwLSLWGRLSAED-NARVNVAMNQTRINHlAVRR 135
Cdd:COG4172 83 EREL-RRIrgnriamifqepmtSLNPLH-------TIGKQIAEV----LRLHRGLSGAAaRARALELLERVGIPD-PERR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 136 LT----ELSGGQRQRAFLAMVLAqNTPVVLL-DEPTTYLDINHQVDLMRLMGELRTQGKTvvAVL---HDLNQASRYCDQ 207
Cdd:COG4172 150 LDayphQLSGGQRQRVMIAMALA-NEPDLLIaDEPTTALDVTVQAQILDLLKDLQRELGM--ALLlitHDLGVVRRFADR 226
|
250 260
....*....|....*....|
gi 16132108 208 LVVMANGHVMAQGTPEEVMT 227
Cdd:COG4172 227 VAVMRQGEIVEQGPTAELFA 246
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
16-220 |
2.34e-26 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 102.28 E-value: 2.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 16 KVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLPQH-HL----TPEG 90
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDvTLfygtLRDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 91 ITVqelvsygrnpwlslwGRLSAEDNARVNVAM----NQTRINH-----LAVR-RLTELSGGQRQRAFLAMVLAQNTPVV 160
Cdd:cd03245 98 ITL---------------GAPLADDERILRAAElagvTDFVNKHpngldLQIGeRGRGLSGGQRQAVALARALLNDPPIL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16132108 161 LLDEPTTYLDINHQvdlMRLMGELR--TQGKTVVAVLH-----DLnqasryCDQLVVMANGHVMAQG 220
Cdd:cd03245 163 LLDEPTSAMDMNSE---ERLKERLRqlLGDKTLIIITHrpsllDL------VDRIIVMDSGRIVADG 220
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
6-225 |
3.22e-26 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 102.50 E-value: 3.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVflgdnpinmlsSRQLARRLSLLPQH- 84
Cdd:PRK09544 8 ENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIGYVPQKl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 85 HLTPegiTVQELVSYgrnpWLSLWGRLSAEDnarVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDE 164
Cdd:PRK09544 77 YLDT---TLPLTVNR----FLRLRPGTKKED---ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16132108 165 PTTYLDINHQVDLMRLMGELRTQ-GKTVVAVLHDLNQASRYCDQlVVMANGHVMAQGTPEEV 225
Cdd:PRK09544 147 PTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDE-VLCLNHHICCSGTPEVV 207
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-220 |
4.24e-26 |
|
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: 101.58 E-value: 4.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 16 KVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLmpQSGTVFLGDNPIN-MLSSRQLAR-RLSLLPQHHLTPEGITV 93
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRV--EGGGTTSGQILFNgQPRKPDQFQkCVAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 94 QELVSYG---RNPWLSLWGRLSAEDnarVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLD 170
Cdd:cd03234 99 RETLTYTailRLPRKSSDAIRKKRV---EDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16132108 171 INHQVDLMRLMGELRTQGKTVVAVLH----DLnqaSRYCDQLVVMANGHVMAQG 220
Cdd:cd03234 176 SFTALNLVSTLSQLARRNRIVILTIHqprsDL---FRLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
16-238 |
4.30e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 103.16 E-value: 4.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 16 KVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPI-----NMLSSRQLARRLSLL---PQHHLT 87
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkKIKEVKRLRKEIGLVfqfPEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 88 PEgiTVQELVSYGRnpwLSLwGRLSAEDNARVNVAMNQTRINHLAVRRLT-ELSGGQRQRAFLAMVLAQNTPVVLLDEPT 166
Cdd:PRK13645 105 QE--TIEKDIAFGP---VNL-GENKQEAYKKVPELLKLVQLPEDYVKRSPfELSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16132108 167 TYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMTPGLLRTVFSVE 238
Cdd:PRK13645 179 GGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQELLTKIEID 251
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
6-227 |
9.66e-26 |
|
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: 105.33 E-value: 9.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSY--GTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLPQ 83
Cdd:TIGR03375 467 RNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVPQ 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 84 HHLTPEGiTVQELVSYGRnpwlslwgrLSAEDNARVNVAMnQTRINHLaVRRLTE------------LSGGQRQRAFLAM 151
Cdd:TIGR03375 547 DPRLFYG-TLRDNIALGA---------PYADDEEILRAAE-LAGVTEF-VRRHPDgldmqigergrsLSGGQRQAVALAR 614
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16132108 152 VLAQNTPVVLLDEPTTYLDINHQvdlMRLMGELR--TQGKTVVAVLHDLnQASRYCDQLVVMANGHVMAQGTPEEVMT 227
Cdd:TIGR03375 615 ALLRDPPILLLDEPTSAMDNRSE---ERFKDRLKrwLAGKTLVLVTHRT-SLLDLVDRIIVMDNGRIVADGPKDQVLE 688
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-206 |
1.30e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 101.27 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQS-----GTV-FLGDN----PINMlssR 72
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVeFFNQNiyerRVNL---N 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 73 QLARRLSLL-PQHHLTPegITVQELVSYGRNpwLSLWgRLSAEDNARVNVAMNQT----RINHLAVRRLTELSGGQRQRA 147
Cdd:PRK14258 85 RLRRQVSMVhPKPNLFP--MSVYDNVAYGVK--IVGW-RPKLEIDDIVESALKDAdlwdEIKHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16132108 148 FLAMVLAQNTPVVLLDEPTTYLD------INHQVDLMRLMGELrtqgkTVVAVLHDLNQASRYCD 206
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDpiasmkVESLIQSLRLRSEL-----TMVIVSHNLHQVSRLSD 219
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-227 |
1.49e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 104.91 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSY--GTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSL 80
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 81 LPQH-HL------------TPEG-----ITVQELV--------SYGRNPWLSLWGRlsaednarvnvamnqtrinhlavr 134
Cdd:PRK11160 419 VSQRvHLfsatlrdnlllaAPNAsdealIEVLQQVgleklledDKGLNAWLGEGGR------------------------ 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 135 rltELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELrTQGKTVVAVLHDLNQASRYcDQLVVMANG 214
Cdd:PRK11160 475 ---QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEH-AQNKTVLMITHRLTGLEQF-DRICVMDNG 549
|
250
....*....|...
gi 16132108 215 HVMAQGTPEEVMT 227
Cdd:PRK11160 550 QIIEQGTHQELLA 562
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
22-227 |
1.67e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 100.04 E-value: 1.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 22 SLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFL-GDNPINMLSSRqlaRRLSLLPQ-HHLTPEgITVQELVSY 99
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLnGQDHTTTPPSR---RPVSMLFQeNNLFSH-LTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 100 GRNPWLslwgRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMR 179
Cdd:PRK10771 95 GLNPGL----KLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16132108 180 LMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMT 227
Cdd:PRK10771 171 LVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-227 |
1.87e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 101.85 E-value: 1.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTD-----KVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGD-------------- 63
Cdd:PRK13631 22 LRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnhelit 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 64 --NPINMLSSRQLARRLSLL---PQHHLTPEgiTVQELVSYGrnPWLSLWGRLSAEDNARVNVAMNQTRINHLAvRRLTE 138
Cdd:PRK13631 102 npYSKKIKNFKELRRRVSMVfqfPEYQLFKD--TIEKDIMFG--PVALGVKKSEAKKLAKFYLNKMGLDDSYLE-RSPFG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 139 LSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMA 218
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILK 256
|
....*....
gi 16132108 219 QGTPEEVMT 227
Cdd:PRK13631 257 TGTPYEIFT 265
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-214 |
2.11e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 100.54 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSsrqlARRLSLLP 82
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG----AERGVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 83 QHHLTPeGITVQELVSYGrnpwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLL 162
Cdd:PRK11248 78 NEGLLP-WRNVQDNVAFG----LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16132108 163 DEPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANG 214
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-225 |
3.15e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 100.47 E-value: 3.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPIN-----MLSSRQLARR 77
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskrgLLALRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 78 LSLLPQHHLTPEGITVQELVSYgRNpwlslWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNT 157
Cdd:PRK13638 82 VFQDPEQQIFYTDIDSDIAFSL-RN-----LGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16132108 158 PVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV 223
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2-219 |
7.41e-25 |
|
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: 99.11 E-value: 7.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 2 TLRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINML---SSRQLARRL 78
Cdd:TIGR02769 11 TYRTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQRRAFRRDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 79 SLLPQHhlTPEGITVQELVSYGRNPWLSLWGRLSAednarvnvAMNQTRINHL----------AVRRLTELSGGQRQRAF 148
Cdd:TIGR02769 91 QLVFQD--SPSAVNPRMTVRQIIGEPLRHLTSLDE--------SEQKARIAELldmvglrsedADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16132108 149 LAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTV-VAVLHDLNQASRYCDQLVVMANGHVMAQ 219
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAyLFITHDLRLVQSFCQRVAVMDKGQIVEE 232
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-216 |
8.38e-25 |
|
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: 97.86 E-value: 8.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSYGTD-KVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLA---RRLSLL 81
Cdd:cd03292 4 INVTKTYPNGtAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPylrRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 82 PQHHLTPEGITVQELVSYGrnpwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVL 161
Cdd:cd03292 84 FQDFRLLPDRNVYENVAFA----LEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16132108 162 LDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHV 216
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
33-225 |
9.26e-25 |
|
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: 100.26 E-value: 9.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 33 LIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQlaRRLSLLPQHHLTPEGITVQELVSYGrnpwLSLWGRLS 112
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHL--RHINMVFQSYALFPHMTVEENVAFG----LKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 113 AEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQvDLMRLmgELRTQ----G 188
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLR-DQMQL--ELKTIqeqlG 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 16132108 189 KTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:TIGR01187 152 ITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-232 |
1.06e-24 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 102.17 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRqLARRL--SL 80
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-LAAQLgiGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 81 LPQHHLTPEGITVQELVSYGRNPWLSLWG-RLSAEDNARVNVAMNQTRINhLAV---RRLTELSGGQRQRAFLAMVLAQN 156
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGRHLTKKVCGvNIIDWREMRVRAAMMLLRVG-LKVdldEKVANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16132108 157 TPVVLLDEPTTYLdINHQVD-LMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMTPGLLR 232
Cdd:PRK09700 164 AKVIIMDEPTSSL-TNKEVDyLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVR 239
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
17-226 |
1.08e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 98.23 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 17 VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFlgdnpINMlssrqlaRRLSLLpqhhltpeGITVqel 96
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE-----VNG-------RVSALL--------ELGA--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 97 vsyGRNPwlslwgRLSAEDNARVNVA---MNQTRINHL--AVRRLTEL-----------SGGQRQR-AFlAMVLAQNTPV 159
Cdd:COG1134 98 ---GFHP------ELTGRENIYLNGRllgLSRKEIDEKfdEIVEFAELgdfidqpvktySSGMRARlAF-AVATAVDPDI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16132108 160 VLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVM 226
Cdd:COG1134 168 LLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVI 234
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-224 |
1.46e-24 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 100.49 E-value: 1.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 2 TLRteNLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQlaRRLSLL 81
Cdd:PRK11000 5 TLR--NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 82 PQHH-LTPEgITVQELVSYGrnpwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVV 160
Cdd:PRK11000 81 FQSYaLYPH-LSVAENMSFG----LKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16132108 161 LLDEPTTYLD----INHQVDLMRLMGELrtqGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEE 224
Cdd:PRK11000 156 LLDEPLSNLDaalrVQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLE 220
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
3-226 |
1.55e-24 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 102.13 E-value: 1.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTD--KVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLsl 80
Cdd:TIGR01846 456 ITFENIRFRYAPDspEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQM-- 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 81 lpqhhltpeGITVQELVSYGRnpwlslwgrlSAEDNARV-NVAMNQTRINHLA--------VRRLTE------------L 139
Cdd:TIGR01846 534 ---------GVVLQENVLFSR----------SIRDNIALcNPGAPFEHVIHAAklagahdfISELPQgyntevgekganL 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 140 SGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELrTQGKTVVAVLHDLNqASRYCDQLVVMANGHVMAQ 219
Cdd:TIGR01846 595 SGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREI-CRGRTVIIIAHRLS-TVRACDRIIVLEKGQIAES 672
|
....*..
gi 16132108 220 GTPEEVM 226
Cdd:TIGR01846 673 GRHEELL 679
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
3-225 |
1.65e-24 |
|
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: 97.60 E-value: 1.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARR-LSLL 81
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 82 PQhhltpegitvqelvsyGRNpwlsLWGRLSAEDNARVnVAMNQTRINH---------------LAVRRLTELSGGQRQR 146
Cdd:TIGR03410 81 PQ----------------GRE----IFPRLTVEENLLT-GLAALPRRSRkipdeiyelfpvlkeMLGRRGGDLSGGQQQQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 147 AFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGK-TVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:TIGR03410 140 LAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGmAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-234 |
6.34e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 96.98 E-value: 6.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSY--GTdKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRL-S 79
Cdd:PRK13644 2 IRLENVSYSYpdGT-PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLvG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 80 LLPQHhltPE----GITVQELVSYG-RNPWLSlwgrlSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLA 154
Cdd:PRK13644 81 IVFQN---PEtqfvGRTVEEDLAFGpENLCLP-----PIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 155 QNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQAsRYCDQLVVMANGHVMAQGTPEEVMTPGLLRTV 234
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
7-229 |
8.02e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 96.72 E-value: 8.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 7 NLTVSYGTDK---VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLPQ 83
Cdd:PRK13650 9 NLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 84 HhltPE----GITVQELVSYG-RNPWLSLwgrlsAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTP 158
Cdd:PRK13650 89 N---PDnqfvGATVEDDVAFGlENKGIPH-----EEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16132108 159 VVLLDEPTTYLDINHQVDLMRLMGELRTQ-GKTVVAVLHDLNQASrYCDQLVVMANGHVMAQGTPEEVMTPG 229
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFSRG 231
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-224 |
1.10e-23 |
|
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: 95.19 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDK----VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARrl 78
Cdd:COG4181 9 IELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 79 sLLPQH--------HLTPeGITVQELVSYgrnPwLSLWGRLSAEDNA-----RVNVAmnqTRINHLAvrrlTELSGGQRQ 145
Cdd:COG4181 87 -LRARHvgfvfqsfQLLP-TLTALENVML---P-LELAGRRDARARAralleRVGLG---HRLDHYP----AQLSGGEQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 146 RAFLAMVLAQNTPVVLLDEPTTYLDIN--HQVdlMRLMGEL-RTQGKTVVAVLHDLNQASRyCDQLVVMANGHVMAQGTP 222
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAAtgEQI--IDLLFELnRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAA 230
|
..
gi 16132108 223 EE 224
Cdd:COG4181 231 TA 232
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-225 |
1.22e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 95.68 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPI---NMLSSR----QLA 75
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLfgrNIYSPDvdpiEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 76 RRLSLLPQHHLTPEGITVQELVSYGrnpwLSLWGRLSAED--NARVNVAMNQTRINHLAVRRLTE----LSGGQRQRAFL 149
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIG----VKLNGLVKSKKelDERVEWALKKAALWDEVKDRLNDypsnLSGGQRQRLVI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16132108 150 AMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQgKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-215 |
1.55e-23 |
|
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: 92.51 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPinmlssrqlarRLSLLPQhh 85
Cdd:cd03221 4 ENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-----------KIGYFEQ-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 86 ltpegitvqelvsygrnpwlslwgrlsaednarvnvamnqtrinhlavrrlteLSGGQRQRAFLAMVLAQNTPVVLLDEP 165
Cdd:cd03221 71 -----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16132108 166 TTYLDINHQvdlMRLMGELRTQGKTVVAVLHD---LNQAsryCDQLVVMANGH 215
Cdd:cd03221 98 TNHLDLESI---EALEEALKEYPGTVILVSHDryfLDQV---ATKIIELEDGK 144
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-214 |
2.41e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 98.06 E-value: 2.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQ-LARRLSLL 81
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 82 PQH-HLTPEgITVQElvsygrNPWLslwGRLSAED---NARVNVAMNQTRINHLAVR-----RLTELSGGQRQRAFLAMV 152
Cdd:PRK11288 85 YQElHLVPE-MTVAE------NLYL---GQLPHKGgivNRRLLNYEAREQLEHLGVDidpdtPLKYLSIGQRQMVEIAKA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16132108 153 LAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANG 214
Cdd:PRK11288 155 LARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-220 |
3.51e-23 |
|
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: 93.94 E-value: 3.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 17 VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNpINMLSSRQLARRLSLLpqhhltpegitvqel 96
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPWKRRKKFLRRIGVV--------------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 97 vsYG-RNpwlSLWGRLSAEDNARVNVAMN-------QTRINHLA------------VRRlteLSGGQRQRAFLAMVLAQN 156
Cdd:cd03267 100 --FGqKT---QLWWDLPVIDSFYLLAAIYdlpparfKKRLDELSelldleelldtpVRQ---LSLGQRMRAEIAAALLHE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16132108 157 TPVVLLDEPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQG 220
Cdd:cd03267 172 PEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
6-225 |
3.78e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 95.25 E-value: 3.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSYGTDK--VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSgtvfLGDNPINMLSSRQLAR------- 76
Cdd:PRK13640 9 KHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDD----NPNSKITVDGITLTAKtvwdire 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 77 RLSLLPQHhltPE----GITVQELVSYG-------RNPWLSLwgrlsaednarVNVAMNQTRINHLAVRRLTELSGGQRQ 145
Cdd:PRK13640 85 KVGIVFQN---PDnqfvGATVGDDVAFGlenravpRPEMIKI-----------VRDVLADVGMLDYIDSEPANLSGGQKQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 146 RAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQ-GKTVVAVLHDLNQASrYCDQLVVMANGHVMAQGTPEE 224
Cdd:PRK13640 151 RVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVE 229
|
.
gi 16132108 225 V 225
Cdd:PRK13640 230 I 230
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
3-226 |
4.22e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 96.64 E-value: 4.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLA----RRL 78
Cdd:PRK10070 29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 79 SLLPQHHLTPEGITVQELVSYGrnpwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTP 158
Cdd:PRK10070 109 AMVFQSFALMPHMTVLDNTAFG----MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPD 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16132108 159 VVLLDEPTTYLD----INHQVDLMRLMGElrtQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVM 226
Cdd:PRK10070 185 ILLMDEAFSALDplirTEMQDELVKLQAK---HQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-226 |
5.46e-23 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 97.50 E-value: 5.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYG-TDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLL 81
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 82 PQHHLTPEGiTVQELVSYGRNPWLS---LWGRLS-AEDNARV-NVAMN-QTRINHLAvrrlTELSGGQRQRAFLAMVLAQ 155
Cdd:TIGR01193 554 PQEPYIFSG-SILENLLLGAKENVSqdeIWAACEiAEIKDDIeNMPLGyQTELSEEG----SSISGGQKQRIALARALLT 628
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16132108 156 NTPVVLLDEPTTYLD-INHQVDLMRLMgelRTQGKTVVAVLHDLNQASRyCDQLVVMANGHVMAQGTPEEVM 226
Cdd:TIGR01193 629 DSKVLILDESTSNLDtITEKKIVNNLL---NLQDKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELL 696
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-216 |
8.89e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 93.60 E-value: 8.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 4 RTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLlncfSRLLM----PQSGTVFLGDNPINMLSSRQLA--RR 77
Cdd:PRK10419 14 AHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTL----ARLLVglesPSQGNVSWRGEPLAKLNRAQRKafRR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 78 LSLL----------PQHhltpegiTVQELVsygRNPWLSLWGRLSAEDNARVNVAMNQTRIN-HLAVRRLTELSGGQRQR 146
Cdd:PRK10419 90 DIQMvfqdsisavnPRK-------TVREII---REPLRHLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16132108 147 AFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTV-VAVLHDLNQASRYCDQLVVMANGHV 216
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTAcLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
2-201 |
9.35e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 92.16 E-value: 9.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 2 TLRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQ---SGTVFLGDNPINMLSSRQlaRRL 78
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQ--RRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 79 SLLPQHHLTpegitvqelvsygrNPWLSLWGRLS---------AEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFL 149
Cdd:COG4136 79 GILFQDDLL--------------FPHLSVGENLAfalpptigrAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVAL 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 16132108 150 AMVLAQNTPVVLLDEPTTYLDINHQVDLMRLM-GELRTQGKTVVAVLHDLNQA 201
Cdd:COG4136 145 LRALLAEPRALLLDEPFSKLDAALRAQFREFVfEQIRQRGIPALLVTHDEEDA 197
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
3-225 |
1.30e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 93.61 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSY-----GTDK-VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGD----NPINMLSSR 72
Cdd:PRK13633 5 IKCKNVSYKYesneeSTEKlALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsDEENLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 73 QLARRLSLLPQHHLTpeGITVQELVSYG-RNpwlslWGRLSAEDNARVNVAMNqtRINHLAVRRLTE--LSGGQRQRAFL 149
Cdd:PRK13633 85 NKAGMVFQNPDNQIV--ATIVEEDVAFGpEN-----LGIPPEEIRERVDESLK--KVGMYEYRRHAPhlLSGGQKQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16132108 150 AMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRyCDQLVVMANGHVMAQGTPEEV 225
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEI 231
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-216 |
1.59e-22 |
|
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: 90.95 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVsygtDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQ-LARRLSLL 81
Cdd:cd03215 5 LEVRGLSV----KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 82 PqhhltpegitvqelvsygrnpwlslwgrlsaEDNARVNVAMNQTRINHLAVRRLteLSGGQRQRAFLAMVLAQNTPVVL 161
Cdd:cd03215 81 P-------------------------------EDRKREGLVLDLSVAENIALSSL--LSGGNQQKVVLARWLARDPRVLI 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16132108 162 LDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHV 216
Cdd:cd03215 128 LDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
3-225 |
2.13e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 92.36 E-value: 2.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARR-LSLL 81
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMgVVRT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 82 PQHHLTPEGITVQE--LVSYGRNPWLSLWGRL-------SAEDNARVNVAMNQTRIN--HLAVRRLTELSGGQRQRAFLA 150
Cdd:PRK11300 86 FQHVRLFREMTVIEnlLVAQHQQLKTGLFSGLlktpafrRAESEALDRAATWLERVGllEHANRQAGNLAYGQQRRLEIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16132108 151 MVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQ-GKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:PRK11300 166 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
29-222 |
2.56e-22 |
|
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: 95.85 E-value: 2.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 29 KITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPI--NMLSSRQlarRLSLLPQHHLTPEGITVQELVSYgrnpWLS 106
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIetNLDAVRQ---SLGMCPQHNILFHHLTVAEHILF----YAQ 1029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 107 LWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRT 186
Cdd:TIGR01257 1030 LKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRS 1109
|
170 180 190
....*....|....*....|....*....|....*.
gi 16132108 187 qGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTP 222
Cdd:TIGR01257 1110 -GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-227 |
3.62e-22 |
|
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: 94.75 E-value: 3.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSY-----------GTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLmPQSGTVFLGDNPINMLSS 71
Cdd:COG4172 276 LEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 72 RQLaRRL-------------SLLPQHhltpegiTVQELVSYGrnpwLSLWGR-LSAED-NARVNVAMNQTRINHLAVRRL 136
Cdd:COG4172 355 RAL-RPLrrrmqvvfqdpfgSLSPRM-------TVGQIIAEG----LRVHGPgLSAAErRARVAEALEEVGLDPAARHRY 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 137 -TELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDLnQASRY-CDQLVVMAN 213
Cdd:COG4172 423 pHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLqREHGLAYLFISHDL-AVVRAlAHRVMVMKD 501
|
250
....*....|....
gi 16132108 214 GHVMAQGTPEEVMT 227
Cdd:COG4172 502 GKVVEQGPTEQVFD 515
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
6-226 |
3.77e-22 |
|
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: 91.39 E-value: 3.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSYGTDK--VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLsllpq 83
Cdd:cd03252 4 EHVRFRYKPDGpvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 84 hhltpeGITVQELVsygrnpwlsLWGRLSAEDNARVNVAMNQTRINHLA--------VRRLTE------------LSGGQ 143
Cdd:cd03252 79 ------GVVLQENV---------LFNRSIRDNIALADPGMSMERVIEAAklagahdfISELPEgydtivgeqgagLSGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 144 RQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELrTQGKTVVAVLHDLNqASRYCDQLVVMANGHVMAQGTPE 223
Cdd:cd03252 144 RQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDI-CAGRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHD 221
|
...
gi 16132108 224 EVM 226
Cdd:cd03252 222 ELL 224
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-249 |
4.21e-22 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 93.33 E-value: 4.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSYGTDK----VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQL--ARR-L 78
Cdd:PRK11153 5 KNISKVFPQGGrtihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkARRqI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 79 SLLPQHHLTPEGITVQELVSYgrnPwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTP 158
Cdd:PRK11153 85 GMIFQHFNLLSSRTVFDNVAL---P-LELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 159 VVLLDEPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGT-------PEEVMTPGL 230
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTvsevfshPKHPLTREF 240
|
250 260
....*....|....*....|....*
gi 16132108 231 LRTVFSVE------AEIHPEPVSGR 249
Cdd:PRK11153 241 IQSTLHLDlpedylARLQAEPTTGS 265
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-225 |
5.20e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 92.08 E-value: 5.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTD---KVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLS 79
Cdd:PRK13642 5 LEVENLVFKYEKEsdvNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 80 LLPQHhltPE----GITVQELVSYGrnpwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQ 155
Cdd:PRK13642 85 MVFQN---PDnqfvGATVEDDVAFG----MENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16132108 156 NTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGK-TVVAVLHDLNQASRyCDQLVVMANGHVMAQGTPEEV 225
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
6-226 |
7.35e-22 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 94.32 E-value: 7.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSY-GTDK-VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLPQ 83
Cdd:PRK11176 345 RNVTFTYpGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQ 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 84 H-HLTPEgiTVQELVSYGRNPWLSlwgRLSAEDNARVNVAMN---------QTRINHLAVrrltELSGGQRQRAFLAMVL 153
Cdd:PRK11176 425 NvHLFND--TIANNIAYARTEQYS---REQIEEAARMAYAMDfinkmdnglDTVIGENGV----LLSGGQRQRIAIARAL 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16132108 154 AQNTPVVLLDEPTTYLDINHQVDLMRLMGELRtQGKTVVAVLHDLNQASRyCDQLVVMANGHVMAQGTPEEVM 226
Cdd:PRK11176 496 LRDSPILILDEATSALDTESERAIQAALDELQ-KNRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELL 566
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
17-229 |
7.48e-22 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 94.24 E-value: 7.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 17 VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLPQHHLTPEGiTVQEl 96
Cdd:TIGR03796 494 LIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEG-TVRD- 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 97 vsygrNpwLSLWGRLSAEDNarVNVAMNQTRINHLAVRR-------LTE----LSGGQRQRAFLAMVLAQNTPVVLLDEP 165
Cdd:TIGR03796 572 -----N--LTLWDPTIPDAD--LVRACKDAAIHDVITSRpggydaeLAEgganLSGGQRQRLEIARALVRNPSILILDEA 642
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16132108 166 TTYLDInhQVDLmRLMGELRTQGKTVVAVLHDLNqASRYCDQLVVMANGHVMAQGTPEEVMTPG 229
Cdd:TIGR03796 643 TSALDP--ETEK-IIDDNLRRRGCTCIIVAHRLS-TIRDCDEIIVLERGKVVQRGTHEELWAVG 702
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-233 |
1.36e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 93.37 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 2 TLRTENLTVSYGTDKVLND-VSLSLPTGKITALIGPNGCGKSTLLNCfsrLL--MPQSGTVFLGDNPINMLSSRQLARRL 78
Cdd:PRK11174 349 TIEAEDLEILSPDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNA---LLgfLPYQGSLKINGIELRELDPESWRKHL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 79 SLLPQHHLTPEGiTVQELVsygrnpwlsLWGRLSAEDnARVNVAMNQTRINHLaVRRLTE------------LSGGQRQR 146
Cdd:PRK11174 426 SWVGQNPQLPHG-TLRDNV---------LLGNPDASD-EQLQQALENAWVSEF-LPLLPQgldtpigdqaagLSVGQAQR 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 147 AFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELrTQGKTVVAVLHDLNQASRyCDQLVVMANGHVMAQGTPEEVM 226
Cdd:PRK11174 494 LALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAA-SRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAELS 571
|
....*...
gi 16132108 227 T-PGLLRT 233
Cdd:PRK11174 572 QaGGLFAT 579
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
3-214 |
1.57e-21 |
|
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: 89.07 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDK-----VLNDVSLSLPTGKITALIGPNGCGKSTLLNCfsrLL--MPQ-SGTVFLGdnpinmlssrql 74
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSA---LLgeLEKlSGSVSVP------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 75 aRRLSLLPQhhltpegitvqelvsygrNPWLS--------LWGrlSAEDNARVNVAMN----QTRINHLAVRRLTE---- 138
Cdd:cd03250 66 -GSIAYVSQ------------------EPWIQngtireniLFG--KPFDEERYEKVIKacalEPDLEILPDGDLTEigek 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 139 ---LSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMR--LMGELRtQGKTVVAVLHDLnQASRYCDQLVVMAN 213
Cdd:cd03250 125 ginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLL-NNKTRILVTHQL-QLLPHADQIVVLDN 202
|
.
gi 16132108 214 G 214
Cdd:cd03250 203 G 203
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-226 |
1.66e-21 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 91.33 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSY-----------GTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSS 71
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 72 RQLaRRL-------------SLLPQHhltpegiTVQELVSYGrnpwLSLWGRLSAED-NARVNVAMNQTRINHLAVRRLT 137
Cdd:COG4608 88 REL-RPLrrrmqmvfqdpyaSLNPRM-------TVGDIIAEP----LRIHGLASKAErRERVAELLELVGLRPEHADRYP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 138 -ELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQ-GKTVVAVLHDLNqASRY-CDQLVVMANG 214
Cdd:COG4608 156 hEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLS-VVRHiSDRVAVMYLG 234
|
250
....*....|..
gi 16132108 215 HVMAQGTPEEVM 226
Cdd:COG4608 235 KIVEIAPRDELY 246
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
2-227 |
1.67e-21 |
|
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: 93.18 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 2 TLRTENLTVSY--GTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLS 79
Cdd:TIGR01842 316 HLSVENVTIVPpgGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 80 LLPQHHLTPEGITVQELVSYGRNpwlslwgrlsAEDNARVNVAmnqtRIN--HLAVRRLTE------------LSGGQRQ 145
Cdd:TIGR01842 396 YLPQDVELFPGTVAENIARFGEN----------ADPEKIIEAA----KLAgvHELILRLPDgydtvigpggatLSGGQRQ 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 146 RAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHD---LNQAsrycDQLVVMANGHVMAQGTP 222
Cdd:TIGR01842 462 RIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRpslLGCV----DKILVLQDGRIARFGER 537
|
....*
gi 16132108 223 EEVMT 227
Cdd:TIGR01842 538 DEVLA 542
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-214 |
1.90e-21 |
|
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: 89.45 E-value: 1.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 18 LNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLA--RRLSLLPQhhltpegITVQE 95
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVvfQNYSLLPW-------LTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 96 LVSYGRNPWLSLWGRLSAEDNARVNVAMnqTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDI---- 171
Cdd:TIGR01184 74 NIALAVDRVLPDLSKSERRAIVEEHIAL--VGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAltrg 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16132108 172 NHQVDLMRLMGELRTqgkTVVAVLHDLNQASRYCDQLVVMANG 214
Cdd:TIGR01184 152 NLQEELMQIWEEHRV---TVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-226 |
4.39e-21 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 88.83 E-value: 4.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVF--LGDNPINMLSSRQLARRLSL 80
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrMRDGQLRDLYALSEAERRRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 81 L-------PQHHLtpEGITVQelVSYGRNPWLSL-------WGRLSAEDN---ARVNVAMNqtRINHLAvrrlTELSGGQ 143
Cdd:PRK11701 87 LrtewgfvHQHPR--DGLRMQ--VSAGGNIGERLmavgarhYGDIRATAGdwlERVEIDAA--RIDDLP----TTFSGGM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 144 RQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTP 222
Cdd:PRK11701 157 QQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLT 236
|
....
gi 16132108 223 EEVM 226
Cdd:PRK11701 237 DQVL 240
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
3-225 |
4.97e-21 |
|
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: 87.58 E-value: 4.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNcfsrLLM------PQSGTVFLGDNPINMLSSRQLAR 76
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAK----TIMghpkyeVTEGEILFKGEDITDLPPEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 77 R-LSLLPQHHLTPEGITVQELVSYgrnpwlslwgrlsaednarVNVAmnqtrinhlavrrlteLSGGQRQRAFLAMVLAQ 155
Cdd:cd03217 77 LgIFLAFQYPPEIPGVKNADFLRY-------------------VNEG----------------FSGGEKKRNEILQLLLL 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16132108 156 NTPVVLLDEPTTYLDInhqvDLMRLMGE----LRTQGKTVVAVLH-----DLNQAsrycDQLVVMANGHVMAQGTPEEV 225
Cdd:cd03217 122 EPDLAILDEPDSGLDI----DALRLVAEvinkLREEGKSVLIITHyqrllDYIKP----DRVHVLYDGRIVKSGDKELA 192
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-211 |
5.78e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 87.85 E-value: 5.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 1 MTLRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSL 80
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 81 LPQhhlTPE--GITVQELVSYgrnPWLSlwgRLSAEDNARVNVAMNQTRI-NHLAVRRLTELSGGQRQRAFLAMVLaQNT 157
Cdd:PRK10247 86 CAQ---TPTlfGDTVYDNLIF---PWQI---RNQQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNL-QFM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 16132108 158 P-VVLLDEPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASrYCDQLVVM 211
Cdd:PRK10247 156 PkVLLLDEITSALDESNKHNVNEIIHRYvREQNIAVLWVTHDKDEIN-HADKVITL 210
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
7-225 |
5.85e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 89.05 E-value: 5.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 7 NLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTV-FLGDNpINMLSSRQL--AR-RLSLLP 82
Cdd:PRK11831 12 GVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEIlFDGEN-IPAMSRSRLytVRkRMSMLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 83 QHHLTPEGITVQELVSYgrnPwLSLWGRLSAEdNARVNVAMNQTRINHLAVRRL--TELSGGQRQRAFLAMVLAQNTPVV 160
Cdd:PRK11831 91 QSGALFTDMNVFDNVAY---P-LREHTQLPAP-LLHSTVMMKLEAVGLRGAAKLmpSELSGGMARRAALARAIALEPDLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16132108 161 LLDEPTTYLD-INHQVdLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:PRK11831 166 MFDEPFVGQDpITMGV-LVKLISELnSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-216 |
6.05e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 88.60 E-value: 6.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSY--GTD---KVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARR 77
Cdd:COG1101 2 LELKNLSKTFnpGTVnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 78 LSLLPQHHL--TPEGITVQE--LVSYGRNPWLSLWGRLSAEDNARVnvamnQTRINHLAV---RRLTE----LSGGQRQR 146
Cdd:COG1101 82 IGRVFQDPMmgTAPSMTIEEnlALAYRRGKRRGLRRGLTKKRRELF-----RELLATLGLgleNRLDTkvglLSGGQRQA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16132108 147 AFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGK-TVVAVLHDLNQASRYCDQLVVMANGHV 216
Cdd:COG1101 157 LSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNlTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
6-227 |
7.74e-21 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 88.27 E-value: 7.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINmlSSRQLARRLSL---LP 82
Cdd:PRK11264 7 KNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITID--TARSLSQQKGLirqLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 83 QH--------HLTP---------EGITV------QELVSYGRnpwlslwgrlsaEDNARVNVAMNQTRINhlavRRlteL 139
Cdd:PRK11264 85 QHvgfvfqnfNLFPhrtvleniiEGPVIvkgepkEEATARAR------------ELLAKVGLAGKETSYP----RR---L 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 140 SGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQ 219
Cdd:PRK11264 146 SGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQ 225
|
....*...
gi 16132108 220 GTPEEVMT 227
Cdd:PRK11264 226 GPAKALFA 233
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
16-243 |
7.92e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 88.99 E-value: 7.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 16 KVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTV------------------FLGDNPINMLSSR----- 72
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekVLEKLVIQKTRFKkikki 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 73 -QLARRLSLLPQ---HHLTPEgiTVQE-----LVSYGRNPwlslwgrLSAEDNARVNVAMNQTRINHLAvRRLTELSGGQ 143
Cdd:PRK13651 101 kEIRRRVGVVFQfaeYQLFEQ--TIEKdiifgPVSMGVSK-------EEAKKRAAKYIELVGLDESYLQ-RSPFELSGGQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 144 RQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPE 223
Cdd:PRK13651 171 KRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTY 250
|
250 260
....*....|....*....|
gi 16132108 224 EVmtpgLLRTVFSVEAEIHP 243
Cdd:PRK13651 251 DI----LSDNKFLIENNMEP 266
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-224 |
1.12e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 90.94 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSY----GTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLAR-- 76
Cdd:PRK10535 5 LELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 77 ---------RLSLLPqhHLTPEGiTVQELVSY---GRNPWL----SLWGRLSAEDnaRVNVAMNQtrinhlavrrlteLS 140
Cdd:PRK10535 85 rehfgfifqRYHLLS--HLTAAQ-NVEVPAVYaglERKQRLlraqELLQRLGLED--RVEYQPSQ-------------LS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 141 GGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHD---LNQASRycdqLVVMANGHVM 217
Cdd:PRK10535 147 GGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDpqvAAQAER----VIEIRDGEIV 222
|
....*..
gi 16132108 218 AQGTPEE 224
Cdd:PRK10535 223 RNPPAQE 229
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
17-214 |
1.18e-20 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 87.10 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 17 VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFL--GDNPINM--LSSRQLA--RR---------LSLL 81
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLaqASPREILalRRrtigyvsqfLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 82 PQhhLTPEGITVQELVSYGrnpwlslWGRLSAEDNARvnvAMnqtrINHLAV-RRLTEL-----SGGQRQRAFLAMVLAQ 155
Cdd:COG4778 106 PR--VSALDVVAEPLLERG-------VDREEARARAR---EL----LARLNLpERLWDLppatfSGGEQQRVNIARGFIA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 156 NTPVVLLDEPTTYLD-INHQVdLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANG 214
Cdd:COG4778 170 DPPLLLLDEPTASLDaANRAV-VVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-227 |
1.65e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 90.17 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 17 VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLPQHHLTPEGiTVQEL 96
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSG-SVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 97 VSYGRNpwlslwgrlSAEDNARVNVAMN----------QTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEPT 166
Cdd:TIGR00958 575 IAYGLT---------DTPDEEIMAAAKAanahdfimefPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16132108 167 TYLDINHQvdlmRLMGELRT-QGKTVVAVLHDLNQASRyCDQLVVMANGHVMAQGTPEEVMT 227
Cdd:TIGR00958 646 SALDAECE----QLLQESRSrASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLME 702
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-172 |
5.04e-20 |
|
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: 88.84 E-value: 5.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGtDKVL-NDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDnpinmlsSRQLA----RR 77
Cdd:TIGR03719 323 IEAENLTKAFG-DKLLiDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE-------TVKLAyvdqSR 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 78 LSLLPQHhltpegiTVQELVSYGrNPWLSLWGRlsaEDNARVNVAmnqtRINHLAV---RRLTELSGGQRQRAFLAMVLA 154
Cdd:TIGR03719 395 DALDPNK-------TVWEEISGG-LDIIKLGKR---EIPSRAYVG----RFNFKGSdqqKKVGQLSGGERNRVHLAKTLK 459
|
170
....*....|....*...
gi 16132108 155 QNTPVVLLDEPTTYLDIN 172
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVE 477
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
3-220 |
5.31e-20 |
|
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: 85.28 E-value: 5.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDK----------------------VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVf 60
Cdd:cd03220 1 IELENVSKSYPTYKggssslkklgilgrkgevgefwALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 61 lgdnpinmlssrQLARRLSLLPqhhltpeGITVqelvsyGRNPwlslwgRLSAEDNARVNVAMN-------QTRIN---- 129
Cdd:cd03220 80 ------------TVRGRVSSLL-------GLGG------GFNP------ELTGRENIYLNGRLLglsrkeiDEKIDeiie 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 130 --------HLAVRrltELSGGQRQR-AFlAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQ 200
Cdd:cd03220 129 fselgdfiDLPVK---TYSSGMKARlAF-AIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSS 204
|
250 260
....*....|....*....|
gi 16132108 201 ASRYCDQLVVMANGHVMAQG 220
Cdd:cd03220 205 IKRLCDRALVLEKGKIRFDG 224
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-222 |
6.07e-20 |
|
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: 85.24 E-value: 6.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSY--GTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLPQ 83
Cdd:cd03244 6 KNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 84 HHLTPEGiTVQE-LVSYGRNPWLSLWgrlsaedNARVNVAMNQtRINHLAVR---RLTE----LSGGQRQRAFLAMVLAQ 155
Cdd:cd03244 86 DPVLFSG-TIRSnLDPFGEYSDEELW-------QALERVGLKE-FVESLPGGldtVVEEggenLSVGQRQLLCLARALLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 156 NTPVVLLDEPTTYLDinhqVDLMRLMGE-LRTQ--GKTVVAVLHDLNqASRYCDQLVVMANGHVMAQGTP 222
Cdd:cd03244 157 KSKILVLDEATASVD----PETDALIQKtIREAfkDCTVLTIAHRLD-TIIDSDRILVLDKGRVVEFDSP 221
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
6-231 |
6.14e-20 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 88.47 E-value: 6.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSYGTD--KVLNDVSLSLPTGKITALIGPNGCGKSTLLncfsRLLM----PQSGTVFLGDNPINMLSSRQLARRLS 79
Cdd:TIGR03797 455 DRVTFRYRPDgpLILDDVSLQIEPGEFVAIVGPSGSGKSTLL----RLLLgfetPESGSVFYDGQDLAGLDVQAVRRQLG 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 80 LLPQH-HLTP----EGITVQELVSYGRnPWLSLwgRLS--AEDNARVNVAMNqTRINHLAvrrlTELSGGQRQRAFLAMV 152
Cdd:TIGR03797 531 VVLQNgRLMSgsifENIAGGAPLTLDE-AWEAA--RMAglAEDIRAMPMGMH-TVISEGG----GTLSGGQRQRLLIARA 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 153 LAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTqgkTVVAVLHDLNQAsRYCDQLVVMANGHVMAQGTPEEVM-TPGLL 231
Cdd:TIGR03797 603 LVRKPRILLFDEATSALDNRTQAIVSESLERLKV---TRIVIAHRLSTI-RNADRIYVLDAGRVVQQGTYDELMaREGLF 678
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-227 |
6.93e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 85.87 E-value: 6.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 12 YGTDK-VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLL------MPQSGTVFLGDNPINMLSSRQLARRLSLLPQH 84
Cdd:PRK14246 19 YINDKaILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 85 -----HLTPEGITVQELVSYGRNPWLSLwGRLSAEDNARVNVAMN-QTRINHLAvrrlTELSGGQRQRAFLAMVLAQNTP 158
Cdd:PRK14246 99 pnpfpHLSIYDNIAYPLKSHGIKEKREI-KKIVEECLRKVGLWKEvYDRLNSPA----SQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16132108 159 VVLLDEPTTYLDINHQVDLMRLMGELRTQgKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMT 227
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFT 241
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-216 |
9.47e-20 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 87.93 E-value: 9.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 2 TLRTENLTVSYGTDK-----VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMlSSRQLAR 76
Cdd:COG4615 327 TLELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTA-DNREAYR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 77 RL--SLLPQHHLTPEgitvqelvsygrnpwlsLWGRLSAEDNARVNVAMNQTRINH-LAVR--RL--TELSGGQRQRafL 149
Cdd:COG4615 406 QLfsAVFSDFHLFDR-----------------LLGLDGEADPARARELLERLELDHkVSVEdgRFstTDLSQGQRKR--L 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 150 AMVLA--QNTPVVLLDE------PTT----YldinHQvdlmrLMGELRTQGKTVVAVLHDlnqaSRY---CDQLVVMANG 214
Cdd:COG4615 467 ALLVAllEDRPILVFDEwaadqdPEFrrvfY----TE-----LLPELKARGKTVIAISHD----DRYfdlADRVLKMDYG 533
|
..
gi 16132108 215 HV 216
Cdd:COG4615 534 KL 535
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-225 |
1.05e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 85.14 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 2 TLRTENLTVSygTDKVL-NDVSLSLPTGKITALIGPNGCGKStlLNCFSRL-LMP-----QSGTVFLGDNPINMLSSRql 74
Cdd:PRK10418 4 QIELRNIALQ--AAQPLvHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALgILPagvrqTAGRVLLDGKPVAPCALR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 75 ARRLSLL---PQHHLTPegitVQELVSYGRNPWLSLwGRLSaeDNARVNVAMNQTRI-NHLAVRRLT--ELSGGQRQRAF 148
Cdd:PRK10418 78 GRKIATImqnPRSAFNP----LHTMHTHARETCLAL-GKPA--DDATLTAALEAVGLeNAARVLKLYpfEMSGGMLQRMM 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16132108 149 LAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:PRK10418 151 IALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
3-201 |
1.37e-19 |
|
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: 83.56 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLssRQLARRLSLLP 82
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ--RDEPHENILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 83 QHH--LTPEgITVQElvsygrNpwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVV 160
Cdd:TIGR01189 79 GHLpgLKPE-LSALE------N--LHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLW 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16132108 161 LLDEPTTYLDINHQVDLMRLM-GELRTQGKTVVAVLHDLNQA 201
Cdd:TIGR01189 150 ILDEPTTALDKAGVALLAGLLrAHLARGGIVLLTTHQDLGLV 191
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-227 |
2.04e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.07 E-value: 2.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDK-----------VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQsGTVFLGDNPINMLSS 71
Cdd:PRK15134 276 LDVEQLQVAFPIRKgilkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLNR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 72 RQL---ARRLSLL---PQHHLTPEgITVQELVSYG---RNPWLSlwgrlSAEDNARVNVAMNQTRINHLAVRRL-TELSG 141
Cdd:PRK15134 355 RQLlpvRHRIQVVfqdPNSSLNPR-LNVLQIIEEGlrvHQPTLS-----AAQREQQVIAVMEEVGLDPETRHRYpAEFSG 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 142 GQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELrtQGKTVVAVL---HDLNQASRYCDQLVVMANGHVMA 218
Cdd:PRK15134 429 GQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSL--QQKHQLAYLfisHDLHVVRALCHQVIVLRQGEVVE 506
|
....*....
gi 16132108 219 QGTPEEVMT 227
Cdd:PRK15134 507 QGDCERVFA 515
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-227 |
3.12e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 84.38 E-value: 3.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 7 NLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLL-----MPQSGTVFLGDNPI-NMLSSRQLARRLSL 80
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdkvsgYRYSGDVLLGGRSIfNYRDVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 81 LPQHHlTPEGITVQELVSYGRNPwlslwGRLSAEDNARvnvAMNQTRINHL----AVR-RLTE----LSGGQRQRAFLAM 151
Cdd:PRK14271 106 LFQRP-NPFPMSIMDNVLAGVRA-----HKLVPRKEFR---GVAQARLTEVglwdAVKdRLSDspfrLSGGQQQLLCLAR 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16132108 152 VLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQgKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMT 227
Cdd:PRK14271 177 TLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-226 |
3.22e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 86.23 E-value: 3.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVsygtDKVLNDVSLSLPTGKITALIGPNGCGKSTLLncfsRLLM----PQSGTVFLGDNPINMLSSRQ-LARR 77
Cdd:COG1129 257 LEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELA----RALFgadpADSGEIRLDGKPVRIRSPRDaIRAG 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 78 LSLLPQHHLTpEGI----TVQE---LVSYGRnpwLSLWGRLS-AEDNARVNVAMNQTRIN----HLAVRrltELSGGQRQ 145
Cdd:COG1129 329 IAYVPEDRKG-EGLvldlSIREnitLASLDR---LSRGGLLDrRRERALAEEYIKRLRIKtpspEQPVG---NLSGGNQQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 146 RAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMA-----QG 220
Cdd:COG1129 402 KVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGeldreEA 481
|
....*.
gi 16132108 221 TPEEVM 226
Cdd:COG1129 482 TEEAIM 487
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-198 |
6.22e-19 |
|
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: 83.18 E-value: 6.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 25 LPT---GKITALIGPNGCGKSTLLNCFSRLLMPQSGTvfLGDNP-----INMLSSRQLARRLSLL----------PQH-H 85
Cdd:cd03236 20 LPVpreGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPdwdeiLDEFRGSELQNYFTKLlegdvkvivkPQYvD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 86 LTPEGI--TVQELVSygrnpwlslwgrlSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLD 163
Cdd:cd03236 98 LIPKAVkgKVGELLK-------------KKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFD 164
|
170 180 190
....*....|....*....|....*....|....*
gi 16132108 164 EPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDL 198
Cdd:cd03236 165 EPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-242 |
7.29e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 83.98 E-value: 7.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 16 KVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTV-FLGDNPINmlSSRQLARRlsllpqhhltpegITV- 93
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVrVLGYVPFK--RRKEFARR-------------IGVv 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 94 --QelvsygRNpwlSLWGRLSAEDNARVNVAMN-------QTRINHLA------------VRrltELSGGQRQRAFLAMV 152
Cdd:COG4586 101 fgQ------RS---QLWWDLPAIDSFRLLKAIYripdaeyKKRLDELVelldlgelldtpVR---QLSLGQRMRCELAAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 153 LAQNTPVVLLDEPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEvmtpglL 231
Cdd:COG4586 169 LLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEE------L 242
|
250
....*....|.
gi 16132108 232 RTVFSVEAEIH 242
Cdd:COG4586 243 KERFGPYKTIV 253
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
3-201 |
8.93e-19 |
|
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: 81.39 E-value: 8.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGtvflgdnpinmlssrqlarRLSLLP 82
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAG-------------------RVLLNG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 83 QHHLTPEGITVQELVSYGRNPWLSlwGRLSAEDNAR----------VNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMV 152
Cdd:cd03231 62 GPLDFQRDSIARGLLYLGHAPGIK--TTLSVLENLRfwhadhsdeqVEEALARVGLNGFEDRPVAQLSAGQQRRVALARL 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16132108 153 LAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLH-DLNQA 201
Cdd:cd03231 140 LLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHqDLGLS 189
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
3-223 |
1.10e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 82.04 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLlncfSRLLM------PQSGTVFLGDNPINMLSSRQLAR 76
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTL----AKVLMghpkyeVTSGSILLDGEDILELSPDERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 77 R-LSLLPQHhltP---EGITVQELV--SYG--RNPWLSLwgrlsAEDNARVNVAMNQTRINHLAVRR-LTE-LSGGQRQR 146
Cdd:COG0396 77 AgIFLAFQY---PveiPGVSVSNFLrtALNarRGEELSA-----REFLKLLKEKMKELGLDEDFLDRyVNEgFSGGEKKR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 147 AFLAMVLAQNTPVVLLDEPTTYLDInhqvDLMRLMGE----LRTQGKTVVAVLH-----DLNQAsrycDQLVVMANGHVM 217
Cdd:COG0396 149 NEILQMLLLEPKLAILDETDSGLDI----DALRIVAEgvnkLRSPDRGILIITHyqrilDYIKP----DFVHVLVDGRIV 220
|
....*.
gi 16132108 218 AQGTPE 223
Cdd:COG0396 221 KSGGKE 226
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-172 |
1.76e-18 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 84.01 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSYGtDKVL-NDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPinmlssrqlarRLSLLPQH 84
Cdd:PRK11819 328 ENLSKSFG-DRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETV-----------KLAYVDQS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 85 H--LTPEGiTVQELVSYGrNPWLSLWGRlsaEDNARVNVAmnqtRINHLAV---RRLTELSGGQRQRAFLAMVLAQNTPV 159
Cdd:PRK11819 396 RdaLDPNK-TVWEEISGG-LDIIKVGNR---EIPSRAYVG----RFNFKGGdqqKKVGVLSGGERNRLHLAKTLKQGGNV 466
|
170
....*....|...
gi 16132108 160 VLLDEPTTYLDIN 172
Cdd:PRK11819 467 LLLDEPTNDLDVE 479
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-222 |
2.12e-18 |
|
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: 80.53 E-value: 2.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTD--KVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSL 80
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 81 LPQHHLTPEGITVQELVSYGRNPWLSLWGRLSAEDNArvnvamnqtrinhlavrrlTELSGGQRQRAFLAMVLAQNTPVV 160
Cdd:cd03369 87 IPQDPTLFSGTIRSNLDPFDEYSDEEIYGALRVSEGG-------------------LNLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16132108 161 LLDEPTTYLDINHQVDLMRLMGELrTQGKTVVAVLHDLNQASRyCDQLVVMANGHVMAQGTP 222
Cdd:cd03369 148 VLDEATASIDYATDALIQKTIREE-FTNSTILTIAHRLRTIID-YDKILVMDAGEVKEYDHP 207
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-227 |
3.44e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 83.64 E-value: 3.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 4 RTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVF-LGDnpiNMLSSR---QLARRLS 79
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvLGG---DMADARhrrAVCPRIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 80 LLPQ---HHLTPEgITVQELVSY-GRnpwlsLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQ 155
Cdd:NF033858 80 YMPQglgKNLYPT-LSVFENLDFfGR-----LFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 156 NTPVVLLDEPTTyldinhQVD-LMR-----LMGELRTQ--GKTVVAVLHDLNQASRYcDQLVVMANGHVMAQGTPEEVMT 227
Cdd:NF033858 154 DPDLLILDEPTT------GVDpLSRrqfweLIDRIRAErpGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLA 226
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
2-225 |
4.32e-18 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 82.20 E-value: 4.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 2 TLRTENLTVSY-GTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQlaRRLSL 80
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 81 LPQHH-LTPEgITVQELVSYGrnpwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRafLAM--VLAQNT 157
Cdd:PRK11650 81 VFQNYaLYPH-MSVRENMAYG----LKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQR--VAMgrAIVREP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16132108 158 PVVLLDEPTTYLD----INHQVDLMRLMGELRTqgkTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:PRK11650 154 AVFLFDEPLSNLDaklrVQMRLEIQRLHRRLKT---TSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-216 |
4.37e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 80.30 E-value: 4.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSY-GTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQ---LARRL 78
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 79 SLLPQ-HHLTPEGiTVQELVSYGrnpwLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNT 157
Cdd:PRK10908 82 GMIFQdHHLLMDR-TVYDNVAIP----LIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16132108 158 PVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHV 216
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
13-224 |
7.79e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 82.40 E-value: 7.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 13 GTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMP---QSGTVFLGDNPINmlsSRQLARRLSLLPQHHLTPE 89
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPID---AKEMRAISAYVQQDDLFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 90 GITVQELVSYGRNpwLSLWGRLSA-EDNARVN---VAMN-----QTRINhlAVRRLTELSGGQRQRAFLAMVLAQNTPVV 160
Cdd:TIGR00955 113 TLTVREHLMFQAH--LRMPRRVTKkEKRERVDevlQALGlrkcaNTRIG--VPGRVKGLSGGERKRLAFASELLTDPPLL 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 161 LLDEPTTYLD--INHQVdlMRLMGELRTQGKTVVAVLHdlnQASR--YC--DQLVVMANGHVMAQGTPEE 224
Cdd:TIGR00955 189 FCDEPTSGLDsfMAYSV--VQVLKGLAQKGKTIICTIH---QPSSelFElfDKIILMAEGRVAYLGSPDQ 253
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
11-214 |
8.31e-18 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 79.30 E-value: 8.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 11 SYGTD-KVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLgDNPINMLSSRQLARRLSLLPQHHLTPE 89
Cdd:cd03290 9 SWGSGlATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHW-SNKNESEPSFEATRSRNRYSVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 90 ----GITVQELVSYG----RNPWLSLWGRLSAEDNARVNVAMNQTRINhlavRRLTELSGGQRQRAFLAMVLAQNTPVVL 161
Cdd:cd03290 88 pwllNATVEENITFGspfnKQRYKAVTDACSLQPDIDLLPFGDQTEIG----ERGINLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16132108 162 LDEPTTYLDINHQVDLMR--LMGELRTQGKTVVAVLHDLnQASRYCDQLVVMANG 214
Cdd:cd03290 164 LDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKDG 217
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-216 |
1.39e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 79.34 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPinmLSSRQLARRL---- 78
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAP---LAEAREDTRLmfqd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 79 -SLLPQHhltpegiTVQELVSYG-RNPWlslwgrlsaEDNARVNVAmnqtrinhlAV---RRLTE----LSGGQRQRAFL 149
Cdd:PRK11247 90 aRLLPWK-------KVIDNVGLGlKGQW---------RDAALQALA---------AVglaDRANEwpaaLSGGQKQRVAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16132108 150 AMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANGHV 216
Cdd:PRK11247 145 ARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
16-219 |
2.44e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.82 E-value: 2.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 16 KVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSR--QLA------RRLSLLPQhhlt 87
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKssQEAgigiihQELNLIPQ---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 88 pegITVQELVSYGR---NPWLSL-WGRLSAEDN---ARVNVamnqtriNHLAVRRLTELSGGQRQRAFLAMVLAQNTPVV 160
Cdd:PRK10762 94 ---LTIAENIFLGRefvNRFGRIdWKKMYAEADkllARLNL-------RFSSDKLVGELSIGEQQMVEIAKVLSFESKVI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16132108 161 LLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQ 219
Cdd:PRK10762 164 IMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAE 222
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
3-240 |
3.51e-17 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 79.38 E-value: 3.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDK----VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQ---SGTV-FLGDNPINmLSSRQL 74
Cdd:PRK09473 13 LDVKDLRVTFSTPDgdvtAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSAtFNGREILN-LPEKEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 75 ----ARRLSLLPQHHLTpegitvqelvsyGRNPW----------LSLWGRLSA----EDNARV--NVAMNQTRinhlavR 134
Cdd:PRK09473 92 nklrAEQISMIFQDPMT------------SLNPYmrvgeqlmevLMLHKGMSKaeafEESVRMldAVKMPEAR------K 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 135 RLT----ELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKT-VVAVLHDLNQASRYCDQLV 209
Cdd:PRK09473 154 RMKmyphEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGICDKVL 233
|
250 260 270
....*....|....*....|....*....|....*...
gi 16132108 210 VMANGHVMAQGTPEEVM-------TPGLLRTVFSVEAE 240
Cdd:PRK09473 234 VMYAGRTMEYGNARDVFyqpshpySIGLLNAVPRLDAE 271
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
6-245 |
4.11e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 80.39 E-value: 4.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSY-GTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLsllpqh 84
Cdd:PRK13657 338 DDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNI------ 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 85 hltpeGITVQELVSYGRnpwlslwgrlSAEDNARVN---------------------VAMNQTRINHLAVRRLTELSGGQ 143
Cdd:PRK13657 412 -----AVVFQDAGLFNR----------SIEDNIRVGrpdatdeemraaaeraqahdfIERKPDGYDTVVGERGRQLSGGE 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 144 RQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRtQGKTVVAVLHDLNQAsRYCDQLVVMANGHVMAQGTPE 223
Cdd:PRK13657 477 RQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELM-KGRTTFIIAHRLSTV-RNADRILVFDNGRVVESGSFD 554
|
250 260
....*....|....*....|....*..
gi 16132108 224 EVMTPG-----LLRTVFSVEAEIHPEP 245
Cdd:PRK13657 555 ELVARGgrfaaLLRAQGMLQEDERRKQ 581
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-230 |
4.81e-17 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 79.87 E-value: 4.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTD---KVLNDVSLSLPTGKITALIGPNGCGKSTLLNC-FSRLLMPQSGTVFLGDNPINMLSSRQ-LARR 77
Cdd:TIGR02633 258 LEARNLTCWDVINphrKRVDDVSFSLRRGEILGVAGLVGAGRTELVQAlFGAYPGKFEGNVFINGKPVDIRNPAQaIRAG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 78 LSLLPQHHlTPEGITVQELVsyGRNPWLSLWGRLSAEdnARVNVAMNQ----TRINHLAVRR------LTELSGGQRQRA 147
Cdd:TIGR02633 338 IAMVPEDR-KRHGIVPILGV--GKNITLSVLKSFCFK--MRIDAAAELqiigSAIQRLKVKTaspflpIGRLSGGNQQKA 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 148 FLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMA-----QGTP 222
Cdd:TIGR02633 413 VLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGdfvnhALTQ 492
|
....*...
gi 16132108 223 EEVMTPGL 230
Cdd:TIGR02633 493 EQVLAAAL 500
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
24-198 |
4.83e-17 |
|
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: 80.21 E-value: 4.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 24 SLPT---GKITALIGPNGCGKSTLLNCFSRLLMPQ-----------------SGTVfLGDNpINMLSSRQLarRLSLLPQ 83
Cdd:COG1245 92 GLPVpkkGKVTGILGPNGIGKSTALKILSGELKPNlgdydeepswdevlkrfRGTE-LQDY-FKKLANGEI--KVAHKPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 84 H-HLTPEGI--TVQELVSYG--RNPWLSLWGRLSaednarvnvamnqtrINHLAVRRLTELSGGQRQRAFLAMVLAQNTP 158
Cdd:COG1245 168 YvDLIPKVFkgTVRELLEKVdeRGKLDELAEKLG---------------LENILDRDISELSGGELQRVAIAAALLRDAD 232
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16132108 159 VVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDL 198
Cdd:COG1245 233 FYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDL 272
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
6-198 |
7.46e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 79.47 E-value: 7.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSYGTdkvlNDVSL-SLPT---GKITALIGPNGCGKSTLLNCFSRLLMPQ-----------------SGTVFLgdN 64
Cdd:PRK13409 77 EEPVHRYGV----NGFKLyGLPIpkeGKVTGILGPNGIGKTTAVKILSGELIPNlgdyeeepswdevlkrfRGTELQ--N 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 65 PINMLSSRQLarRLSLLPQH-HLTPEGI--TVQELVSYG--RNPWLSLWGRLSaednarvnvamnqtrINHLAVRRLTEL 139
Cdd:PRK13409 151 YFKKLYNGEI--KVVHKPQYvDLIPKVFkgKVRELLKKVdeRGKLDEVVERLG---------------LENILDRDISEL 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16132108 140 SGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELrTQGKTVVAVLHDL 198
Cdd:PRK13409 214 SGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIREL-AEGKYVLVVEHDL 271
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
13-225 |
1.93e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 77.31 E-value: 1.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 13 GTDKVLNDVSLSLPTGKITALIGPNGCGKSTLlncfSRLLM----PQSGTVFLgdNPINMLSS-----RQLARRLSLLPQ 83
Cdd:PRK11308 26 RLVKALDGVSFTLERGKTLAVVGESGCGKSTL----ARLLTmietPTGGELYY--QGQDLLKAdpeaqKLLRQKIQIVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 84 hhltpegitvqelvsygrNPWLSLWGR----------------LSAEDNARVNVAMNQT---RINHlAVRRLTELSGGQR 144
Cdd:PRK11308 100 ------------------NPYGSLNPRkkvgqileepllintsLSAAERREKALAMMAKvglRPEH-YDRYPHMFSGGQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 145 QRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQ-GKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPE 223
Cdd:PRK11308 161 QRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKE 240
|
..
gi 16132108 224 EV 225
Cdd:PRK11308 241 QI 242
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
3-235 |
2.52e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 75.69 E-value: 2.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGT-VFLGDNPINMLSSRQLARRLSLL 81
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRiVFDGKDITDWQTAKIMREAVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 82 PQHHLTPEGITVQELVSYGrnpwlslwGRLSAEDNARVNVAMNQTRINHLAVRRLTE---LSGGQRQRAFLAMVLAQNTP 158
Cdd:PRK11614 86 PEGRRVFSRMTVEENLAMG--------GFFAERDQFQERIKWVYELFPRLHERRIQRagtMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16132108 159 VVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMTPGLLRTVF 235
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAY 234
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
6-226 |
3.42e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 77.45 E-value: 3.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSYGTDK-VLNDVSLSLPTGKITALIGPNGCGKSTLLNcfsrLLM----PQSGTVFLGDNPINMLSSRQLARRLSL 80
Cdd:PRK10790 344 DNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLAS----LLMgyypLTEGEIRLDGRPLSSLSHSVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 81 LPQHHLTPEGiTVQELVSYGRNpwlslwgrLSAEdnaRVNVAMNQTRINHLaVRRLTE------------LSGGQRQRAF 148
Cdd:PRK10790 420 VQQDPVVLAD-TFLANVTLGRD--------ISEE---QVWQALETVQLAEL-ARSLPDglytplgeqgnnLSVGQKQLLA 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16132108 149 LAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQgKTVVAVLHDLNQASRyCDQLVVMANGHVMAQGTPEEVM 226
Cdd:PRK10790 487 LARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH-TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLL 562
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-226 |
3.46e-16 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 77.36 E-value: 3.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 22 SLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLPQHHLTpegitvqELVSYGR 101
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQRNNT-------DMLSPGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 102 NPWlslwGRLSAE-------DNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQ 174
Cdd:PRK10938 96 DDT----GRTTAEiiqdevkDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 16132108 175 VDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVM 226
Cdd:PRK10938 172 QQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEIL 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-226 |
6.73e-16 |
|
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: 76.76 E-value: 6.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSY-----GTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVF--LGDNPINMLSSRQLA 75
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrVGDEWVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 76 R-----RLSLLPQHH-LTPEGITVQELVSYgrnpwLSL-----WGRLSAEDNARVnVAMNQTRINHLAVRRLTELSGGQR 144
Cdd:TIGR03269 360 RgrakrYIGILHQEYdLYPHRTVLDNLTEA-----IGLelpdeLARMKAVITLKM-VGFDEEKAEEILDKYPDELSEGER 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 145 QRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQ-GKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPE 223
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPE 513
|
...
gi 16132108 224 EVM 226
Cdd:TIGR03269 514 EIV 516
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-224 |
1.03e-15 |
|
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: 76.01 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 2 TLRTENLTVSYGTD-KVLNDVSLSLPTGKITALIGPNGCGKSTLlncfSRLLM----PQSGTVFLGDNPINMLSSRQLAR 76
Cdd:COG5265 357 EVRFENVSFGYDPErPILKGVSFEVPAGKTVAIVGPSGAGKSTL----ARLLFrfydVTSGRILIDGQDIRDVTQASLRA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 77 RLSLLPQHhltpegiTV------QELVSYGRnpwlslwgrLSAEDNARVNVAmnqtRINHLA--VRRLTE---------- 138
Cdd:COG5265 433 AIGIVPQD-------TVlfndtiAYNIAYGR---------PDASEEEVEAAA----RAAQIHdfIESLPDgydtrvgerg 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 139 --LSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLD------InhqvdlmrlMGELR--TQGKTVVAVLHDLnqaS--RYCD 206
Cdd:COG5265 493 lkLSGGEKQRVAIARTLLKNPPILIFDEATSALDsrteraI---------QAALRevARGRTTLVIAHRL---StiVDAD 560
|
250
....*....|....*...
gi 16132108 207 QLVVMANGHVMAQGTPEE 224
Cdd:COG5265 561 EILVLEAGRIVERGTHAE 578
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-225 |
1.24e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.83 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTV-SYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARR-LSL 80
Cdd:COG3845 258 LEVENLSVrDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 81 LP---QHHLTPEGITVQE--LVSYGRNPWLSLWGRLS---AEDNARvnvamnqTRINHLAVR------RLTELSGGQRQR 146
Cdd:COG3845 338 IPedrLGRGLVPDMSVAEnlILGRYRRPPFSRGGFLDrkaIRAFAE-------ELIEEFDVRtpgpdtPARSLSGGNQQK 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 147 AFLAMVLAQNTPVVLLDEPTTYLDIN-----HQvdlmRLMgELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGT 221
Cdd:COG3845 411 VILARELSRDPKLLIAAQPTRGLDVGaiefiHQ----RLL-ELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVP 485
|
....
gi 16132108 222 PEEV 225
Cdd:COG3845 486 AAEA 489
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
3-223 |
2.41e-15 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 73.06 E-value: 2.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLlncfSRLLMPQ------SGTVFLGDNPINMLSSRQLAR 76
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTL----SKTIAGHpsyevtSGTILFKGQDLLELEPDERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 77 R-LSLLPQHHLTPEGITVQELVSYGRNPWLSLWGR--LSAED-NARVNVAMNQTRIN-HLAVRRLTE-LSGGQRQRAFLA 150
Cdd:TIGR01978 77 AgLFLAFQYPEEIPGVSNLEFLRSALNARRSARGEepLDLLDfEKLLKEKLALLDMDeEFLNRSVNEgFSGGEKKRNEIL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16132108 151 MVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDlNQASRYC--DQLVVMANGHVMAQGTPE 223
Cdd:TIGR01978 157 QMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHY-QRLLNYIkpDYVHVLLDGRIVKSGDVE 230
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-230 |
3.41e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.58 E-value: 3.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTD---KVLNDVSLSLPTGKITALIGPNGCGKSTLLNC-FSRLLMPQSGTVFLGDNPINMLSSRQ-LARR 77
Cdd:PRK13549 260 LEVRNLTAWDPVNphiKRVDDVSFSLRRGEILGIAGLVGAGRTELVQClFGAYPGRWEGEIFIDGKPVKIRNPQQaIAQG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 78 LSLLP----QHHLTP-----EGITvqeLVSYGRnpwLSLWGRLsaEDNARVNVAmnQTRINHLAVR------RLTELSGG 142
Cdd:PRK13549 340 IAMVPedrkRDGIVPvmgvgKNIT---LAALDR---FTGGSRI--DDAAELKTI--LESIQRLKVKtaspelAIARLSGG 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 143 QRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQ--- 219
Cdd:PRK13549 410 NQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGDlin 489
|
250
....*....|...
gi 16132108 220 --GTPEEVMTPGL 230
Cdd:PRK13549 490 hnLTQEQVMEAAL 502
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
16-250 |
3.87e-15 |
|
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: 72.44 E-value: 3.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 16 KVLNDVSLSLPTGKIT-----ALIGPNGCGKSTLLNCFSRLLMPQSGtvflgDNPINMLSsrqlarrLSLLPQHHLTPEG 90
Cdd:cd03237 8 KTLGEFTLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEG-----DIEIELDT-------VSYKPQYIKADYE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 91 ITVQELVSygrnpwlSLWGRLSAEDNARVNVaMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLD 170
Cdd:cd03237 76 GTVRDLLS-------SITKDFYTHPYFKTEI-AKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 171 INHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMaNGH--VMAQGTPEEVMTPGLLRTVFSVEAEIHPEPVS 247
Cdd:cd03237 148 VEQRLMASKVIRRFaENNEKTAFVVEHDIIMIDYLADRLIVF-EGEpsVNGVANPPQSLRSGMNRFLKNLDITFRRDPET 226
|
...
gi 16132108 248 GRP 250
Cdd:cd03237 227 GRP 229
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
11-229 |
4.33e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 74.32 E-value: 4.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 11 SYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQlARRLS--LLPQHHLTP 88
Cdd:PRK15439 20 QYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAK-AHQLGiyLVPQEPLLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 89 EGITVQELVSYG---RNPWLSLWGRLSAEDNARVNVAMNQTRINhLAVRRLTELSGGqrqraflamvLAQNTPVVLLDEP 165
Cdd:PRK15439 99 PNLSVKENILFGlpkRQASMQKMKQLLAALGCQLDLDSSAGSLE-VADRQIVEILRG----------LMRDSRILILDEP 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16132108 166 TTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHV-----MAQGTPEEV---MTPG 229
Cdd:PRK15439 168 TASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIalsgkTADLSTDDIiqaITPA 239
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
20-243 |
6.60e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 72.98 E-value: 6.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 20 DVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGD-------NPINMLSSR-------QLARrlsLLPqHH 85
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaeKGICLPPEKrrigyvfQDAR---LFP-HY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 86 ltpegiTVQELVSYGrnpwlslwgrLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEP 165
Cdd:PRK11144 92 ------KVRGNLRYG----------MAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 166 TTYLDINHQVDLMRLMGELRTQGKT-VVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV-----MTPGLLR----TVF 235
Cdd:PRK11144 156 LASLDLPRKRELLPYLERLAREINIpILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVwassaMRPWLPKeeqsSIL 235
|
....*....
gi 16132108 236 SVE-AEIHP 243
Cdd:PRK11144 236 KVTvLEHHP 244
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-236 |
7.54e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.55 E-value: 7.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 20 DVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQ-LARRLSLLP----QHHL---TPEGI 91
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPedrqSSGLyldAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 92 TVQELVsYGRNPWlslWGRlSAEDNA---RVNVAMNqTRINHL--AVRRLtelSGGQRQRAFLAMVLAQNTPVVLLDEPT 166
Cdd:PRK15439 361 NVCALT-HNRRGF---WIK-PARENAvleRYRRALN-IKFNHAeqAARTL---SGGNQQKVLIAKCLEASPQLLIVDEPT 431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 167 TYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMTPGLLRTVFS 236
Cdd:PRK15439 432 RGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINVDTIMRLAFG 501
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-221 |
1.02e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.20 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSY----GTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLL------MPQSGTVFLGDNPINmlSSR 72
Cdd:PRK15134 6 LAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLpsppvvYPSGDIRFHGESLLH--ASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 73 QLARRL--------------SLLPQHHLTPEGITVqelvsygrnpwLSLwGRLSAEDNARVNVAMNQTRIN-HLAVRRLT 137
Cdd:PRK15134 84 QTLRGVrgnkiamifqepmvSLNPLHTLEKQLYEV-----------LSL-HRGMRREAARGEILNCLDRVGiRQAAKRLT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 138 ----ELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQ-GKTVVAVLHDLNQASRYCDQLVVMA 212
Cdd:PRK15134 152 dyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQ 231
|
....*....
gi 16132108 213 NGHVMAQGT 221
Cdd:PRK15134 232 NGRCVEQNR 240
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
16-225 |
1.75e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 71.66 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 16 KVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTV-FLGDNPINMLSSRQLARRLSLL-----PQHHLTPE 89
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVaWLGKDLLGMKDDEWRAVRSDIQmifqdPLASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 90 gITVQELVSygrNPWLSLWGRLSAED-NARVNVAMNQT-----RINhlavRRLTELSGGQRQRAFLAMVLAQNTPVVLLD 163
Cdd:PRK15079 115 -MTIGEIIA---EPLRTYHPKLSRQEvKDRVKAMMLKVgllpnLIN----RYPHEFSGGQCQRIGIARALILEPKLIICD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16132108 164 EPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:PRK15079 187 EPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
20-226 |
2.98e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 70.59 E-value: 2.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 20 DVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLL---PQHHLTPEGITVQEL 96
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIfqdPSTSLNPRQRISQIL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 97 vsygrNPWLSLWGRLSAEDNA-RVNVAMNQT--RINHlAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINH 173
Cdd:PRK15112 111 -----DFPLRLNTDLEPEQREkQIIETLRQVglLPDH-ASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSM 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16132108 174 QVDLMRLMGELR-TQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVM 226
Cdd:PRK15112 185 RSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| cyc_pep_trnsptr |
TIGR01194 |
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ... |
18-219 |
3.14e-14 |
|
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]
Pssm-ID: 130262 [Multi-domain] Cd Length: 555 Bit Score: 71.91 E-value: 3.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 18 LNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMlSSRQLARRL--SLLPQHHLTPEGITVQE 95
Cdd:TIGR01194 358 LGPIDLRIAQGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEILLDGAAVSA-DSRDDYRDLfsAIFADFHLFDDLIGPDE 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 96 lvsygrnpwlslwGRLSAEDNA-----RVNVAmNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLD 170
Cdd:TIGR01194 437 -------------GEHASLDNAqqylqRLEIA-DKVKIEDGGFSTTTALSTGQQKRLALICAWLEDRPILLFDEWAADQD 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16132108 171 IN-HQVDLMRLMGELRTQGKTVVAVLHDlNQASRYCDQLVVMANGHVMAQ 219
Cdd:TIGR01194 503 PAfKRFFYEELLPDLKRQGKTIIIISHD-DQYFELADQIIKLAAGCIVKD 551
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-171 |
3.68e-14 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 71.46 E-value: 3.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPinmlssrqlarRLSLLP 82
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENA-----------NIGYYA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 83 QHHLT--PEGITVQElvsygrnpWLSLW--------------GRL--SAED-NARVNVamnqtrinhlavrrlteLSGGQ 143
Cdd:PRK15064 389 QDHAYdfENDLTLFD--------WMSQWrqegddeqavrgtlGRLlfSQDDiKKSVKV-----------------LSGGE 443
|
170 180
....*....|....*....|....*...
gi 16132108 144 RQRAFLAMVLAQNTPVVLLDEPTTYLDI 171
Cdd:PRK15064 444 KGRMLFGKLMMQKPNVLVMDEPTNHMDM 471
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-214 |
4.81e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 71.16 E-value: 4.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 2 TLRTENLTVSYGTDKV-LNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMlSSRQLARRL-- 78
Cdd:PRK10522 322 TLELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA-EQPEDYRKLfs 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 79 -----SLLPQHHLTPEGITVQ-ELVsygrNPWLSLWG---RLSAEDNARVNvamnqtrinhlavrrlTELSGGQRQRAFL 149
Cdd:PRK10522 401 avftdFHLFDQLLGPEGKPANpALV----EKWLERLKmahKLELEDGRISN----------------LKLSKGQKKRLAL 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16132108 150 AMVLAQNTPVVLLDEPTTYLD-----INHQVdlmrLMGELRTQGKTVVAVLHD---LNQAsrycDQLVVMANG 214
Cdd:PRK10522 461 LLALAEERDILLLDEWAADQDphfrrEFYQV----LLPLLQEMGKTIFAISHDdhyFIHA----DRLLEMRNG 525
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
32-216 |
7.66e-14 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 70.66 E-value: 7.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 32 ALIGPNGCGKSTLLNCFSRLLMPQSGTVFlgdnpinmlssRQLARRLSLLPQHHLtpEGItvqELVSygrNPWLSLWGRL 111
Cdd:PLN03073 539 AMVGPNGIGKSTILKLISGELQPSSGTVF-----------RSAKVRMAVFSQHHV--DGL---DLSS---NPLLYMMRCF 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 112 SAEDNARVNVAMNQTRIN-HLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRlmGELRTQGKt 190
Cdd:PLN03073 600 PGVPEQKLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQ--GLVLFQGG- 676
|
170 180
....*....|....*....|....*.
gi 16132108 191 VVAVLHDLNQASRYCDQLVVMANGHV 216
Cdd:PLN03073 677 VLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-227 |
8.10e-14 |
|
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: 70.62 E-value: 8.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLlMPQ---SGTVFLGDNPINMLSSRQLARR-L 78
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIYWSGSPLKASNIRDTERAgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 79 SLLPQHHLTPEGITVQELVSYGRNpwLSLWGRLSAEDNA--RVNVAMNQTRINHLAV-RRLTELSGGQRQRAFLAMVLAQ 155
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNE--ITLPGGRMAYNAMylRAKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16132108 156 NTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQgTPEEVMT 227
Cdd:TIGR02633 159 QARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVAT-KDMSTMS 229
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-196 |
9.03e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 70.22 E-value: 9.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 2 TLRTENLTVSYGTDKVL-NDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNpinmlssrqlaRRLSL 80
Cdd:COG4178 362 ALALEDLTLRTPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAG-----------ARVLF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 81 LPQHHLTPEGiTVQELVSYGRNPwlslwgrlSAEDNARVNVAMNQTRINHLAvRRLTE-------LSGGQRQR-AFlAMV 152
Cdd:COG4178 431 LPQRPYLPLG-TLREALLYPATA--------EAFSDAELREALEAVGLGHLA-ERLDEeadwdqvLSLGEQQRlAF-ARL 499
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 16132108 153 LAQNTPVVLLDEPTTYLDINHQVDLMRLMGElRTQGKTVVAVLH 196
Cdd:COG4178 500 LLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
7-226 |
9.69e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.20 E-value: 9.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 7 NLTvSYGTDKVlNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLS--------------SR 72
Cdd:PRK09700 270 NVT-SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpldavkkgmayiteSR 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 73 qlaRRLSLLPQHHLTpEGITVQELVSYGRnpWLSLWGRLSAEDNARVnvAMNQTRINHLAV----RRLTELSGGQRQRAF 148
Cdd:PRK09700 348 ---RDNGFFPNFSIA-QNMAISRSLKDGG--YKGAMGLFHEVDEQRT--AENQRELLALKChsvnQNITELSGGNQQKVL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 149 LAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHV------MAQGTP 222
Cdd:PRK09700 420 ISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLtqiltnRDDMSE 499
|
....
gi 16132108 223 EEVM 226
Cdd:PRK09700 500 EEIM 503
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
6-214 |
1.08e-13 |
|
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: 67.65 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLT----VSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFS--RLLMPQSGTVFLGDNPINMlssrQLARRLS 79
Cdd:cd03232 7 KNLNytvpVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrKTAGVITGEILINGRPLDK----NFQRSTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 80 LLPQHHLTPEGITVQElvsygrnpwlSLwgRLSAednarvnvamnqtrinhlavrRLTELSGGQRQRAFLAMVLAQNTPV 159
Cdd:cd03232 83 YVEQQDVHSPNLTVRE----------AL--RFSA---------------------LLRGLSVEQRKRLTIGVELAAKPSI 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16132108 160 VLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHdlnQAS----RYCDQLVVMANG 214
Cdd:cd03232 130 LFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIH---QPSasifEKFDRLLLLKRG 185
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-227 |
1.30e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.96 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLlMPQ---SGTVFLGDNPINMLSSRQLARR-- 77
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQASNIRDTERAgi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 78 ------LSLLPQhhLT-PEGITV-QELVSYGRNPWLSLWGRlSAEDNARVNVAMNqtrinhlAVRRLTELSGGQRQRAFL 149
Cdd:PRK13549 85 aiihqeLALVKE--LSvLENIFLgNEITPGGIMDYDAMYLR-AQKLLAQLKLDIN-------PATPVGNLGLGQQQLVEI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 150 AMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANG-HV----MAQGTPEE 224
Cdd:PRK13549 155 AKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGrHIgtrpAAGMTEDD 234
|
...
gi 16132108 225 VMT 227
Cdd:PRK13549 235 IIT 237
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
17-226 |
1.30e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 69.91 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 17 VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQS--GTVFLGDNPInmlsSRQLARRLSLLPQHHLTPEGITVQ 94
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKP----TKQILKRTGFVTQDDILYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 95 E---LVSYGRNP-WLSLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLD 170
Cdd:PLN03211 159 EtlvFCSLLRLPkSLTKQEKILVAESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16132108 171 INHQVDLMRLMGELRTQGKTVVAVLHdlNQASR---YCDQLVVMANGHVMAQGTPEEVM 226
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQKGKTIVTSMH--QPSSRvyqMFDSVLVLSEGRCLFFGKGSDAM 295
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-220 |
1.76e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.50 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 20 DVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLA---RRLSLL---PQHHLTPegitv 93
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQalrRDIQFIfqdPYASLDP----- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 94 QELVSYGRNPWLSLWGRLSAEDnARVNVAMNQTRINHL---AVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLD 170
Cdd:PRK10261 417 RQTVGDSIMEPLRVHGLLPGKA-AAARVAWLLERVGLLpehAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16132108 171 INHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQG 220
Cdd:PRK10261 496 VSIRGQIINLLLDLqRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
6-214 |
7.51e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.45 E-value: 7.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQ-LARRLSLLPQH 84
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 85 HLTPEGITVQELVSYGRNPW--------------LSLWGRLSAEDNARVNVAmnqtrinhlavrrltELSGGQRQRAFLA 150
Cdd:PRK10982 82 LNLVLQRSVMDNMWLGRYPTkgmfvdqdkmyrdtKAIFDELDIDIDPRAKVA---------------TLSVSQMQMIEIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16132108 151 MVLAQNTPVVLLDEPTTYL---DINHqvdLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANG 214
Cdd:PRK10982 147 KAFSYNAKIVIMDEPTSSLtekEVNH---LFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1-244 |
8.81e-13 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 67.66 E-value: 8.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 1 MTLRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCF---------------SRLLMPQSGTV------ 59
Cdd:TIGR00957 637 ITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALlaemdkveghvhmkgSVAYVPQQAWIqndslr 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 60 --FLGDNPINMLSSRQLARRLSLLPQHHLTPEGitvqelvsygrnpwlslwgrlsaednarvnvamNQTRINHLAVrrlt 137
Cdd:TIGR00957 717 enILFGKALNEKYYQQVLEACALLPDLEILPSG---------------------------------DRTEIGEKGV---- 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 138 ELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDIN---HQVD-LMRLMGELRtqGKTVVAVLHDLNQASRyCDQLVVMAN 213
Cdd:TIGR00957 760 NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvgkHIFEhVIGPEGVLK--NKTRILVTHGISYLPQ-VDVIIVMSG 836
|
250 260 270
....*....|....*....|....*....|....*.
gi 16132108 214 GHVMAQGTPEEVMT-----PGLLRTVFSVEAEIHPE 244
Cdd:TIGR00957 837 GKISEMGSYQELLQrdgafAEFLRTYAPDEQQGHLE 872
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
16-198 |
9.19e-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: 67.50 E-value: 9.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 16 KVLNDVSLSLPTGKI-----TALIGPNGCGKSTllncFSRLLM----PQSGTVFLGDnpinmlssrqlarRLSLLPQHhL 86
Cdd:COG1245 349 KSYGGFSLEVEGGEIregevLGIVGPNGIGKTT----FAKILAgvlkPDEGEVDEDL-------------KISYKPQY-I 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 87 TPE-GITVQELvsygrnpwlslwgrLSAEDNARVNVAMNQT------RINHLAVRRLTELSGGQRQRAFLAMVLAQNTPV 159
Cdd:COG1245 411 SPDyDGTVEEF--------------LRSANTDDFGSSYYKTeiikplGLEKLLDKNVKDLSGGELQRVAIAACLSRDADL 476
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 16132108 160 VLLDEPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDL 198
Cdd:COG1245 477 YLLDEPSAHLDVEQRLAVAKAIRRFaENRGKTAMVVDHDI 516
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
18-220 |
1.05e-12 |
|
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: 64.65 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 18 LNDVSLSLPTGKITALIGPNGCGKSTLLNcfsrllmpqsgtvflgdnpiNMLSSRQLARRLSLLPqhhltpegitvqelv 97
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN--------------------EGLYASGKARLISFLP--------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 98 SYGRNPWLSLwGRLSAednaRVNVAMNQTRINhlavRRLTELSGGQRQRAFLAMVLAQNTP--VVLLDEPTTYLdinHQV 175
Cdd:cd03238 56 KFSRNKLIFI-DQLQF----LIDVGLGYLTLG----QKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGL---HQQ 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 16132108 176 DLMRLMGELRT---QGKTVVAVLHDLnQASRYCDQLVVMA------NGHVMAQG 220
Cdd:cd03238 124 DINQLLEVIKGlidLGNTVILIEHNL-DVLSSADWIIDFGpgsgksGGKVVFSG 176
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
16-233 |
1.21e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.86 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 16 KVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLPQHHLTPEGI---- 91
Cdd:PRK11288 267 GLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCPEDRKAEGIipvh 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 92 TVQELVSYGRNPWLSLWGRLSaedNARVNVAMNQTRINHLAVR------RLTELSGGQRQRAFLAMVLAQNTPVVLLDEP 165
Cdd:PRK11288 347 SVADNINISARRHHLRAGCLI---NNRWEAENADRFIRSLNIKtpsreqLIMNLSGGNQQKAILGRWLSEDMKVILLDEP 423
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16132108 166 TTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVM-----AQGTPEEVMTPGLLRT 233
Cdd:PRK11288 424 TRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAgelarEQATERQALSLALPRT 496
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
7-226 |
2.74e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 66.12 E-value: 2.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 7 NLTVSY--GTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLPQH 84
Cdd:TIGR00957 1289 NYCLRYreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQD 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 85 HLTPEGITVQELVSYGRNPWLSLWGRLSAEdNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDE 164
Cdd:TIGR00957 1369 PVLFSGSLRMNLDPFSQYSDEEVWWALELA-HLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDE 1447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16132108 165 PTTYLDINHQvDLMRlmGELRTQGK--TVVAVLHDLNQASRYCdQLVVMANGHVMAQGTPEEVM 226
Cdd:TIGR00957 1448 ATAAVDLETD-NLIQ--STIRTQFEdcTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLL 1507
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-227 |
3.20e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.15 E-value: 3.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 2 TLRTENLTVSY--GTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLS 79
Cdd:PLN03232 1234 SIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLS 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 80 LLPQHHLTPEGITVQELVSYGRNPWLSLWGRLSAEDNARVnVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPV 159
Cdd:PLN03232 1314 IIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDV-IDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKI 1392
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16132108 160 VLLDEPTTYLDINHQVDLMRLMGElRTQGKTVVAVLHDLNQASRyCDQLVVMANGHVMAQGTPEEVMT 227
Cdd:PLN03232 1393 LVLDEATASVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLS 1458
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-198 |
4.05e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.60 E-value: 4.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 28 GKITALIGPNGCGKSTllncFSRLLM----PQSGTVFLgdnpinmlssrqlARRLSLLPQHHLTPEGITVQELVS----- 98
Cdd:PRK13409 365 GEVIGIVGPNGIGKTT----FAKLLAgvlkPDEGEVDP-------------ELKISYKPQYIKPDYDGTVEDLLRsitdd 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 99 YGRNPWLSLwgrlsaednarvnvAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLM 178
Cdd:PRK13409 428 LGSSYYKSE--------------IIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVA 493
|
170 180
....*....|....*....|.
gi 16132108 179 RLMGEL-RTQGKTVVAVLHDL 198
Cdd:PRK13409 494 KAIRRIaEEREATALVVDHDI 514
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-225 |
4.57e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 65.26 E-value: 4.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDK----VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGdnpiNMLSSRQLARRL 78
Cdd:PRK10261 13 LAVENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCD----KMLLRRRSRQVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 79 SLLPQHHLTPEGITVQELVSYGRNPWLSL-----------------WGRLSAEDNARVNVAMNQTRI---NHLAVRRLTE 138
Cdd:PRK10261 89 ELSEQSAAQMRHVRGADMAMIFQEPMTSLnpvftvgeqiaesirlhQGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 139 LSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQ-GKTVVAVLHDLNQASRYCDQLVVMANGHVM 217
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
....*...
gi 16132108 218 AQGTPEEV 225
Cdd:PRK10261 249 ETGSVEQI 256
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-226 |
4.78e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.53 E-value: 4.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPI--NMLSSRqlaRRL----- 78
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdaGDIATR---RRVgymsq 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 79 --SLLpqhhltpEGITVQElvsygrNpwLSLWGRL----SAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMV 152
Cdd:NF033858 347 afSLY-------GELTVRQ------N--LELHARLfhlpAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVA 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 153 LAQNTPVVLLDEPTTyldinhQVD------LMRLMGEL-RTQGKTVVAVLHDLNQASRyCDQLVVMANGHVMAQGTPEEV 225
Cdd:NF033858 412 VIHKPELLILDEPTS------GVDpvardmFWRLLIELsREDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAAL 484
|
.
gi 16132108 226 M 226
Cdd:NF033858 485 V 485
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-204 |
6.03e-12 |
|
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: 64.96 E-value: 6.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 7 NLTVSYGTDK-VLNDVSLS-LPTGKItALIGPNGCGKSTLLNcfsrlLMPQSGTVFLGDnpinmlSSRQLARRLSLLPQH 84
Cdd:TIGR03719 9 RVSKVVPPKKeILKDISLSfFPGAKI-GVLGLNGAGKSTLLR-----IMAGVDKDFNGE------ARPQPGIKVGYLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 85 -HLTPEgITVQELVSYGRNPWLSLWGRLS------AEDNARVNVAMN-----QTRINHL--------------AVR---- 134
Cdd:TIGR03719 77 pQLDPT-KTVRENVEEGVAEIKDALDRFNeisakyAEPDADFDKLAAeqaelQEIIDAAdawdldsqleiamdALRcppw 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16132108 135 --RLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELrtQGkTVVAVLHDlnqasRY 204
Cdd:TIGR03719 156 daDVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY--PG-TVVAVTHD-----RY 219
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
3-202 |
9.38e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.51 E-value: 9.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSrqlARRLSLLP 82
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD---EYHQDLLY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 83 QHHLTpeGI----TVQELVSYgrnpWLSLWGRLSAEDNARVNVAMNQTRINHLAVRRlteLSGGQRQRAFLAMVLAQNTP 158
Cdd:PRK13538 79 LGHQP--GIktelTALENLRF----YQRLHGPGDDEALWEALAQVGLAGFEDVPVRQ---LSAGQQRRVALARLWLTRAP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 16132108 159 VVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLH-DLNQAS 202
Cdd:PRK13538 150 LWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHqDLPVAS 194
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
18-227 |
1.04e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 64.14 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 18 LNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLPQHHLTP--EGIT--- 92
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGIENIELKGlmMGLTkek 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 93 VQELVSygrnpwlslwgrlSAEDNARVNVAMNQTrinhlavrrLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDIN 172
Cdd:PRK13545 120 IKEIIP-------------EIIEFADIGKFIYQP---------VKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 16132108 173 HQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMT 227
Cdd:PRK13545 178 FTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVD 232
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
6-196 |
1.13e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.28 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSYGTDK--VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLL--MPQSGTVFLGDNPINmlssrqlaRRLSLL 81
Cdd:COG2401 32 EAFGVELRVVEryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFG--------REASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 82 pqHHLTPEGITVQELvsygrnpwlslwGRLSAednarvnVAMNQtriNHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVL 161
Cdd:COG2401 104 --DAIGRKGDFKDAV------------ELLNA-------VGLSD---AVLWLRRFKELSTGQKFRFRLALLLAERPKLLV 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 16132108 162 LDEPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLH 196
Cdd:COG2401 160 IDEFCSHLDRQTAKRVARNLQKLaRRAGITLVVATH 195
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
19-204 |
1.30e-11 |
|
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: 61.22 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 19 NDVSLSLPtgKITALIGPNGCGKSTLLNCFS-RLLMPQSGTVFLGDNPINMLSSRQLARRLSLLPQhhltpegitvqelv 97
Cdd:cd03227 14 NDVTFGEG--SLTIITGPNGSGKSTILDAIGlALGGAQSATRRRSGVKAGCIVAAVSAELIFTRLQ-------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 98 sygrnpwlslwgrlsaednarvnvamnqtrinhlavrrlteLSGGQRQRAFLAMVLA----QNTPVVLLDEPTTYLDINH 173
Cdd:cd03227 78 -----------------------------------------LSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRD 116
|
170 180 190
....*....|....*....|....*....|.
gi 16132108 174 QVDLMRLMGELRTQGKTVVAVLHDLNQASRY 204
Cdd:cd03227 117 GQALAEAILEHLVKGAQVIVITHLPELAELA 147
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
134-226 |
2.06e-11 |
|
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: 63.49 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 134 RRLTELSGGQRQRAFLAMVLAQNTPVVL--LDEPTTYLdinHQVDLMRLMG---ELRTQGKTVVAVLHDlNQASRYCDQL 208
Cdd:TIGR00630 484 RAAGTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGL---HQRDNRRLINtlkRLRDLGNTLIVVEHD-EDTIRAADYV 559
|
90 100
....*....|....*....|....
gi 16132108 209 VVMA------NGHVMAQGTPEEVM 226
Cdd:TIGR00630 560 IDIGpgagehGGEVVASGTPEEIL 583
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-248 |
2.14e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 63.19 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 17 VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLPQhhlTPE--GITVQ 94
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQ---TPFlfSDTVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 95 ELVSYGRnPWLSlwgRLSAEDNARV-NVamnqtrinHLAVRRL-----TE-------LSGGQRQRAFLAMVLAQNTPVVL 161
Cdd:PRK10789 407 NNIALGR-PDAT---QQEIEHVARLaSV--------HDDILRLpqgydTEvgergvmLSGGQKQRISIARALLLNAEILI 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 162 LDEPTTYLD--INHQVdlmrlMGELRT--QGKTVVAVLHDLNqASRYCDQLVVMANGHVMAQGTPEE-VMTPGLLRTVF- 235
Cdd:PRK10789 475 LDDALSAVDgrTEHQI-----LHNLRQwgEGRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQlAQQSGWYRDMYr 548
|
250
....*....|....*
gi 16132108 236 --SVEAEIHPEPVSG 248
Cdd:PRK10789 549 yqQLEAALDDAPEIR 563
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
16-221 |
2.30e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 63.71 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 16 KVLNDVSLSLPTGKITALIGPNGCGKSTLLNCfsrLLMPQSGTVFLGDNPINMLSSRQ--LARRLSLLPQHHLTPEGITV 93
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDV---LAGRKTGGYIEGDIRISGFPKKQetFARISGYCEQNDIHSPQVTV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 94 QELVSYgrNPWLSLWGRLSAEDNAR-VNVAMNQTRINHL--AVRRL---TELSGGQRQRAFLAMVLAQNTPVVLLDEPTT 167
Cdd:PLN03140 971 RESLIY--SAFLRLPKEVSKEEKMMfVDEVMELVELDNLkdAIVGLpgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTS 1048
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16132108 168 YLDINHQVDLMRLMGELRTQGKTVVAVLH----DLNQAsryCDQLVVMA-NGHVMAQGT 221
Cdd:PLN03140 1049 GLDARAAAIVMRTVRNTVDTGRTVVCTIHqpsiDIFEA---FDELLLMKrGGQVIYSGP 1104
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
14-231 |
2.58e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.46 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 14 TDKVLNDVSLSLPTGKITALIGPNGCGKSTLLncfsrllmpqsgTVFLGDNPINMLSSRQLARRLSLLPQHHLTPEGiTV 93
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLI------------SAMLGELSHAETSSVVIRGSVAYVPQVSWIFNA-TV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 94 QELVSYGRNPWLSLWGRlsaednaRVNVAMNQTRINHLAVRRLTEL-------SGGQRQRAFLAMVLAQNTPVVLLDEPT 166
Cdd:PLN03232 696 RENILFGSDFESERYWR-------AIDVTALQHDLDLLPGRDLTEIgergvniSGGQKQRVSMARAVYSNSDIYIFDDPL 768
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 167 TYLD--INHQVDLMRLMGELrtQGKTVVAV---LHDLNQAsrycDQLVVMANGHVMAQGTPEEVMTPGLL 231
Cdd:PLN03232 769 SALDahVAHQVFDSCMKDEL--KGKTRVLVtnqLHFLPLM----DRIILVSEGMIKEEGTFAELSKSGSL 832
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1-216 |
5.27e-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: 61.41 E-value: 5.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 1 MTLRteNLTVSY--GTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQsGTVFLGDNPINMLSSRQLARRL 78
Cdd:cd03289 3 MTVK--DLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 79 SLLPQHHLTPEGITVQELVSYGRNPWLSLWgRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTP 158
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIW-KVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 16132108 159 VVLLDEPTTYLD-INHQVdlMRLMGELRTQGKTVVAVLHDLnQASRYCDQLVVMANGHV 216
Cdd:cd03289 159 ILLLDEPSAHLDpITYQV--IRKTLKQAFADCTVILSEHRI-EAMLECQRFLVIEENKV 214
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
7-205 |
6.64e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.96 E-value: 6.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 7 NLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTV-FLGDNPINMLSSRQlaRRLSLLpqHH 85
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEIlFERQSIKKDLCTYQ--KQLCFV--GH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 86 LTpegitvqelvsyGRNPWLSL-----WGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVV 160
Cdd:PRK13540 82 RS------------GINPYLTLrenclYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLW 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16132108 161 LLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHD---LNQA--SRYC 205
Cdd:PRK13540 150 LLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQdlpLNKAdyEEYH 199
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-240 |
6.98e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 62.10 E-value: 6.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 16 KVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLgdnpinmlssrqlARRLSLLPQHhltpegitvqe 95
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA-------------ERSIAYVPQQ----------- 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 96 lvsygrnPWL---SLWGRL---SAEDNAR----VNVAMNQTRINHLAVRRLTE-------LSGGQRQRAFLAMVLAQNTP 158
Cdd:PTZ00243 730 -------AWImnaTVRGNIlffDEEDAARladaVRVSQLEADLAQLGGGLETEigekgvnLSGGQKARVSLARAVYANRD 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 159 VVLLDEPTTYLD--INHQVDLMRLMGELRtqGKTVVAVLHDLNQASRyCDQLVVMANGHVMAQGTPEEVMTPGLLRTVFS 236
Cdd:PTZ00243 803 VYLLDDPLSALDahVGERVVEECFLGALA--GKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFMRTSLYATLAA 879
|
....
gi 16132108 237 VEAE 240
Cdd:PTZ00243 880 ELKE 883
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-225 |
7.72e-11 |
|
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: 61.74 E-value: 7.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRL--LMPQSGTV-----------------FLGD 63
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpsKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 64 N-PI--NMLSS-------------RQLARRLSLLPQHHLtpegitvqelvsygrnpwlSLWGrlsaEDNARVNV--AMNQ 125
Cdd:TIGR03269 81 PcPVcgGTLEPeevdfwnlsdklrRRIRKRIAIMLQRTF-------------------ALYG----DDTVLDNVleALEE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 126 T----------------------RINHLAvrrlTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLD-----INHQVdlm 178
Cdd:TIGR03269 138 IgyegkeavgravdliemvqlshRITHIA----RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpqtakLVHNA--- 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 16132108 179 rLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEV 225
Cdd:TIGR03269 211 -LEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
30-197 |
8.28e-11 |
|
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: 59.54 E-value: 8.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 30 ITALIGPNGCGKSTLLNCfsrLLMPQSGTVFLGDNPINMLssRQLARRLSLLPQHHLTPEGITVQELVSYgRNPwlslwg 109
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEA---LKYALTGELPPNSKGGAHD--PKLIREGEVRAQVKLAFENANGKKYTIT-RSL------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 110 rlsaedNARVNVAM-NQTRINHLAVRRLTELSGGQRQ------RAFLAMVLAQNTPVVLLDEPTTYLD---INHQ-VDLM 178
Cdd:cd03240 92 ------AILENVIFcHQGESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDeenIEESlAEII 165
|
170
....*....|....*....
gi 16132108 179 RLMGELRtqGKTVVAVLHD 197
Cdd:cd03240 166 EERKSQK--NFQLIVITHD 182
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-231 |
9.42e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 61.68 E-value: 9.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 18 LNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLgdnpinmlssrqLARRLSLLPQHHLTPEGiTVQELV 97
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVAYVPQVSWIFNA-TVRDNI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 98 SYGrnpwlslwgrlSAEDNARVNVAMNQTRINH----LAVRRLTE-------LSGGQRQRAFLAMVLAQNTPVVLLDEPT 166
Cdd:PLN03130 700 LFG-----------SPFDPERYERAIDVTALQHdldlLPGGDLTEigergvnISGGQKQRVSMARAVYSNSDVYIFDDPL 768
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 167 TYLD--INHQVDLMRLMGELRtqGKTVVAV---LHDLNQAsrycDQLVVMANGHVMAQGTPEEVMTPGLL 231
Cdd:PLN03130 769 SALDahVGRQVFDKCIKDELR--GKTRVLVtnqLHFLSQV----DRIILVHEGMIKEEGTYEELSNNGPL 832
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
3-196 |
1.00e-10 |
|
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: 58.70 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVL-NDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTvflgdnpINMLSSRQLArrlsLL 81
Cdd:cd03223 1 IELENLSLATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGR-------IGMPEGEDLL----FL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 82 PQHHLTPEGiTVQELVSYgrnPWLSlwgrlsaednarvnvamnqtrinhlavrrltELSGGQRQRAFLAMVLAQNTPVVL 161
Cdd:cd03223 70 PQRPYLPLG-TLREQLIY---PWDD-------------------------------VLSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190
....*....|....*....|....*....|....*
gi 16132108 162 LDEPTTYLDINHQVDLMRLmgeLRTQGKTVVAVLH 196
Cdd:cd03223 115 LDEATSALDEESEDRLYQL---LKELGITVISVGH 146
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-197 |
1.10e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.12 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDnpinmlssrQLarRLSLLPQHH 85
Cdd:PRK11147 323 ENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGT---------KL--EVAYFDQHR 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 86 --LTPEGiTVQELVSYGRNpwlslwgrlsaednarvNVAMN-QTRinHL-------------AVRRLTELSGGQRQRAFL 149
Cdd:PRK11147 392 aeLDPEK-TVMDNLAEGKQ-----------------EVMVNgRPR--HVlgylqdflfhpkrAMTPVKALSGGERNRLLL 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 16132108 150 AMVLAQNTPVVLLDEPTTYLDInhqvDLMRLMGELRT--QGkTVVAVLHD 197
Cdd:PRK11147 452 ARLFLKPSNLLILDEPTNDLDV----ETLELLEELLDsyQG-TVLLVSHD 496
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-197 |
1.10e-10 |
|
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: 58.15 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 27 TGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLgdnpinmlssrqlarrlsllpqhhltpegitvqelvsygrnpwls 106
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------------------------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 107 lwgrLSAEDNARVNVamnQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMR------L 180
Cdd:smart00382 36 ----IDGEDILEEVL---DQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrlL 108
|
170
....*....|....*..
gi 16132108 181 MGELRTQGKTVVAVLHD 197
Cdd:smart00382 109 LLLKSEKNLTVILTTND 125
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-204 |
1.70e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.52 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 7 NLTVSYGTDK-VLNDVSLS-LPTGKItALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNpinmlssrqlaRRLSLLPQH 84
Cdd:PRK11819 11 RVSKVVPPKKqILKDISLSfFPGAKI-GVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPG-----------IKVGYLPQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 85 -HLTPEgITVQELVSYGRNPWLSLWGRLS------AEDNARVNVAMN-----QTRINHL--------------AVR---- 134
Cdd:PRK11819 79 pQLDPE-KTVRENVEEGVAEVKAALDRFNeiyaayAEPDADFDALAAeqgelQEIIDAAdawdldsqleiamdALRcppw 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16132108 135 --RLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDI-------NHqvdLMRLMGelrtqgkTVVAVLHDlnqasRY 204
Cdd:PRK11819 158 daKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAesvawleQF---LHDYPG-------TVVAVTHD-----RY 221
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-216 |
2.20e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 60.18 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDnpinmlssrqlARRLSLLP 82
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAK-----------GIKLGYFA 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 83 QHHLtpegitvqELVSYGRNPwLSLWGRLSAEDnarvnvaMNQTRINHLA--------VRRLTE-LSGGQRQRAFLAMVL 153
Cdd:PRK10636 382 QHQL--------EFLRADESP-LQHLARLAPQE-------LEQKLRDYLGgfgfqgdkVTEETRrFSGGEKARLVLALIV 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16132108 154 AQNTPVVLLDEPTTYLDINHQVDLMRLMGELrtQGKTVVaVLHDLNQASRYCDQLVVMANGHV 216
Cdd:PRK10636 446 WQRPNLLLLDEPTNHLDLDMRQALTEALIDF--EGALVV-VSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
6-175 |
2.86e-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: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSYGTD--KVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQsGTVFLGDNPINMLSSRQLARRLSLLPQ 83
Cdd:TIGR01271 1221 QGLTAKYTEAgrAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQ 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 84 HHLTPEGITVQELVSYGRNPWLSLWgRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLD 163
Cdd:TIGR01271 1300 KVFIFSGTFRKNLDPYEQWSDEEIW-KVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLD 1378
|
170
....*....|...
gi 16132108 164 EPTTYLD-INHQV 175
Cdd:TIGR01271 1379 EPSAHLDpVTLQI 1391
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
138-232 |
3.10e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 59.37 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 138 ELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANGHV 216
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
90 100
....*....|....*....|...
gi 16132108 217 MAQGTPEEVM-------TPGLLR 232
Cdd:PRK11022 233 VETGKAHDIFraprhpyTQALLR 255
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-214 |
4.91e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.03 E-value: 4.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRlLMPQ---SGTVFLGDNPINMLSSRQLARR-- 77
Cdd:NF040905 2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDGEVCRFKDIRDSEALgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 78 ------LSLLPQHHLTpEGITV-QELVSYGRNPWLSLWGRlSAEDNARVNVAMN-QTRINHLAVrrltelsgGQRQRAFL 149
Cdd:NF040905 81 viihqeLALIPYLSIA-ENIFLgNERAKRGVIDWNETNRR-ARELLAKVGLDESpDTLVTDIGV--------GKQQLVEI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16132108 150 AMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANG 214
Cdd:NF040905 151 AKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDG 215
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
18-192 |
5.79e-10 |
|
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: 58.86 E-value: 5.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 18 LNDVSLSLPTGkITALIGPNGCGKSTLLNCFSRLLMPQSGTVF------LGDNP----------INMLSSRQLARRLSLL 81
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSRKFdeedfyLGDDPdlpeieieltFGSLLSRLLRLLLKEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 82 PQHHLTPEGITVQELVSYGRNPWLSL----WGRLSAEDNARVNVAMNQT---------RINHLAVRRLTELSGGQRQRAF 148
Cdd:COG3593 93 DKEELEEALEELNEELKEALKALNELlseyLKELLDGLDLELELSLDELedllkslslRIEDGKELPLDRLGSGFQRLIL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16132108 149 LAMVLA-------QNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVV 192
Cdd:COG3593 173 LALLSAlaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVI 223
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-221 |
6.84e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 59.26 E-value: 6.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSY-GTDK-VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPInMLSSRQLARRLSL 80
Cdd:TIGR01257 1938 LRLNELTKVYsGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISDVHQNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 81 LPQHHLTPEGITVQE-LVSYGRnpwlsLWGRLSAEDNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPV 159
Cdd:TIGR01257 2017 CPQFDAIDDLLTGREhLYLYAR-----LRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPL 2091
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16132108 160 VLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGT 221
Cdd:TIGR01257 2092 VLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGT 2153
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
136-225 |
2.02e-09 |
|
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: 57.72 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 136 LTELSGGQRQRAFLAMVL---AQNTPVVLLDEPTTYL---DINHqvdLMRLMGELRTQGKTVVAVLHDLN---QAsrycD 206
Cdd:TIGR00630 827 ATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLhfdDIKK---LLEVLQRLVDKGNTVVVIEHNLDvikTA----D 899
|
90 100
....*....|....*....|....*
gi 16132108 207 QLVVM------ANGHVMAQGTPEEV 225
Cdd:TIGR00630 900 YIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
3-227 |
2.17e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 56.73 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTD----KVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRL----LMPQSGTVFLGDNPINMLSSRQ- 73
Cdd:PRK15093 4 LDIRNLTIEFKTSdgwvKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSPREr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 74 ---LARRLSLL---PQHHLTPEGITVQELV------SYGRNPWLSLWGRL--SAEDNARVNVAmnqtriNHLAVRRL--T 137
Cdd:PRK15093 84 rklVGHNVSMIfqePQSCLDPSERVGRQLMqnipgwTYKGRWWQRFGWRKrrAIELLHRVGIK------DHKDAMRSfpY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 138 ELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRYCDQLVVMANGHV 216
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQT 237
|
250
....*....|.
gi 16132108 217 MAQGTPEEVMT 227
Cdd:PRK15093 238 VETAPSKELVT 248
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
17-214 |
2.62e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 55.94 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 17 VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQ----LARRLSLLPQHHLTPEGIT 92
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEAraklRAKHVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 93 VQELVSYgrnPWLsLWGRLSAEDNARVNVAMNQ----TRINHLAvrrlTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTY 168
Cdd:PRK10584 105 ALENVEL---PAL-LRGESSRQSRNGAKALLEQlglgKRLDHLP----AQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16132108 169 LDINHQVDLMRLMGEL-RTQGKTVVAVLHDLNQASRyCDQLVVMANG 214
Cdd:PRK10584 177 LDRQTGDKIADLLFSLnREHGTTLILVTHDLQLAAR-CDRRLRLVNG 222
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
136-222 |
2.68e-09 |
|
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: 56.08 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 136 LTELSGGQRQRAFLAMVLAQNTP---VVLLDEPTTYL---DINHqvdLMRLMGELRTQGKTVVAVLHDLNQAsRYCDQLV 209
Cdd:cd03271 167 ATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLhfhDVKK---LLEVLQRLVDKGNTVVVIEHNLDVI-KCADWII 242
|
90
....*....|....*....
gi 16132108 210 VM------ANGHVMAQGTP 222
Cdd:cd03271 243 DLgpeggdGGGQVVASGTP 261
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
6-213 |
2.73e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.35 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 6 ENLTVSYGTDK---VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDN----PINMLSSRQLARRL 78
Cdd:PTZ00265 386 KNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkDINLKWWRSKIGVV 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 79 SLLP------------------------QHHLTPEGITVQELVSYGRNPWLSLWGRLSAEDNARVNVAMNQTRINH---- 130
Cdd:PTZ00265 466 SQDPllfsnsiknnikyslyslkdlealSNYYNEDGNDSQENKNKRNSCRAKCAGDLNDMSNTTDSNELIEMRKNYqtik 545
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 131 --------------------------LAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGEL 184
Cdd:PTZ00265 546 dsevvdvskkvlihdfvsalpdkyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL 625
|
250 260 270
....*....|....*....|....*....|
gi 16132108 185 R-TQGKTVVAVLHDLNQAsRYCDQLVVMAN 213
Cdd:PTZ00265 626 KgNENRITIIIAHRLSTI-RYANTIFVLSN 654
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-228 |
3.12e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.10 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 17 VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLPQHHLTPEGiTVQEL 96
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDG-TVRQN 1403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 97 VsygrNPWL-----SLWGRLSAEdNARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLA-MVLAQNTPVVLLDEPTTylD 170
Cdd:PTZ00243 1404 V----DPFLeassaEVWAALELV-GLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMArALLKKGSGFILMDEATA--N 1476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16132108 171 INHQVDlMRLMGELRT--QGKTVVAVLHDLNQASRYcDQLVVMANGHVMAQGTPEE-VMTP 228
Cdd:PTZ00243 1477 IDPALD-RQIQATVMSafSAYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRElVMNR 1535
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
4-196 |
3.17e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.04 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 4 RTENLTVSYGTDK--VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFS-RLLMpqsGTVFLGDNPIN---MLSSRQlaRR 77
Cdd:TIGR00956 763 RNLTYEVKIKKEKrvILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAeRVTT---GVITGGDRLVNgrpLDSSFQ--RS 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 78 LSLLPQHHLTPEGITVQELVSYgrnpwlSLWGRLSA-----EDNARVNVAMNQTRINHLA---VRRLTE-LSGGQRQRAF 148
Cdd:TIGR00956 838 IGYVQQQDLHLPTSTVRESLRF------SAYLRQPKsvsksEKMEYVEEVIKLLEMESYAdavVGVPGEgLNVEQRKRLT 911
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 16132108 149 LAMVLAQNTP-VVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLH 196
Cdd:TIGR00956 912 IGVELVAKPKlLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
137-226 |
5.27e-09 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 56.19 E-value: 5.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 137 TELSGGQRQRAFLAMVLAQ----NTpVVLLDEPTTYL---DINHqvdLMRLMGELRTQGKTVVAVLHDLnqasrycDqlv 209
Cdd:COG0178 825 TTLSGGEAQRVKLASELSKrstgKT-LYILDEPTTGLhfhDIRK---LLEVLHRLVDKGNTVVVIEHNL-------D--- 890
|
90 100 110
....*....|....*....|....*....|..
gi 16132108 210 VMAN---------------GHVMAQGTPEEVM 226
Cdd:COG0178 891 VIKTadwiidlgpeggdggGEIVAEGTPEEVA 922
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
12-225 |
7.43e-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: 56.07 E-value: 7.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 12 YGTdKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVflgdnpinmlssrQLARRLSLLPQHHLTPEGi 91
Cdd:TIGR01271 437 YVT-PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-------------KHSGRISFSPQTSWIMPG- 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 92 TVQEL----VSYGRNPWLSLWGRLSAEDNARVNVAMNQTRINHLAVrrltELSGGQRQRAFLAMVLAQNTPVVLLDEPTT 167
Cdd:TIGR01271 502 TIKDNiifgLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGI----TLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16132108 168 YLDINHQVD-----LMRLMGElrtqgKTVVAVLHDLNQASRyCDQLVVMANGHVMAQGTPEEV 225
Cdd:TIGR01271 578 HLDVVTEKEifescLCKLMSN-----KTRILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSEL 634
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
138-210 |
1.07e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 53.34 E-value: 1.07e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16132108 138 ELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQG-KTVVAVLHDLNQASRYCDQLVV 210
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGkKTALVVEHDLAVLDYLSDRIHV 144
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-220 |
1.43e-08 |
|
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: 53.42 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 1 MTLRTENLTVSYGTDK--VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQ---SGTVFLGDNPINMLSSRqLA 75
Cdd:cd03233 4 LSWRNISFTTGKGRSKipILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEK-YP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 76 RRLSLLPQHHLTPEGITVQELVSYgrnpwlslwgRLSAEDNARVNVamnqtrinhlavrrlteLSGGQRQRAFLAMVLAQ 155
Cdd:cd03233 83 GEIIYVSEEDVHFPTLTVRETLDF----------ALRCKGNEFVRG-----------------ISGGERKRVSIAEALVS 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16132108 156 NTPVVLLDEPTTYLDIN---HQVDLMRLMGelRTQGKTVVAVLHdlnQAS----RYCDQLVVMANGHVMAQG 220
Cdd:cd03233 136 RASVLCWDNSTRGLDSStalEILKCIRTMA--DVLKTTTFVSLY---QASdeiyDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
18-220 |
1.71e-08 |
|
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: 53.42 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 18 LNDVSLSLPTGKITALIGPNGCGKSTL----------------LNCFSRLLMPQSGT--VFLGDNPINMLSSRQlaRRLS 79
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryvesLSAYARQFLGQMDKpdVDSIEGLSPAIAIDQ--KTTS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 80 LLPQHHLTpegiTVQELVSYGRnpwlSLWGRLSAEdnARVNVaMNQTRINHLAVRRLTE-LSGGQRQRAFLAMVLAQNTP 158
Cdd:cd03270 89 RNPRSTVG----TVTEIYDYLR----LLFARVGIR--ERLGF-LVDVGLGYLTLSRSAPtLSGGEAQRIRLATQIGSGLT 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16132108 159 VVL--LDEPTTYLdinHQVDLMRLMG---ELRTQGKTVVAVLHDLnQASRYCDQLVVMA------NGHVMAQG 220
Cdd:cd03270 158 GVLyvLDEPSIGL---HPRDNDRLIEtlkRLRDLGNTVLVVEHDE-DTIRAADHVIDIGpgagvhGGEIVAQG 226
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
3-223 |
1.78e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 53.49 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTllncFSRLLM--PQ----SGTVFLGDNPINMLSSRQLAR 76
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKST----LSKVIAghPAykilEGDILFKGESILDLEPEERAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 77 R-LSLLPQHHLTPEGITVQELVSYGRNPWLSLWGRLSAED-------NARVN-VAMNQTRINhlavRRLTE-LSGGQRQR 146
Cdd:CHL00131 84 LgIFLAFQYPIEIPGVSNADFLRLAYNSKRKFQGLPELDPlefleiiNEKLKlVGMDPSFLS----RNVNEgFSGGEKKR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 147 -AFLAMVLAqNTPVVLLDEPTTYLDInhqvDLMRLMGE----LRTQGKTVVAVLHdlnqASRYCDQLV-----VMANGHV 216
Cdd:CHL00131 160 nEILQMALL-DSELAILDETDSGLDI----DALKIIAEginkLMTSENSIILITH----YQRLLDYIKpdyvhVMQNGKI 230
|
....*..
gi 16132108 217 MAQGTPE 223
Cdd:CHL00131 231 IKTGDAE 237
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-200 |
2.00e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.51 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNpinmlssrqlaRRLSLLP 82
Cdd:PRK15064 2 LSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPN-----------ERLGKLR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 83 QHHLTPEGITVQELVSYGRNPwlsLWGRLSAEDNARVNVAMNQ---TRINHLAVR-----------RLTEL--------- 139
Cdd:PRK15064 71 QDQFAFEEFTVLDTVIMGHTE---LWEVKQERDRIYALPEMSEedgMKVADLEVKfaemdgytaeaRAGELllgvgipee 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16132108 140 ---------SGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINhqvdLMR-LMGELRTQGKTVVAVLHD---LNQ 200
Cdd:PRK15064 148 qhyglmsevAPGWKLRVLLAQALFSNPDILLLDEPTNNLDIN----TIRwLEDVLNERNSTMIIISHDrhfLNS 217
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-227 |
2.58e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 54.36 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 17 VLNDVSLSL-PTGKItALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLPQHHLTPEGITVQE 95
Cdd:PLN03130 1254 VLHGLSFEIsPSEKV-GIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 96 LVSYGRNPWLSLWGRLSAEdnarvnvamnqtrinHL--AVRR--------LTE----LSGGQRQRAFLAMVLAQNTPVVL 161
Cdd:PLN03130 1333 LDPFNEHNDADLWESLERA---------------HLkdVIRRnslgldaeVSEagenFSVGQRQLLSLARALLRRSKILV 1397
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16132108 162 LDEPTTYLDINHQVDLMRLMGElRTQGKTVVAVLHDLNQASRyCDQLVVMANGHVMAQGTPEEVMT 227
Cdd:PLN03130 1398 LDEATAAVDVRTDALIQKTIRE-EFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLS 1461
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
139-226 |
5.78e-08 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 53.11 E-value: 5.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 139 LSGGQRQRAFLAmvlaqnTPV------VL--LDEPTTYLdinHQVDLMRLMG---ELRTQGKTVVAVLHDLnQASRYCDQ 207
Cdd:COG0178 486 LSGGEAQRIRLA------TQIgsglvgVLyvLDEPSIGL---HQRDNDRLIEtlkRLRDLGNTVIVVEHDE-DTIRAADY 555
|
90 100
....*....|....*....|....*
gi 16132108 208 LVVM------ANGHVMAQGTPEEVM 226
Cdd:COG0178 556 IIDIgpgageHGGEVVAQGTPEEIL 580
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
139-227 |
6.49e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.11 E-value: 6.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 139 LSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQG-KTVVAVLHDLNQASRyCDQLVVMAN---- 213
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIKR-SDKIVVFNNpdrt 1437
|
90
....*....|....*
gi 16132108 214 -GHVMAQGTPEEVMT 227
Cdd:PTZ00265 1438 gSFVQAHGTHEELLS 1452
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
111-227 |
2.44e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.89 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 111 LSAED-NARVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGK 189
Cdd:NF000106 116 LSRKDaRARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGA 195
|
90 100 110
....*....|....*....|....*....|....*...
gi 16132108 190 TVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVMT 227
Cdd:NF000106 196 TVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKT 233
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
17-236 |
3.47e-07 |
|
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: 50.24 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 17 VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVflgdnpinmlssrQLARRLSLLPQHHLTPEGiTVQEL 96
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-------------KHSGRISFSSQFSWIMPG-TIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 97 ----VSYGRNPWLSLWGRLSAEDN-----ARVNVAMNQTRINhlavrrlteLSGGQRQRAFLAMVLAQNTPVVLLDEPTT 167
Cdd:cd03291 118 iifgVSYDEYRYKSVVKACQLEEDitkfpEKDNTVLGEGGIT---------LSGGQRARISLARAVYKDADLYLLDSPFG 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16132108 168 YLDINHQVDLM-----RLMGElrtqgKTVVAVLHDLNQASRyCDQLVVMANGHVMAQGTPEEVMTpglLRTVFS 236
Cdd:cd03291 189 YLDVFTEKEIFescvcKLMAN-----KTRILVTSKMEHLKK-ADKILILHEGSSYFYGTFSELQS---LRPDFS 253
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
137-225 |
3.61e-07 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 50.84 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 137 TELSGGQRQRAFLAMVLAQ----NTpVVLLDEPTTYL---DINHqvdLMRLMGELRTQGKTVVAVLHDLNqASRYCDQLV 209
Cdd:PRK00349 829 TTLSGGEAQRVKLAKELSKrstgKT-LYILDEPTTGLhfeDIRK---LLEVLHRLVDKGNTVVVIEHNLD-VIKTADWII 903
|
90 100
....*....|....*....|..
gi 16132108 210 VM------ANGHVMAQGTPEEV 225
Cdd:PRK00349 904 DLgpeggdGGGEIVATGTPEEV 925
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
139-226 |
5.69e-07 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 50.07 E-value: 5.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 139 LSGGQRQRAFLAmvlaqnTPV------VL--LDEPTTYLdinHQVDLMRLMG---ELRTQGKTVVAVLHDlNQASRYCDQ 207
Cdd:PRK00349 490 LSGGEAQRIRLA------TQIgsgltgVLyvLDEPSIGL---HQRDNDRLIEtlkHLRDLGNTLIVVEHD-EDTIRAADY 559
|
90 100
....*....|....*....|....*
gi 16132108 208 LVVMA------NGHVMAQGTPEEVM 226
Cdd:PRK00349 560 IVDIGpgagvhGGEVVASGTPEEIM 584
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
115-226 |
7.72e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.73 E-value: 7.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 115 DNARVNVAMNQTRINhlavrrltELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAV 194
Cdd:PRK10982 376 DSMRVKTPGHRTQIG--------SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIII 447
|
90 100 110
....*....|....*....|....*....|....*..
gi 16132108 195 LHDLNQASRYCDQLVVMANGHV-----MAQGTPEEVM 226
Cdd:PRK10982 448 SSEMPELLGITDRILVMSNGLVagivdTKTTTQNEIL 484
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
3-192 |
8.62e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 48.31 E-value: 8.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLP 82
Cdd:PRK13543 12 LAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 83 QhhLTPEGITVQEL----VSYGRNPwlslwgrlsaednarvnvamNQTRINHLAVRRLT--------ELSGGQRQRAFLA 150
Cdd:PRK13543 92 G--LKADLSTLENLhflcGLHGRRA--------------------KQMPGSALAIVGLAgyedtlvrQLSAGQKKRLALA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 16132108 151 MVLAQNTPVVLLDEPTTYLDINHQVDLMRLM-GELRTQGKTVV 192
Cdd:PRK13543 150 RLWLSPAPLWLLDEPYANLDLEGITLVNRMIsAHLRGGGAALV 192
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-171 |
1.50e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.79 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 1 MTL-RTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLncfsRLLmpqSGTVFLGDNPINMLSSRQLARrls 79
Cdd:PRK11147 1 MSLiSIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLM----KIL---NGEVLLDDGRIIYEQDLIVAR--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 80 lLPQHHLTPEGITVQELVSYG---RNPWLSLWGRLS---AEDNARVNvaMNQ-----------------TRINHL----- 131
Cdd:PRK11147 71 -LQQDPPRNVEGTVYDFVAEGieeQAEYLKRYHDIShlvETDPSEKN--LNElaklqeqldhhnlwqleNRINEVlaqlg 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 16132108 132 --AVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDI 171
Cdd:PRK11147 148 ldPDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI 189
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
134-226 |
1.90e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.67 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 134 RRLTELSGGQRQRAFLAMVLAQNTPVV--LLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDlNQASRYCDQLVVM 211
Cdd:PRK00635 472 RALATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQMISLADRIIDI 550
|
90 100
....*....|....*....|.
gi 16132108 212 A------NGHVMAQGTPEEVM 226
Cdd:PRK00635 551 GpgagifGGEVLFNGSPREFL 571
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
3-196 |
4.64e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.16 E-value: 4.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLL-------------NCfsRLLMPQSGTVflGDNPINM- 68
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLrymamhaidgipkNC--QILHVEQEVV--GDDTTALq 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 69 --LSS-----RQLARRLSLLPQHHLTP-EGITVQ-----------ELVS------YGRnpwLSLWGRLSAEDNARVNVAm 123
Cdd:PLN03073 254 cvLNTdiertQLLEEEAQLVAQQRELEfETETGKgkgankdgvdkDAVSqrleeiYKR---LELIDAYTAEARAASILA- 329
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16132108 124 NQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDInHQVdlMRLMGELRTQGKTVVAVLH 196
Cdd:PLN03073 330 GLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL-HAV--LWLETYLLKWPKTFIVVSH 399
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
16-170 |
5.78e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.63 E-value: 5.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 16 KVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINmlssrQLARRLSLLPQHHLtpeGITVQE 95
Cdd:PRK13541 14 KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNIN-----NIAKPYCTYIGHNL---GLKLEM 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16132108 96 LVSYGRNPWLSLWGrlSAEdnaRVNVAMNQTRINHLAVRRLTELSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLD 170
Cdd:PRK13541 86 TVFENLKFWSEIYN--SAE---TLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
22-192 |
9.54e-06 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 45.73 E-value: 9.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 22 SLSLPTGKITALIGPNGCGKSTLLNCFsrLLMPQSGTVFLGdnpinmlSSRQLARRL--SLLPQH-HLTPEGITVQELVS 98
Cdd:COG4938 14 EAELELKPLTLLIGPNGSGKSTLIQAL--LLLLQSNFIYLP-------AERSGPARLypSLVRELsDLGSRGEYTADFLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 99 ygrnpWLSLWGRLSAEDN-----------------ARVNVAMNQTRI----NHLAVR-RLTELSGGQRQraFLAMVLA-- 154
Cdd:COG4938 85 -----ELENLEILDDKSKelleqveewlekifpgkVEVDASSDLVRLvfrpSGNGKRiPLSNVGSGVSE--LLPILLAll 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16132108 155 ---QNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVV 192
Cdd:COG4938 158 saaKPGSLLIIEEPEAHLHPKAQSALAELLAELANSGVQVI 198
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
127-226 |
1.15e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 127 RINHLAV-RRLTELSGGQRQRAFLAMVLAQNTP---VVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNqAS 202
Cdd:PRK00635 797 GLDYLPLgRPLSSLSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMH-VV 875
|
90 100 110
....*....|....*....|....*....|
gi 16132108 203 RYCDQLVVMA------NGHVMAQGTPEEVM 226
Cdd:PRK00635 876 KVADYVLELGpeggnlGGYLLASCSPEELI 905
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
18-186 |
1.66e-05 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 44.99 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 18 LNDVSLSLPTG-KITALIGPNGCGKSTLLNCFSRLL---------------------MPQSGTVFLG--------DNPIN 67
Cdd:COG3950 14 FEDLEIDFDNPpRLTVLVGENGSGKTTLLEAIALALsgllsrlddvkfrkllirngeFGDSAKLILYygtsrlllDGPLK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 68 MLsSRQLARRLSLLPQHH-LTPEGITVQELVSYGRNPWLSLWGRLSAEDNAR---VNVAMNQ--TRINHLAVRR------ 135
Cdd:COG3950 94 KL-ERLKEEYFSRLDGYDsLLDEDSNLREFLEWLREYLEDLENKLSDELDEKleaVREALNKllPDFKDIRIDRdpgrlv 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16132108 136 ----------LTELSGGQRQraFLAMV------LAQNTP----------VVLLDEPTTYLDINHQvdlMRLMGELRT 186
Cdd:COG3950 173 ildkngeelpLNQLSDGERS--LLALVgdlarrLAELNPalenplegegIVLIDEIDLHLHPKWQ---RRILPDLRK 244
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-226 |
2.22e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.42 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 18 LNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVfLGDNPINMLS-SRQLARRLSLLPQ------------- 83
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-DRNGEVSVIAiSAGLSGQLTGIENiefkmlcmgfkrk 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 84 --HHLTPEGITVQELVSYGRNPwlslwgrlsaednarvnvamnqtrinhlavrrLTELSGGQRQRAFLAMVLAQNTPVVL 161
Cdd:PRK13546 119 eiKAMTPKIIEFSELGEFIYQP--------------------------------VKKYSSGMRAKLGFSINITVNPDILV 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16132108 162 LDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVMAQGTPEEVM 226
Cdd:PRK13546 167 IDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL 231
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
8-197 |
4.01e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.39 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 8 LTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDN-------------PINMLSS--- 71
Cdd:PRK10636 7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlawvnqetpalPQPALEYvid 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 72 -----RQLARRLSLLPQHHltpEGITVQELvsYGRNPWLSLWGRLSAEDNARVNVAMNQTRINhlavRRLTELSGGQRQR 146
Cdd:PRK10636 87 gdreyRQLEAQLHDANERN---DGHAIATI--HGKLDAIDAWTIRSRAASLLHGLGFSNEQLE----RPVSDFSGGWRMR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 16132108 147 AFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLmgeLRTQGKTVVAVLHD 197
Cdd:PRK10636 158 LNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKW---LKSYQGTLILISHD 205
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
19-60 |
4.42e-05 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 40.28 E-value: 4.42e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 16132108 19 NDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVF 60
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPAKRARF 54
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
16-52 |
4.60e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 43.77 E-value: 4.60e-05
10 20 30
....*....|....*....|....*....|....*..
gi 16132108 16 KVLNDVSLSLptGKITALIGPNGCGKSTLLNCFsRLL 52
Cdd:COG4637 11 KSLRDLELPL--GPLTVLIGANGSGKSNLLDAL-RFL 44
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-44 |
5.01e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 40.54 E-value: 5.01e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 16132108 3 LRTENLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTL 44
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTL 43
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
7-46 |
5.62e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.77 E-value: 5.62e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 16132108 7 NLTVSYGTDKVLNDVSLSLPTGKITALIGPNGCGKSTLLN 46
Cdd:PRK10938 265 NGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLS 304
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-226 |
6.08e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 40.76 E-value: 6.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 18 LNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQ-LA---------RR---LSLlpqh 84
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLAngivyisedRKrdgLVL---- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 85 hltpeGITVQELVSYGRNPWLS-LWGRLS-AEDNARV-------NV---AMNQTrinhlavrrLTELSGGQRQRAFLAMV 152
Cdd:PRK10762 344 -----GMSVKENMSLTALRYFSrAGGSLKhADEQQAVsdfirlfNIktpSMEQA---------IGLLSGGNQQKVAIARG 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16132108 153 LAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHV-----MAQGTPEEVM 226
Cdd:PRK10762 410 LMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRIsgeftREQATQEKLM 488
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
30-52 |
6.24e-04 |
|
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: 40.45 E-value: 6.24e-04
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
139-226 |
6.62e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.54 E-value: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 139 LSGGQRQRAFLAMVLAQNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLNQASRYCDQLVVMANGHVM- 217
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITg 484
|
90
....*....|...
gi 16132108 218 ----AQGTPEEVM 226
Cdd:NF040905 485 elprEEASQERIM 497
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
30-48 |
9.25e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 39.02 E-value: 9.25e-04
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
134-170 |
1.09e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 1.09e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 16132108 134 RRLTELSGGQRQ------RAFLAMVLAQNTPVVLLDEPTTYLD 170
Cdd:PRK03918 784 RPLTFLSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLD 826
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
26-54 |
2.16e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 2.16e-03
10 20
....*....|....*....|....*....
gi 16132108 26 PTGKITALIGPNGCGKSTLLNCFSRLLMP 54
Cdd:COG4913 22 FDGRGTLLTGDNGSGKSTLLDAIQTLLVP 50
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
15-44 |
2.87e-03 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 38.58 E-value: 2.87e-03
10 20 30
....*....|....*....|....*....|
gi 16132108 15 DKVLNDVSLSLPTGKITALIGPNGCGKSTL 44
Cdd:TIGR00954 465 DVLIESLSFEVPSGNNLLICGPNGCGKSSL 494
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
139-197 |
3.17e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 38.48 E-value: 3.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16132108 139 LSGGQRQ------RAFLAMVLAQN------TPVVLLDEPTTYLDINHQVDLMRLMGELRTQG-KTVVAVLHD 197
Cdd:PRK02224 782 LSGGERAlfnlslRCAIYRLLAEGiegdapLPPLILDEPTVFLDSGHVSQLVDLVESMRRLGvEQIVVVSHD 853
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
129-198 |
3.52e-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: 38.14 E-value: 3.52e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16132108 129 NHLAVRRLTELSGGQRQraFLAMVLA-----QNTPVVLLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDL 198
Cdd:pfam13304 227 GGGGELPAFELSDGTKR--LLALLAAllsalPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSP 299
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
27-46 |
4.34e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 37.14 E-value: 4.34e-03
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
17-108 |
4.70e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 37.72 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 17 VLNDVSLSLPTGKITALIGPNGCGKSTLLNCFSRLLMPQSGTVFLGDNPINMLSSRQLARRLSLLPQHHLTPEGITVQEL 96
Cdd:COG1106 18 TLSMVASGLRLLRVNLIYGANASGKSNLLEALYFLRNLVLNSSQPGDKLVEPFLLDSESKNEPSEFEILFLLDGVRYEYG 97
|
90
....*....|..
gi 16132108 97 VSYGRNPWLSLW 108
Cdd:COG1106 98 FELDKERIISEW 109
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
28-46 |
5.06e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 36.99 E-value: 5.06e-03
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
153-227 |
6.01e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.89 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 153 LAQNTPVV-LLDEPTTYLDINHQVDLMRLMGELRTQGKTVVAVLHDLnQASRYCDQLVVMA------NGHVMAQGTPEEV 225
Cdd:PRK00635 1716 LPPKHPTLfLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDP-ALLKQADYLIEMGpgsgktGGKILFSGPPKDI 1794
|
..
gi 16132108 226 MT 227
Cdd:PRK00635 1795 SA 1796
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
136-173 |
6.15e-03 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (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: 213240 [Multi-domain] Cd Length: 251 Bit Score: 37.28 E-value: 6.15e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 16132108 136 LTELSGGQRQRAFLAMVLA----QNTPVVLLDEPTTYLDINH 173
Cdd:cd03273 164 LTELSGGQRSLVALSLILAlllfKPAPMYILDEVDAALDLSH 205
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
125-184 |
6.43e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (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: 213239 [Multi-domain] Cd Length: 243 Bit Score: 36.85 E-value: 6.43e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16132108 125 QTRINHLA------VRRLTELSGGQRQRAFLAMVLA----QNTPVVLLDEPTTYLDINHQVDLMRLMGEL 184
Cdd:cd03272 139 QGKINSLTnmkqdeQQEMQQLSGGQKSLVALALIFAiqkcDPAPFYLFDEIDAALDAQYRTAVANMIKEL 208
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
28-46 |
6.48e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 37.11 E-value: 6.48e-03
|
| |
