|
Name |
Accession |
Description |
Interval |
E-value |
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-252 |
1.22e-177 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 488.05 E-value: 1.22e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVL 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 RQENHFTSRLTVEDLVGFGRYPWSKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLD 160
Cdd:COG4604 81 RQENHINSRLTVRELVAFGRFPYSKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 161 EPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMRPEVIEAIFDTKVHIE 240
Cdd:COG4604 161 EPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDTDIEVE 240
|
250
....*....|..
gi 1353453005 241 TLHGQHIAIYYR 252
Cdd:COG4604 241 EIDGKRICVYFR 252
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-241 |
7.18e-102 |
|
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: 296.57 E-value: 7.18e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVL 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 RQENHFTSRLTVEDLVGFGRYPWSK--GRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVL 158
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRYPHLGlfGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 159 LDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMRPEVIEAIFDTKVH 238
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEAR 240
|
...
gi 1353453005 239 IET 241
Cdd:COG1120 241 VIE 243
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-239 |
2.23e-77 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 234.52 E-value: 2.23e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVL 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 RQENHFTSRLTVEDLVGFGRYPWSK--GRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVL 158
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYGRSPWLSlwGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 159 LDEPLNNLDMKHSVAMMKQLRRAADElHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMRPEVIEAIFDTKVH 238
Cdd:PRK11231 162 LDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVEAE 240
|
.
gi 1353453005 239 I 239
Cdd:PRK11231 241 I 241
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-239 |
4.23e-69 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 213.44 E-value: 4.23e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVL 80
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 RQENHFTSRLTVEDLVGFGRYPWskGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQ---NTD-- 155
Cdd:COG4559 81 PQHSSLAFPFTVEEVVALGRAPH--GSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwePVDgg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 156 --YVLLDEPLNNLDMKHSVAMMKQLRRAADElHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMRPEVIEAIF 233
Cdd:COG4559 159 prWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERVY 237
|
....*.
gi 1353453005 234 DTKVHI 239
Cdd:COG4559 238 GADLRV 243
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-239 |
5.27e-69 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 213.09 E-value: 5.27e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVL 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 RQENHFTSRLTVEDLVGFGRYPWSKGRltSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTD----- 155
Cdd:PRK13548 82 PQHSSLSFPFTVEEVVAMGRAPHGLSR--AEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQLWEpdgpp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 156 -YVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMRPEVIEAIFD 234
Cdd:PRK13548 160 rWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRRVYG 239
|
....*
gi 1353453005 235 TKVHI 239
Cdd:PRK13548 240 ADVLV 244
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-218 |
3.39e-67 |
|
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: 205.75 E-value: 3.39e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 3 EVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVLRQ 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 83 enhftsrltvedlvgfgrypwskgrltsedrqhietAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEP 162
Cdd:cd03214 81 ------------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1353453005 163 LNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRG 218
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
15-233 |
3.01e-62 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 196.16 E-value: 3.01e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 15 TVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVLRQENHFTSRLTVED 94
Cdd:PRK10575 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVRE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 95 LVGFGRYPW--SKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMKHSV 172
Cdd:PRK10575 105 LVAIGRYPWhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQV 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1353453005 173 AMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMRPEVIEAIF 233
Cdd:PRK10575 185 DVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIY 245
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-243 |
3.99e-61 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 192.61 E-value: 3.99e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDE-----QMAK 75
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRigyvpQRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 76 VlsvlrqENHFtsRLTVEDLVGFGRYPWSK--GRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQN 153
Cdd:COG1121 86 V------DWDF--PITVRDVVLMGRYGRRGlfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 154 TDYVLLDEPLNNLDMKHSVAMMKQLRRAADElHKTIILVIHDINFASAYSDHIIAMKQGeVLYRGTPQEIMRPEVIEAIF 233
Cdd:COG1121 158 PDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTPENLSRAY 235
|
250
....*....|
gi 1353453005 234 DTKVHIETLH 243
Cdd:COG1121 236 GGPVALLAHG 245
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-234 |
1.54e-56 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 181.02 E-value: 1.54e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQN-TTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKvlsv 79
Cdd:COG3638 2 MLELRNLSKRYPGgTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 LR-------QENHFTSRLTVED--LVG-FGRYPWSK---GRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACV 146
Cdd:COG3638 78 LRrrigmifQQFNLVPRLSVLTnvLAGrLGRTSTWRsllGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 147 AMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEImRP 226
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL-TD 236
|
....*...
gi 1353453005 227 EVIEAIFD 234
Cdd:COG3638 237 AVLREIYG 244
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-233 |
2.70e-55 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 177.18 E-value: 2.70e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVlSVLR 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRI-GYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 82 QENHFTSRLTVEDLVGF-GRYpwsKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLD 160
Cdd:COG1131 80 QEPALYPDLTVRENLRFfARL---YGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1353453005 161 EPLNNLDMKHSVAMMKQLRRAADElHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMRpEVIEAIF 233
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA-RLLEDVF 227
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-234 |
6.14e-55 |
|
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: 176.59 E-value: 6.14e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKvLSVL 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ-IGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 RQENHFTSRLTVEDLVGFgrYPWSKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLD 160
Cdd:COG4555 80 PDERGLYDRLTVRENIRY--FAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 161 EPLNNLDMKHSVAMMKQLRRAADElHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEI--------MRPEVIEAI 232
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELreeigeenLEDAFVALI 236
|
..
gi 1353453005 233 FD 234
Cdd:COG4555 237 GS 238
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
11-239 |
7.98e-54 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 174.79 E-value: 7.98e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 11 YQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVLRQENHFTSRL 90
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 91 TVEDLVGFGRYPWSK--GRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDM 168
Cdd:PRK10253 97 TVQELVARGRYPHQPlfTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1353453005 169 KHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMRPEVIEAIFDTKVHI 239
Cdd:PRK10253 177 SHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRCMI 247
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-225 |
2.20e-52 |
|
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: 169.82 E-value: 2.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQN-TTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVL 80
Cdd:COG1122 1 IELENLSFSYPGgTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 RQ--ENHFTSRlTVEDLVGFGryPWSKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVL 158
Cdd:COG1122 81 FQnpDDQLFAP-TVEEDVAFG--PENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1353453005 159 LDEPLNNLDMKHSVAMMKQLRRAADElHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMR 225
Cdd:COG1122 158 LDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-218 |
5.48e-52 |
|
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: 168.10 E-value: 5.48e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 3 EVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDE--QMAKVLSVL 80
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRigYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 RqenhfTSRLTVEDLVGFGRYP--WSKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVL 158
Cdd:cd03235 81 R-----DFPISVRDVVLMGLYGhkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 159 LDEPLNNLDMKHSVAMMKQLRRAADElHKTIILVIHDINFASAYSDHIIAMKqGEVLYRG 218
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-233 |
1.32e-51 |
|
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: 168.13 E-value: 1.32e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQN-TTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDeqmaKVLSVL 80
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKG----KALRQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 R-------QENHFTSRLTVED--LVG-FGRYPWSK---GRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVA 147
Cdd:cd03256 77 RrqigmifQQFNLIERLSVLEnvLSGrLGRRSTWRslfGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 148 MVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEImRPE 227
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL-TDE 235
|
....*.
gi 1353453005 228 VIEAIF 233
Cdd:cd03256 236 VLDEIY 241
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-232 |
1.40e-50 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 165.31 E-value: 1.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVlnRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQmaKVLSVL 80
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 RQENHFTSRLTVEDLVGFGRYPwsKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLD 160
Cdd:COG3840 77 FQENNLFPHLTVAQNIGLGLRP--GLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1353453005 161 EPLNNLD--MKHSvaMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMRPEVIEAI 232
Cdd:COG3840 155 EPFSALDpaLRQE--MLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPAL 226
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-234 |
5.91e-50 |
|
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: 164.01 E-value: 5.91e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQN-TTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDE---QMAKV 76
Cdd:TIGR02315 1 MLEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKklrKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 77 LSVLRQENHFTSRLTVEDLVGFGRYPWSK------GRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVL 150
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGRLGYKPtwrsllGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 151 CQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEImRPEVIE 230
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL-DDEVLR 239
|
....
gi 1353453005 231 AIFD 234
Cdd:TIGR02315 240 HIYG 243
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-213 |
1.28e-48 |
|
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: 159.55 E-value: 1.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 3 EVKAICKSY--QNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVL 80
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 RQE-NHFTSRLTVEDLVGFG--RYPWSKgrltSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYV 157
Cdd:cd03225 81 FQNpDDQFFGPTVEEEVAFGleNLGLPE----EEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1353453005 158 LLDEPLNNLDMKHSVAMMKQLRRAADElHKTIILVIHDINFASAYSDHIIAMKQGE 213
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-215 |
3.01e-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: 3.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAkvLSVLR 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRN--IGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 82 QENHFTSRLTVEDLVGFGRYPwsKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDE 161
Cdd:cd03259 79 QDYALFPHLTVAENIAFGLKL--RGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1353453005 162 PLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVL 215
Cdd:cd03259 157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-214 |
5.12e-47 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 155.97 E-value: 5.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQN----TTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKv 76
Cdd:COG1136 4 LLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 77 lsvLRQEN--------HFTSRLTVEDLVGFGRYPwsKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAM 148
Cdd:COG1136 83 ---LRRRHigfvfqffNLLPELTALENVALPLLL--AGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1353453005 149 VLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFAsAYSDHIIAMKQGEV 214
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLRDGRI 222
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-225 |
4.40e-46 |
|
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: 160.84 E-value: 4.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSY-----QNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAK 75
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 76 vlsvLRQE------NHFTS---RLTVEDLVGFGryPWSKGRLTSEDR-QHIETAMDFLDLLP-LRARYLDQLSGGQRQRA 144
Cdd:COG1123 340 ----LRRRvqmvfqDPYSSlnpRMTVGDIIAEP--LRLHGLLSRAERrERVAELLERVGLPPdLADRYPHELSGGQRQRV 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 145 CVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIM 224
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVF 493
|
.
gi 1353453005 225 R 225
Cdd:COG1123 494 A 494
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-228 |
9.95e-46 |
|
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: 152.98 E-value: 9.95e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKvLSVLR 81
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIAR-LGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 82 --QENHFTSRLTVED--LVG---FGRYPWSKGRLTSEDRQHIETAMDFLD---LLPLRARYLDQLSGGQRQRACVAMVLC 151
Cdd:cd03219 80 tfQIPRLFPELTVLEnvMVAaqaRTGSGLLLARARREEREARERAEELLErvgLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1353453005 152 QNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADElHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMR-PEV 228
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNnPRV 236
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-231 |
1.31e-45 |
|
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: 153.27 E-value: 1.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKV---- 76
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLgiar 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 77 ----------LSVLrqEN-----HFTSRltvEDLVGFGRYPWSKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQR 141
Cdd:COG0411 84 tfqnprlfpeLTVL--ENvlvaaHARLG---RGLLAALLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 142 QRACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQ 221
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPA 238
|
250
....*....|.
gi 1353453005 222 EIMR-PEVIEA 231
Cdd:COG0411 239 EVRAdPRVIEA 249
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-241 |
2.61e-45 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 156.54 E-value: 2.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVL 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 RQENHFTSRLTVEDLVGFGRYPwSKGRL---TSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYV 157
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGRTP-HRSRFdtwTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 158 LLDEPLNNLDMKHSVAMMKQLRRAADElHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMRPEVIEAIFDTKV 237
Cdd:PRK09536 162 LLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDART 240
|
....
gi 1353453005 238 HIET 241
Cdd:PRK09536 241 AVGT 244
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-214 |
2.99e-45 |
|
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: 151.10 E-value: 2.99e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQN----TTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKV- 76
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 77 ---LSVLRQENHFTSRLTVEDLVGFGRYPwsKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQN 153
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVELPLLL--AGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1353453005 154 TDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASaYSDHIIAMKQGEV 214
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-214 |
2.03e-43 |
|
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: 144.85 E-value: 2.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVlSVLR 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRI-GYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 82 QENHFTSRLTVEDlvgfgrypwskgrltsedrqhietamdfldllplrarYLDqLSGGQRQRACVAMVLCQNTDYVLLDE 161
Cdd:cd03230 80 EEPSLYENLTVRE-------------------------------------NLK-LSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1353453005 162 PLNNLDMKHSVAMMKQLRRAADElHKTIILVIHDINFASAYSDHIIAMKQGEV 214
Cdd:cd03230 122 PTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-213 |
2.72e-41 |
|
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: 139.63 E-value: 2.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMA--KVLSV 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPlrRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 LRQENHFTSRLTVEDLVGFGrypwskgrltsedrqhietamdfldllplraryldqLSGGQRQRACVAMVLCQNTDYVLL 159
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG------------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1353453005 160 DEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGE 213
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-225 |
8.85e-41 |
|
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: 140.13 E-value: 8.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQN-TTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVL 80
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 RQENHFTSRLTVEDLVGFgrYP----WSKGRLtsedRQHIETAMDFLDLLP--LRARYLDQLSGGQRQRACVAMVLCQNT 154
Cdd:cd03295 81 IQQIGLFPHMTVEENIAL--VPkllkWPKEKI----RERADELLALVGLDPaeFADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1353453005 155 DYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMR 225
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-209 |
1.17e-40 |
|
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: 139.14 E-value: 1.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQN----TTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGlEVAKTPDEQMAKVL 77
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG-EPVTGPGPDRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 78 svlrQENHFTSRLTVEDLVGFGryPWSKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYV 157
Cdd:cd03293 80 ----QQDALLPWLTVLDNVALG--LELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1353453005 158 LLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAM 209
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-218 |
3.23e-40 |
|
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: 138.41 E-value: 3.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQN----TTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMA-- 74
Cdd:cd03257 1 LLEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 75 -KVLSVLRQeNHFTS---RLTVEDLVGFGryPWSKGRLTSEDRQhIETAMDFLDLLPLRARYLD----QLSGGQRQRACV 146
Cdd:cd03257 81 rKEIQMVFQ-DPMSSlnpRMTIGEQIAEP--LRIHGKLSKKEAR-KEAVLLLLVGVGLPEEVLNryphELSGGQRQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1353453005 147 AMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRG 218
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-225 |
4.06e-40 |
|
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: 138.78 E-value: 4.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSY----QNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKV 76
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 77 LSVLRQeNHFTS---RLTVEDLVgfgRYP-WSKGRLTSEDRqhIETAMDFLDLLP-LRARYLDQLSGGQRQRACVAMVLC 151
Cdd:COG1124 81 VQMVFQ-DPYASlhpRHTVDRIL---AEPlRIHGLPDREER--IAELLEQVGLPPsFLDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1353453005 152 QNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMR 225
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-223 |
6.66e-40 |
|
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: 137.75 E-value: 6.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQmakvlsvlR 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK--------R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 82 QENH-FTS-----RLTVEDLVGFGRYpwSKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTD 155
Cdd:cd03300 73 PVNTvFQNyalfpHLTVFENIAFGLR--LKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1353453005 156 YVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
10-209 |
1.51e-39 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 135.44 E-value: 1.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 10 SYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVlvnglevAKTPDEQMAKVlsVLRQENHFTSR 89
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-------RRAGGARVAYV--PQRSEVPDSLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 90 LTVEDLVGFGRY----PWskGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNN 165
Cdd:NF040873 72 LTVRDLVAMGRWarrgLW--RRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1353453005 166 LDMKHSVAMMKQLRRAADElHKTIILVIHDINFASAySDHIIAM 209
Cdd:NF040873 150 LDAESRERIIALLAEEHAR-GATVVVVTHDLELVRR-ADPCVLL 191
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-164 |
4.53e-39 |
|
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: 132.77 E-value: 4.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 17 LNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVLRQENHFTSRLTVEDLV 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1353453005 97 GFGRYPwsKGRLTSEDRQHIETAMDFLDLLPLRARYLD----QLSGGQRQRACVAMVLCQNTDYVLLDEPLN 164
Cdd:pfam00005 81 RLGLLL--KGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-225 |
7.69e-39 |
|
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: 134.94 E-value: 7.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAK-TPDEQ--MAKVLS 78
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlSEAELyrLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 79 VLRQENH-FTSrLTVEDLVGFGRYpwSKGRLTSEDRQHIetAMDFLDLLPLRA---RYLDQLSGGQRQRACVAMVLCQNT 154
Cdd:cd03261 81 MLFQSGAlFDS-LTVFENVAFPLR--EHTRLSEEEIREI--VLEKLEAVGLRGaedLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1353453005 155 DYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMR 225
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-249 |
1.59e-38 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 135.34 E-value: 1.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTAD--------SGSVLVNGLEVAKTPDEQ 72
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 73 MAKVLSVLRQENHFTSRLTVEDLVGFGRYPWSK--GRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVL 150
Cdd:PRK13547 81 LARLRAVLPQAAQPAFAFSAREIVLLGRYPHARraGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 151 CQ---------NTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQ 221
Cdd:PRK13547 161 AQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
250 260
....*....|....*....|....*....
gi 1353453005 222 EIMRPEVIEAIFDTKVH-IETLHGQHIAI 249
Cdd:PRK13547 241 DVLTPAHIARCYGFAVRlVDAGDGVPPVI 269
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-223 |
1.88e-38 |
|
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: 134.00 E-value: 1.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTP--DEQMAKVLsv 79
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPvqERNVGFVF-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 lrQENHFTSRLTVEDLVGFGRYPWSKGRLTSED--RQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYV 157
Cdd:cd03296 81 --QHYALFRHMTVFDNVAFGLRVKPRSERPPEAeiRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1353453005 158 LLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-226 |
2.39e-38 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 136.77 E-value: 2.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQmakvlsvl 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK-------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 RQEN----------HftsrLTVEDLVGFG---RypwskgRLTSEDRQhiETAMDFLDLL---PLRARYLDQLSGGQRQRA 144
Cdd:COG3842 77 RNVGmvfqdyalfpH----LTVAENVAFGlrmR------GVPKAEIR--ARVAELLELVgleGLADRYPHQLSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 145 CVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEI- 223
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIy 224
|
...
gi 1353453005 224 MRP 226
Cdd:COG3842 225 ERP 227
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-225 |
2.74e-38 |
|
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: 133.57 E-value: 2.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKV---L 77
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrrrI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 78 SVLRQENH-FTSrLTVEDLVGFG-RYpwsKGRLTSEDRQHI-ETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNT 154
Cdd:COG1127 85 GMLFQGGAlFDS-LTVFENVAFPlRE---HTDLSEAEIRELvLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1353453005 155 DYVLLDEPLNNLD---MKHSVAMMKQLRraaDELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMR 225
Cdd:COG1127 161 EILLYDEPTAGLDpitSAVIDELIRELR---DELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-225 |
3.49e-38 |
|
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: 139.27 E-value: 3.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSY--QNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTAD---SGSVLVNGLEVAKTPDEQMAK 75
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 76 VLSVLRQE--NHFTSrLTVEDLVGFGryPWSKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQN 153
Cdd:COG1123 84 RIGMVFQDpmTQLNP-VTVGDQIAEA--LENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1353453005 154 TDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMR 225
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-223 |
8.26e-38 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 132.43 E-value: 8.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEqmakvLSVL 80
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKD-----INKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 RQE--------NHFtSRLTVEDLVGFGryP-WSKGRLTSEDRqhiETAMDFLDLLPLRAR---YLDQLSGGQRQRACVAM 148
Cdd:COG1126 76 RRKvgmvfqqfNLF-PHLTVLENVTLA--PiKVKKMSKAEAE---ERAMELLERVGLADKadaYPAQLSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1353453005 149 VLCQNTDYVLLDEPLNNLD--MKHSV-AMMKQLrraADElHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:COG1126 150 ALAMEPKVMLFDEPTSALDpeLVGEVlDVMRDL---AKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEF 223
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-213 |
1.36e-37 |
|
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: 129.29 E-value: 1.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 3 EVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMakvlsvlrq 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 83 enhftsrltvedlvgfgrypwskgrltsedRQHIEtamdfldllplrarYLDQLSGGQRQRACVAMVLCQNTDYVLLDEP 162
Cdd:cd00267 72 ------------------------------RRRIG--------------YVPQLSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1353453005 163 LNNLDMKHSVAMMKQLRRAADElHKTIILVIHDINFASAYSDHIIAMKQGE 213
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-232 |
1.62e-37 |
|
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: 132.96 E-value: 1.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQ-----NTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDeqmaKV 76
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKK----KK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 77 LSVLRQ---------ENH-FtsRLTVEDLVGFGryPWSKGrlTSEDRQHiETAMDFLDLLPLRARYLDQ----LSGGQRQ 142
Cdd:TIGR04521 77 LKDLRKkvglvfqfpEHQlF--EETVYKDIAFG--PKNLG--LSEEEAE-ERVKEALELVGLDEEYLERspfeLSGGQMR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 143 RACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQE 222
Cdd:TIGR04521 150 RVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPRE 229
|
250
....*....|.
gi 1353453005 223 I-MRPEVIEAI 232
Cdd:TIGR04521 230 VfSDVDELEKI 240
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-225 |
2.75e-37 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 134.12 E-value: 2.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGlEVAKTpdeqmakVLSVlR 81
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG-RDLFT-------NLPP-R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 82 QEN------------HftsrLTVEDLVGFG--RYPWSKGrltsEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRacVA 147
Cdd:COG1118 74 ERRvgfvfqhyalfpH----MTVAENIAFGlrVRPPSKA----EIRARVEELLELVQLEGLADRYPSQLSGGQRQR--VA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 148 M---------VLcqntdyvLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRG 218
Cdd:COG1118 144 LaralavepeVL-------LLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVG 216
|
....*..
gi 1353453005 219 TPQEIMR 225
Cdd:COG1118 217 TPDEVYD 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-218 |
6.60e-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: 129.54 E-value: 6.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 23 SIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEqmAKVLSVLRQENHFTSRLTVEDLVGFGRYP 102
Cdd:cd03298 20 TFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAHLTVEQNVGLGLSP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 103 wsKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAA 182
Cdd:cd03298 98 --GLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLH 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 1353453005 183 DELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRG 218
Cdd:cd03298 176 AETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-212 |
2.20e-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: 129.44 E-value: 2.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQ----NTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKtPDEQMAKV 76
Cdd:COG1116 7 ALELRGVSKRFPtgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-PGPDRGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 77 LsvlrQEnhftSRL----TVEDLVGFGryPWSKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQ 152
Cdd:COG1116 86 F----QE----PALlpwlTVLDNVALG--LELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1353453005 153 NTDYVLLDEPLNNLD--MKHSvaMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQG 212
Cdd:COG1116 156 DPEVLLMDEPFGALDalTRER--LQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-195 |
2.87e-36 |
|
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: 127.60 E-value: 2.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKtPDEQMAKVLSVL 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 RQENHFTSRLTVEDLVGFgrypWSKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLD 160
Cdd:COG4133 81 GHADGLKPELTVRENLRF----WAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190
....*....|....*....|....*....|....*
gi 1353453005 161 EPLNNLDmKHSVAMMKQLRRAADELHKTIILVIHD 195
Cdd:COG4133 157 EPFTALD-AAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-223 |
8.41e-36 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 130.19 E-value: 8.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQ--MAKVls 78
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDrnIAMV-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 79 vlrqenhFTS-----RLTVEDLVGFG----RYPwskgrlTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRacVAM- 148
Cdd:COG3839 81 -------FQSyalypHMTVYENIAFPlklrKVP------KAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQR--VALg 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1353453005 149 -VLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:COG3839 146 rALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
12-250 |
9.20e-36 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 127.26 E-value: 9.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 12 QNTTVLNR---ITESIPVGGITSIIGANGAGKSTLLSVISRLLTAdSGSVLVNGLEVAKTPDEQMAKVLSVLRQENHFTS 88
Cdd:COG4138 4 NDVAVAGRlgpISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAELARHRAYLSQQQSPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 89 RLTVEDLVGFGRYPwskgrltSEDRQHIETAMDF----LDLLPLRARYLDQLSGGQRQRACVAMVLCQ-----NTD--YV 157
Cdd:COG4138 83 AMPVFQYLALHQPA-------GASSEAVEQLLAQlaeaLGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptiNPEgqLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 158 LLDEPLNNLDMKHSVAMMKQLRRAAdELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMRPEVIEAIFDTKV 237
Cdd:COG4138 156 LLDEPMNSLDVAQQAALDRLLRELC-QQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVKF 234
|
250
....*....|...
gi 1353453005 238 HIETLHGQHIAIY 250
Cdd:COG4138 235 RRLEVEGHRWLIP 247
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-225 |
4.02e-35 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 131.81 E-value: 4.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSY--QNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSV 79
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 LRQENH-FTSrlTVED--LVGfgrypwsKGRLTSEDrqhIETAM------DFLDLLPLRaryLD--------QLSGGQRQ 142
Cdd:COG4987 414 VPQRPHlFDT--TLREnlRLA-------RPDATDEE---LWAALervglgDWLAALPDG---LDtwlgeggrRLSGGERR 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 143 RACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADElhKTIILVIHDINFASAYsDHIIAMKQGEVLYRGTPQE 222
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAG--RTVLLITHRLAGLERM-DRILVLEDGRIVEQGTHEE 555
|
...
gi 1353453005 223 IMR 225
Cdd:COG4987 556 LLA 558
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-218 |
1.03e-34 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 123.46 E-value: 1.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGgITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEqMAKVLSVLR 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 82 QENHFTSRLTVEDLVgfgRY-PWSKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLD 160
Cdd:cd03264 79 QEFGVYPNFTVREFL---DYiAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1353453005 161 EPLNNLDMKHSVAMMKQLRRAADElhKTIILVIHDINFASAYSDHIIAMKQGEVLYRG 218
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELGED--RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-225 |
1.47e-34 |
|
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: 129.88 E-value: 1.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSY-QNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVL 80
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 RQENHFTSrLTVEDLVGFGRypwskgrlTSEDRQHIETAM------DFLDLLPL--------RARyldQLSGGQRQRACV 146
Cdd:COG4988 417 PQNPYLFA-GTIRENLRLGR--------PDASDEELEAALeaagldEFVAALPDgldtplgeGGR---GLSGGQAQRLAL 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1353453005 147 AMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADelHKTIILVIHDINFASAYsDHIIAMKQGEVLYRGTPQEIMR 225
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQA-DRILVLDDGRIVEQGTHEELLA 560
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-223 |
4.10e-34 |
|
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: 122.23 E-value: 4.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQN--TTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMaKVLSV 79
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAAR-QSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 LRQENHFTSRLTVED-LVGFGRYpwsKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVL 158
Cdd:cd03263 80 CPQFDALFDELTVREhLRFYARL---KGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1353453005 159 LDEPLNNLD--MKHSV-AMMKQLRRaadelHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:cd03263 157 LDEPTSGLDpaSRRAIwDLILEVRK-----GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-214 |
4.25e-34 |
|
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: 122.25 E-value: 4.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEqmakvLSVLR 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKN-----INELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 82 QE-----NHFT--SRLTVEDLVGFGryP-WSKGRltsEDRQHIETAMDFLDLLPLRAR---YLDQLSGGQRQRACVAMVL 150
Cdd:cd03262 76 QKvgmvfQQFNlfPHLTVLENITLA--PiKVKGM---SKAEAEERALELLEKVGLADKadaYPAQLSGGQQQRVAIARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1353453005 151 CQNTDYVLLDEPLNNLD--MKHSV-AMMKQLrraADElHKTIILVIHDINFASAYSDHIIAMKQGEV 214
Cdd:cd03262 151 AMNPKVMLFDEPTSALDpeLVGEVlDVMKDL---AEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-214 |
4.33e-34 |
|
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: 121.98 E-value: 4.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTP--DEQMAKVLsv 79
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPpkDRDIAMVF-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 lrQENHFTSRLTVEDLVGFGRypwsKGRLTSED--RQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYV 157
Cdd:cd03301 79 --QNYALYPHMTVYDNIAFGL----KLRKVPKDeiDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1353453005 158 LLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEV 214
Cdd:cd03301 153 LMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-225 |
7.25e-34 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 125.22 E-value: 7.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQmaKVLSVLR 81
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--RDICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 82 QENHFTSRLTVEDLVGFGRYpwSKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDE 161
Cdd:PRK11432 85 QSYALFPHMSLGENVGYGLK--MLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1353453005 162 PLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMR 225
Cdd:PRK11432 163 PLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYR 226
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-224 |
2.26e-33 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 120.97 E-value: 2.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEV--AKTPDEQMAKVLS 78
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 79 VLRQENHFTSRLTVEDLVGFGryPWSKGRLTSEDRQhiETAMDFLDLLPLRAR---YLDQLSGGQRQRACVAMVLCQNTD 155
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFG--PLRVRGASKEEAE--KQARELLAKVGLAERahhYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1353453005 156 YVLLDEPLNNLD--MKHSV-AMMKQLrraADElHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIM 224
Cdd:PRK09493 157 LMLFDEPTSALDpeLRHEVlKVMQDL---AEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLI 224
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-225 |
7.41e-33 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 121.35 E-value: 7.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQN-TTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQmakvlsv 79
Cdd:COG1125 1 MIEFENVTKRYPDgTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVE------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 LR-------QEN----HftsrLTVED-------LVGfgrypWSKGRLtsedRQHIETAMDFLDLLP--LRARYLDQLSGG 139
Cdd:COG1125 74 LRrrigyviQQIglfpH----MTVAEniatvprLLG-----WDKERI----RARVDELLELVGLDPeeYRDRYPHELSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 140 QRQRACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGT 219
Cdd:COG1125 141 QQQRVGVARALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDT 220
|
....*.
gi 1353453005 220 PQEIMR 225
Cdd:COG1125 221 PEEILA 226
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-223 |
3.03e-32 |
|
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: 117.47 E-value: 3.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEqMAKVLSVLR 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE-VRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 82 QENHFTSRLT-VEDLVGFGR---YPWSkgrltsEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYV 157
Cdd:cd03265 80 QDLSVDDELTgWENLYIHARlygVPGA------ERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1353453005 158 LLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-223 |
3.78e-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: 117.68 E-value: 3.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNT----TVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQM--- 73
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 74 -AKVLSVLRQENHFTSRlTVEDLVGfgrYP-----WSKgrltSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVA 147
Cdd:cd03258 81 rRRIGMIFQHFNLLSSR-TVFENVA---LPleiagVPK----AEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1353453005 148 MVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:cd03258 153 RALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-223 |
3.96e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 118.80 E-value: 3.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQN-TTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGlevakTPDEQMAKVLSV 79
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDG-----KPIDYSRKGLMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 LRQ---------ENHFTSRLTVEDlVGFGryPWSKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVL 150
Cdd:PRK13636 80 LREsvgmvfqdpDNQLFSASVYQD-VSFG--AVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1353453005 151 CQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-231 |
5.65e-32 |
|
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: 117.01 E-value: 5.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKV-LSV 79
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 LRQENHFTSRLTVED---LVGFGRypwskgrltsEDRQHIETAMDF-LDLLP-LRARyLDQ----LSGGQRQRACVAMVL 150
Cdd:COG0410 83 VPEGRRIFPSLTVEEnllLGAYAR----------RDRAEVRADLERvYELFPrLKER-RRQragtLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 151 CQNTDYVLLDEPLNNLdmkhSVAMMKQLRRAADELHK---TIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMR-P 226
Cdd:COG0410 152 MSRPKLLLLDEPSLGL----APLIVEEIFEIIRRLNRegvTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLAdP 227
|
....*
gi 1353453005 227 EVIEA 231
Cdd:COG0410 228 EVREA 232
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-224 |
6.16e-32 |
|
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: 116.76 E-value: 6.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKV-LSVL 80
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 RQENHFTSRLTVED--LVGFGRYPWSKGRltsEDRQHIetamdfLDLLP-LRARyLDQ----LSGGQRQRACVAMVLCQN 153
Cdd:cd03224 81 PEGRRIFPELTVEEnlLLGAYARRRAKRK---ARLERV------YELFPrLKER-RKQlagtLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1353453005 154 TDYVLLDEPLNNLdmkhSVAMMKQLRRAADELHK---TIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIM 224
Cdd:cd03224 151 PKLLLLDEPSEGL----APKIVEEIFEAIRELRDegvTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-231 |
6.26e-32 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 116.99 E-value: 6.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVlnRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQmaKVLSVL 80
Cdd:PRK10771 1 MLKLTDITWLYHHLPM--RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR--RPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 RQENHFTSRLTVEDLVGFGRYPwskG-RLTSEDR---QHIETAMDFLDLLPlraRYLDQLSGGQRQRACVAMVLCQNTDY 156
Cdd:PRK10771 77 FQENNLFSHLTVAQNIGLGLNP---GlKLNAAQReklHAIARQMGIEDLLA---RLPGQLSGGQRQRVALARCLVREQPI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1353453005 157 VLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMRPEVIEA 231
Cdd:PRK10771 151 LLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASAS 225
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-214 |
6.61e-32 |
|
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: 116.50 E-value: 6.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 23 SIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQmaKVLSVLRQENHFTSRLTVEDLVGFGRYP 102
Cdd:TIGR01277 20 NVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ--RPVSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 103 WSKgrLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAA 182
Cdd:TIGR01277 98 GLK--LNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLC 175
|
170 180 190
....*....|....*....|....*....|..
gi 1353453005 183 DELHKTIILVIHDINFASAYSDHIIAMKQGEV 214
Cdd:TIGR01277 176 SERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-240 |
1.10e-31 |
|
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: 116.72 E-value: 1.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSG---SVLvnglevaktpDEQMAKVl 77
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLF----------GERRGGE- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 78 SV--LRQE---------NHFTSRLTVEDLV--GF----GRYPwskgRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQ 140
Cdd:COG1119 72 DVweLRKRiglvspalqLRFPRDETVLDVVlsGFfdsiGLYR----EPTDEQRERARELLELLGLAHLADRPFGTLSQGE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 141 RQRACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTP 220
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPK 227
|
250 260
....*....|....*....|
gi 1353453005 221 QEIMRPEVIEAIFDTKVHIE 240
Cdd:COG1119 228 EEVLTSENLSEAFGLPVEVE 247
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-214 |
1.13e-31 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 115.43 E-value: 1.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 3 EVKAICKSY-QNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGlevAKTPDEQMAKVLSVLR 81
Cdd:cd03226 1 RIENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 82 QE---NHFTSrlTVEDLVGFGRypwskgRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVL 158
Cdd:cd03226 78 QDvdyQLFTD--SVREELLLGL------KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1353453005 159 LDEPLNNLDMKHSVAMMKQLRRAADElHKTIILVIHDINFASAYSDHIIAMKQGEV 214
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-231 |
1.82e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 116.76 E-value: 1.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQN-TTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEV-AKTPDEQMAKVLSV 79
Cdd:PRK13647 5 IEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVnAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 LRQENHFTSRLTVEDLVGFGryPWSKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLL 159
Cdd:PRK13647 85 FQDPDDQVFSSTVWDDVAFG--PVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1353453005 160 DEPLNNLDMKHSVAMMKQLrraaDELH---KTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMRPEVIEA 231
Cdd:PRK13647 163 DEPMAYLDPRGQETLMEIL----DRLHnqgKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQ 233
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-223 |
2.68e-31 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 118.51 E-value: 2.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQmakvlsvlR 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN--------R 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 82 QENH-FTS-----RLTVEDLVGFGRypwskgRLTSEDRQHIET-AMDFLDLLPLRA---RYLDQLSGGQRQRACVAMVLC 151
Cdd:PRK09452 87 HVNTvFQSyalfpHMTVFENVAFGL------RMQKTPAAEITPrVMEALRMVQLEEfaqRKPHQLSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1353453005 152 QNTDYVLLDEPLNNLDMKHSVAM---MKQLRRaadELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:PRK09452 161 NKPKVLLLDESLSALDYKLRKQMqneLKALQR---KLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-213 |
5.01e-31 |
|
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: 112.86 E-value: 5.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTT--VLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSV 79
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 LRQENHFTSRlTVEDLVgfgrypwskgrltsedrqhietamdfldllplraryldqLSGGQRQRACVAMVLCQNTDYVLL 159
Cdd:cd03228 81 VPQDPFLFSG-TIRENI---------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1353453005 160 DEPLNNLDMKHSVAMMKQLRRAADElhKTIILVIHDINfASAYSDHIIAMKQGE 213
Cdd:cd03228 121 DEATSALDPETEALILEALRALAKG--KTVIVIAHRLS-TIRDADRIIVLDDGR 171
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-214 |
1.95e-30 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 112.84 E-value: 1.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQN-TTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKvlsv 79
Cdd:COG2884 1 MIRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPY---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 LR-------QENHFTSRLTVEDLVGFG-RYpwsKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLC 151
Cdd:COG2884 77 LRrrigvvfQDFRLLPDRTVYENVALPlRV---TGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1353453005 152 QNTDYVLLDEPLNNLDMKHSVAMMKQLrraaDELHK---TIILVIHDINFASAYSDHIIAMKQGEV 214
Cdd:COG2884 154 NRPELLLADEPTGNLDPETSWEIMELL----EEINRrgtTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-218 |
6.04e-30 |
|
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: 111.31 E-value: 6.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTT----VLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKv 76
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 77 LSVLRQENHFTSRLTV-EDLVGFGRYPWSKGRltsEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTD 155
Cdd:cd03266 80 LGFVSDSTGLYDRLTArENLEYFAGLYGLKGD---ELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1353453005 156 YVLLDEPLNNLDMKhSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRG 218
Cdd:cd03266 157 VLLLDEPTTGLDVM-ATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-225 |
6.60e-30 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 114.41 E-value: 6.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAK--TPDEQMAKVLsv 79
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRlhARDRKVGFVF-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 lrQENHFTSRLTVEDLVGFGR--YPWSKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYV 157
Cdd:PRK10851 81 --QHYALFRHMTVFDNIAFGLtvLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1353453005 158 LLDEPLNNLDMKhsvaMMKQLRRAADELHK----TIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMR 225
Cdd:PRK10851 159 LLDEPFGALDAQ----VRKELRRWLRQLHEelkfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWR 226
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
27-225 |
6.67e-30 |
|
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: 112.74 E-value: 6.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 27 GGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKV----LSVLRQenHFT--SRLTVEDLVGFGR 100
Cdd:cd03294 50 GEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQ--SFAllPHRTVLENVAFGL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 101 YpwSKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRR 180
Cdd:cd03294 128 E--VQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLR 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1353453005 181 AADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMR 225
Cdd:cd03294 206 LQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-224 |
3.13e-29 |
|
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: 115.70 E-value: 3.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSY--QNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSV 79
Cdd:COG2274 474 IELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 LRQENHFTSRlTVEDLVGFGRypwskgrlTSEDRQHIETA------MDFLDLLPLRaryLD--------QLSGGQRQRAC 145
Cdd:COG2274 554 VLQDVFLFSG-TIRENITLGD--------PDATDEEIIEAarlaglHDFIEALPMG---YDtvvgeggsNLSGGQRQRLA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1353453005 146 VAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADelHKTIILVIHDINFAsAYSDHIIAMKQGEVLYRGTPQEIM 224
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEELL 697
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-218 |
4.01e-29 |
|
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: 109.31 E-value: 4.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 27 GGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNG---LEVAK---TPDEQMAkvLSVLRQENHFTSRLTVEDLVGFGr 100
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSRKkinLPPQQRK--IGLVFQQYALFPHLNVRENLAFG- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 101 ypwSKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRR 180
Cdd:cd03297 100 ---LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQ 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 1353453005 181 AADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRG 218
Cdd:cd03297 177 IKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-225 |
4.40e-29 |
|
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: 112.51 E-value: 4.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 20 ITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAK------TPDEQMAkvLSVLRQENHFTSRLTVE 93
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKRR--IGYVFQEARLFPHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 94 DLVGFGRYpwskgRLTSEDRQHIETAM-DFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMKHSV 172
Cdd:TIGR02142 94 GNLRYGMK-----RARPSERRISFERViELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1353453005 173 AMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMR 225
Cdd:TIGR02142 169 EILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-232 |
7.75e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 110.08 E-value: 7.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTT--VLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLS 78
Cdd:PRK13632 7 MIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 79 VLRQ--ENHFTSrLTVEDLVGFG----RYPWSKGRLTSEDRQHIETAMDFLDLLPLraryldQLSGGQRQRACVAMVLCQ 152
Cdd:PRK13632 87 IIFQnpDNQFIG-ATVEDDIAFGlenkKVPPKKMKDIIDDLAKKVGMEDYLDKEPQ------NLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 153 NTDYVLLDEPLNNLDMKHS---VAMMKQLRRAADelhKTIILVIHDINFAsAYSDHIIAMKQGEVLYRGTPQEIMR-PEV 228
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKreiKKIMVDLRKTRK---KTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEILNnKEI 235
|
....
gi 1353453005 229 IEAI 232
Cdd:PRK13632 236 LEKA 239
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-223 |
8.11e-29 |
|
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: 108.96 E-value: 8.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNrITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQmaKVLSVLR 81
Cdd:cd03299 1 LKVENLSKDWKEFKLKN-VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 82 QENHFTSRLTVEDLVGFGRypwskgRLTSEDRQHIETAMD----FLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYV 157
Cdd:cd03299 78 QNYALFPHMTVYKNIAYGL------KKRKVDKKEIERKVLeiaeMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKIL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1353453005 158 LLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:cd03299 152 LLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEV 217
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-214 |
1.20e-28 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 107.59 E-value: 1.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVLR 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 82 QEnhftSRL---TVEDLVgfgRYPWSkgrlTSEDRQHIETAMDFLDLLPLRARYLDQ----LSGGQRQRACVAMVLCQNT 154
Cdd:COG4619 81 QE----PALwggTVRDNL---PFPFQ----LRERKFDRERALELLERLGLPPDILDKpverLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1353453005 155 DYVLLDEPLNNLD--MKHSV-AMMKQLRRAADelhKTIILVIHDINFASAYSDHIIAMKQGEV 214
Cdd:COG4619 150 DVLLLDEPTSALDpeNTRRVeELLREYLAEEG---RAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-223 |
2.95e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 108.30 E-value: 2.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTT--VLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLS 78
Cdd:PRK13648 7 IIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 79 VLRQ--ENHFTSRLTVEDlVGFGRypwsKGRLTSEDRQH--IETAMDFLDLLPlRARYLDQ-LSGGQRQRACVAMVLCQN 153
Cdd:PRK13648 87 IVFQnpDNQFVGSIVKYD-VAFGL----ENHAVPYDEMHrrVSEALKQVDMLE-RADYEPNaLSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 154 TDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFAsAYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA-MEADHVIVMNKGTVYKEGTPTEI 229
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-223 |
8.06e-28 |
|
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: 106.11 E-value: 8.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLL-----TADSGSVLVNGLEVAK---TPDEQM 73
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDldvDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 74 AKVLSVLRQENHFtsRLTVEDLVGFGryPWSKGRLTSEDRQHI-ETAMDFLDLLPLRARYLD--QLSGGQRQRACVAMVL 150
Cdd:cd03260 81 RRVGMVFQKPNPF--PGSIYDNVAYG--LRLHGIKLKEELDERvEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1353453005 151 CQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELhkTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-224 |
1.30e-27 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 106.42 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVL 80
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDGELVPADR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 RQENHFTSRLTvedLV--GFGRypWS---------------KGRltsEDRQHIETAMDFLD---LLPLRARYLDQLSGGQ 140
Cdd:COG4598 88 RQLQRIRTRLG---MVfqSFNL--WShmtvlenvieapvhvLGR---PKAEAIERAEALLAkvgLADKRDAYPAHLSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 141 RQRACVAMVLCQNTDYVLLDEPLNNLD---MKHSVAMMKQLrraADElHKTIILVIHDINFASAYSDHIIAMKQGEVLYR 217
Cdd:COG4598 160 QQRAAIARALAMEPEVMLFDEPTSALDpelVGEVLKVMRDL---AEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQ 235
|
....*..
gi 1353453005 218 GTPQEIM 224
Cdd:COG4598 236 GPPAEVF 242
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-225 |
1.64e-27 |
|
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: 108.26 E-value: 1.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 23 SIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGlEV-----AKT--PDEQMAkvLSVLRQENHFTSRLTVEDL 95
Cdd:COG4148 21 TLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG-EVlqdsaRGIflPPHRRR--IGYVFQEARLFPHLSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 96 VGFGRypwsKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRacVAMV--LCQNTDYVLLDEPLNNLDMKHSVA 173
Cdd:COG4148 98 LLYGR----KRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQR--VAIGraLLSSPRLLLMDEPLAALDLARKAE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1353453005 174 MMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMR 225
Cdd:COG4148 172 ILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLS 223
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-229 |
1.66e-27 |
|
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: 105.32 E-value: 1.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKV-LSVL 80
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 RQENHFTSRLTVED---LVGFGRYPWSKGRltsedRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYV 157
Cdd:cd03218 81 PQEASIFRKLTVEEnilAVLEIRGLSKKER-----EEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1353453005 158 LLDEPLNNLDMKhSVA----MMKQLRRaadelhKTIILVIHDINFASAYS--DHIIAMKQGEVLYRGTPQEIMRPEVI 229
Cdd:cd03218 156 LLDEPFAGVDPI-AVQdiqkIIKILKD------RGIGVLITDHNVRETLSitDRAYIIYEGKVLAEGTPEEIAANELV 226
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-223 |
1.87e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 106.35 E-value: 1.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSY---QNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVakTPD---EQMA 74
Cdd:PRK13650 4 IIEVKNLTFKYkedQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL--TEEnvwDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 75 KVLSVLRQ-ENHFTSRlTVEDLVGFGRYpwSKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQN 153
Cdd:PRK13650 82 KIGMVFQNpDNQFVGA-TVEDDVAFGLE--NKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 154 TDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINfASAYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLD-EVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
14-218 |
2.19e-27 |
|
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: 104.17 E-value: 2.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 14 TTVLNRITESIPVGGITSIIGANGAGKSTLLSVIS--RLLTADSGSVLVNGlevAKTPDEQMAKVLSVLRQENHFTSRLT 91
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLING---RPLDKRSFRKIIGYVPQDDILHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 92 VEDlvgfgrypwskgrltsedrqhietAMDFldllplrARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMKHS 171
Cdd:cd03213 99 VRE------------------------TLMF-------AAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1353453005 172 VAMMKQLRRAADElHKTIILVIHdinfASAYS-----DHIIAMKQGEVLYRG 218
Cdd:cd03213 148 LQVMSLLRRLADT-GRTIICSIH----QPSSEifelfDKLLLLSQGRVIYFG 194
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-223 |
2.57e-27 |
|
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: 107.19 E-value: 2.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 32 IIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQmaKVLSVLRQENHFTSRLTVEDLVGFGRypwskgRLTSE 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHL--RHINMVFQSYALFPHMTVEENVAFGL------KMRKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 112 DRQHI-ETAMDFLDLLPLR---ARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHK 187
Cdd:TIGR01187 73 PRAEIkPRVLEALRLVQLEefaDRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGI 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 1353453005 188 TIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:TIGR01187 153 TFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-230 |
2.72e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 105.93 E-value: 2.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQN-TTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNG----------LEVAKT- 68
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikydkkslLEVRKTv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 69 ------PDEQMakvlsvlrqenhFTSrlTVEDLVGFGryPWSKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQ 142
Cdd:PRK13639 81 givfqnPDDQL------------FAP--TVEEDVAFG--PLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 143 RACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRraadELHK---TIILVIHDINFASAYSDHIIAMKQGEVLYRGT 219
Cdd:PRK13639 145 RVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLY----DLNKegiTIIISTHDVDLVPVYADKVYVMSDGKIIKEGT 220
|
250
....*....|..
gi 1353453005 220 PQEIMR-PEVIE 230
Cdd:PRK13639 221 PKEVFSdIETIR 232
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-214 |
3.25e-27 |
|
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: 104.03 E-value: 3.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTV-LNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKV---L 77
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLrrkI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 78 SVLRQENHFTSRLTVEDLVGFGRypwskgRLTSEDRQHI-ETAMDFLDLLPLRAR---YLDQLSGGQRQRACVAMVLCQN 153
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFAL------EVTGVPPREIrKRVPAALELVGLSHKhraLPAELSGGEQQRVAIARAIVNS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1353453005 154 TDYVLLDEPLNNLDMKHSVAMMKQLRRaADELHKTIILVIHDINFASAYSDHIIAMKQGEV 214
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIMNLLKK-INKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-232 |
3.71e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 105.87 E-value: 3.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNR-----ITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEqmaKV 76
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFERralydVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKN---KK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 77 LSVLRQE--------NHFTSRLTVEDLVGFGryPWSKGrLTSEDRQhiETAMDFLDLLPLRARYLDQ----LSGGQRQRA 144
Cdd:PRK13634 80 LKPLRKKvgivfqfpEHQLFEETVEKDICFG--PMNFG-VSEEDAK--QKAREMIELVGLPEELLARspfeLSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 145 CVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRaadeLHK----TIILVIHDINFASAYSDHIIAMKQGEVLYRGTP 220
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYK----LHKekglTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTP 230
|
250
....*....|...
gi 1353453005 221 QEIMR-PEVIEAI 232
Cdd:PRK13634 231 REIFAdPDELEAI 243
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-225 |
7.78e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 104.71 E-value: 7.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTT--VLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVA-KTPDEQMAKVLS 78
Cdd:PRK13635 6 IRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSeETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 79 VLRQ-ENHFTSRlTVEDLVGFGRYPWSKGRLTSEDRqhIETAM------DFLDLLPLRaryldqLSGGQRQRACVAMVLC 151
Cdd:PRK13635 86 VFQNpDNQFVGA-TVQDDVAFGLENIGVPREEMVER--VDQALrqvgmeDFLNREPHR------LSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1353453005 152 QNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFAsAYSDHIIAMKQGEVLYRGTPQEIMR 225
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
1-212 |
2.27e-26 |
|
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: 102.04 E-value: 2.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQN----TTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKV 76
Cdd:TIGR02211 1 LLKCENLGKRYQEgkldTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 77 ----LSVLRQENHFTSRLTVEDLVGFgryPWSKGRLTSEDRQhiETAMDFLDLLPLRAR---YLDQLSGGQRQRACVAMV 149
Cdd:TIGR02211 81 rnkkLGFIYQFHHLLPDFTALENVAM---PLLIGKKSVKEAK--ERAYEMLEKVGLEHRinhRPSELSGGERQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1353453005 150 LCQNTDYVLLDEPLNNLDMKHSVA---MMKQLRRaadELHKTIILVIHDINFAsAYSDHIIAMKQG 212
Cdd:TIGR02211 156 LVNQPSLVLADEPTGNLDNNNAKIifdLMLELNR---ELNTSFLVVTHDLELA-KKLDRVLEMKDG 217
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-233 |
2.84e-26 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 103.04 E-value: 2.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNT-TVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSvL 80
Cdd:PRK15056 7 IVVNDVTVTWRNGhTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVP-Q 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 RQENHFTSRLTVEDLVGFGRYP---WSKgRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYV 157
Cdd:PRK15056 86 SEEVDWSFPVLVEDVVMMGRYGhmgWLR-RAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1353453005 158 LLDEPLNNLDMKHSVAMMKQLRRAADElHKTIILVIHDINFASAYSDHIIaMKQGEVLYRGTPQEIMRPEVIEAIF 233
Cdd:PRK15056 165 LLDEPFTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASGPTETTFTAENLELAF 238
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-223 |
3.39e-26 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 104.39 E-value: 3.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSY----QNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKv 76
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 77 lsvLRQE--------NHFTSRlTVEDLVGFgryP-----WSKgrltsEDRQhiETAMDFLDLLPLRAR---YLDQLSGGQ 140
Cdd:COG1135 80 ---ARRKigmifqhfNLLSSR-TVAENVAL---PleiagVPK-----AEIR--KRVAELLELVGLSDKadaYPSQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 141 RQRACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTP 220
Cdd:COG1135 146 KQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPV 225
|
...
gi 1353453005 221 QEI 223
Cdd:COG1135 226 LDV 228
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-218 |
1.06e-25 |
|
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: 99.98 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKtpDEQMAKVLSVLR 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK--NIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 82 QENHFTSRLTVEDLVGFgrypwsKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDE 161
Cdd:cd03268 79 EAPGFYPNLTARENLRL------LARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1353453005 162 PLNNLDMKhSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRG 218
Cdd:cd03268 153 PTNGLDPD-GIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-216 |
1.12e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 101.32 E-value: 1.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTV-----LNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAK 75
Cdd:COG1101 1 MLELKNLSKTFNPGTVnekraLDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 76 VLSVLRQeNHF--TS-RLTVED--LVGFGR---YPWSKGrLTSEDRQHIETAMDFLDL-LPLRaryLDQ----LSGGQRQ 142
Cdd:COG1101 81 YIGRVFQ-DPMmgTApSMTIEEnlALAYRRgkrRGLRRG-LTKKRRELFRELLATLGLgLENR---LDTkvglLSGGQRQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1353453005 143 RACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLY 216
Cdd:COG1101 156 ALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIIL 229
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-213 |
3.51e-25 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 98.86 E-value: 3.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQ-NTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKV--- 76
Cdd:TIGR02673 1 MIEFHNVSKAYPgGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 77 LSVLRQENHFTSRLTVEDLVGFGRYpwSKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDY 156
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLE--VRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 157 VLLDEPLNNLDMKHSVAMMKQLRRaadeLHK---TIILVIHDINFASAYSDHIIAMKQGE 213
Cdd:TIGR02673 159 LLADEPTGNLDPDLSERILDLLKR----LNKrgtTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-214 |
5.37e-25 |
|
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: 96.73 E-value: 5.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVaktpdeqmakvlsvlr 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 82 qenHFTSRltvedlvgfgrypwskgrltSEDRQH-IETAMdfldllplraryldQLSGGQRQRACVAMVLCQNTDYVLLD 160
Cdd:cd03216 65 ---SFASP--------------------RDARRAgIAMVY--------------QLSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1353453005 161 EPLNNLDMKHSVAMMKQLRRAADElHKTIILVIHDINFASAYSDHIIAMKQGEV 214
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
23-224 |
8.02e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 101.65 E-value: 8.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 23 SIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKV----LSVLRQENHFTSRLTVEDLVGF 98
Cdd:PRK10070 50 AIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPHMTVLDNTAF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 99 GRypwSKGRLTSEDRQhiETAMDFLDLLPLRAR---YLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMM 175
Cdd:PRK10070 130 GM---ELAGINAEERR--EKALDALRQVGLENYahsYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1353453005 176 KQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIM 224
Cdd:PRK10070 205 DELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
12-245 |
8.28e-25 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 98.85 E-value: 8.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 12 QNTTVLNR---ITESIPVGGITSIIGANGAGKSTLLSVISRLLTAdSGSVLVNGLEVAKTPDEQMAKVLSVLRQENHFTS 88
Cdd:PRK03695 4 NDVAVSTRlgpLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 89 RLTVEDLVGFGRYPwskGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQ-------NTDYVLLDE 161
Cdd:PRK03695 83 AMPVFQYLTLHQPD---KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 162 PLNNLDMKHSVAMMKQLRRAAdELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMRPEVIEAIFDTKVHIET 241
Cdd:PRK03695 160 PMNSLDVAQQAALDRLLSELC-QQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVNFRRLD 238
|
....
gi 1353453005 242 LHGQ 245
Cdd:PRK03695 239 VEGH 242
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-249 |
8.71e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 99.49 E-value: 8.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQ-NTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSV 79
Cdd:PRK13652 3 LIETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 LRQ---ENHFTSrlTVEDLVGFGryPWSKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDY 156
Cdd:PRK13652 83 VFQnpdDQIFSP--TVEQDIAFG--PINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 157 VLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEI-MRPEVIeaifdT 235
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIfLQPDLL-----A 233
|
250 260
....*....|....*....|...
gi 1353453005 236 KVH---------IETLHGQHIAI 249
Cdd:PRK13652 234 RVHldlpslpklIRSLQAQGIAI 256
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-245 |
9.83e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 98.93 E-value: 9.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 11 YQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNG--LEVAK----TPDEQMAKVLSVLRQEN 84
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKrgllALRQQVATVFQDPEQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 85 HFTSrltVEDLVGFGRYpwSKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLN 164
Cdd:PRK13638 91 FYTD---IDSDIAFSLR--NLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 165 NLDMKHSVAMMKQLRRAADELHKTIIlVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIM-RPEVIEAIFDTKVHIETLH 243
Cdd:PRK13638 166 GLDPAGRTQMIAIIRRIVAQGNHVII-SSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFaCTEAMEQAGLTQPWLVKLH 244
|
..
gi 1353453005 244 GQ 245
Cdd:PRK13638 245 TQ 246
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-216 |
1.04e-24 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 97.35 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAkvlsVLR 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIG----YLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 82 QENHFTSRLTVED-LVGFGRYpwsKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLD 160
Cdd:cd03269 77 EERGLYPKMKVIDqLVYLAQL---KGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1353453005 161 EPLNNLDmKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGE-VLY 216
Cdd:cd03269 154 EPFSGLD-PVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRaVLY 209
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-222 |
1.80e-24 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 98.16 E-value: 1.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADS---------GSVLVNGLEVAKTPDE 71
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQREGRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 72 QMAKVLSVLRQENhFTSRLTVED--LVG-FGRYPWSKGRL---TSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRAC 145
Cdd:PRK09984 84 SRANTGYIFQQFN-LVNRLSVLEnvLIGaLGSTPFWRTCFswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1353453005 146 VAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQE 222
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
11-225 |
5.05e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 97.54 E-value: 5.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 11 YQNTT-----VLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEV-AKTPDeqmaKVLSVLRQEN 84
Cdd:PRK13646 12 YQKGTpyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKD----KYIRPVRKRI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 85 HFT-----SRL---TVEDLVGFGRYPWSKGRLTSEDRQHiETAMDF------LDLLPLraryldQLSGGQRQRACVAMVL 150
Cdd:PRK13646 88 GMVfqfpeSQLfedTVEREIIFGPKNFKMNLDEVKNYAH-RLLMDLgfsrdvMSQSPF------QMSGGQMRKIAIVSIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1353453005 151 CQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMR 225
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-223 |
5.12e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 97.49 E-value: 5.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKT--------PDEq 72
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEdrrrigylPEE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 73 makvlsvlrqenhftsR-----LTVED-LVGFGRYpwsKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACV 146
Cdd:COG4152 80 ----------------RglypkMKVGEqLVYLARL---KGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 147 AMVLCQNTDYVLLDEPLNNLDmkhSVA---MMKQLRRAADElHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:COG4152 141 IAALLHDPELLILDEPFSGLD---PVNvelLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-206 |
5.19e-24 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 95.63 E-value: 5.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTAD---SGSVLVNGLEVAKTPDEQmaKVL 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQ--RRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 78 SVLRQENHFTSRLTVEDLVGFGrYPWSKGRltSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYV 157
Cdd:COG4136 79 GILFQDDLLFPHLSVGENLAFA-LPPTIGR--AQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRAL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1353453005 158 LLDEPLNNLDMkhsvAMMKQLRR----AADELHKTIILVIHDINFASAYSDHI 206
Cdd:COG4136 156 LLDEPFSKLDA----ALRAQFREfvfeQIRQRGIPALLVTHDEEDAPAAGRVL 204
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-213 |
7.62e-24 |
|
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: 93.28 E-value: 7.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLvnglevaktpdeqmakvlsvlr 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 82 qenhftsrltvedlvgfgrypWSKGrltsedrqhietamdfldllpLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDE 161
Cdd:cd03221 59 ---------------------WGST---------------------VKIGYFEQLSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1353453005 162 PLNNLDMKHSVAMMKQLRraadELHKTIILVIHDINFASAYSDHIIAMKQGE 213
Cdd:cd03221 97 PTNHLDLESIEALEEALK----EYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
3-232 |
7.63e-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: 95.67 E-value: 7.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 3 EVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKV-LSVLR 81
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 82 QENHFTSRLTVED--LVGFGRYPwskgrltsedRQHIETAMDFLDLLP----LRARYLDQLSGGQRQRACVAMVLCQNTD 155
Cdd:TIGR03410 82 QGREIFPRLTVEEnlLTGLAALP----------RRSRKIPDEIYELFPvlkeMLGRRGGDLSGGQQQQLAIARALVTRPK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1353453005 156 YVLLDEPLNNLdmKHSVA--MMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMRPEVIEAI 232
Cdd:TIGR03410 152 LLLLDEPTEGI--QPSIIkdIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKVRRYL 228
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-218 |
7.73e-24 |
|
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: 95.42 E-value: 7.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 16 VLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTAD---SGSVLVNGLEVAKtpdEQMAKVLSVLRQENHFTSRLTV 92
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKP---DQFQKCVAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 93 EDLVGF-----GRYPWSKGRLTSEDRQhieTAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLD 167
Cdd:cd03234 99 RETLTYtailrLPRKSSDAIRKKRVED---VLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1353453005 168 MKHSVAMMKQLRRAADElHKTIILVIHDINfASAYS--DHIIAMKQGEVLYRG 218
Cdd:cd03234 176 SFTALNLVSTLSQLARR-NRIVILTIHQPR-SDLFRlfDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-232 |
1.57e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 96.02 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNT--TVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGS---VLVNGLEV-AKTPDEQMAK 75
Cdd:PRK13640 6 VEFKHVSFTYPDSkkPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLtAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 76 VLSVLRQ-ENHFTSRlTVEDLVGFGRypwskgrltsEDRQHIETAM--------------DFLDLLPlrarylDQLSGGQ 140
Cdd:PRK13640 86 VGIVFQNpDNQFVGA-TVGDDVAFGL----------ENRAVPRPEMikivrdvladvgmlDYIDSEP------ANLSGGQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 141 RQRACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASaYSDHIIAMKQGEVLYRGTP 220
Cdd:PRK13640 149 KQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSP 227
|
250
....*....|...
gi 1353453005 221 QEIM-RPEVIEAI 232
Cdd:PRK13640 228 VEIFsKVEMLKEI 240
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-223 |
1.78e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 95.93 E-value: 1.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQ---NTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVL 77
Cdd:PRK13642 4 ILEVENLVFKYEkesDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 78 SVLRQ--ENHFTSRlTVEDLVGFGRYpwSKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTD 155
Cdd:PRK13642 84 GMVFQnpDNQFVGA-TVEDDVAFGME--NQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1353453005 156 YVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFAsAYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAPSEL 227
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-209 |
2.00e-23 |
|
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: 98.51 E-value: 2.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTT-VLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVL 80
Cdd:TIGR02857 322 LEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 RQENHFTSRlTVEDLVGFGRypwsKGRLTSEDRQHIETA--MDFLDLLPLR-ARYLDQ----LSGGQRQRACVAMVLCQN 153
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIRLAR----PDASDAEIREALERAglDEFVAALPQGlDTPIGEggagLSGGQAQRLALARAFLRD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1353453005 154 TDYVLLDEPLNNLDMKHSVAMMKQLRRAADelHKTIILVIHDINFASAYsDHIIAM 209
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALA-DRIVVL 529
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-195 |
2.72e-23 |
|
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: 98.20 E-value: 2.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSY-QNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVL 80
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 RQENH-FTSrlTVEDLVGFGRypwskGRLTSEDrqhIETAMDFLDLLPLRARYLD-----------QLSGGQRQRACVAM 148
Cdd:TIGR02868 415 AQDAHlFDT--TVRENLRLAR-----PDATDEE---LWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALAR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1353453005 149 VLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADElhKTIILVIHD 195
Cdd:TIGR02868 485 ALLADAPILLLDEPTEHLDAETADELLEDLLAALSG--RTVVLITHH 529
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
14-232 |
3.02e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 95.50 E-value: 3.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 14 TTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTP---DEQMAKVLSVLRQENHFTSRL 90
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKvklSDIRKKVGLVFQYPEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 91 TVEDLVGFGryPWSKGRLTSEDRQHIETAMDF--LDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDM 168
Cdd:PRK13637 100 TIEKDIAFG--PINLGLSEEEIENRVKRAMNIvgLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1353453005 169 KHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMRP-EVIEAI 232
Cdd:PRK13637 178 KGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEvETLESI 242
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-223 |
3.78e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 95.15 E-value: 3.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSY------QNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLE---------- 64
Cdd:PRK13633 4 MIKCKNVSYKYesneesTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDtsdeenlwdi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 65 ------VAKTPDEQMAKVLsvlrqenhftsrltVEDLVGFGryPWSKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSG 138
Cdd:PRK13633 84 rnkagmVFQNPDNQIVATI--------------VEEDVAFG--PENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 139 GQRQRACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFAsAYSDHIIAMKQGEVLYRG 218
Cdd:PRK13633 148 GQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEG 226
|
....*
gi 1353453005 219 TPQEI 223
Cdd:PRK13633 227 TPKEI 231
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-223 |
8.88e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 95.67 E-value: 8.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQmaKVLSVL 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ--RPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 RQENHFTSRLTVEDLVGFGrypWSKGRLT-SEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLL 159
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAFG---LKQDKLPkAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1353453005 160 DEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:PRK11607 174 DEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-218 |
1.03e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 96.29 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 4 VKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGsvlvnglEVAKTPDEQMAkvlsVLRQE 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSG-------EVSIPKGLRIG----YLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 84 NHFTSRLTVEDLV--GFGRYpwskgRLTSEDRQHIETAMDFLDLLPLRA------------------------------R 131
Cdd:COG0488 70 PPLDDDLTVLDTVldGDAEL-----RALEAELEELEAKLAEPDEDLERLaelqeefealggweaearaeeilsglgfpeE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 132 YLDQ----LSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMkHSVA----MMKQLRraadelhKTIILVIHDINFASAYS 203
Cdd:COG0488 145 DLDRpvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLDL-ESIEwleeFLKNYP-------GTVLVVSHDRYFLDRVA 216
|
250
....*....|....*.
gi 1353453005 204 DHIIAMKQGEV-LYRG 218
Cdd:COG0488 217 TRILELDRGKLtLYPG 232
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-214 |
1.21e-22 |
|
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: 92.50 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNT----TVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKV 76
Cdd:COG4181 8 IIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 77 LS-----VLrQENHFTSRLTVEDLVGfgrypwskgrLTSE---DRQHIETAMDFLDLLPLRAR---YLDQLSGGQRQRAC 145
Cdd:COG4181 88 RArhvgfVF-QSFQLLPTLTALENVM----------LPLElagRRDARARARALLERVGLGHRldhYPAQLSGGEQQRVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1353453005 146 VAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFAsAYSDHIIAMKQGEV 214
Cdd:COG4181 157 LARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRL 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-223 |
1.35e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 92.89 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEV-AKTPDEQMAKVLSV 79
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSLSQQKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 LRQE--------NHFTSRLTVEDLVgfgrypwsKGRLT--SEDR-QHIETAMDFLDLLPLRAR---YLDQLSGGQRQRAC 145
Cdd:PRK11264 83 LRQHvgfvfqnfNLFPHRTVLENII--------EGPVIvkGEPKeEATARARELLAKVGLAGKetsYPRRLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1353453005 146 VAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADElHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-223 |
1.43e-22 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 94.48 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQ----NTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQmakv 76
Cdd:PRK11153 1 MIELKNISKVFPqggrTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKE---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 77 LSVLRQE-----NHF---TSRlTVEDLVGFgryPWskgRLTSEDRQHIETAMD-FLDLLPL---RARYLDQLSGGQRQRA 144
Cdd:PRK11153 77 LRKARRQigmifQHFnllSSR-TVFDNVAL---PL---ELAGTPKAEIKARVTeLLELVGLsdkADRYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1353453005 145 CVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEV 228
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
11-218 |
1.62e-22 |
|
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: 92.40 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 11 YQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVLRQENHFTSRL 90
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 91 TVEDLVGFGR--YPWSKGRLtsedRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDM 168
Cdd:cd03267 111 PVIDSFYLLAaiYDLPPARF----KKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1353453005 169 KHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRG 218
Cdd:cd03267 187 VAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-238 |
2.15e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 92.74 E-value: 2.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQN-TTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQ-MAKVLS 78
Cdd:PRK13644 1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQgIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 79 VLRQ--ENHFTSRlTVEDLVGFGryPWSKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDY 156
Cdd:PRK13644 81 IVFQnpETQFVGR-TVEEDLAFG--PENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 157 VLLDEPLNNLDMKHSVAMMKQLRRaadeLH---KTIILVIHDINFASAySDHIIAMKQGEVLYRGTPQEIMR-------- 225
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKK----LHekgKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSdvslqtlg 232
|
250
....*....|....*.
gi 1353453005 226 ---PEVIEAIFDTKVH 238
Cdd:PRK13644 233 ltpPSLIELAENLKMH 248
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-226 |
2.20e-22 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 91.91 E-value: 2.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQ-NTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVL 80
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 RQEnhftsrlTV--EDLVGFG-RYpwskGRLTSEDRQHIETAM-----DFLDLLP------LRARYLdQLSGGQRQRACV 146
Cdd:cd03253 81 PQD-------TVlfNDTIGYNiRY----GRPDATDEEVIEAAKaaqihDKIMRFPdgydtiVGERGL-KLSGGEKQRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 147 AMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADelHKTIILVIHDINFASAySDHIIAMKQGEVLYRGTPQEIMRP 226
Cdd:cd03253 149 ARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAK 225
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-222 |
2.54e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 95.56 E-value: 2.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQN----TTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKv 76
Cdd:PRK10535 4 LLELKDIRRSYPSgeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 77 lsvLRQEN--------HFTSRLTVEDLVGFGRYPWSKGRltsedRQHIETAMDFLDLLPLRAR---YLDQLSGGQRQRAC 145
Cdd:PRK10535 83 ---LRREHfgfifqryHLLSHLTAAQNVEVPAVYAGLER-----KQRLLRAQELLQRLGLEDRveyQPSQLSGGQQQRVS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1353453005 146 VAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHkTIILVIHDINFAsAYSDHIIAMKQGEVLYRGTPQE 222
Cdd:PRK10535 155 IARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGH-TVIIVTHDPQVA-AQAERVIEIRDGEIVRNPPAQE 229
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-225 |
2.88e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 93.23 E-value: 2.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTT-----VLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSV------------------ 58
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 59 LVNGLEVAKTPDEQMAKVLSVLRQ--------ENH-FTSrlTVEDLVGFGryPWSKGRLTSEDRqhiETAMDFLDLLPLR 129
Cdd:PRK13651 83 VLEKLVIQKTRFKKIKKIKEIRRRvgvvfqfaEYQlFEQ--TIEKDIIFG--PVSMGVSKEEAK---KRAAKYIELVGLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 130 ARYLDQ----LSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLrraaDELH---KTIILVIHDINFASAY 202
Cdd:PRK13651 156 ESYLQRspfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIF----DNLNkqgKTIILVTHDLDNVLEW 231
|
250 260
....*....|....*....|...
gi 1353453005 203 SDHIIAMKQGEVLYRGTPQEIMR 225
Cdd:PRK13651 232 TKRTIFFKDGKIIKDGDTYDILS 254
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-214 |
3.01e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 92.05 E-value: 3.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 4 VKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEqmakvLSVLRQE 83
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED-----TRLMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 84 nhftSRL----TVEDLVGFGrypwskgrLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLL 159
Cdd:PRK11247 90 ----ARLlpwkKVIDNVGLG--------LKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1353453005 160 DEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEV 214
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-223 |
3.47e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 91.90 E-value: 3.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLL-----TADSGSVLVNGLEVAKTPDEQMAKV 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 77 LSVLRQENHFTSRLTVEDLVGFG----RYPWSKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQ 152
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGlklnRLVKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAF 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1353453005 153 NTDYVLLDEPLNNLDMKHSV---AMMKQLRRaadelHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAkieSLFLELKK-----DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
9-224 |
3.96e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 91.95 E-value: 3.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 9 KSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEV--AKTPDEQM----AKVLSVLRQ 82
Cdd:PRK10619 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlVRDKDGQLkvadKNQLRLLRT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 83 E-----NHFT--SRLTVedLVGFGRYPWSKGRLTSEDRQhiETAMDFLDLLPL----RARYLDQLSGGQRQRACVAMVLC 151
Cdd:PRK10619 93 RltmvfQHFNlwSHMTV--LENVMEAPIQVLGLSKQEAR--ERAVKYLAKVGIderaQGKYPVHLSGGQQQRVSIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1353453005 152 QNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADElHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIM 224
Cdd:PRK10619 169 MEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-215 |
6.41e-22 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 91.41 E-value: 6.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSY---------QNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDE 71
Cdd:TIGR02769 2 LLEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 72 QMAKV---LSVLRQENH--FTSRLTVEDLVGfgrYPWSKGRLTSEDRQHiETAMDFLDLLPLRARYLD----QLSGGQRQ 142
Cdd:TIGR02769 82 QRRAFrrdVQLVFQDSPsaVNPRMTVRQIIG---EPLRHLTSLDESEQK-ARIAELLDMVGLRSEDADklprQLSGGQLQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1353453005 143 RACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVL 215
Cdd:TIGR02769 158 RINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-225 |
6.52e-22 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 94.08 E-value: 6.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQN-TTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVL 80
Cdd:COG1132 340 IEFENVSFSYPGdRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 RQENHFTSRlTVEDLVGFGRypwskgrlTSEDRQHIETA------MDFLDLLPLRaryLD--------QLSGGQRQRACV 146
Cdd:COG1132 420 PQDTFLFSG-TIRENIRYGR--------PDATDEEVEEAakaaqaHEFIEALPDG---YDtvvgergvNLSGGQRQRIAI 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1353453005 147 AMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADelHKTIILVIHDINFASAySDHIIAMKQGEVLYRGTPQEIMR 225
Cdd:COG1132 488 ARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEELLA 563
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-218 |
8.04e-22 |
|
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: 88.91 E-value: 8.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSY--QNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDeQMAKVLSV 79
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK-ALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 LRQENHFTSRLTVEDLvgfgrypwskGRltsedrqhietamdfldllplraryldQLSGGQRQRACVAMVLCQNTDYVLL 159
Cdd:cd03247 80 LNQRPYLFDTTLRNNL----------GR---------------------------RFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1353453005 160 DEPLNNLDMKHSVAMMKQLRRAADElhKTIILVIHDINfASAYSDHIIAMKQGEVLYRG 218
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIFEVLKD--KTLIWITHHLT-GIEHMDKILFLENGKIIMQG 178
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-219 |
1.03e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.59 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVN-GLEVA------KTPDEQM 73
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGeTVKIGyfdqhqEELDPDK 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 74 aKVLSVLRQENHFTSRLTVEDLVG-FgrypwskgrLTSEDRQHietamdfldllplraRYLDQLSGGQRQRACVAMVLCQ 152
Cdd:COG0488 395 -TVLDELRDGAPGGTEQEVRGYLGrF---------LFSGDDAF---------------KPVGVLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1353453005 153 NTDYVLLDEPLNNLDMkhsvAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEV-LYRGT 219
Cdd:COG0488 450 PPNVLLLDEPTNHLDI----ETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVrEYPGG 513
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-219 |
1.32e-21 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 90.07 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNG--LEVAKTPDEQMAKVL-- 77
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqFDFSQKPSEKAIRLLrq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 78 --SVLRQENHFTSRLTV-EDLVgfgRYPWSKGRLTSEdrQHIETAMDFLDLLPL---RARYLDQLSGGQRQRACVAMVLC 151
Cdd:COG4161 83 kvGMVFQQYNLWPHLTVmENLI---EAPCKVLGLSKE--QAREKAMKLLARLRLtdkADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1353453005 152 QNTDYVLLDEPLNNLDMKhsvaMMKQLRRAADELHKTII---LVIHDINFASAYSDHIIAMKQGEVLYRGT 219
Cdd:COG4161 158 MEPQVLLFDEPTAALDPE----ITAQVVEIIRELSQTGItqvIVTHEVEFARKVASQVVYMEKGRIIEQGD 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-227 |
1.45e-21 |
|
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: 89.85 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 16 VLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVLRQENHFTSRlTVEDL 95
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLFNR-SIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 96 VGFGRYPWSKGRLTSEDRqhIETAMDFLDLLPLRARYL-----DQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMKH 170
Cdd:cd03252 96 IALADPGMSMERVIEAAK--LAGAHDFISELPEGYDTIvgeqgAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYES 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1353453005 171 SVAMMKQLRRAADelHKTIILVIHDINfASAYSDHIIAMKQGEVLYRGTPQEIMRPE 227
Cdd:cd03252 174 EHAIMRNMHDICA--GRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-224 |
1.65e-21 |
|
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: 89.59 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTT-VLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVL 80
Cdd:cd03254 3 IEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 RQENHFTSRLTVEDLvgfgRYpwskGRLTSEDRQHIET-----AMDFLDLLP------LRARYlDQLSGGQRQRACVAMV 149
Cdd:cd03254 83 LQDTFLFSGTIMENI----RL----GRPNATDEEVIEAakeagAHDFIMKLPngydtvLGENG-GNLSQGERQLLAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1353453005 150 LCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADElhKTIILVIHDINfASAYSDHIIAMKQGEVLYRGTPQEIM 224
Cdd:cd03254 154 MLRDPKILILDEATSNIDTETEKLIQEALEKLMKG--RTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-223 |
2.15e-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: 89.06 E-value: 2.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 17 LNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMakvlsVLRQENHFTSRLTVEDLV 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 97 GFGRYPWSKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMK 176
Cdd:TIGR01184 76 ALAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1353453005 177 QLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:TIGR01184 156 ELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEV 202
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-225 |
3.63e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 89.79 E-value: 3.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQ-NTTVLNR----ITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQ--- 72
Cdd:PRK13643 1 MIKFEKVNYTYQpNSPFASRalfdIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 73 -MAKVLSVLRQ--ENHFTSRLTVEDlVGFGryPWSKGrLTSEDRQHIetAMDFLDLLPLRARYLD----QLSGGQRQRAC 145
Cdd:PRK13643 81 pVRKKVGVVFQfpESQLFEETVLKD-VAFG--PQNFG-IPKEKAEKI--AAEKLEMVGLADEFWEkspfELSGGQMRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 146 VAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKqLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMR 225
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQ-LFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-196 |
4.04e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 89.15 E-value: 4.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSY----QNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAkTPDEQMAKV 76
Cdd:COG4525 3 MLTVRHVSVRYpgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT-GPGADRGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 77 LsvlrQENHFTSRLTVEDLVGFGRypwskgRLTSEDRQHI-ETAMDFLDLLPLRA---RYLDQLSGGQRQRACVAMVLCQ 152
Cdd:COG4525 82 F----QKDALLPWLNVLDNVAFGL------RLRGVPKAERrARAEELLALVGLADfarRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1353453005 153 NTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDI 196
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSV 195
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-222 |
4.37e-21 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 92.03 E-value: 4.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 15 TVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTAD---SGSVLVNGLEVAKtpdEQMAKVLSVLRQENHFTSRLT 91
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDA---KEMRAISAYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 92 V-EDLVGFGRYPWSKGRLTSEDRQHIETAMDFLDLLPLR------ARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLN 164
Cdd:TIGR00955 116 VrEHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCAntrigvPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1353453005 165 NLD--MKHSVamMKQLRRAADElHKTIILVIH----DI--NFasaysDHIIAMKQGEVLYRGTPQE 222
Cdd:TIGR00955 196 GLDsfMAYSV--VQVLKGLAQK-GKTIICTIHqpssELfeLF-----DKIILMAEGRVAYLGSPDQ 253
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-225 |
5.85e-21 |
|
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: 89.73 E-value: 5.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQ----NTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLL---TADSGSVLVNGLEVAKTPDEQM 73
Cdd:COG0444 1 LLEVRNLKVYFPtrrgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 74 AKV----LSVLRQENhFTS---RLTVEDLVGFGryPWSKGRLTSEDRQhiETAMDFLDL--LPLRARYLD----QLSGGQ 140
Cdd:COG0444 81 RKIrgreIQMIFQDP-MTSlnpVMTVGDQIAEP--LRIHGGLSKAEAR--ERAIELLERvgLPDPERRLDryphELSGGM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 141 RQRACVAMVLCQNTDYVLLDEPLNNLDMkhSV-----AMMKQLRRaadELHKTIILVIHDINFASAYSDHIIAMKQGEVL 215
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDV--TIqaqilNLLKDLQR---ELGLAILFITHDLGVVAEIADRVAVMYAGRIV 230
|
250
....*....|
gi 1353453005 216 YRGTPQEIMR 225
Cdd:COG0444 231 EEGPVEELFE 240
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
13-212 |
5.94e-21 |
|
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: 87.77 E-value: 5.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 13 NTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGlevaKTPDEQMAKVLSVLRQ-------ENH 85
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN----KNESEPSFEATRSRNRysvayaaQKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 86 FTSRLTVEDLVGFGRyPWSKGRLTS-EDRQHIETAMDFL---DLLPLRARYLDqLSGGQRQRACVAMVLCQNTDYVLLDE 161
Cdd:cd03290 89 WLLNATVEENITFGS-PFNKQRYKAvTDACSLQPDIDLLpfgDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1353453005 162 PLNNLDMKHSVAMMKQ--LRRAADElHKTIILVIHDINFASaYSDHIIAMKQG 212
Cdd:cd03290 167 PFSALDIHLSDHLMQEgiLKFLQDD-KRTLVLVTHKLQYLP-HADWIIAMKDG 217
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-241 |
6.52e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 91.24 E-value: 6.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVA-KTPDEQMAKVLSV 79
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRiRSPRDAIALGIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 LRQenHFT--SRLTV-EDLVgFGRYPWSKGRL-TSEDRQHIETAMDFLDL-LPLRARyLDQLSGGQRQRACVAMVLCQNT 154
Cdd:COG3845 85 VHQ--HFMlvPNLTVaENIV-LGLEPTKGGRLdRKAARARIRELSERYGLdVDPDAK-VEDLSVGEQQRVEILKALYRGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 155 DYVLLDEPLNNLDMKHSVAMMKQLRRAADElHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMRPEVIEAIFD 234
Cdd:COG3845 161 RILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMVG 239
|
....*..
gi 1353453005 235 TKVHIET 241
Cdd:COG3845 240 REVLLRV 246
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-223 |
6.94e-21 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 89.90 E-value: 6.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTT-VLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVL-----VNGLEVAktpDEQMA 74
Cdd:PRK11650 3 GLKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWiggrvVNELEPA---DRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 75 KVLsvlrqEN-----HftsrLTVEDLVGFGRypwsKGRLTSED--RQHIETAMDFLDLLPLRARYLDQLSGGQRQRacVA 147
Cdd:PRK11650 80 MVF-----QNyalypH----MSVRENMAYGL----KIRGMPKAeiEERVAEAARILELEPLLDRKPRELSGGQRQR--VA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1353453005 148 M--VLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:PRK11650 145 MgrAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-240 |
7.64e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.91 E-value: 7.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 17 LNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVN------GLEVAKTPDEQMAKVLSVLRQENHFTSRL 90
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyaipaNLKKIKEVKRLRKEIGLVFQFPEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 91 TVEDLVGFGryPWSKGrltsEDRQHIETAM-DFLDLLPLRARYLD----QLSGGQRQRACVAMVLCQNTDYVLLDEPLNN 165
Cdd:PRK13645 107 TIEKDIAFG--PVNLG----ENKQEAYKKVpELLKLVQLPEDYVKrspfELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1353453005 166 LDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMRPevIEAIfdTKVHIE 240
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN--QELL--TKIEID 251
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
9-213 |
8.29e-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: 87.14 E-value: 8.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 9 KSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGlEVAKTPdeQMAKVLSvlrqenhfts 88
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-SIAYVS--QEPWIQN---------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 89 rLTVEDLVGFGrYPWSKGRLtsedrqhiETAMDF------LDLLPLRarylDQ---------LSGGQRQRACVAMVLCQN 153
Cdd:cd03250 80 -GTIRENILFG-KPFDEERY--------EKVIKAcalepdLEILPDG----DLteigekginLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 154 TDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASaYSDHIIAMKQGE 213
Cdd:cd03250 146 ADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLP-HADQIVVLDNGR 204
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
5-223 |
8.61e-21 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 90.09 E-value: 8.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 5 KAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQmaKVLSVLRQEN 84
Cdd:PRK11000 7 RNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 85 HFTSRLTVEDLVGFGRYPWSKGRltSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLN 164
Cdd:PRK11000 85 ALYPHLSVAENMSFGLKLAGAKK--EEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1353453005 165 NLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:PRK11000 163 NLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-219 |
2.24e-20 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 86.61 E-value: 2.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSG--SVLVNGLEVAKTPDEqmaKVLSV 79
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGtlNIAGNHFDFSKTPSD---KAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 LR-------QENHFTSRLTV-EDLVgfgRYPWSKGRLTSEdrQHIETAMDFLDLLPLRA---RYLDQLSGGQRQRACVAM 148
Cdd:PRK11124 80 LRrnvgmvfQQYNLWPHLTVqQNLI---EAPCRVLGLSKD--QALARAEKLLERLRLKPyadRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1353453005 149 VLCQNTDYVLLDEPLNNLD---MKHSVAMMKQLRraadELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGT 219
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDpeiTAQIVSIIRELA----ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD 224
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-230 |
2.29e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 86.62 E-value: 2.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKV-LSV 79
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 LRQEnhfTS---RLTVED-------LVGFGRypwskgrltSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMV 149
Cdd:COG1137 83 LPQE---ASifrKLTVEDnilavleLRKLSK---------KEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 150 LCQNTDYVLLDEPLNNLDMKhSVA----MMKQLRraadelHKTI-ILVihdinfasaySDH-------II--A--MKQGE 213
Cdd:COG1137 151 LATNPKFILLDEPFAGVDPI-AVAdiqkIIRHLK------ERGIgVLI----------TDHnvretlgICdrAyiISEGK 213
|
250
....*....|....*...
gi 1353453005 214 VLYRGTPQEIMR-PEVIE 230
Cdd:COG1137 214 VLAEGTPEEILNnPLVRK 231
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-225 |
2.63e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 86.67 E-value: 2.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSY----------------------QNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSV 58
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 59 LVNG-----LEVAktpdeqMAkvlsvlrqenhFTSRLTVEDLVGFGrypwskGRLTSEDRQHIETAMD----------FL 123
Cdd:COG1134 84 EVNGrvsalLELG------AG-----------FHPELTGRENIYLN------GRLLGLSRKEIDEKFDeivefaelgdFI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 124 DlLPLRaRYldqlSGGQRQRACVAMVLCQNTDYVLLDEPLNNLD---MKHSVAMMKQLRRAAdelhKTIILVIHDINFAS 200
Cdd:COG1134 141 D-QPVK-TY----SSGMRARLAFAVATAVDPDILLVDEVLAVGDaafQKKCLARIRELRESG----RTVIFVSHSMGAVR 210
|
250 260
....*....|....*....|....*
gi 1353453005 201 AYSDHIIAMKQGEVLYRGTPQEIMR 225
Cdd:COG1134 211 RLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-225 |
2.63e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 89.52 E-value: 2.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAIC-KSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLtADSGSVLVNGLEVAKTPDEQMAKVLSVL 80
Cdd:PRK11174 350 IEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 RQENHftsrL---TVEDLVGFGRYPWSKGRLtsedRQHIETA--MDFLDLLPLRARYL--DQ---LSGGQRQRACVAMVL 150
Cdd:PRK11174 429 GQNPQ----LphgTLRDNVLLGNPDASDEQL----QQALENAwvSEFLPLLPQGLDTPigDQaagLSVGQAQRLALARAL 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1353453005 151 CQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAAdeLHKTIILVIHDINFASAYsDHIIAMKQGEVLYRGTPQEIMR 225
Cdd:PRK11174 501 LQPCQLLLLDEPTASLDAHSEQLVMQALNAAS--RRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQ 572
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-224 |
2.77e-20 |
|
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: 86.13 E-value: 2.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTT--VLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSV 79
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 LRQENHFTSRlTVEDLVGFGRYPWSKGRLtsEDRQHIETAMDFLDLLPLRaryLD--------QLSGGQRQRACVAMVLC 151
Cdd:cd03251 81 VSQDVFLFND-TVAENIAYGRPGATREEV--EEAARAANAHEFIMELPEG---YDtvigergvKLSGGQRQRIAIARALL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1353453005 152 QNTDYVLLDEPLNNLDMKHSvammKQLRRAADEL--HKTIILVIHDINfASAYSDHIIAMKQGEVLYRGTPQEIM 224
Cdd:cd03251 155 KDPPILILDEATSALDTESE----RLVQAALERLmkNRTTFVIAHRLS-TIENADRIVVLEDGKIVERGTHEELL 224
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
16-227 |
3.84e-20 |
|
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: 89.03 E-value: 3.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 16 VLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVLRQENHFTSRlTVEDL 95
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSR-SIRDN 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 96 VGFGRYPWSKGRLTSEDRqhIETAMDFLDLLPlraRYLDQ--------LSGGQRQRACVAMVLCQNTDYVLLDEPLNNLD 167
Cdd:TIGR01846 551 IALCNPGAPFEHVIHAAK--LAGAHDFISELP---QGYNTevgekganLSGGQRQRIAIARALVGNPRILIFDEATSALD 625
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 168 MKHSVAMMKQLRRAADelHKTIILVIHDINfASAYSDHIIAMKQGEVLYRGTPQEIMRPE 227
Cdd:TIGR01846 626 YESEALIMRNMREICR--GRTVIIIAHRLS-TVRACDRIIVLEKGQIAESGRHEELLALQ 682
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-207 |
4.64e-20 |
|
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: 85.92 E-value: 4.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 23 SIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKvlsvlrqenhftSRLTVEDLVgfgryp 102
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKAD------------YEGTVRDLL------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 103 WSKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAA 182
Cdd:cd03237 83 SSITKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFA 162
|
170 180
....*....|....*....|....*
gi 1353453005 183 DELHKTIILVIHDINFASAYSDHII 207
Cdd:cd03237 163 ENNEKTAFVVEHDIIMIDYLADRLI 187
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-208 |
1.40e-19 |
|
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: 87.30 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLV-------------NGLEVAKT 68
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgetvklayvdqsrDALDPNKT 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 69 PDEQMAKVLSVLRQENH-FTSRLTVedlvgfGRYPWSKGrltseDRQhietamdfldllplraRYLDQLSGGQRQRACVA 147
Cdd:TIGR03719 403 VWEEISGGLDIIKLGKReIPSRAYV------GRFNFKGS-----DQQ----------------KKVGQLSGGERNRVHLA 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1353453005 148 MVLCQNTDYVLLDEPLNNLDmkhsVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIA 208
Cdd:TIGR03719 456 KTLKSGGNVLLLDEPTNDLD----VETLRALEEALLNFAGCAVVISHDRWFLDRIATHILA 512
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-199 |
3.42e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 83.98 E-value: 3.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQmakvlSVL 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 RQENHFTSRLTVEDLVGFGRypwskgRLTSEDR-QHIETAMDFLDLLPLR---ARYLDQLSGGQRQRACVAMVLCQNTDY 156
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFGL------QLAGVEKmQRLEIAHQMLKKVGLEgaeKRYIWQLSGGQRQRVGIARALAANPQL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1353453005 157 VLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFA 199
Cdd:PRK11248 150 LLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEA 192
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
27-234 |
3.86e-19 |
|
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: 82.98 E-value: 3.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 27 GGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGlevaKTPDEQMAKVLSV-LRQENHFTSRLTVEDLVGFGR---YP 102
Cdd:TIGR03771 6 GELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAG----ASPGKGWRHIGYVpQRHEFAWDFPISVAHTVMSGRtghIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 103 WSKgRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAA 182
Cdd:TIGR03771 82 WLR-RPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIELA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1353453005 183 DELHkTIILVIHDINFASAYSDHIIAMkQGEVLYRGTPQEIMRPEVIEAIFD 234
Cdd:TIGR03771 161 GAGT-AILMTTHDLAQAMATCDRVVLL-NGRVIADGTPQQLQDPAPWMTTFG 210
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-232 |
4.75e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 85.84 E-value: 4.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVA-KTPDEQMAKVLSV 79
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfRSPRDAQAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 LRQENHFTSRLTVEDLVGFGRYPWSKGRL-TSEDRQHIETAMDFLDL-LPLRARyLDQLSGGQRQracvaMV-----LCQ 152
Cdd:COG1129 84 IHQELNLVPNLSVAENIFLGREPRRGGLIdWRAMRRRARELLARLGLdIDPDTP-VGDLSVAQQQ-----LVeiaraLSR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 153 NTDYVLLDEPLNNLDMKHSVAMMKQLRRAADElHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMRPEVIEAI 232
Cdd:COG1129 158 DARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVRLM 236
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-214 |
6.54e-19 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 82.25 E-value: 6.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSY--QNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSV 79
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 LRQENHFTSRlTVEDLVGFGRypwskgrlTSEDRQHIETAMDFLDLLPLRARY---LD--------QLSGGQRQRACVAM 148
Cdd:cd03245 83 VPQDVTLFYG-TLRDNITLGA--------PLADDERILRAAELAGVTDFVNKHpngLDlqigergrGLSGGQRQAVALAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1353453005 149 VLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADelHKTIILVIHDINFASaYSDHIIAMKQGEV 214
Cdd:cd03245 154 ALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLD-LVDRIIVMDSGRI 216
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-230 |
1.34e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 83.34 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVLR 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 82 QEN---HFTSRltvEDLVGFGRYpwsKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVL 158
Cdd:PRK13536 122 FDNldlEFTVR---ENLLVFGRY---FGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1353453005 159 LDEPLNNLDmKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMRP----EVIE 230
Cdd:PRK13536 196 LDEPTTGLD-PHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEhigcQVIE 270
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
32-225 |
2.09e-18 |
|
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: 83.97 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 32 IIGANGAGKSTLLSVISRLLTAdSGSVLVNGLEVAKTPDEQMAKvlsvLRQE------NHFTS---RLTVEDLVGFG--- 99
Cdd:COG4172 317 LVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDGLSRRALRP----LRRRmqvvfqDPFGSlspRMTVGQIIAEGlrv 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 100 -RYPWSKgrltSEDRQHIETAMDFLDLLP-LRARYLDQLSGGQRQRACVA--MVLcqNTDYVLLDEPLNNLDMkhSVAmm 175
Cdd:COG4172 392 hGPGLSA----AERRARVAEALEEVGLDPaARHRYPHEFSGGQRQRIAIAraLIL--EPKLLVLDEPTSALDV--SVQ-- 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1353453005 176 KQ----LRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMR 225
Cdd:COG4172 462 AQildlLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
9-230 |
2.26e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 82.59 E-value: 2.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 9 KSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVLRQENHFtS 88
Cdd:PRK13631 34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNPYSKKIKNF-K 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 89 RL------------------TVEDLVGFGryPWSKGRLTSEDRQhieTAMDFLDLLPLRARYLD----QLSGGQRQRACV 146
Cdd:PRK13631 113 ELrrrvsmvfqfpeyqlfkdTIEKDIMFG--PVALGVKKSEAKK---LAKFYLNKMGLDDSYLErspfGLSGGQKRRVAI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 147 AMVLCQNTDYVLLDEPLNNLDMKHSVAMMkQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEI-MR 225
Cdd:PRK13631 188 AGILAIQPEILIFDEPTAGLDPKGEHEMM-QLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIfTD 266
|
....*
gi 1353453005 226 PEVIE 230
Cdd:PRK13631 267 QHIIN 271
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
29-220 |
3.23e-18 |
|
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: 83.91 E-value: 3.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 29 ITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDeQMAKVLSVLRQENHFTSRLTVEDLVGFgrYPWSKGRL 108
Cdd:TIGR01257 958 ITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLD-AVRQSLGMCPQHNILFHHLTVAEHILF--YAQLKGRS 1034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 109 TSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLD--MKHSVAMMKQLRRAAdelh 186
Cdd:TIGR01257 1035 WEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDpySRRSIWDLLLKYRSG---- 1110
|
170 180 190
....*....|....*....|....*....|....
gi 1353453005 187 KTIILVIHDINFASAYSDHIIAMKQGEVLYRGTP 220
Cdd:TIGR01257 1111 RTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-231 |
3.50e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 81.19 E-value: 3.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKvLSVL 80
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIAR-MGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 RQENH---FTSRLTVEDLVgFGRYPWSKGRLTS----------EDRQHIETAMDFLD---LLPLRARYLDQLSGGQRQRA 144
Cdd:PRK11300 84 RTFQHvrlFREMTVIENLL-VAQHQQLKTGLFSgllktpafrrAESEALDRAATWLErvgLLEHANRQAGNLAYGQQRRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 145 CVAMVLCQNTDYVLLDEP---LNNLDMKHSVAMMKQLRRaadELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQ 221
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPaagLNPKETKELDELIAELRN---EHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPE 239
|
250
....*....|.
gi 1353453005 222 EIMR-PEVIEA 231
Cdd:PRK11300 240 EIRNnPDVIKA 250
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-227 |
3.51e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 83.34 E-value: 3.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSY--QNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSV 79
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 LRQENHFTSRLTVEDLVgfgrypWSKGRLTSEDRQHIETAMDFLDLL----PLRA------RyldQLSGGQRQRACVAMV 149
Cdd:PRK11160 419 VSQRVHLFSATLRDNLL------LAAPNASDEALIEVLQQVGLEKLLeddkGLNAwlgeggR---QLSGGEQRRLGIARA 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1353453005 150 LCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADelHKTIILVIHDINfASAYSDHIIAMKQGEVLYRGTPQEIMRPE 227
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLT-GLEQFDRICVMDNGQIIEQGTHQELLAQQ 564
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-228 |
3.74e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 81.78 E-value: 3.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVlSVLR 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRV-GVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 82 QENHFTSRLTV-EDLVGFGRYpwsKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLD 160
Cdd:PRK13537 87 QFDNLDPDFTVrENLLVFGRY---FGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1353453005 161 EPLNNLDMKHSVAMMKQLRRAADElHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMRPEV 228
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEI 230
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-227 |
2.07e-17 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 78.74 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSY---QNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLS 78
Cdd:cd03249 1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 79 VLRQENHFTSRlTVEDLVGFGRYPwskgrLTSEDRQHIET---AMDFLDLLP------LRARYLdQLSGGQRQRACVAMV 149
Cdd:cd03249 81 LVSQEPVLFDG-TIAENIRYGKPD-----ATDEEVEEAAKkanIHDFIMSLPdgydtlVGERGS-QLSGGQKQRIAIARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 150 LCQNTDYVLLDEPLNNLDmKHSvamMKQLRRAADELHK--TIILVIHDINfASAYSDHIIAMKQGEVLYRGTPQEIMRPE 227
Cdd:cd03249 154 LLRNPKILLLDEATSALD-AES---EKLVQEALDRAMKgrTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDELMAQK 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-214 |
2.07e-17 |
|
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: 77.26 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTT--VLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSV 79
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 LRQEnhftsrltVEDLVGfgrypwskgrltsedrqhieTAMDFLdllplraryldqLSGGQRQRACVAMVLCQNTDYVLL 159
Cdd:cd03246 81 LPQD--------DELFSG--------------------SIAENI------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1353453005 160 DEPLNNLDMKHSVAMMKQLRRaADELHKTIILVIHDIN-FASAysDHIIAMKQGEV 214
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAA-LKAAGATRIVIAHRPEtLASA--DRILVLEDGRV 173
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-223 |
2.62e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 79.10 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 17 LNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVakTPdEQMAKVLSVLRQ---------ENHFT 87
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHI--TP-ETGNKNLKKLRKkvslvfqfpEAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 88 SRLTVEDlVGFGryPWSKGrlTSEDRQHiETAMDFLDLLPLRARYLD----QLSGGQRQRACVAMVLCQNTDYVLLDEPL 163
Cdd:PRK13641 100 ENTVLKD-VEFG--PKNFG--FSEDEAK-EKALKWLKKVGLSEDLISkspfELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 164 NNLDMKHSVAMMKQLRRAADELHkTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:PRK13641 174 AGLDPEGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
32-209 |
2.95e-17 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 79.39 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 32 IIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKvlsvLRQE------NHFTS---RLTVEDLVGFGryP 102
Cdd:COG4608 49 LVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRP----LRRRmqmvfqDPYASlnpRMTVGDIIAEP--L 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 103 WSKGRLTSEDRQhiETAMDFLDLLPLRARYLD----QLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMkhSV-A---- 173
Cdd:COG4608 123 RIHGLASKAERR--ERVAELLELVGLRPEHADryphEFSGGQRQRIGIARALALNPKLIVCDEPVSALDV--SIqAqvln 198
|
170 180 190
....*....|....*....|....*....|....*.
gi 1353453005 174 MMKQLRraaDELHKTIILVIHDINFASAYSDHIIAM 209
Cdd:COG4608 199 LLEDLQ---DELGLTYLFISHDLSVVRHISDRVAVM 231
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-224 |
3.43e-17 |
|
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: 80.53 E-value: 3.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTT--VLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSV 79
Cdd:TIGR02203 331 VEFRNVTFRYPGRDrpALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 LRQENHFTSRlTVEDLVGFGRypwskgrLTSEDRQHIETA------MDFLDLLPLRaryLDQ--------LSGGQRQRAC 145
Cdd:TIGR02203 411 VSQDVVLFND-TIANNIAYGR-------TEQADRAEIERAlaaayaQDFVDKLPLG---LDTpigengvlLSGGQRQRLA 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 146 VAMVLCQNTDYVLLDEPLNNLDMKHSvammKQLRRAADELHK--TIILVIHDINfASAYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:TIGR02203 480 IARALLKDAPILILDEATSALDNESE----RLVQAALERLMQgrTTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNEL 554
|
.
gi 1353453005 224 M 224
Cdd:TIGR02203 555 L 555
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-224 |
3.74e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 80.45 E-value: 3.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQ--NTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSV 79
Cdd:PRK11176 342 IEFRNVTFTYPgkEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 LRQENH-FTSrlTVEDLVGFGRypwsKGRLTSEDrqhIETA------MDFLDLLPlraRYLDQ--------LSGGQRQRA 144
Cdd:PRK11176 422 VSQNVHlFND--TIANNIAYAR----TEQYSREQ---IEEAarmayaMDFINKMD---NGLDTvigengvlLSGGQRQRI 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 145 CVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLrraaDELHK--TIILVIHDINFASAySDHIIAMKQGEVLYRGTPQE 222
Cdd:PRK11176 490 AIARALLRDSPILILDEATSALDTESERAIQAAL----DELQKnrTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAE 564
|
..
gi 1353453005 223 IM 224
Cdd:PRK11176 565 LL 566
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
8-218 |
5.08e-17 |
|
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: 77.19 E-value: 5.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 8 CKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGlevaktpdeqmaKVLSVLRQENHFT 87
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------------RVSSLLGLGGGFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 88 SRLTVEDLVGF-GRYpwsKGRLTSEDRQHIETAMDFLDL-----LPLRaryldQLSGGQRQRACVAMVLCQNTDYVLLDE 161
Cdd:cd03220 97 PELTGRENIYLnGRL---LGLSRKEIDEKIDEIIEFSELgdfidLPVK-----TYSSGMKARLAFAIATALEPDILLIDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 162 PLNNLD---MKHSVAMMKQLRRAAdelhKTIILVIHDINFASAYSDHIIAMKQGEVLYRG 218
Cdd:cd03220 169 VLAVGDaafQEKCQRRLRELLKQG----KTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
7-212 |
5.94e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 77.16 E-value: 5.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 7 ICKSYQN----TTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKV----LS 78
Cdd:PRK11629 11 LCKRYQEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqkLG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 79 VLRQENHFTSRLTVEDLVGFgryPWSKGRLTSEDRQhiETAMDFLDLLPLRARYL---DQLSGGQRQRACVAMVLCQNTD 155
Cdd:PRK11629 91 FIYQFHHLLPDFTALENVAM---PLLIGKKKPAEIN--SRALEMLAAVGLEHRANhrpSELSGGERQRVAIARALVNNPR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1353453005 156 YVLLDEPLNNLDMKHSVAMMkQLRRAADELHKTIILVI-HDINFASAYSDHiIAMKQG 212
Cdd:PRK11629 166 LVLADEPTGNLDARNADSIF-QLLGELNRLQGTAFLVVtHDLQLAKRMSRQ-LEMRDG 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-229 |
8.12e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.44 E-value: 8.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKV-LSV 79
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 LRQENHFTSRLTVEDLVGFGRYPWSK--GRLTSEDRQHIETAMDFLDLLPLRaRYLDQ----LSGGQRQRACVAMVLCQN 153
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGRHLTKKvcGVNIIDWREMRVRAAMMLLRVGLK-VDLDEkvanLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1353453005 154 TDYVLLDEP---LNNLDMKHSVAMMKQLRRAAdelhKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMRPEVI 229
Cdd:PRK09700 164 AKVIIMDEPtssLTNKEVDYLFLIMNQLRKEG----TAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIV 238
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
7-233 |
9.03e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 76.86 E-value: 9.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 7 ICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTP-DEQMAKVLSVLRQENH 85
Cdd:PRK10895 9 LAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQEAS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 86 FTSRLTVED-LVGFGRYpwsKGRLTSEDRQ-HIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPL 163
Cdd:PRK10895 89 IFRRLSVYDnLMAVLQI---RDDLSAEQREdRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 164 NNLDmKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMRPEVIEAIF 233
Cdd:PRK10895 166 AGVD-PISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVY 234
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-223 |
1.01e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 77.48 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTT-----VLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEV---AKTPD-EQ 72
Cdd:PRK13649 3 INLQNVSYTYQAGTpfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstSKNKDiKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 73 MAKVLSVLRQ--ENHFTSRLTVEDlVGFGryPWSKGrLTSEDRQHIetAMDFLDLLPLRARYLDQ----LSGGQRQRACV 146
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKD-VAFG--PQNFG-VSQEEAEAL--AREKLALVGISESLFEKnpfeLSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 147 AMVLCQNTDYVLLDEPLNNLDMKHSvammKQLRRAADELHK---TIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGR----KELMTLFKKLHQsgmTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
20-226 |
1.26e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 77.99 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 20 ITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNG---LEVAKT---PDEQMaKVLSVLrQEnhftSRL--- 90
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKGiclPPEKR-RIGYVF-QD----ARLfph 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 91 -TVEdlvGFGRYPWSKgrltsEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMK 169
Cdd:PRK11144 91 yKVR---GNLRYGMAK-----SMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1353453005 170 HSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEI-----MRP 226
Cdd:PRK11144 163 RKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVwassaMRP 224
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
2-224 |
2.01e-16 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 78.37 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQN--TTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSV 79
Cdd:TIGR03375 464 IEFRNVSFAYPGqeTPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGY 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 LRQEnhftSRL---TVEDLVGFGRypwskgrLTSEDRQHIETAM-----DFLDLLPL--------RARyldQLSGGQRQR 143
Cdd:TIGR03375 544 VPQD----PRLfygTLRDNIALGA-------PYADDEEILRAAElagvtEFVRRHPDgldmqigeRGR---SLSGGQRQA 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 144 ACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAAdeLHKTIILVIHDINFASaYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:TIGR03375 610 VALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWL--AGKTLVLVTHRTSLLD-LVDRIIVMDNGRIVADGPKDQV 686
|
.
gi 1353453005 224 M 224
Cdd:TIGR03375 687 L 687
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-220 |
2.91e-16 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 75.22 E-value: 2.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNT--TVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSV 79
Cdd:cd03244 3 IEFKNVSLRYRPNlpPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 LRQENH-FTSrlTV-EDLVGFGRYPWSKGRLTSEDRQHIETAMDFLDLLPLR-ARYLDQLSGGQRQRACVAMVLCQNTDY 156
Cdd:cd03244 83 IPQDPVlFSG--TIrSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVvEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1353453005 157 VLLDEPLNNLDMKHSVAMMKQLRRAADelHKTIILVIHDINfASAYSDHIIAMKQGEVLYRGTP 220
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFK--DCTVLTIAHRLD-TIIDSDRILVLDKGRVVEFDSP 221
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-227 |
5.33e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 74.88 E-value: 5.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTAD-----SGSVLVNGLEVAKT---PDEQM 73
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPdvdPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 74 AKVLSVLRQENHFtSRLTVEDLVGFG----RYPWSKGRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMV 149
Cdd:PRK14267 85 REVGMVFQYPNPF-PHLTIYDNVAIGvklnGLVKSKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIARA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1353453005 150 LCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELhkTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMR-PE 227
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFEnPE 240
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
12-220 |
5.92e-16 |
|
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: 75.10 E-value: 5.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 12 QNTTVLNRItesiPV---GGITSIIGANGAGKSTLLSVISrlltadsGSVLVNGLEVAKTPDEQmaKVLSVLRQ---ENH 85
Cdd:cd03236 12 PNSFKLHRL----PVpreGQVLGLVGPNGIGKSTALKILA-------GKLKPNLGKFDDPPDWD--EILDEFRGselQNY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 86 FTSRLtvEDLVGFGRYPWS--------KGRL-----TSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQ 152
Cdd:cd03236 79 FTKLL--EGDVKVIVKPQYvdlipkavKGKVgellkKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALAR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1353453005 153 NTDYVLLDEPLNNLDMKHSVAMMKQLRRAADElHKTIILVIHDINFASAYSDHIiamkqgEVLYrGTP 220
Cdd:cd03236 157 DADFYFFDEPSSYLDIKQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYI------HCLY-GEP 216
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
15-194 |
6.49e-16 |
|
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: 73.68 E-value: 6.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 15 TVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEqMAKVLSVLRQENHFTSRLTVED 94
Cdd:cd03231 14 ALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDS-IARGLLYLGHAPGIKTTLSVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 95 LVGFGRypwskgrlTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDmKHSVAM 174
Cdd:cd03231 93 NLRFWH--------ADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD-KAGVAR 163
|
170 180
....*....|....*....|
gi 1353453005 175 MKQLRRAADELHKTIILVIH 194
Cdd:cd03231 164 FAEAMAGHCARGGMVVLTTH 183
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-223 |
1.28e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 73.93 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 13 NTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTA-DS-----GSVLVNGLEVAKTPDEQMAKVLSVLRQENHF 86
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIyDSkikvdGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 87 TSRLTVEDLVGfgrYPWsKGRLTSEDRQHIETAMDFLDLLPLRARYLD-------QLSGGQRQRACVAMVLCQNTDYVLL 159
Cdd:PRK14246 102 FPHLSIYDNIA---YPL-KSHGIKEKREIKKIVEECLRKVGLWKEVYDrlnspasQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1353453005 160 DEPLNNLDMKHSVAMMKQLRRAADELhkTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
12-224 |
1.62e-15 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 75.46 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 12 QNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVLRQENHFTSRLT 91
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 92 VEDLVGFGRYPwskgrltsEDRQHIETAMdFLDLLPLRARYLD-----------QLSGGQRQRACVAMVLCQNTDYVLLD 160
Cdd:TIGR01842 409 AENIARFGENA--------DPEKIIEAAK-LAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLD 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1353453005 161 EPLNNLDMKHSVAMMKQLRRAADElHKTIILVIHDINFASAySDHIIAMKQGEVLYRGTPQEIM 224
Cdd:TIGR01842 480 EPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLLGC-VDKILVLQDGRIARFGERDEVL 541
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
27-181 |
1.74e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 72.60 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 27 GGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVaktPDEQMAKVLSVLRQENHFTSRLTVEDLVGFgrypWSkg 106
Cdd:PRK13539 28 GEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---DDPDVAEACHYLGHRNAMKPALTVAENLEF----WA-- 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1353453005 107 RLTSEDRQHIETAMDFLDL---LPLRARYldqLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDmKHSVAMMKQLRRA 181
Cdd:PRK13539 99 AFLGGEELDIAAALEAVGLaplAHLPFGY---LSAGQKRRVALARLLVSNRPIWILDEPTAALD-AAAVALFAELIRA 172
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-223 |
1.76e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 74.03 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQM---AKVL 77
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 78 SVLRQENHFTSRLTVEDLVGfgrYPWSKGRLTSEDRQHiETAMDFLDLLPLR-ARYL--DQLSGGQRQRACVAMVLCQNT 154
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVA---YPLREHTQLPAPLLH-STVMMKLEAVGLRgAAKLmpSELSGGMARRAALARAIALEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1353453005 155 DYVLLDEPLNNLD---MKHSVAMMKQLRRAadeLHKTIILVIHDINFASAYSDH--IIAMKQgeVLYRGTPQEI 223
Cdd:PRK11831 163 DLIMFDEPFVGQDpitMGVLVKLISELNSA---LGVTCVVVSHDVPEVLSIADHayIVADKK--IVAHGSAQAL 231
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-207 |
1.99e-15 |
|
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: 75.21 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 23 SIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNgLEVA-K----TPDEQMAkVLSVLRQENhfTSRLTvedlvg 97
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-LKISyKpqyiSPDYDGT-VEEFLRSAN--TDDFG------ 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 98 fgrypwskgrlTSEDRQHIetaMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQ 177
Cdd:COG1245 432 -----------SSYYKTEI---IKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKA 497
|
170 180 190
....*....|....*....|....*....|
gi 1353453005 178 LRRAADELHKTIILVIHDINFASAYSDHII 207
Cdd:COG1245 498 IRRFAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-229 |
2.17e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.22 E-value: 2.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVN-GLEVAKTPdeqmakvlsv 79
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNgKLRIGYVP---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 lrQENHF--TSRLTVEdlvgfgRYPWSKGRLTSEDrqhIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYV 157
Cdd:PRK09544 74 --QKLYLdtTLPLTVN------RFLRLRPGTKKED---ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1353453005 158 LLDEPLNNLDMKHSVA---MMKQLRRaadELHKTIILVIHDINFASAYSDHIIAMKQgEVLYRGTPQEI-MRPEVI 229
Cdd:PRK09544 143 VLDEPTQGVDVNGQVAlydLIDQLRR---ELDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEVVsLHPEFI 214
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-227 |
2.28e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 73.27 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRL--LTAD---SGSVLVNGLEV--AKTPDEQM 73
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIysPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 74 AKVLS-VLRQENHFTsrLTVEDLVGFGRypwskgRLTSEDRQHI-----ETAMDFLDLL-PLRARYLDQ---LSGGQRQR 143
Cdd:PRK14239 85 RKEIGmVFQQPNPFP--MSIYENVVYGL------RLKGIKDKQVldeavEKSLKGASIWdEVKDRLHDSalgLSGGQQQR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 144 ACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELhkTIILVIHDINFASAYSDHIIAMKQGEVL-YRGTPQE 222
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIeYNDTKQM 234
|
....*
gi 1353453005 223 IMRPE 227
Cdd:PRK14239 235 FMNPK 239
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
27-225 |
2.33e-15 |
|
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: 74.84 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 27 GGITSIIGANGAGKSTLLSVISRLLTADSGSVLVN-GLE----VAKTPDEQ--MAKVLSVLRQE-NHFTSRLTVEDL--- 95
Cdd:TIGR03269 310 GEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEwvdmTKPGPDGRgrAKRYIGILHQEyDLYPHRTVLDNLtea 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 96 VGFgRYPWSKGRLT----------SEDRqhietAMDFLDllplraRYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNN 165
Cdd:TIGR03269 390 IGL-ELPDELARMKavitlkmvgfDEEK-----AEEILD------KYPDELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 166 LDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMR 225
Cdd:TIGR03269 458 MDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-224 |
4.13e-15 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 74.39 E-value: 4.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQ-NTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVL 80
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 RQENHFTSRLTVEDLVgFGrypwSKGRLTSEDrqhIETAMDFLDL------LPLR-----ARYLDQLSGGQRQRACVAMV 149
Cdd:TIGR01193 554 PQEPYIFSGSILENLL-LG----AKENVSQDE---IWAACEIAEIkddienMPLGyqtelSEEGSSISGGQKQRIALARA 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1353453005 150 LCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADelhKTIILVIHDINFASAySDHIIAMKQGEVLYRGTPQEIM 224
Cdd:TIGR01193 626 LLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD---KTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELL 696
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-241 |
6.20e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 72.44 E-value: 6.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 11 YQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTA-----DSGSVLVNGLEVAKTPD--EQMAKVLSVLRQE 83
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRDvlEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 84 NHFTSRLTVEDLVGFGRY---PWSKGRLTSEDRQH----IETAMDFLDLLPLRaryldqLSGGQRQRACVAMVLCQNTDY 156
Cdd:PRK14271 111 NPFPMSIMDNVLAGVRAHklvPRKEFRGVAQARLTevglWDAVKDRLSDSPFR------LSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 157 VLLDEPLNNLDMKHSVAMMKQLRRAADELhkTIILVIHDINFASAYSDHIIAMKQGEVLYRGTpqeimrpevIEAIFDTK 236
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRLVEEGP---------TEQLFSSP 253
|
....*
gi 1353453005 237 VHIET 241
Cdd:PRK14271 254 KHAET 258
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-207 |
7.77e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 73.69 E-value: 7.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 24 IPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNgLEVA-K----TPDEQMakvlsvlrqenhftsrlTVEDLVGF 98
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISyKpqyiKPDYDG-----------------TVEDLLRS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 99 grypwSKGRLTSEdrQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQL 178
Cdd:PRK13409 424 -----ITDDLGSS--YYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAI 496
|
170 180
....*....|....*....|....*....
gi 1353453005 179 RRAADELHKTIILVIHDINFASAYSDHII 207
Cdd:PRK13409 497 RRIAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
10-214 |
8.78e-15 |
|
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: 71.35 E-value: 8.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 10 SYQN---TTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVLRQENHF 86
Cdd:cd03248 20 AYPTrpdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 87 TSRlTVEDLVGFGRYPWSKGRLT-SEDRQHietAMDFLDLLPLrARYLD------QLSGGQRQRACVAMVLCQNTDYVLL 159
Cdd:cd03248 100 FAR-SLQDNIAYGLQSCSFECVKeAAQKAH---AHSFISELAS-GYDTEvgekgsQLSGGQKQRVAIARALIRNPQVLIL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1353453005 160 DEPLNNLDMKhSVAMMKQLRRAADELHkTIILVIHDINFASaYSDHIIAMKQGEV 214
Cdd:cd03248 175 DEATSALDAE-SEQQVQQALYDWPERR-TVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-233 |
9.74e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 71.45 E-value: 9.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQ-MAKVLSV 79
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 LRQENHFTSRLTVEDLVGFGRYPWSKgrltSEDRQHIETAMD-FLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVL 158
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMGGFFAER----DQFQERIKWVYElFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1353453005 159 LDEP---LNNLDMKHSVAMMKQLRraadELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMRPEVIEAIF 233
Cdd:PRK11614 161 LDEPslgLAPIIIQQIFDTIEQLR----EQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAY 234
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-220 |
9.86e-15 |
|
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: 70.52 E-value: 9.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQN--TTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSV 79
Cdd:cd03369 7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 LRQENHFTSRLTVEDLVGFGRYpwskgrltsEDRQhIETAMDFldllplrARYLDQLSGGQRQRACVAMVLCQNTDYVLL 159
Cdd:cd03369 87 IPQDPTLFSGTIRSNLDPFDEY---------SDEE-IYGALRV-------SEGGLNLSQGQRQLLCLARALLKRPRVLVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1353453005 160 DEPLNNLDMKHSVAMMKQLRraaDELHKTIILVI-HDINFASAYsDHIIAMKQGEVLYRGTP 220
Cdd:cd03369 150 DEATASIDYATDALIQKTIR---EEFTNSTILTIaHRLRTIIDY-DKILVMDAGEVKEYDHP 207
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-242 |
1.23e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 72.04 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSY-------------------QNTTV--LNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVL 59
Cdd:COG4586 1 IIEVENLSKTYrvyekepglkgalkglfrrEYREVeaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 60 VNGLevakTPdeqmakvlsvLRQENHFTSRLTVedlVgFGrypwSKGRL--------------------TSEDRQHIETA 119
Cdd:COG4586 81 VLGY----VP----------FKRRKEFARRIGV---V-FG----QRSQLwwdlpaidsfrllkaiyripDAEYKKRLDEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 120 MDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDmkhsVAMMKQLRRAADELHK----TIILVIHD 195
Cdd:COG4586 139 VELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLD----VVSKEAIREFLKEYNRergtTILLTSHD 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1353453005 196 INFASAYSDHIIAMKQGEVLYRGTPQEI----MRPEVIEAIFDTKVHIETL 242
Cdd:COG4586 215 MDDIEALCDRVIVIDHGRIIYDGSLEELkerfGPYKTIVLELAEPVPPLEL 265
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-214 |
1.61e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 71.26 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNT---------TVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDE 71
Cdd:PRK10419 3 LLNVSGLSHHYAHGglsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 72 QMA---KVLSVLRQE--NHFTSRLTVEDLVgfgRYPWSkgRLTSEDR-QHIETAMDFLDLLPLRARYLD----QLSGGQR 141
Cdd:PRK10419 83 QRKafrRDIQMVFQDsiSAVNPRKTVREII---REPLR--HLLSLDKaERLARASEMLRAVDLDDSVLDkrppQLSGGQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1353453005 142 QRACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEV 214
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-232 |
2.37e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.01 E-value: 2.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAK-TPDEQMAKVLSV 79
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARlTPAKAHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 LRQENHFTSRLTVED--LVGFGRYPWSKGRLTSEDRQ---HIETAMdfldllplRARYLDQlsgGQRQRACVAMVLCQNT 154
Cdd:PRK15439 91 VPQEPLLFPNLSVKEniLFGLPKRQASMQKMKQLLAAlgcQLDLDS--------SAGSLEV---ADRQIVEILRGLMRDS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1353453005 155 DYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKtIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMRPEVIEAI 232
Cdd:PRK15439 160 RILILDEPTASLTPAETERLFSRIRELLAQGVG-IVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDIIQAI 236
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
2-223 |
3.15e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 71.67 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVLR 81
Cdd:PRK10789 316 VNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 82 QENHFTSRlTVEDLVGFGRypwskgrlTSEDRQHIETAMDFL----DLLPLRARYLDQ-------LSGGQRQRACVAMVL 150
Cdd:PRK10789 396 QTPFLFSD-TVANNIALGR--------PDATQQEIEHVARLAsvhdDILRLPQGYDTEvgergvmLSGGQKQRISIARAL 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1353453005 151 CQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADelHKTIILVIHDINfASAYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:PRK10789 467 LLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQL 536
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
14-181 |
3.39e-14 |
|
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: 68.92 E-value: 3.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 14 TTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEqMAKVLSVLRQENHFTSRLTVE 93
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-PHENILYLGHLPGLKPELSAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 94 DLVGFgrypWSkgRLTSEDRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDmKHSVA 173
Cdd:TIGR01189 92 ENLHF----WA--AIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD-KAGVA 164
|
....*...
gi 1353453005 174 MMKQLRRA 181
Cdd:TIGR01189 165 LLAGLLRA 172
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-224 |
3.72e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 71.68 E-value: 3.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQN---TTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLS 78
Cdd:TIGR00958 479 IEFQDVSFSYPNrpdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 79 VLRQENHFTSRlTVEDLVGFGRYPWSKGRLTSEDRQhiETAMDFLDLLPLR-----ARYLDQLSGGQRQRACVAMVLCQN 153
Cdd:TIGR00958 559 LVGQEPVLFSG-SVRENIAYGLTDTPDEEIMAAAKA--ANAHDFIMEFPNGydtevGEKGSQLSGGQKQRIAIARALVRK 635
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1353453005 154 TDYVLLDEPLNNLDMKhSVAMMKQLRRAADelhKTIILVIHDINFASAySDHIIAMKQGEVLYRGTPQEIM 224
Cdd:TIGR00958 636 PRVLILDEATSALDAE-CEQLLQESRSRAS---RTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLM 701
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
32-223 |
3.98e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 70.89 E-value: 3.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 32 IIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVLRQ--ENHFTS---RLTVEDLVG-----FgrY 101
Cdd:PRK15079 52 VVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMifQDPLASlnpRMTIGEIIAeplrtY--H 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 102 PwskgRLTSED-RQHIETAMDFLDLLP-LRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMK---HSVAMMK 176
Cdd:PRK15079 130 P----KLSRQEvKDRVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSiqaQVVNLLQ 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1353453005 177 QLRRaadELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:PRK15079 206 QLQR---EMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 249
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
27-218 |
4.66e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 69.57 E-value: 4.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 27 GGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQM--AKVLSVLRQENHFTS-------RLTV----- 92
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseAERRRLLRTEWGFVHqhprdglRMQVsaggn 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 93 --EDLVGFGRYPWSKGRLTSED-RQHIETAMDFLDLLPlrarylDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMK 169
Cdd:PRK11701 112 igERLMAVGARHYGDIRATAGDwLERVEIDAARIDDLP------TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVS 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1353453005 170 HSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRG 218
Cdd:PRK11701 186 VQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-214 |
6.81e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 68.75 E-value: 6.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSY-QNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQ---MAKV 76
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 77 LSVLRQENHFTSRLTVEDLVGFgryPWSKGRLTSED-RQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTD 155
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAI---PLIIAGASGDDiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1353453005 156 YVLLDEPLNNLDMkhsvAMMKQLRRAADELHK---TIILVIHDINFASAYSDHIIAMKQGEV 214
Cdd:PRK10908 158 VLLADEPTGNLDD----ALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
12-225 |
8.60e-14 |
|
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: 70.55 E-value: 8.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 12 QNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVLRQEnhftSRL- 90
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQD----VELf 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 91 --TVEDLVGfgrypwskgRLTSEDRQHIETA------MDFLDLLPLRarYlD--------QLSGGQRQRACVAMVLCQNT 154
Cdd:COG4618 419 dgTIAENIA---------RFGDADPEKVVAAaklagvHEMILRLPDG--Y-DtrigeggaRLSGGQRQRIGLARALYGDP 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1353453005 155 DYVLLDEPLNNLDMKHSVAMMKQLRRAADElHKTIILVIHDINFASAySDHIIAMKQGEVLYRGTPQEIMR 225
Cdd:COG4618 487 RLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLAA-VDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-224 |
1.05e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 70.54 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 17 LNRITESIPVGGITSIIGANGAGKSTLLS-VISRLLTADSGSVLVNGlEVAKTPdeQMAKVLSVlrqenhftsrlTVEDL 95
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG-TVAYVP--QVSWIFNA-----------TVRDN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 96 VGFG------RYpWSKGRLTSEDRQhietamdfLDLLP------LRARYLDqLSGGQRQRACVAMVLCQNTDYVLLDEPL 163
Cdd:PLN03130 699 ILFGspfdpeRY-ERAIDVTALQHD--------LDLLPggdlteIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPL 768
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1353453005 164 NNLDMKhsVAMMKQLRRAADEL-HKTIILVIHDINFASaYSDHIIAMKQGEVLYRGTPQEIM 224
Cdd:PLN03130 769 SALDAH--VGRQVFDKCIKDELrGKTRVLVTNQLHFLS-QVDRIILVHEGMIKEEGTYEELS 827
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-167 |
1.53e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 69.76 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVlvnglEVAKTpdeqmAKVLSVLR 81
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI-----KIGET-----VKLAYVDQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 82 QENHFTSRLTVedlvgfgrypWskgrltsedrQHIETAMDFLDL----LPLRArYL--------DQ------LSGGQRQR 143
Cdd:PRK11819 395 SRDALDPNKTV----------W----------EEISGGLDIIKVgnreIPSRA-YVgrfnfkggDQqkkvgvLSGGERNR 453
|
170 180
....*....|....*....|....
gi 1353453005 144 ACVAMVLCQNTDYVLLDEPLNNLD 167
Cdd:PRK11819 454 LHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
12-218 |
2.02e-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: 66.88 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 12 QNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTAD--SGSVLVNGLEVAKTpdeqMAKVLSVLRQENHFTSR 89
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDKN----FQRSTGYVEQQDVHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 90 LTVEDLVGFGRYpwskgrltsedrqhietamdfldllpLRAryldqLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMK 169
Cdd:cd03232 94 LTVREALRFSAL--------------------------LRG-----LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1353453005 170 HSVAMMKQLRRAADElHKTIILVIH----DInFasAYSDHIIAMKQ-GEVLYRG 218
Cdd:cd03232 143 AAYNIVRFLKKLADS-GQAILCTIHqpsaSI-F--EKFDRLLLLKRgGKTVYFG 192
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-212 |
2.62e-13 |
|
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: 67.07 E-value: 2.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSY----QNTT---VLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVN----GLEVAKTP 69
Cdd:COG4778 4 LLEVENLSKTFtlhlQGGKrlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 70 DEQMakvLSVLRQENHFTS-------RLTVEDLVGFGRYPWSKGRLTSEDRqhietAMDFLDLLPLRARyLDQL-----S 137
Cdd:COG4778 84 PREI---LALRRRTIGYVSqflrvipRVSALDVVAEPLLERGVDREEARAR-----ARELLARLNLPER-LWDLppatfS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1353453005 138 GGQRQRACVAMVLCQNTDYVLLDEPLNNLDMKHS---VAMMKQLRRAAdelhKTIILVIHDINFASAYSDHIIAMKQG 212
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRavvVELIEEAKARG----TAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
14-210 |
2.93e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.91 E-value: 2.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 14 TTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTadsgsvlvnglevaKTPDEQMAKVlsvlrQENHFTSRLTVE 93
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK--------------GTPVAGCVDV-----PDNQFGREASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 94 DLVGfgrypwskgrltseDRQHIETAMDFL------DLLPLRARYlDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLD 167
Cdd:COG2401 104 DAIG--------------RKGDFKDAVELLnavglsDAVLWLRRF-KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1353453005 168 MKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMK 210
Cdd:COG2401 169 RQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIFV 211
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-224 |
3.07e-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: 69.20 E-value: 3.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 17 LNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGlEVAKTPdeQMAKVLSVLRQENhftsrltvedlV 96
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-SVAYVP--QQAWIQNDSLREN-----------I 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 97 GFGRyPWSKGRLtsedRQHIETAMDFLDLLPLRARylDQ---------LSGGQRQRACVAMVLCQNTDYVLLDEPLNNLD 167
Cdd:TIGR00957 720 LFGK-ALNEKYY----QQVLEACALLPDLEILPSG--DRteigekgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1353453005 168 -------MKHSVAMMKQLRraadelHKTIILVIHDINFASAySDHIIAMKQGEVLYRGTPQEIM 224
Cdd:TIGR00957 793 ahvgkhiFEHVIGPEGVLK------NKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQELL 849
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-212 |
3.53e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.40 E-value: 3.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 3 EVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVA-KTPDEQMAKVLSVLR 81
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVAIIY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 82 QENHFTSRLTVEDLVGFGRYPWSKGRLTSedRQHIETAMDFLDLLPLR---ARYLDQLSGGQRQRACVAMVLCQNTDYVL 158
Cdd:PRK11288 86 QELHLVPEMTVAENLYLGQLPHKGGIVNR--RLLNYEAREQLEHLGVDidpDTPLKYLSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1353453005 159 LDEPLNNLDMKHSVAMMKQLRRAADElHKTIILVIHDINFASAYSDHIIAMKQG 212
Cdd:PRK11288 164 FDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-223 |
5.00e-13 |
|
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: 68.17 E-value: 5.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 12 QNTTVLNRITESIPVGGITSIIGANGAGKS-TLLSVIsRLLTAD----SGSVLVNGLEVAKTPDEQMAKV----LSVLRQ 82
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLLPDPaahpSGSILFDGQDLLGLSERELRRIrgnrIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 83 E-----N--HftsrlTVEDLV--------GFGRypwskgrltSEDRQHIetamdfLDLL-------PLR--ARYLDQLSG 138
Cdd:COG4172 100 EpmtslNplH-----TIGKQIaevlrlhrGLSG---------AAARARA------LELLervgipdPERrlDAYPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 139 GQRQRACVAMVLCQNTDYVLLDEPLNNLDMkhSV-----AMMKQLRRaadELHKTIILVIHDINFASAYSDHIIAMKQGE 213
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALDV--TVqaqilDLLKDLQR---ELGMALLLITHDLGVVRRFADRVAVMRQGE 234
|
250
....*....|
gi 1353453005 214 VLYRGTPQEI 223
Cdd:COG4172 235 IVEQGPTAEL 244
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
9-224 |
5.74e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.98 E-value: 5.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 9 KSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADS--GSVLVNGLEVAKtpdeQMAKVLSVLRQENHF 86
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK----QILKRTGFVTQDDIL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 87 TSRLTVEDLVGFG---RYPWSkgrLTSEDRQHI-ETAMDFLDLLP-----LRARYLDQLSGGQRQRACVAMVLCQNTDYV 157
Cdd:PLN03211 152 YPHLTVRETLVFCsllRLPKS---LTKQEKILVaESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLL 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1353453005 158 LLDEPLNNLDMKHSVAMMKQLRRAADElHKTIILVIHDINfASAYS--DHIIAMKQGEVLYRGTPQEIM 224
Cdd:PLN03211 229 ILDEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQPS-SRVYQmfDSVLVLSEGRCLFFGKGSDAM 295
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-230 |
8.78e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 67.22 E-value: 8.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVlvNGLEVAKtpdeqmakvLSVLR 81
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--KWSENAN---------IGYYA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 82 Q--ENHFTSRLTVEDlvgfgrypW-SKGRLTSEDRQHIETAMDFL----DLLPLRARYLdqlSGGQRQRACVAMVLCQNT 154
Cdd:PRK15064 389 QdhAYDFENDLTLFD--------WmSQWRQEGDDEQAVRGTLGRLlfsqDDIKKSVKVL---SGGEKGRMLFGKLMMQKP 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1353453005 155 DYVLLDEPLNNLDMKHsvamMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMK-QGEVLYRGTPQEIMRPEVIE 230
Cdd:PRK15064 458 NVLVMDEPTNHMDMES----IESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITpDGVVDFSGTYEEYLRSQGIE 530
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
31-200 |
1.00e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 65.57 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 31 SIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKvlsvLRQEN---HFTSRLTVEDLVGFGRYPWSKGR 107
Cdd:PRK10584 40 ALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAK----LRAKHvgfVFQSFMLIPTLNALENVELPALL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 108 LTSEDRQHIETAMDFLDLLPL--RARYLD-QLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADE 184
Cdd:PRK10584 116 RGESSRQSRNGAKALLEQLGLgkRLDHLPaQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNRE 195
|
170
....*....|....*.
gi 1353453005 185 LHKTIILVIHDINFAS 200
Cdd:PRK10584 196 HGTTLILVTHDLQLAA 211
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-227 |
1.06e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 67.69 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 32 IIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVLRQenhftSRLTVEDLVGFGRYPWSK----GR 107
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQ-----SPVLFSGTVRFNIDPFSEhndaDL 1341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 108 LTSEDRQHIETAMDfLDLLPLRARYL---DQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRraaDE 184
Cdd:PLN03232 1342 WEALERAHIKDVID-RNPFGLDAEVSeggENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIR---EE 1417
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1353453005 185 LHKTIILVI-HDINfASAYSDHIIAMKQGEVLYRGTPQEIMRPE 227
Cdd:PLN03232 1418 FKSCTMLVIaHRLN-TIIDCDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-224 |
1.44e-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: 67.28 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTT--VLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSV 79
Cdd:TIGR00957 1285 VEFRNYCLRYREDLdlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITI 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 LRQENHFTSRLTVEDLVGFGRYP----WskgrlTSEDRQHIEtamDFLDLLPLR-----ARYLDQLSGGQRQRACVAMVL 150
Cdd:TIGR00957 1365 IPQDPVLFSGSLRMNLDPFSQYSdeevW-----WALELAHLK---TFVSALPDKldhecAEGGENLSVGQRQLVCLARAL 1436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1353453005 151 CQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELhkTIILVIHDINFASAYSdHIIAMKQGEVLYRGTPQEIM 224
Cdd:TIGR00957 1437 LRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDC--TVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLL 1507
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-223 |
1.68e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 66.65 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 15 TVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLtADSGSVLVNGLEVAKTPDEQMAKV---LSVLRQE--NHFTSR 89
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLLPVrhrIQVVFQDpnSSLNPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 90 LTVEDLVGFG---RYPwskgRLTSEDR-QHIETAMDFLDLLP-LRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLN 164
Cdd:PRK15134 379 LNVLQIIEEGlrvHQP----TLSAAQReQQVIAVMEEVGLDPeTRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1353453005 165 NLD---MKHSVAMMKQLRraadELHKTIILVI-HDINFASAYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:PRK15134 455 SLDktvQAQILALLKSLQ----QKHQLAYLFIsHDLHVVRALCHQVIVLRQGEVVEQGDCERV 513
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
11-241 |
2.12e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 65.19 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 11 YQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRL------LTADsGSVLVNGLEVAKT---PDEQMAKVLSVLR 81
Cdd:PRK14243 20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndlipgFRVE-GKVTFHGKNLYAPdvdPVEVRRRIGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 82 QENHFTSrlTVEDLVGFG-RYPWSKGRLTsedrQHIETAMDFLDLLPLRARYLDQ----LSGGQRQRACVAMVLCQNTDY 156
Cdd:PRK14243 99 KPNPFPK--SIYDNIAYGaRINGYKGDMD----ELVERSLRQAALWDEVKDKLKQsglsLSGGQQQRLCIARAIAVQPEV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 157 VLLDEPLNNLDMKHSVA---MMKQLRRaadelHKTIILVIHDINFASAYSDhIIAMKQGEVLYRGTPQ-EIMRPEVIEAI 232
Cdd:PRK14243 173 ILMDEPCSALDPISTLRieeLMHELKE-----QYTIIIVTHNMQQAARVSD-MTAFFNVELTEGGGRYgYLVEFDRTEKI 246
|
....*....
gi 1353453005 233 FDTKVHIET 241
Cdd:PRK14243 247 FNSPQQQAT 255
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-225 |
3.11e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.15 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 17 LNRITESIPVGGITSIIGANGAGKSTLLS-VISRLLTADSGSVLVNGlEVAKTPdeQMAKVLSVLRQEN-HFTSRLTVEd 94
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRG-SVAYVP--QVSWIFNATVRENiLFGSDFESE- 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 95 lvgfgRYpWSKGRLTSedRQHIetamdfLDLLPLRARYLD-----QLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLD-- 167
Cdd:PLN03232 709 -----RY-WRAIDVTA--LQHD------LDLLPGRDLTEIgergvNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDah 774
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1353453005 168 MKHSV--AMMKqlrraaDELH-KTIILVIHDINFASAYsDHIIAMKQGEVLYRGTPQEIMR 225
Cdd:PLN03232 775 VAHQVfdSCMK------DELKgKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSK 828
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-213 |
3.41e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.52 E-value: 3.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 7 ICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVA-KTPDEQMAKVLSVLRQENH 85
Cdd:PRK10982 4 ISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 86 FTSRLTVEDLVGFGRYPwSKGRLTSEDRQHIETAMDFLDL---LPLRARYLDqLSGGQRQRACVAMVLCQNTDYVLLDEP 162
Cdd:PRK10982 84 LVLQRSVMDNMWLGRYP-TKGMFVDQDKMYRDTKAIFDELdidIDPRAKVAT-LSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1353453005 163 LNNLDMK---HSVAMMKQLRraadELHKTIILVIHDINFASAYSDHIIAMKQGE 213
Cdd:PRK10982 162 TSSLTEKevnHLFTIIRKLK----ERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
27-178 |
3.49e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 63.67 E-value: 3.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 27 GGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEqmakvlsvLRQenhftsrltveDLVGFGRYPWSKG 106
Cdd:PRK13538 27 GELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE--------YHQ-----------DLLYLGHQPGIKT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 107 RLTSE----------DRQHIETAMDFLDLLPLrARYLD----QLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDmKHSV 172
Cdd:PRK13538 88 ELTALenlrfyqrlhGPGDDEALWEALAQVGL-AGFEDvpvrQLSAGQQRRVALARLWLTRAPLWILDEPFTAID-KQGV 165
|
....*.
gi 1353453005 173 AMMKQL 178
Cdd:PRK13538 166 ARLEAL 171
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-225 |
3.55e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.92 E-value: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVIS--RLLtaDSGSVLVNGLEVAKT----------- 68
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAgaRKI--QQGRVEVLGGDMADArhrravcpria 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 69 -----------PDeqmakvLSVlrQEN-HFTSRLtvedlvgFGRypwskGRltSEDRQHIETAMDFLDLLPLRARYLDQL 136
Cdd:NF033858 80 ympqglgknlyPT------LSV--FENlDFFGRL-------FGQ-----DA--AERRRRIDELLRATGLAPFADRPAGKL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 137 SGGQRQRA--CVAmvLCQNTDYVLLDEPLNNLDmkhsvammkQL-RRAADELHKTI--------ILVihdinfASAYS-- 203
Cdd:NF033858 138 SGGMKQKLglCCA--LIHDPDLLILDEPTTGVD---------PLsRRQFWELIDRIraerpgmsVLV------ATAYMee 200
|
250 260
....*....|....*....|....*.
gi 1353453005 204 ----DHIIAMKQGEVLYRGTPQEIMR 225
Cdd:NF033858 201 aerfDWLVAMDAGRVLATGTPAELLA 226
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
12-194 |
4.64e-12 |
|
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: 62.56 E-value: 4.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 12 QNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVlvnglevAKTPDEQMAkvlsVLRQENHFTsRLT 91
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-------GMPEGEDLL----FLPQRPYLP-LGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 92 VEDLVgfgRYPWSkgrltsedrqhietamdfldllplrarylDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDmkhs 171
Cdd:cd03223 80 LREQL---IYPWD-----------------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD---- 123
|
170 180
....*....|....*....|...
gi 1353453005 172 VAMMKQLRRAADELHKTIILVIH 194
Cdd:cd03223 124 EESEDRLYQLLKELGITVISVGH 146
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-223 |
5.99e-12 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 63.52 E-value: 5.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRL--LTAD---SGSVLVNGLEV-AKTPDeqmak 75
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEILLDGEDIyDPDVD----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 76 vLSVLRQE--------NHFTsrLTVEDLVGFG-RYpwsKGRLTSEDRQHI-ETAmdfldllpLRA---------RyLDQ- 135
Cdd:COG1117 87 -VVELRRRvgmvfqkpNPFP--KSIYDNVAYGlRL---HGIKSKSELDEIvEES--------LRKaalwdevkdR-LKKs 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 136 ---LSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDmkhSVAMMK--QLrraADELHK--TIILVIHDINFASAYSDHIIA 208
Cdd:COG1117 152 algLSGGQQQRLCIARALAVEPEVLLMDEPTSALD---PISTAKieEL---ILELKKdyTIVIVTHNMQQAARVSDYTAF 225
|
250
....*....|....*
gi 1353453005 209 MKQGEVLYRGTPQEI 223
Cdd:COG1117 226 FYLGELVEFGPTEQI 240
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-220 |
9.64e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 64.42 E-value: 9.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 23 SIPV---GGITSIIGANGAGKSTLLSVIS-----------------RLLTADSGSVL-------VNG-LEVAKTPD--EQ 72
Cdd:COG1245 92 GLPVpkkGKVTGILGPNGIGKSTALKILSgelkpnlgdydeepswdEVLKRFRGTELqdyfkklANGeIKVAHKPQyvDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 73 MAKVLSvlrqenhftsrLTVEDLvgfgrypwskgrLTSED-RQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLC 151
Cdd:COG1245 172 IPKVFK-----------GTVREL------------LEKVDeRGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALL 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1353453005 152 QNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADElHKTIILVIHDINFASAYSDHIiamkqgEVLYrGTP 220
Cdd:COG1245 229 RDADFYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYV------HILY-GEP 289
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-213 |
1.15e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 63.13 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADsGSVLVNG---------LEVAKTPDEQ 72
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGrveffnqniYERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 73 MAKVLSVLRQENHFTsrLTVEDLVGFGR--YPWskgRLTSEDRQHIETAMDFLDLL-----PLRARYLDqLSGGQRQRAC 145
Cdd:PRK14258 87 RRQVSMVHPKPNLFP--MSVYDNVAYGVkiVGW---RPKLEIDDIVESALKDADLWdeikhKIHKSALD-LSGGQQQRLC 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1353453005 146 VAMVLCQNTDYVLLDEPLNNLDmkhSVAMMK-----QLRRAADELhkTIILVIHDINFASAYSDHIIAMKQGE 213
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLD---PIASMKvesliQSLRLRSEL--TMVIVSHNLHQVSRLSDFTAFFKGNE 228
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
9-198 |
3.34e-11 |
|
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: 62.65 E-value: 3.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 9 KSYQ-NTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSV----------------LVNGLEVAKTPDE 71
Cdd:TIGR03719 12 KVVPpKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEArpqpgikvgylpqepqLDPTKTVRENVEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 72 QMAKVLSVLRQENHFTSRLTVEDlVGFGRYPWSKGRLTSE---------DRQhIETAMDFLDLLPLRARyLDQLSGGQRQ 142
Cdd:TIGR03719 92 GVAEIKDALDRFNEISAKYAEPD-ADFDKLAAEQAELQEIidaadawdlDSQ-LEIAMDALRCPPWDAD-VTKLSGGERR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1353453005 143 RACVAMVLCQNTDYVLLDEPLNNLDMKhSVAMmkqLRRAADELHKTIILVIHDINF 198
Cdd:TIGR03719 169 RVALCRLLLSKPDMLLLDEPTNHLDAE-SVAW---LERHLQEYPGTVVAVTHDRYF 220
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
13-223 |
3.71e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 62.05 E-value: 3.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 13 NTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTAD---SGSVLVNGLEVAKTPDEQMAKvlsvLRQENhfTSR 89
Cdd:PRK09473 28 DVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKELNK----LRAEQ--ISM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 90 LTVEDLVGFGRYPWSKGRLTSEDRQH--------IETAMDFLDLLPL---RAR---YLDQLSGGQRQRACVAMVLCQNTD 155
Cdd:PRK09473 102 IFQDPMTSLNPYMRVGEQLMEVLMLHkgmskaeaFEESVRMLDAVKMpeaRKRmkmYPHEFSGGMRQRVMIAMALLCRPK 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1353453005 156 YVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:PRK09473 182 LLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
14-197 |
7.60e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 60.11 E-value: 7.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 14 TTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVLRQenhfTSRL--- 90
Cdd:PRK10247 20 AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQ----TPTLfgd 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 91 TVEDLVGFgryPWsKGRLTSEDRQHIetaMDFLDLLPLRARYLDQ----LSGGQRQRacvaMVLCQNTDY----VLLDEP 162
Cdd:PRK10247 96 TVYDNLIF---PW-QIRNQQPDPAIF---LDDLERFALPDTILTKniaeLSGGEKQR----ISLIRNLQFmpkvLLLDEI 164
|
170 180 190
....*....|....*....|....*....|....*
gi 1353453005 163 LNNLDMKHSVAMMKQLRRAADELHKTIILVIHDIN 197
Cdd:PRK10247 165 TSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKD 199
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-194 |
7.64e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.05 E-value: 7.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 16 VLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTA---DSGSVLVNGLEVaktpDEQMAKVLSVLRQENHFTSRLTV 92
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPL----DSSFQRSIGYVQQQDLHLPTSTV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 93 EDLVGFGRYPWSKGRLT-SEDRQHIETAMDFLDLlplrARYLDQLSG--------GQRQRACVAMVLCQNTDYVL-LDEP 162
Cdd:TIGR00956 854 RESLRFSAYLRQPKSVSkSEKMEYVEEVIKLLEM----ESYADAVVGvpgeglnvEQRKRLTIGVELVAKPKLLLfLDEP 929
|
170 180 190
....*....|....*....|....*....|..
gi 1353453005 163 LNNLDMKHSVAMMKQLRRAADElHKTIILVIH 194
Cdd:TIGR00956 930 TSGLDSQTAWSICKLMRKLADH-GQAILCTIH 960
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
9-218 |
7.73e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 59.58 E-value: 7.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 9 KSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTAD---SGSVLVNGLEVAKTPDEQMAKVLSVLRQENH 85
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 86 FTSrLTVEDLvgfgrypwskgrltsedrqhietaMDFldllPLRAR---YLDQLSGGQRQRACVAMVLCQNTDYVLLDEP 162
Cdd:cd03233 95 FPT-LTVRET------------------------LDF----ALRCKgneFVRGISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1353453005 163 LNNLDMKHSVAMMKQLRRAADELHKTiilvihdiNFASAYS---------DHIIAMKQGEVLYRG 218
Cdd:cd03233 146 TRGLDSSTALEILKCIRTMADVLKTT--------TFVSLYQasdeiydlfDKVLVLYEGRQIYYG 202
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
16-219 |
9.07e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 61.79 E-value: 9.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 16 VLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTAD--SGSVLVNGLEVAKtpdEQMAKVLSVLRQENHFTSRLTV- 92
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKKQ---ETFARISGYCEQNDIHSPQVTVr 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 93 EDLV--GFGRYPWSKGRltSEDRQHIETAMDFLDLLPLRARY-----LDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNN 165
Cdd:PLN03140 972 ESLIysAFLRLPKEVSK--EEKMMFVDEVMELVELDNLKDAIvglpgVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1049
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1353453005 166 LDMKHSVAMMKQLRRAADElHKTIILVIH--DINFASAYsDHIIAMKQ-GEVLYRGT 219
Cdd:PLN03140 1050 LDARAAAIVMRTVRNTVDT-GRTVVCTIHqpSIDIFEAF-DELLLMKRgGQVIYSGP 1104
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
31-224 |
9.09e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 60.57 E-value: 9.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 31 SIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVLRQE--NHFTSRLTVEDLVGFgryPWS-KGR 107
Cdd:PRK15112 43 AIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDpsTSLNPRQRISQILDF---PLRlNTD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 108 LTSEDR-QHIETAMDFLDLLPLRARYLDQ-LSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMkhsvAMMKQLRRAADEL 185
Cdd:PRK15112 120 LEPEQReKQIIETLRQVGLLPDHASYYPHmLAPGQKQRLGLARALILRPKVIIADEALASLDM----SMRSQLINLMLEL 195
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1353453005 186 HK----TIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIM 224
Cdd:PRK15112 196 QEkqgiSYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-213 |
1.25e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.99 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADS--GSVLVNGLE-VAKTPDEQMAKVL 77
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPlKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 78 SVLRQENHFTSRLTVEDLVGFGRYPWSKGRLTSED----RQHIETAMDFLDLLPLrARYLDQLSGGQRQRACVAMVLCQN 153
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNamylRAKNLLRELQLDADNV-TRPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1353453005 154 TDYVLLDEPLNNLDMKHSVAMMKQLRraaDELHKTI--ILVIHDINFASAYSDHIIAMKQGE 213
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIR---DLKAHGVacVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
12-225 |
1.73e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 60.64 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 12 QNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGL----------EVAKTPDEQMAKV----L 77
Cdd:PRK10261 27 QKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEQSAAQMRHVrgadM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 78 SVLRQE--NHFTSRLTVEDLV--------GFGRYPWSKGRLTSEDRQHIETAMDFLdllplrARYLDQLSGGQRQRACVA 147
Cdd:PRK10261 107 AMIFQEpmTSLNPVFTVGEQIaesirlhqGASREEAMVEAKRMLDQVRIPEAQTIL------SRYPHQLSGGMRQRVMIA 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1353453005 148 MVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMR 225
Cdd:PRK10261 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFH 258
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-198 |
2.07e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.35 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 3 EVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLV-NGLEVAKTpDEQMAkvlsVLR 81
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCgTKLEVAYF-DQHRA----ELD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 82 QENhftsrlTVEDLVGFGrypwsKGRLT--SEDRQHIETAMDFLdLLPLRARY-LDQLSGGQRQRACVAMVLCQNTDYVL 158
Cdd:PRK11147 396 PEK------TVMDNLAEG-----KQEVMvnGRPRHVLGYLQDFL-FHPKRAMTpVKALSGGERNRLLLARLFLKPSNLLI 463
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1353453005 159 LDEPLNNLDmkhsVAMMKQLRRAADELHKTIILVIHDINF 198
Cdd:PRK11147 464 LDEPTNDLD----VETLELLEELLDSYQGTVLLVSHDRQF 499
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-214 |
2.27e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.10 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 12 QNTTVLNRITESIPVGGITSIIGANGAGKS-TLLSVIsRLLTAD-----SGSVLVNGLEVAKTPDEQMAKV----LSVLR 81
Cdd:PRK15134 20 TVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSIL-RLLPSPpvvypSGDIRFHGESLLHASEQTLRGVrgnkIAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 82 QEN-------HFTSRLTVEDLV---GFGRYPWSKGRLTSEDRQHIETAMDFLdllplrARYLDQLSGGQRQRACVAMVLC 151
Cdd:PRK15134 99 QEPmvslnplHTLEKQLYEVLSlhrGMRREAARGEILNCLDRVGIRQAAKRL------TDYPHQLSGGERQRVMIAMALL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1353453005 152 QNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEV 214
Cdd:PRK15134 173 TRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRC 235
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
32-223 |
2.32e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 60.36 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 32 IIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVLRQENHFTSRlTVEDLVGFGRypwskgrltsE 111
Cdd:PRK13657 366 IVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNR-SIEDNIRVGR----------P 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 112 DRQHIE--------TAMDFLDLLPL--------RARyldQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDmkhsVAMM 175
Cdd:PRK13657 435 DATDEEmraaaeraQAHDFIERKPDgydtvvgeRGR---QLSGGERQRLAIARALLKDPPILILDEATSALD----VETE 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1353453005 176 KQLRRAADELHK--TIILVIHDINfASAYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:PRK13657 508 AKVKAALDELMKgrTTFIIAHRLS-TVRNADRILVFDNGRVVESGSFDEL 556
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
27-214 |
3.43e-10 |
|
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: 57.44 E-value: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 27 GGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEV-AKTPDEQMAKvlsvlrqenhftsrltvedlvGFGrypwsk 105
Cdd:cd03215 26 GEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtRRSPRDAIRA---------------------GIA------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 106 grLTSEDRQH--IETAMDFLDLLPLRAryldQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAAD 183
Cdd:cd03215 79 --YVPEDRKRegLVLDLSVAENIALSS----LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAD 152
|
170 180 190
....*....|....*....|....*....|.
gi 1353453005 184 ElHKTIILVIHDINFASAYSDHIIAMKQGEV 214
Cdd:cd03215 153 A-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-179 |
8.27e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.88 E-value: 8.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTpDEQMAKVLSVL 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKD-LCTYQKQLCFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 RQENHFTSRLTVEDLVGFgrypwskgrltseDRQHIETAMDFLDLLPLRA--RYLD----QLSGGQRQRACVAMVLCQNT 154
Cdd:PRK13540 80 GHRSGINPYLTLRENCLY-------------DIHFSPGAVGITELCRLFSleHLIDypcgLLSSGQKRQVALLRLWMSKA 146
|
170 180
....*....|....*....|....*
gi 1353453005 155 DYVLLDEPLNNLDMKHSVAMMKQLR 179
Cdd:PRK13540 147 KLWLLDEPLVALDELSLLTIITKIQ 171
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-196 |
8.87e-10 |
|
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: 57.56 E-value: 8.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQN--TTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADsGSVLVNGLEVAKTPDEQMAKVLSV 79
Cdd:cd03289 3 MTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 LRQENHFTSRLTVEDLVGFGRypWSKGRL--TSED---RQHIETAMDFLDLLPLRARYLdqLSGGQRQRACVAMVLCQNT 154
Cdd:cd03289 82 IPQKVFIFSGTFRKNLDPYGK--WSDEEIwkVAEEvglKSVIEQFPGQLDFVLVDGGCV--LSHGHKQLMCLARSVLSKA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1353453005 155 DYVLLDEPLNNLDMKHSVAMMKQLRRAADELhkTIILVIHDI 196
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQAFADC--TVILSEHRI 197
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-196 |
1.06e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.28 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 27 GGITSIIGANGAGKSTLLSVIS-----------------RLLTADSGSVLVNGLE--------VAKTPD--EQMAKVLsv 79
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSgelipnlgdyeeepswdEVLKRFRGTELQNYFKklyngeikVVHKPQyvDLIPKVF-- 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 lrqenhftsRLTVEDLvgfgrypwskgrLTSED-RQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVL 158
Cdd:PRK13409 177 ---------KGKVREL------------LKKVDeRGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190
....*....|....*....|....*....|....*...
gi 1353453005 159 LDEPLNNLDMKHSVAMMKQLRRAADElhKTIILVIHDI 196
Cdd:PRK13409 236 FDEPTSYLDIRQRLNVARLIRELAEG--KYVLVVEHDL 271
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
23-224 |
1.21e-09 |
|
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: 58.03 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 23 SIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVLRQENhFTSRLTVEDLVGFgryp 102
Cdd:TIGR03796 501 TLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDI-FLFEGTVRDNLTL---- 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 103 WSKgrlTSEDRQHIETAMD--FLDLLPLRARYLDQ--------LSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMKHSV 172
Cdd:TIGR03796 576 WDP---TIPDADLVRACKDaaIHDVITSRPGGYDAelaegganLSGGQRQRLEIARALVRNPSILILDEATSALDPETEK 652
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1353453005 173 AMMKQLRRAAdelhKTIILVIHDInfaSAY--SDHIIAMKQGEVLYRGTPQEIM 224
Cdd:TIGR03796 653 IIDDNLRRRG----CTCIIVAHRL---STIrdCDEIIVLERGKVVQRGTHEELW 699
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-214 |
2.09e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.49 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 3 EVKAIcKSYQNTTVLNrITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVA-KTPDEQMAKVLSVL- 80
Cdd:PRK09700 267 EVRNV-TSRDRKKVRD-ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAYIt 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 --RQENHFTSRLTVEDLVGF------GRYPWSKGRLTSEDRQhiETAMDFLDLLPLRARYLDQ----LSGGQRQRACVAM 148
Cdd:PRK09700 345 esRRDNGFFPNFSIAQNMAIsrslkdGGYKGAMGLFHEVDEQ--RTAENQRELLALKCHSVNQniteLSGGNQQKVLISK 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1353453005 149 VLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADElHKTIILVIHDINFASAYSDHIIAMKQGEV 214
Cdd:PRK09700 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-223 |
2.16e-09 |
|
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: 57.12 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRL--LTADSGSVLVN--------GLEVAKTPDE 71
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcgYVERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 72 QMAKVLSVLRQEN------------HFTSRLTVEDLVGFGRYP---------WSKGRLTSEDRQHIETAMDFLDLLPLRA 130
Cdd:TIGR03269 81 PCPVCGGTLEPEEvdfwnlsdklrrRIRKRIAIMLQRTFALYGddtvldnvlEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 131 RYLD---QLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHII 207
Cdd:TIGR03269 161 RITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250
....*....|....*.
gi 1353453005 208 AMKQGEVLYRGTPQEI 223
Cdd:TIGR03269 241 WLENGEIKEEGTPDEV 256
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
15-225 |
2.51e-09 |
|
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: 57.14 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 15 TVLNRITESIPVGGITSIIGANGAGKSTllsvISRLLT----ADSGSVLVNGLEVAKTPDEQMAKVLSVLRQEnhftsrl 90
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKST----LARLLFrfydVTSGRILIDGQDIRDVTQASLRAAIGIVPQD------- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 91 TV--EDLVGFG-RYpwskGRLTSEDRQHIETA-----MDFLDLLP-----------LRaryldqLSGGQRQRACVAMVLC 151
Cdd:COG5265 441 TVlfNDTIAYNiAY----GRPDASEEEVEAAAraaqiHDFIESLPdgydtrvgergLK------LSGGEKQRVAIARTLL 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 152 QNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADElHKTIIL------VIHdinfasaySDHIIAMKQGEVLYRGTPQEIMR 225
Cdd:COG5265 511 KNPPILIFDEATSALDSRTERAIQAALREVARG-RTTLVIahrlstIVD--------ADEILVLEAGRIVERGTHAELLA 581
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
16-211 |
2.79e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.10 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 16 VLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGlevaktpDEQMAKVlsvlRQENHFTSRLTVEDL 95
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG-------NWQLAWV----NQETPALPQPALEYV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 96 VGFGR-YPWSKGRLTSEDRQ-------HIETAMDFLDLLPLRARYL----------DQL-------SGGQRQRACVAMVL 150
Cdd:PRK10636 85 IDGDReYRQLEAQLHDANERndghaiaTIHGKLDAIDAWTIRSRAAsllhglgfsnEQLerpvsdfSGGWRMRLNLAQAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1353453005 151 CQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADelhkTIILVIHDINFASAYSDHIIAMKQ 211
Cdd:PRK10636 165 ICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG----TLILISHDRDFLDPIVDKIIHIEQ 221
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-218 |
3.51e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.79 E-value: 3.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 16 VLNRITESIPV----------GGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQmakvLSVLRQENH 85
Cdd:PRK10261 329 LLNRVTREVHAvekvsfdlwpGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGK----LQALRRDIQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 86 FT-----SRLTVEDLVGFG-RYPWSKGRLTSED--RQHIETAMDFLDLLPLRA-RYLDQLSGGQRQRACVAMVLCQNTDY 156
Cdd:PRK10261 405 FIfqdpyASLDPRQTVGDSiMEPLRVHGLLPGKaaAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKV 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1353453005 157 VLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRG 218
Cdd:PRK10261 485 IIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
129-207 |
3.88e-09 |
|
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: 54.50 E-value: 3.88e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1353453005 129 RARYLDqLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHII 207
Cdd:cd03222 66 KPQYID-LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIH 143
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-225 |
4.77e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 56.71 E-value: 4.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 16 VLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGlEVAKTPdeQMAKVLSVlrqenhftsrlTVEDL 95
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAER-SIAYVP--QQAWIMNA-----------TVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 96 VGFgrypwskgrLTSEDRQHIETAMDFLDL---LPLRARYLD--------QLSGGQRQRACVAMVLCQNTDYVLLDEPLN 164
Cdd:PTZ00243 741 ILF---------FDEEDAARLADAVRVSQLeadLAQLGGGLEteigekgvNLSGGQKARVSLARAVYANRDVYLLDDPLS 811
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1353453005 165 NLDMKHSVAMMKQLRRAAdeLH-KTIILVIHDINFAsAYSDHIIAMKQGEVLYRGTPQEIMR 225
Cdd:PTZ00243 812 ALDAHVGERVVEECFLGA--LAgKTRVLATHQVHVV-PRADYVVALGDGRVEFSGSSADFMR 870
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
33-224 |
6.03e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.05 E-value: 6.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 33 IGANGAGKSTLLSVISRLLTADSGsvlvnglEVAKTPDEQMAKvlsvLRQENHFTSRLTVEDLVGFGRYP-W-------- 103
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAG-------NVSLDPNERLGK----LRQDQFAFEEFTVLDTVIMGHTElWevkqerdr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 104 --SKGRLTSEDRQHI-ETAMDFL------------DLL-----PLRARY--LDQLSGGQRQRACVAMVLCQNTDYVLLDE 161
Cdd:PRK15064 102 iyALPEMSEEDGMKVaDLEVKFAemdgytaearagELLlgvgiPEEQHYglMSEVAPGWKLRVLLAQALFSNPDILLLDE 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1353453005 162 PLNNLDMkHSVammkqlRRAADELHK---TIILVIHDINFASAYSDHIIAMKQGEV-LYRGTPQEIM 224
Cdd:PRK15064 182 PTNNLDI-NTI------RWLEDVLNErnsTMIIISHDRHFLNSVCTHMADLDYGELrVYPGNYDEYM 241
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
32-223 |
6.85e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 55.36 E-value: 6.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 32 IIGANGAGKSTLlsviSRLLT----ADSGSVLVNGLEVAKtPDEQMAKVLsvlRQE------NHFTS---RLTVEDLVGf 98
Cdd:PRK11308 46 VVGESGCGKSTL----ARLLTmietPTGGELYYQGQDLLK-ADPEAQKLL---RQKiqivfqNPYGSlnpRKKVGQILE- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 99 grYPWS-KGRLTSEDRQhiETAMDFLDLLPLRA----RYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMkhSVA 173
Cdd:PRK11308 117 --EPLLiNTSLSAAERR--EKALAMMAKVGLRPehydRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDV--SVQ 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1353453005 174 -----MMKQLRraaDELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:PRK11308 191 aqvlnLMMDLQ---QELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 242
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-166 |
9.04e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.39 E-value: 9.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVA-KTPDEQMAKVLSV 79
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEAGIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 LRQENHFTSRLTV--------EDLVGFGRYPWSKGRltsedrqhiETAMDFLDLLPLR---ARYLDQLSGGQRQRACVAM 148
Cdd:PRK10762 84 IHQELNLIPQLTIaeniflgrEFVNRFGRIDWKKMY---------AEADKLLARLNLRfssDKLVGELSIGEQQMVEIAK 154
|
170
....*....|....*...
gi 1353453005 149 VLCQNTDYVLLDEPLNNL 166
Cdd:PRK10762 155 VLSFESKVIIMDEPTDAL 172
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-237 |
1.48e-08 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 54.14 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNT--TVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSV 79
Cdd:cd03288 20 IKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 LRQENHFTSrltvedlvGFGRYPWSKGRLTSEDR--QHIETAM--DFLDLLP--LRARYLD---QLSGGQRQRACVAMVL 150
Cdd:cd03288 100 ILQDPILFS--------GSIRFNLDPECKCTDDRlwEALEIAQlkNMVKSLPggLDAVVTEggeNFSVGQRQLFCLARAF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 151 CQNTDYVLLDEPLNNLDMKHSVAMMKQLRRA-ADELHKTIILVIHDINFAsaysDHIIAMKQGEVLYRGTPQEIMRPEvi 229
Cdd:cd03288 172 VRKSSILIMDEATASIDMATENILQKVVMTAfADRTVVTIAHRVSTILDA----DLVLVLSRGILVECDTPENLLAQE-- 245
|
....*...
gi 1353453005 230 EAIFDTKV 237
Cdd:cd03288 246 DGVFASLV 253
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
31-222 |
1.50e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.87 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 31 SIIGANGAGKSTLLSVISRLLTADSGSVLvnglevaKTPDEQMAkvlsVLRQENHFTSRLTVEDLVGFGR-YPwskGRLT 109
Cdd:PLN03073 539 AMVGPNGIGKSTILKLISGELQPSSGTVF-------RSAKVRMA----VFSQHHVDGLDLSSNPLLYMMRcFP---GVPE 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 110 SEDRQHIeTAMDFLDLLPLRARYldQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRaadeLHKTI 189
Cdd:PLN03073 605 QKLRAHL-GSFGVTGNLALQPMY--TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVL----FQGGV 677
|
170 180 190
....*....|....*....|....*....|....
gi 1353453005 190 ILVIHDINFASAYSDHIIAMKQGEVL-YRGTPQE 222
Cdd:PLN03073 678 LMVSHDEHLISGSVDELWVVSEGKVTpFHGTFHD 711
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
17-225 |
1.76e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 53.98 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 17 LNRITESIPVGGITSIIGANGAGKSTLLSVISRLL------TADSgsVLVNGLEVAKTPDEQMAKV----LSVLRQENhF 86
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgrvMAEK--LEFNGQDLQRISEKERRNLvgaeVAMIFQDP-M 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 87 TSrLTVEDLVGFGRYPWSKGRLTSEDRQHIETAMDFLDL--LPLRARYLD----QLSGGQRQRACVAMVLCQNTDYVLLD 160
Cdd:PRK11022 100 TS-LNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQvgIPDPASRLDvyphQLSGGMSQRVMIAMAIACRPKLLIAD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1353453005 161 EPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMR 225
Cdd:PRK11022 179 EPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFR 243
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
32-193 |
2.06e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 54.43 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 32 IIGANGAGKSTLLSVISRLLTADSGSVLVNGLE-------------------------VAKTPDEQMAKVLSVLRQEnHF 86
Cdd:COG4178 394 ITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGArvlflpqrpylplgtlreallypatAEAFSDAELREALEAVGLG-HL 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 87 TSRLTVEDlvgfgryPWSKgrltsedrqhietamdfldllplraryldQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNL 166
Cdd:COG4178 473 AERLDEEA-------DWDQ-----------------------------VLSLGEQQRLAFARLLLHKPDWLFLDEATSAL 516
|
170 180
....*....|....*....|....*..
gi 1353453005 167 DMKHSVAMMKQLRraaDELHKTIILVI 193
Cdd:COG4178 517 DEENEAALYQLLR---EELPGTTVISV 540
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
16-225 |
2.08e-08 |
|
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: 52.91 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 16 VLNRITESIPVGGITSIIGANGAGKSTLLSVISRL--LTADSGSVLVNGLEV-AKTPDEQMAKVLSVLRQenhftsrltv 92
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDItDLPPEERARLGIFLAFQ---------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 93 edlvgfgrYPwskgrltsedrqhIE----TAMDFLdllplraRYLDQ-LSGGQRQRACVAMVLCQNTDYVLLDEPLNNLD 167
Cdd:cd03217 85 --------YP-------------PEipgvKNADFL-------RYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1353453005 168 MKHSVAMMKQLRRAADElHKTIILVIHDINFAsaysDHIIA-----MKQGEVLYRGtPQEIMR 225
Cdd:cd03217 137 IDALRLVAEVINKLREE-GKSVLIITHYQRLL----DYIKPdrvhvLYDGRIVKSG-DKELAL 193
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-229 |
2.35e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.40 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 16 VLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVLRQENHF---TSRLTV 92
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLfdgTVRQNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 93 E--------------DLVGFgrypwsKGRLTSEDrQHIEtamdfldllplrARYLD---QLSGGQRQRACVAMVLCQ-NT 154
Cdd:PTZ00243 1405 DpfleassaevwaalELVGL------RERVASES-EGID------------SRVLEggsNYSVGQRQLMCMARALLKkGS 1465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1353453005 155 DYVLLDEPLNNLDMkhsvAMMKQLR---RAADELHkTIILVIHDINFASAYsDHIIAMKQGEVLYRGTPQE-IMRPEVI 229
Cdd:PTZ00243 1466 GFILMDEATANIDP----ALDRQIQatvMSAFSAY-TVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRElVMNRQSI 1538
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
15-196 |
2.37e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.53 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 15 TVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADsGSVLVNGLEVAKTPDEQMAKVLSVLRQENHFTSRLTVED 94
Cdd:TIGR01271 1233 AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKN 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 95 LVGFGRYP----WskgRLTSED--RQHIETAMDFLDLLPLRARYLdqLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDM 168
Cdd:TIGR01271 1312 LDPYEQWSdeeiW---KVAEEVglKSVIEQFPDKLDFVLVDGGYV--LSNGHKQLMCLARSILSKAKILLLDEPSAHLDP 1386
|
170 180
....*....|....*....|....*...
gi 1353453005 169 KHSVAMMKQLRRAADELhkTIILVIHDI 196
Cdd:TIGR01271 1387 VTLQIIRKTLKQSFSNC--TVILSEHRV 1412
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-224 |
2.41e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 54.34 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQN-TTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVL 80
Cdd:PRK10790 341 IDIDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 RQE-----NHFTSRLTVedlvgfgrypwskGRLTSEDR--QHIETAM--DFLDLLP--LRARYLDQ---LSGGQRQRACV 146
Cdd:PRK10790 421 QQDpvvlaDTFLANVTL-------------GRDISEEQvwQALETVQlaELARSLPdgLYTPLGEQgnnLSVGQKQLLAL 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1353453005 147 AMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADelHKTIILVIHDINfASAYSDHIIAMKQGEVLYRGTPQEIM 224
Cdd:PRK10790 488 ARVLVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLS-TIVEADTILVLHRGQAVEQGTHQQLL 562
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
16-227 |
2.79e-08 |
|
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: 54.19 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 16 VLNRITESIPVGGITSIIGANGAGKSTLLsvisRLL----TADSGSVLVNGLEVAKTPDEQMAKVLSVLRQENHFTSRLT 91
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLL----RLLlgfeTPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSI 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 92 VEDLVGFGRYP----WSKGRLT--SEDRQHIETAMDfldllplraRYLDQ----LSGGQRQRACVAMVLCQNTDYVLLDE 161
Cdd:TIGR03797 544 FENIAGGAPLTldeaWEAARMAglAEDIRAMPMGMH---------TVISEgggtLSGGQRQRLLIARALVRKPRILLFDE 614
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1353453005 162 PLNNLDMKHSVAMMKQLRRaadeLHKTIILVIHDINfASAYSDHIIAMKQGEVLYRGTPQEIMRPE 227
Cdd:TIGR03797 615 ATSALDNRTQAIVSESLER----LKVTRIVIAHRLS-TIRNADRIYVLDAGRVVQQGTYDELMARE 675
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
32-195 |
2.99e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.97 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 32 IIGANGAGKSTLLSVISRLLTADSGsvlvnglEVAKTPDeqmAKVlSVLRQENHFTSRLTVEDLV--GFG-------RY- 101
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEG-------EARPAPG---IKV-GYLPQEPQLDPEKTVRENVeeGVAevkaaldRFn 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 102 --------PWSK--------GRLTSE---------DRQhIETAMDFLDLLPLRARyLDQLSGGQRQRacVAmvLC----Q 152
Cdd:PRK11819 107 eiyaayaePDADfdalaaeqGELQEIidaadawdlDSQ-LEIAMDALRCPPWDAK-VTKLSGGERRR--VA--LCrlllE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1353453005 153 NTDYVLLDEPLNNLDMKhSVAMMKQLrraadeLHK---TIILVIHD 195
Cdd:PRK11819 181 KPDMLLLDEPTNHLDAE-SVAWLEQF------LHDypgTVVAVTHD 219
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-182 |
6.08e-08 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 51.55 E-value: 6.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAIcKSYQNTTVLNritesiPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMA------- 74
Cdd:COG0419 5 LRLENF-RSYRDTETID------FDDGLNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRSDLINVGSEEASvelefeh 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 75 --KVLSVLRQENHFTSRLT---------VEDLVGFGRYPWSKGRLTSEDRQHIETAMDFLDLLPLRARYL---------D 134
Cdd:COG0419 78 ggKRYRIERRQGEFAEFLEakpserkeaLKRLLGLEIYEELKERLKELEEALESALEELAELQKLKQEILaqlsgldpiE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1353453005 135 QLSGGQRQRACVAMVLcqntdYVLLDepLNNLDMKHSVAMMKQLRRAA 182
Cdd:COG0419 158 TLSGGERLRLALADLL-----SLILD--FGSLDEERLERLLDALEELA 198
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
28-207 |
6.31e-08 |
|
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: 51.45 E-value: 6.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 28 GITSIIGANGAGKSTLLSVISRLLTadsGSVLVNGLEVAKTPDeqMAKVLSVLRQenhftSRLTVEDLVGfgrypwskgr 107
Cdd:cd03240 23 PLTLIVGQNGAGKTTIIEALKYALT---GELPPNSKGGAHDPK--LIREGEVRAQ-----VKLAFENANG---------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 108 ltseDRQHIETAMDFL---------DLLPLRARYLDQLSGGQRQRAC------VAMVLCQNTDYVLLDEPLNNLDMKH-S 171
Cdd:cd03240 83 ----KKYTITRSLAILenvifchqgESNWPLLDMRGRCSGGEKVLASliirlaLAETFGSNCGILALDEPTTNLDEENiE 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 1353453005 172 VAMMKQLRRAADELHKTIILVIHDINFAsAYSDHII 207
Cdd:cd03240 159 ESLAEIIEERKSQKNFQLIVITHDEELV-DAADHIY 193
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
54-224 |
8.41e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.72 E-value: 8.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 54 DSGSVLVNGLEVAKTPDEQMAKVLSVLRQENHFTSrLTVEDLVGFGrypwsKGRLTSEDRQHIE--TAMD-FLDLLPLR- 129
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFN-MSIYENIKFG-----KEDATREDVKRACkfAAIDeFIESLPNKy 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 130 ----ARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDInfAS-AYSD 204
Cdd:PTZ00265 1349 dtnvGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI--ASiKRSD 1426
|
170 180
....*....|....*....|....*
gi 1353453005 205 HIIAMKQGE-----VLYRGTPQEIM 224
Cdd:PTZ00265 1427 KIVVFNNPDrtgsfVQAHGTHEELL 1451
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
32-236 |
9.89e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.26 E-value: 9.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 32 IIGANGAGKSTLLSVISRLLTADSGS------VLVNGLE-----------------------------------VAKTPD 70
Cdd:PRK11147 34 LVGRNGAGKSTLMKILNGEVLLDDGRiiyeqdLIVARLQqdpprnvegtvydfvaegieeqaeylkryhdishlVETDPS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 71 E----QMAKVLSVLRQEN--HFTSRLTvedlvgfgrypwskgrltsedrqhietamDFLDLLPLRA-RYLDQLSGGQRQR 143
Cdd:PRK11147 114 EknlnELAKLQEQLDHHNlwQLENRIN-----------------------------EVLAQLGLDPdAALSSLSGGWLRK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 144 ACVAMVLCQNTDYVLLDEPLNNLDmkhsVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEV--------L 215
Cdd:PRK11147 165 AALGRALVSNPDVLLLDEPTNHLD----IETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLvsypgnydQ 240
|
250 260
....*....|....*....|..
gi 1353453005 216 YRGTPQEIMRPEVIE-AIFDTK 236
Cdd:PRK11147 241 YLLEKEEALRVEELQnAEFDRK 262
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
32-227 |
1.14e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.43 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 32 IIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVLRQENHFTSRLTVEDLVGFGRYP----WSkgr 107
Cdd:PLN03130 1270 IVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNdadlWE--- 1346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 108 ltSEDRQHIEtamdflDLLPLRARYLD--------QLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLR 179
Cdd:PLN03130 1347 --SLERAHLK------DVIRRNSLGLDaevseageNFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIR 1418
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1353453005 180 raaDELHKTIILVI-HDINfASAYSDHIIAMKQGEVLYRGTPQEIMRPE 227
Cdd:PLN03130 1419 ---EEFKSCTMLIIaHRLN-TIIDCDRILVLDAGRVVEFDTPENLLSNE 1463
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
27-250 |
1.54e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 50.85 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 27 GGITSIIGANGAGKS----TLLSVISRLLTADSGSVLVNGLEVAktPDEQMAKVLSVLRQ--ENHFTSRLT-----VEDL 95
Cdd:PRK10418 29 GRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVA--PCALRGRKIATIMQnpRSAFNPLHTmhthaRETC 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 96 VGFGRypwskgrlTSEDRQHIEtAMDFLDLlPLRARYLD----QLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMKHS 171
Cdd:PRK10418 107 LALGK--------PADDATLTA-ALEAVGL-ENAARVLKlypfEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 172 VAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTpqeimrpevIEAIFDTKVHIET--LHGQHIAI 249
Cdd:PRK10418 177 ARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGD---------VETLFNAPKHAVTrsLVSAHLAL 247
|
.
gi 1353453005 250 Y 250
Cdd:PRK10418 248 Y 248
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
32-247 |
2.13e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.17 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 32 IIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVLRQENHftSRLTVEDLVGFGRYPWSKGRLTSE 111
Cdd:PRK10938 34 FVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQRNN--TDMLSPGEDDTGRTTAEIIQDEVK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 112 DRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDmkhsVAMMKQLRRAADELHK---T 188
Cdd:PRK10938 112 DPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD----VASRQQLAELLASLHQsgiT 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1353453005 189 IILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMRpeviEAIFDTKVHIETLHGQHI 247
Cdd:PRK10938 188 LVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQ----QALVAQLAHSEQLEGVQL 242
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-213 |
2.38e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.13 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTV-LNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEV-AKTPDEqmakvlsv 79
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVtAEQPED-------- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 80 LRQenHFTSRLTveDLVGFGRYPWSKGrlTSEDRQHIETAMDFLDL---LPLR-ARYLD-QLSGGQRQRACVAMVLCQNT 154
Cdd:PRK10522 395 YRK--LFSAVFT--DFHLFDQLLGPEG--KPANPALVEKWLERLKMahkLELEdGRISNlKLSKGQKKRLALLLALAEER 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1353453005 155 DYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDinfaSAYSDH---IIAMKQGE 213
Cdd:PRK10522 469 DILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD----DHYFIHadrLLEMRNGQ 526
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
34-168 |
2.95e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.85 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 34 GANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLS---VLRQ-----EN-HFTSRLTvedlvgfGRYPws 104
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGhlpGLKAdlstlENlHFLCGLH-------GRRA-- 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1353453005 105 kgrltsedRQHIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDM 168
Cdd:PRK13543 115 --------KQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
11-214 |
7.08e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.78 E-value: 7.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 11 YQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSV-LVNGLEVAKTPDEQmakvLSVLRQE----NH 85
Cdd:PRK10636 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQ----LEFLRADesplQH 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 86 FTsRLTVED--------LVGFGrypwSKGRLTSEdrqhiETAmdfldllplraryldQLSGGQRQRACVAMVLCQNTDYV 157
Cdd:PRK10636 398 LA-RLAPQEleqklrdyLGGFG----FQGDKVTE-----ETR---------------RFSGGEKARLVLALIVWQRPNLL 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1353453005 158 LLDEPLNNLDMKhsvaMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEV 214
Cdd:PRK10636 453 LLDEPTNHLDLD----MRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
29-225 |
7.56e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 49.63 E-value: 7.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 29 ITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVA-KTPDEQMAKVLSVL---RQENHFTSRLTVED---LVGFGRY 101
Cdd:COG1129 280 ILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRiRSPRDAIRAGIAYVpedRKGEGLVLDLSIREnitLASLDRL 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 102 pwSKGRLTSEDRQHiETAMDFLDLLPLRARYLDQ----LSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDM--KHSVamM 175
Cdd:COG1129 360 --SRGGLLDRRRER-ALAEEYIKRLRIKTPSPEQpvgnLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVgaKAEI--Y 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1353453005 176 KQLRRAADElHKTIILVIHDINFASAYSDHIIAMKQGEV---LYRG--TPQEIMR 225
Cdd:COG1129 435 RLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIvgeLDREeaTEEAIMA 488
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-214 |
1.27e-06 |
|
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: 49.03 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTT-----VLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVaktPDEQMAkv 76
Cdd:COG4615 328 LELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV---TADNRE-- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 77 lsVLRQenHFTsrlTV-------EDLVGFGRYPwskgrltseDRQHIETAMDFLDL---LPLRARYLD--QLSGGQRQRa 144
Cdd:COG4615 403 --AYRQ--LFS---AVfsdfhlfDRLLGLDGEA---------DPARARELLERLELdhkVSVEDGRFSttDLSQGQRKR- 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 145 cVAMVLC--QNTDYVLLDEplnnldmkhsvammkqlrRAAD---------------ELH---KTIILVIHDIN-FASAys 203
Cdd:COG4615 466 -LALLVAllEDRPILVFDE------------------WAADqdpefrrvfytellpELKargKTVIAISHDDRyFDLA-- 524
|
250
....*....|.
gi 1353453005 204 DHIIAMKQGEV 214
Cdd:COG4615 525 DRVLKMDYGKL 535
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-167 |
1.52e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.47 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVIsrllTADSGSVLVNGL----------EVAKTPDE 71
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI----TGDHPQGYSNDLtlfgrrrgsgETIWDIKK 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 72 QMAKVLSVLRQENHFTSRLTVEDLVGF----GRYpwskgRLTSeDRQHIeTAMDFLDLLPLRARYLDQ----LSGGQRQR 143
Cdd:PRK10938 337 HIGYVSSSLHLDYRVSTSVRNVILSGFfdsiGIY-----QAVS-DRQQK-LAQQWLDILGIDKRTADApfhsLSWGQQRL 409
|
170 180
....*....|....*....|....
gi 1353453005 144 ACVAMVLCQNTDYVLLDEPLNNLD 167
Cdd:PRK10938 410 ALIVRALVKHPTLLILDEPLQGLD 433
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
123-225 |
2.42e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 48.09 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 123 LDLLPLrARYLDQLSGGQRQRACVAM--------VLcqntdYVLlDEPLNNLDMKHSVAMMKQLRRAADeLHKTIILVIH 194
Cdd:TIGR00630 477 LDYLSL-SRAAGTLSGGEAQRIRLATqigsgltgVL-----YVL-DEPSIGLHQRDNRRLINTLKRLRD-LGNTLIVVEH 548
|
90 100 110
....*....|....*....|....*....|....*..
gi 1353453005 195 DINFASAySDHIIAM------KQGEVLYRGTPQEIMR 225
Cdd:TIGR00630 549 DEDTIRA-ADYVIDIgpgageHGGEVVASGTPEEILA 584
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-213 |
2.69e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.00 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADS--GSVLVNGLEV-AKTPDEQMAKVL 77
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELqASNIRDTERAGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 78 SVLRQENHFTSRLTVEDLVGFGRyPWSKGRLTSEDRQHIETAMDF----LDLLPlrARYLDQLSGGQRQRACVAMVLCQN 153
Cdd:PRK13549 85 AIIHQELALVKELSVLENIFLGN-EITPGGIMDYDAMYLRAQKLLaqlkLDINP--ATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1353453005 154 TDYVLLDEPLNNL---DMKHSVAMMKQLRRAAdelhKTIILVIHDINFASAYSDHIIAMKQGE 213
Cdd:PRK13549 162 ARLLILDEPTASLtesETAVLLDIIRDLKAHG----IACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
27-222 |
2.78e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.18 E-value: 2.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 27 GGITSIIGANGAGKSTLLSVIS----RLLTADSGSVLVNGLevakTPDEQM----AKVLSVLRQENHFTSrLTVEDLVGF 98
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGI----TPEEIKkhyrGDVVYNAETDVHFPH-LTVGETLDF 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 99 G---RYPWSKGRLTSED--RQHI-ETAMDFLDLLPLRAR-----YLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLD 167
Cdd:TIGR00956 162 AarcKTPQNRPDGVSREeyAKHIaDVYMATYGLSHTRNTkvgndFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1353453005 168 MKHSVAMMKQLRRAADELHKTIILVIHDINfASAYS--DHIIAMKQGEVLYRGTPQE 222
Cdd:TIGR00956 242 SATALEFIRALKTSANILDTTPLVAIYQCS-QDAYElfDKVIVLYEGYQIYFGPADK 297
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
27-214 |
3.03e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.69 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 27 GGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEV-AKTPDEQMAK--------------VLSVLRQENhftsrLT 91
Cdd:PRK10762 278 GEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvTRSPQDGLANgivyisedrkrdglVLGMSVKEN-----MS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 92 VEDLVGFGRYPwskGRLTSEDRQhiETAMDFLDLLPLRARYLDQ----LSGGQRQRACVAMVLCQNTDYVLLDEPLNNLD 167
Cdd:PRK10762 353 LTALRYFSRAG---GSLKHADEQ--QAVSDFIRLFNIKTPSMEQaiglLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1353453005 168 mkhsVAMMKQLRRAADELHK---TIILVIHDINFASAYSDHIIAMKQGEV 214
Cdd:PRK10762 428 ----VGAKKEIYQLINQFKAeglSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-212 |
4.88e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 45.78 E-value: 4.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 17 LNRITESIPVGGITSIIGANGAGKSTLLSVIsrlLTADSGSVLVNGLevaKTPDEQMAKVLSVLRQenhftsrltvedLV 96
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG---LYASGKARLISFL---PKFSRNKLIFIDQLQF------------LI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 97 GFGrypwskgrltsedrqhietamdfLDLLPLrARYLDQLSGGQRQRACVAMVLCQNTDYVL--LDEPLNNLDMKHSVAM 174
Cdd:cd03238 73 DVG-----------------------LGYLTL-GQKLSTLSGGELQRVKLASELFSEPPGTLfiLDEPSTGLHQQDINQL 128
|
170 180 190
....*....|....*....|....*....|....*...
gi 1353453005 175 MKQLRRAADELHkTIILVIHDINFASaYSDHIIAMKQG 212
Cdd:cd03238 129 LEVIKGLIDLGN-TVILIEHNLDVLS-SADWIIDFGPG 164
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
24-55 |
7.70e-06 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 42.59 E-value: 7.70e-06
10 20 30
....*....|....*....|....*....|..
gi 1353453005 24 IPVGGITSIIGANGAGKSTLLSVISRLLTADS 55
Cdd:pfam13555 19 IDPRGNTLLTGPSGSGKSTLLDAIQTLLVPAK 50
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
131-224 |
1.16e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 131 RYLDQLSGGQRQRACVAMVLCQNTDYV--LLDEPLNNLDMKHSVAMMKQLRRAADElHKTIILVIHD---INFAsaysDH 205
Cdd:PRK00635 472 RALATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQ-GNTVLLVEHDeqmISLA----DR 546
|
90 100
....*....|....*....|....*
gi 1353453005 206 IIAMKQ------GEVLYRGTPQEIM 224
Cdd:PRK00635 547 IIDIGPgagifgGEVLFNGSPREFL 571
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
133-210 |
2.57e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.50 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 133 LDQLSGGQRQRACVAMVL----CQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADElHKTIILVIHDINFASAySDHIIA 208
Cdd:cd03227 75 RLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVK-GAQVIVITHLPELAEL-ADKLIH 152
|
..
gi 1353453005 209 MK 210
Cdd:cd03227 153 IK 154
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-214 |
2.80e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 44.63 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 3 EVKAIC-KSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEV-AKTPDEQMAKVLSVL 80
Cdd:COG3845 259 EVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDItGLSPRERRRLGVAYI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 81 ---RQENHFTSRLTVED---LVGFGRYPWSKGRLTSED--RQHIETAMDFLDLLP----LRARyldQLSGGQRQRACVAM 148
Cdd:COG3845 339 pedRLGRGLVPDMSVAEnliLGRYRRPPFSRGGFLDRKaiRAFAEELIEEFDVRTpgpdTPAR---SLSGGNQQKVILAR 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1353453005 149 VLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADElHKTIILVIHDINFASAYSDHIIAMKQGEV 214
Cdd:COG3845 416 ELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
27-214 |
3.45e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.52 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 27 GGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNG--LEVAKTPDEQMAKVlsVL----RQENHFTSRLTVEDLVGFG- 99
Cdd:PRK11288 279 GEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRDAIRAGI--MLcpedRKAEGIIPVHSVADNINISa 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 100 RYPWSKGRLTSEDRQHIETAMDFLDLLPLRARYLDQ----LSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDM--KHSVA 173
Cdd:PRK11288 357 RRHHLRAGCLINNRWEAENADRFIRSLNIKTPSREQlimnLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVgaKHEIY 436
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1353453005 174 mmkQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEV 214
Cdd:PRK11288 437 ---NVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-71 |
3.55e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.86 E-value: 3.55e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVIS--RLLTADSGSVLVNGLEV-AKTPDE 71
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghPAYKILEGDILFKGESIlDLEPEE 80
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
29-167 |
6.25e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.55 E-value: 6.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 29 ITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDeqmaKVLSVLRQENHFTSRLTVEDLVGFgrypWSKGRL 108
Cdd:PRK13541 28 ITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAK----PYCTYIGHNLGLKLEMTVFENLKF----WSEIYN 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1353453005 109 TSEDrqhIETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLD 167
Cdd:PRK13541 100 SAET---LYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
9-53 |
7.04e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 43.38 E-value: 7.04e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1353453005 9 KSYQNTTVlnritesiPVGGITSIIGANGAGKSTLLSVIsRLLTA 53
Cdd:COG4637 11 KSLRDLEL--------PLGPLTVLIGANGSGKSNLLDAL-RFLSD 46
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-225 |
9.13e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.19 E-value: 9.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 2 IEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKV----- 76
Cdd:NF033858 267 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVgymsq 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 77 -------LSVlRQ--ENHftSRLtvedlvgFgrypwskgRLTSEDR-QHIETAMDFLDLlplrARYLDQLSG----GQRQ 142
Cdd:NF033858 347 afslygeLTV-RQnlELH--ARL-------F--------HLPAAEIaARVAEMLERFDL----ADVADALPDslplGIRQ 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 143 R---AcVAMVlcQNTDYVLLDEPLNNLDmkhSVA------MMKQLRRaadELHKTIILVIHDINFAsAYSDHIIAMKQGE 213
Cdd:NF033858 405 RlslA-VAVI--HKPELLILDEPTSGVD---PVArdmfwrLLIELSR---EDGVTIFISTHFMNEA-ERCDRISLMHAGR 474
|
250
....*....|..
gi 1353453005 214 VLYRGTPQEIMR 225
Cdd:NF033858 475 VLASDTPAALVA 486
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-223 |
1.53e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 42.69 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 1 MIEVKAICKSYQNTT--VLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTpdeqmakvLS 78
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN--------IS 2008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 79 VLRQENHFTSRL-TVEDLVGFGRYPWSKGRLTSEDRQHIETAMDF-LDLLPLrARYLDQL----SGGQRQRACVAMVLCQ 152
Cdd:TIGR01257 2009 DVHQNMGYCPQFdAIDDLLTGREHLYLYARLRGVPAEEIEKVANWsIQSLGL-SLYADRLagtySGGNKRKLSTAIALIG 2087
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1353453005 153 NTDYVLLDEPLNNLDMKHSVAMMKQLRRAADElHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
9-61 |
1.58e-04 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 42.34 E-value: 1.58e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1353453005 9 KSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVN 61
Cdd:COG1106 11 RSFKDELTLSMVASGLRLLRVNLIYGANASGKSNLLEALYFLRNLVLNSSQPG 63
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
27-194 |
3.40e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.55 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 27 GGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKV-LSVLRQE----------NHFTSRLTVEDL 95
Cdd:PTZ00265 411 GKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKWWRSkIGVVSQDpllfsnsiknNIKYSLYSLKDL 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 96 VGFGRYPWSKGRLTSEDRQH--------------IETAMDFLDLLPLRARY----------------------------- 132
Cdd:PTZ00265 491 EALSNYYNEDGNDSQENKNKrnscrakcagdlndMSNTTDSNELIEMRKNYqtikdsevvdvskkvlihdfvsalpdkye 570
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1353453005 133 ------LDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIH 194
Cdd:PTZ00265 571 tlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
14-227 |
4.48e-04 |
|
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: 40.61 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 14 TTVLNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGlEVAKTPdeQMAKVLSVLRQENHFTSrltve 93
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-RISFSS--QFSWIMPGTIKENIIFG----- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 94 dlVGFGRYPWSKGRLTSEDRQHIeTAMDFLDLLPLRARYLDqLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDmkhsVA 173
Cdd:cd03291 122 --VSYDEYRYKSVVKACQLEEDI-TKFPEKDNTVLGEGGIT-LSGGQRARISLARAVYKDADLYLLDSPFGYLD----VF 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1353453005 174 MMKQL-RRAADEL--HKTIILVIHDINFASAySDHIIAMKQGEVLYRGTPQEI--MRPE 227
Cdd:cd03291 194 TEKEIfESCVCKLmaNKTRILVTSKMEHLKK-ADKILILHEGSSYFYGTFSELqsLRPD 251
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
135-224 |
4.69e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 40.94 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 135 QLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMMKQLRRAADELHKTIILVIHDINFASAYSDHIIAMKQGEV 214
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQT 237
|
90
....*....|
gi 1353453005 215 LYRGTPQEIM 224
Cdd:PRK15093 238 VETAPSKELV 247
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-223 |
5.98e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 40.64 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 17 LNRITESIPVGGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGlevaktpdeqMAKVLSVLRQENHFTSRLTVEDLV 96
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG----------SAALIAISSGLNGQLTGIENIELK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 97 GFgrypwsKGRLTSEDRQHI-ETAMDFLDLLPLRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMKHSVAMM 175
Cdd:PRK13545 110 GL------MMGLTKEKIKEIiPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1353453005 176 KQLRRaADELHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEI 223
Cdd:PRK13545 184 DKMNE-FKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
128-218 |
9.25e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.23 E-value: 9.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 128 LRARYLDQLSGGQRQRACVAMVLCQNTDYVLLDEPLNNLDMkHSVAMmkqLRRAADELHKTIILVIHDINFASAYSDHII 207
Cdd:PLN03073 337 MQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL-HAVLW---LETYLLKWPKTFIVVSHAREFLNTVVTDIL 412
|
90
....*....|..
gi 1353453005 208 AMK-QGEVLYRG 218
Cdd:PLN03073 413 HLHgQKLVTYKG 424
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
29-55 |
9.74e-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: 39.68 E-value: 9.74e-04
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
27-56 |
1.02e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 39.60 E-value: 1.02e-03
10 20 30
....*....|....*....|....*....|
gi 1353453005 27 GGITSIIGANGAGKSTLLSVISRLLTADSG 56
Cdd:COG3593 23 DDLTVLVGENNSGKSSILEALRLLLGPSSS 52
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
2-55 |
1.48e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 38.63 E-value: 1.48e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1353453005 2 IEVKAIcKSYQNTTV-LNRitesipvgGITSIIGANGAGKSTLLSVISRLLTADS 55
Cdd:pfam13476 1 LTIENF-RSFRDQTIdFSK--------GLTLITGPNGSGKTTILDAIKLALYGKT 46
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
22-54 |
1.51e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 1.51e-03
10 20 30
....*....|....*....|....*....|....
gi 1353453005 22 ESIPVGG-ITSIIGANGAGKSTLLSVISRLLTAD 54
Cdd:COG4913 18 HTIDFDGrGTLLTGDNGSGKSTLLDAIQTLLVPA 51
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-102 |
2.04e-03 |
|
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: 37.74 E-value: 2.04e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1353453005 27 GGITSIIGANGAGKSTLLSVISRLLTADSGSVLVNGLEVAKTPDEQMAKVLSVLRQENHFTSRLTVEDLVGFGRYP 102
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKL 77
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
158-223 |
2.37e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.04 E-value: 2.37e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1353453005 158 LLDEPLNNLDMKHSVAMMKQLRRAADELHkTIILVIHDINFaSAYSDHIIAM-----KQ-GEVLYRGTPQEI 223
Cdd:PRK00635 1725 LLDEIATSLDNQQKSALLVQLRTLVSLGH-SVIYIDHDPAL-LKQADYLIEMgpgsgKTgGKILFSGPPKDI 1794
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-48 |
2.48e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 38.62 E-value: 2.48e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1353453005 1 MIEVKAICKSYQNTTVLNRITESIPVGGITSIIGANGAGKSTLLSVIS 48
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLS 48
|
|
| YfjP |
cd11383 |
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several ... |
32-139 |
2.61e-03 |
|
YfjP GTPase; The Era (E. coli Ras-like protein)-like YfjP subfamily includes several uncharacterized bacterial GTPases that are similar to Era. They generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain.
Pssm-ID: 206743 [Multi-domain] Cd Length: 140 Bit Score: 37.32 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 32 IIGANGAGKSTLLSVISRLLTADSGSVLvnglevAKTPDEQMAkvlsVLRQENHftsRLTVEDLVGFGrypwSKGRLTSE 111
Cdd:cd11383 2 LMGKTGAGKSSLCNALFGTEVAAVGDRR------PTTRAAQAY----VWQTGGD---GLVLLDLPGVG----ERGRRDRE 64
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1353453005 112 DRQHIETAMDFLDLL------------PLRARYLDQLSGG 139
Cdd:cd11383 65 YEELYRRLLPEADLVlwlldaddralaADHDFYLLPLAGH 104
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
28-58 |
2.73e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 38.44 E-value: 2.73e-03
10 20 30
....*....|....*....|....*....|.
gi 1353453005 28 GITSIIGANGAGKSTLLSVISRLLTADSGSV 58
Cdd:COG3950 26 RLTVLVGENGSGKTTLLEAIALALSGLLSRL 56
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
123-225 |
4.87e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.08 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 123 LDLLPLrARYLDQLSGGQRQRACVAmvlCQ------NTDYVLlDEPLNNL---DMKHSVAMMKQLRraadELHKTIILVI 193
Cdd:COG0178 474 LDYLTL-DRSAGTLSGGEAQRIRLA---TQigsglvGVLYVL-DEPSIGLhqrDNDRLIETLKRLR----DLGNTVIVVE 544
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1353453005 194 HD---INFAsaysDHIIAM------KQGEVLYRGTPQEIMR 225
Cdd:COG0178 545 HDedtIRAA----DYIIDIgpgageHGGEVVAQGTPEEILK 581
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
24-194 |
7.07e-03 |
|
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 36.59 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 24 IPVGGITSIIGANGAGKSTLLSVIS-----------RLLTADSGSVLVNGLEVaktPDEQMAKVLSVLRQENHFTSRLTV 92
Cdd:pfam13481 30 LPAGGLGLLAGAPGTGKTTLALDLAaavatgkpwlgGPRVPEQGKVLYVSAEG---PADELRRRLRAAGADLDLPARLLF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 93 EDLVGFGR--YPWSKGRLTSEDRQHIETAMdfldllplraryldqlsggqRQRACVAMVLCQNTDYVLLDEPLNNLDMKh 170
Cdd:pfam13481 107 LSLVESLPlfFLDRGGPLLDADVDALEAAL--------------------EEVEDPDLVVIDPLARALGGDENSNSDVG- 165
|
170 180
....*....|....*....|....
gi 1353453005 171 svAMMKQLRRAADELHKTIILVIH 194
Cdd:pfam13481 166 --RLVKALDRLARRTGATVLLVHH 187
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-231 |
9.69e-03 |
|
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: 37.11 E-value: 9.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 17 LNRITESIPVGGITSIIGANGAGKSTLLSVI-SRLLTADSGSVLVNGLEVA-KTPDEQMAKVLSVL---RQENHFTSRLT 91
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVDiRNPAQAIRAGIAMVpedRKRHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1353453005 92 VED---LVGFGRYPwSKGRLTSE----------DRQHIETAMDFLDLlplrarylDQLSGGQRQRACVAMVLCQNTDYVL 158
Cdd:TIGR02633 356 VGKnitLSVLKSFC-FKMRIDAAaelqiigsaiQRLKVKTASPFLPI--------GRLSGGNQQKAVLAKMLLTNPRVLI 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1353453005 159 LDEPLNNLDMKHSVAMMKQLRRAADElHKTIILVIHDINFASAYSDHIIAMKQGEVLYRGTPQEIMRPEVIEA 231
Cdd:TIGR02633 427 LDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHALTQEQVLAA 498
|
|
| |
